Any process that activates or increases the frequency, rate or extent of the directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of a nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of a nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of a nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of a nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of a nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of a nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of a purine nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of a pyrimidine nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a purine nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a purine nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a purine nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a purine nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of a purine nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of a purine nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of a purine nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of a purine nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of a purine nucleoside into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of adenosine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of adenosine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of adenosine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of adenosine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of adenosine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of adenosine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of adenosine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of adenosine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of adenosine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of adenosine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process in which a secretory granule is transported to, and/or maintained in, a specific location within the cell.
Any process in which a secretory granule is transported to, and/or maintained in, a specific location within the cell.
Any process in which a dense core granule is transported to, and/or maintained in, a specific location within the cell.
Any process in which a dense core granule is transported to, and/or maintained in, a specific location within the cell.
Any process in which a dense core granule is transported to, and/or maintained in, a specific location within the cell.
The directed movement of a secretory granule to a specific location.
Any process in which a secretory granule is maintained in a specific location within a cell and prevented from moving elsewhere.
The directed movement of a dense core granule to a specific location.
The directed movement of a dense core granule to a specific location.
Any process in which a dense core granule is maintained in a specific location within a cell and prevented from moving elsewhere.
Any process in which a dense core granule is maintained in a specific location within a cell and prevented from moving elsewhere.
A cytoplasm to vacuole targeting pathway that uses machinery common with autophagy. The Cvt vesicle is formed when the receptor protein, Atg19, binds to the complexes of the target protein (aminopeptidase or alpha-mannosidase homododecamers), forming the Cvt complex. Atg11 binds to Atg9 and transports the Cvt complex to the pre-autophagosome (PAS). The phagophore membrane expands around the Cvt complex (excluding bulk cytoplasm) forming the Cvt vesicle. This pathway is mostly observed in yeast.
A cytoplasm to vacuole targeting pathway that uses machinery common with autophagy. The Cvt vesicle is formed when the receptor protein, Atg19, binds to the complexes of the target protein (aminopeptidase or alpha-mannosidase homododecamers), forming the Cvt complex. Atg11 binds to Atg9 and transports the Cvt complex to the pre-autophagosome (PAS). The phagophore membrane expands around the Cvt complex (excluding bulk cytoplasm) forming the Cvt vesicle. This pathway is mostly observed in yeast.
The process in which a methyl group is covalently attached to a molecule.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a jasmonic acid stimulus received in the context of the jasmonic acid- and ethylene (ethene)-dependent process that confers broad spectrum systemic resistance to disease in response to wounding or a pathogen.
Any process which produces a purine nucleotide from derivatives of it, without de novo synthesis.
Any process which produces a pyrimidine nucleotide from derivatives of it, without de novo synthesis.
Any process which produces guanosine monophosphate from derivatives of it, without de novo synthesis.
Any process which produces inosine monophosphate from derivatives of it, without de novo synthesis.
Any process which produces xanthosine monophosphate from derivatives of it, without de novo synthesis.
Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.
Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.
Catalysis of the ligation of lysine onto the cytidine residue present at the wobble position (usually position 34) of an AUA-specific isoleucine tRNA, to form the derivative lysidine. This modification converts both the codon specificity of tRNA(Ile) from AUG to AUA and its amino acid specificity from methionine to isoleucine.
Catalysis of the ligation of lysine onto the cytidine residue present at the wobble position (usually position 34) of an AUA-specific isoleucine tRNA, to form the derivative lysidine. This modification converts both the codon specificity of tRNA(Ile) from AUG to AUA and its amino acid specificity from methionine to isoleucine.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving a protein, occurring at the level of an individual cell.
Any process that modulates the frequency, rate or extent of the process of creating protein polymers.
Any process that stops, prevents, or reduces the frequency, rate or extent of the process of creating protein polymers.
Any process that stops, prevents, or reduces the frequency, rate or extent of the process of creating protein polymers.
Any process that stops, prevents, or reduces the frequency, rate or extent of the process of creating protein polymers.
Any process that stops, prevents, or reduces the frequency, rate or extent of the process of creating protein polymers.
Any process that activates or increases the frequency, rate or extent of the process of creating protein polymers.
Any process that activates or increases the frequency, rate or extent of the process of creating protein polymers.
Any process that activates or increases the frequency, rate or extent of the process of creating protein polymers.
Any process that activates or increases the frequency, rate or extent of the process of creating protein polymers.
Any process that activates or increases the frequency, rate or extent of the process of creating protein polymers.
The regulated release of a gonadotropin, any hormone that stimulates the gonads, especially follicle-stimulating hormone and luteinizing hormone.
The regulated release of luteinizing hormone, a gonadotropic glycoprotein hormone secreted by the anterior pituitary.
Any process that modulates the frequency, rate or extent of the regulated release of a gonadotropin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a gonadotropin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a gonadotropin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a gonadotropin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a gonadotropin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a gonadotropin.
Any process that activates or increases the frequency, rate or extent of the regulated release of a gonadotropin.
Any process that activates or increases the frequency, rate or extent of the regulated release of a gonadotropin.
Any process that activates or increases the frequency, rate or extent of the regulated release of a gonadotropin.
Any process that activates or increases the frequency, rate or extent of the regulated release of a gonadotropin.
Any process that activates or increases the frequency, rate or extent of the regulated release of a gonadotropin.
Any process that activates or increases the frequency, rate or extent of the regulated release of a gonadotropin.
A type of synapse occurring between an axon and a dendritic spine or dendritic shaft. Asymmetric synapses, the most abundant synapse type in the central nervous system, involve axons that contain predominantly spherical vesicles and contain a thickened postsynaptic density.  Most or all synapses of this type are excitatory.
A synapse that lacks an electron dense postsynaptic specialization. In vertebtrates, these occur primarily on dendrite shafts and neuronal cell bodies and involve persynapses containing clusters of predominantly flattened or elongated vesicles and are typcially inhibitory.
An assembly of four or five subunits which form a structure with an extracellular N-terminus and a large loop that together form the ligand binding domain. The C-terminus is intracellular. The ionotropic glutamate receptor complex itself acts as a ligand gated ion channel; on binding glutamate, charged ions pass through a channel in the center of the receptor complex. The AMPA receptors mediate fast synaptic transmission in the CNS and are composed of subunits GluR1-4, products from separate genes. These subunits have an extracellular N-terminus and an intracellular C-terminus.
An assembly of four or five subunits which form a structure with an extracellular N-terminus and a large loop that together form the ligand binding domain. The C-terminus is intracellular. The ionotropic glutamate receptor complex itself acts as a ligand gated ion channel; on binding glutamate, charged ions pass through a channel in the center of the receptor complex. The AMPA receptors mediate fast synaptic transmission in the CNS and are composed of subunits GluR1-4, products from separate genes. These subunits have an extracellular N-terminus and an intracellular C-terminus.
An assembly of four or five subunits which form a structure with an extracellular N-terminus and a large loop that together form the ligand binding domain. The C-terminus is intracellular. The ionotropic glutamate receptor complex itself acts as a ligand gated ion channel; on binding glutamate, charged ions pass through a channel in the center of the receptor complex. The AMPA receptors mediate fast synaptic transmission in the CNS and are composed of subunits GluR1-4, products from separate genes. These subunits have an extracellular N-terminus and an intracellular C-terminus.
An acetyl-CoA carboxylase complex located in the stroma of a plastid.
An acetate CoA-transferase complex located in the stroma of a plastid.
A biotin carboxylase complex located in the stroma of a plastid.
The process in which a non-myelinating glial cell membrane closes around an axon.
The process in which the structure and material content of mature central nervous system myelin is kept in a functional state.
The process in which the structure and material content of mature peripheral nervous system myelin is kept in a functional state.
The process in which the wraps of cell membrane that constitute myelin are laid down around an axon in the central or peripheral nervous system.
The process in which the wraps of cell membrane that constitute myelin are laid down around an axon by an oligodendrocyte in the central nervous system.
The process in which the wraps of cell membrane that constitute myelin are laid down around an axon by an oligodendrocyte in the peripheral nervous system.
The process in which a glial cell membrane closes around an axon in the central nervous system. This can be a myelinating or a non-myelinating neuron-glial interaction.
The process in which a Schwann cell membrane closes around an axon in the peripheral nervous system. This can be a myelinating or a non-myelinating neuron-glial interaction.
The process in which a non-myelinating glial cell membrane encircles an axon in the central nervous system.
The process in which a non-myelinating Schwann cell membrane encircles an axon in the peripheral nervous system. A single non-myelinating Schwann cell will typically associate with multiple axons.
The process in which satellite glial cells isolate neuronal cell bodies.
Catalysis of the hydrolysis of phosphodiester bonds in double-stranded RNA molecules.
Catalysis of the hydrolysis of phosphodiester bonds in double-stranded RNA molecules.
Catalysis of the hydrolysis of phosphodiester bonds in double-stranded RNA molecules.
Any process that stops, prevents, or reduces the frequency, rate or extent of initiation of DNA-dependent DNA replication.
Any process that stops, prevents, or reduces the frequency, rate or extent of initiation of DNA-dependent DNA replication.
Any process that stops, prevents, or reduces the frequency, rate or extent of initiation of DNA-dependent DNA replication.
Any process that stops, prevents, or reduces the frequency, rate or extent of initiation of DNA-dependent DNA replication.
Any process that stops, prevents, or reduces the frequency, rate or extent of initiation of DNA-dependent DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of DNA-dependent DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of DNA-dependent DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of DNA-dependent DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of DNA-dependent DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of DNA-dependent DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of DNA-dependent DNA replication.
A protein complex that possesses ribonuclease H activity, in which the catalytic subunit is a member of the RNase H2 (or HII) class. For example, in Saccharomyces the complex contains Rnh201p, Rnh202p and Rnh203p.
Any complex formed of proteins that act in mismatch repair.
A heterodimer involved in the recognition and repair of base-base and small insertion/deletion mismatches. In human the complex consists of two subunits, MSH2 and MSH6.
A heterodimer involved in the recognition and repair of base-base and small insertion/deletion mismatches. In human the complex consists of two subunits, MSH2 and MSH6.
A heterodimer involved in binding to and correcting insertion/deletion mutations. In human the complex consists of two subunits, MSH2 and MSH3.
A heterodimer involved in binding to and correcting insertion/deletion mutations. In human the complex consists of two subunits, MSH2 and MSH3.
Any process that modulates the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that activates or increases the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that activates or increases the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that activates or increases the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that activates or increases the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that activates or increases the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that activates or increases the frequency, rate or extent of the controlled release of an icosanoid from a cell.
Any process that modulates the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of a prostaglandin from a cell.
The controlled release of icosanoids, any of a group of C20 polyunsaturated fatty acids from a cell or a tissue.
The regulated release of a prostaglandin, any of a group of biologically active metabolites which contain a cyclopentane ring, from a cell or a tissue.
A stable heterodimer of angiogenin and placental ribonuclease inhibitor; interaction between angiogenin and PRI prevents angiogenin binding to its receptor to stimulate angiogenesis.
The chemical reactions and pathways resulting in the breakdown of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the breakdown of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the breakdown of ubiquinone, a lipid-soluble electron-transporting coenzyme.
The chemical reactions and pathways resulting in the breakdown of lipoate.
The chemical reactions and pathways resulting in the breakdown of lipoate.
The chemical reactions and pathways resulting in the breakdown of lipoate.
The chemical reactions and pathways resulting in the formation of the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the formation of the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the formation of the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the formation of the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the breakdown of the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the breakdown of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the breakdown of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the breakdown of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the breakdown of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the breakdown of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the breakdown of the W-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear tungsten ion (W) coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the breakdown of the W-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear tungsten ion (W) coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the breakdown of the W-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear tungsten ion (W) coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the breakdown of the W-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear tungsten ion (W) coordinated by one or two molybdopterin ligands.
The chemical reactions and pathways resulting in the breakdown of the W-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear tungsten ion (W) coordinated by one or two molybdopterin ligands.
The directed movement of alanine, 2-aminopropanoic acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of L-serine, 2-amino-3-hydroxypropanoic acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of L-serine, 2-amino-3-hydroxypropanoic acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of chondrocyte differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of chondrocyte differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of chondrocyte differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of chondrocyte differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of chondrocyte differentiation.
Any process that activates or increases the frequency, rate or extent of chondrocyte differentiation.
Any process that activates or increases the frequency, rate or extent of chondrocyte differentiation.
Any process that activates or increases the frequency, rate or extent of chondrocyte differentiation.
Any process that activates or increases the frequency, rate or extent of chondrocyte differentiation.
Any process that activates or increases the frequency, rate or extent of chondrocyte differentiation.
The regulated release of activin, a nonsteroidal regulator composed of two covalently linked beta subunits, which is synthesized in the pituitary gland and gonads and stimulates the secretion of follicle-stimulating hormone.
The regulated release of an inhibin, either of two glycoproteins (designated A and B), secreted by the gonads and present in seminal plasma and follicular fluid, that inhibit pituitary production of follicle-stimulating hormone.
Any process that modulates the frequency, rate or extent of the regulated release of activin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of activin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of activin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of activin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of activin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of activin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of activin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of activin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of activin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of activin from a cell.
Any process that modulates the frequency, rate or extent of the regulated release of inhibin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of inhibin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of inhibin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of inhibin from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of inhibin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of inhibin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of inhibin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of inhibin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of inhibin from a cell.
Any process that activates or increases the frequency, rate or extent of the regulated release of inhibin from a cell.
The chemical reactions and pathways involving aldosterone, a corticosteroid hormone that is produced by the zona glomerulosa of the adrenal cortex and regulates salt (sodium and potassium) and water balance.
The chemical reactions and pathways resulting in the formation of aldosterone, a corticosteroid hormone that is produced by the zona glomerulosa of the adrenal cortex and regulates salt (sodium and potassium) and water balance.
The chemical reactions and pathways resulting in the breakdown of aldosterone, a corticosteroid hormone that is produced by the zona glomerulosa of the adrenal cortex and regulates salt (sodium and potassium) and water balance.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving aldosterone.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of aldosterone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of aldosterone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of aldosterone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of aldosterone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of aldosterone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of aldosterone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of aldosterone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of aldosterone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of aldosterone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of aldosterone.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving any hormone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of hormones.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of hormones.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of hormones.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of hormones.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a follicle-stimulating hormone stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a follicle-stimulating hormone stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a follicle-stimulating hormone stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of stimulus by estradiol, a C18 steroid hormone hydroxylated at C3 and C17 that acts as a potent estrogen.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of stimulus by estradiol, a C18 steroid hormone hydroxylated at C3 and C17 that acts as a potent estrogen.
Interacting selectively and non-covalently with oxidized residues in DNA.
Interacting selectively and non-covalently with oxidized purine residues in DNA.
Interacting selectively and non-covalently with oxidized purine residues in DNA.
Interacting selectively and non-covalently with oxidized purine residues in DNA.
Interacting selectively and non-covalently with oxidized pyrimidine residues in DNA.
Interacting selectively and non-covalently with oxidized pyrimidine residues in DNA.
Interacting selectively and non-covalently with oxidized pyrimidine residues in DNA.
The molecular events that lead to the excision of a viral genome from the host genome.
The chemical reactions and pathways resulting in the breakdown of pyridoxal phosphate, pyridoxal phosphorylated at the hydroxymethyl group of C-5, the active form of vitamin B6.
The chemical reactions and pathways resulting in the breakdown of FMN, riboflavin 5'-(dihydrogen phosphate), a coenzyme for a number of oxidative enzymes including NADH dehydrogenase.
A homeostatic process involved in the maintenance of an internal steady state of oxygen within an organism or cell.
The directed movement of lipids within cells.
The directed movement of sterols within cells.
The directed movement of cholesterol, cholest-5-en-3-beta-ol, within cells.
Any process that modulates the frequency, rate or extent of the directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of sterols into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of sterols into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of sterols into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of sterols into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of sterols into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of sterols into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of sterols into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of sterols into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of sterols into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of sterols into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of cholesterol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of cholesterol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of cholesterol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of cholesterol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of cholesterol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of cholesterol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of cholesterol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of cholesterol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of cholesterol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of cholesterol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of lipids within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of lipids within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of lipids within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of lipids within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of lipids within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of lipids within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of lipids within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of lipids within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of lipids within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of lipids within cells.
Any process that modulates the frequency, rate or extent of the directed movement of sterols within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of sterols within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of sterols within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of sterols within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of sterols within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of sterols within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of sterols within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of sterols within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of sterols within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of sterols within cells.
Any process that modulates the frequency, rate or extent of the directed movement of cholesterol within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of cholesterol within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of cholesterol within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of cholesterol within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of cholesterol within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of cholesterol within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of cholesterol within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of cholesterol within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of cholesterol within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of cholesterol within cells.
Any process that modulates the frequency, rate or extent of the directed movement of substances within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of substances within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of substances within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of substances within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of substances within cells.
Any process that activates or increases the frequency, rate or extent of the directed movement of substances within cells.
A heterodimer involved in the recognition of base-base and small insertion/deletion mismatches. In human the complex consists of two subunits, MLH1 and PMS2.
A heterodimer involved in the recognition of base-base and small insertion/deletion mismatches. In human the complex consists of two subunits, MLH1 and PMS2.
A heterodimer involved in the recognition of base-base and small insertion/deletion mismatches. In human the complex consists of two subunits, MLH1 and PMS2.
A heterodimer involved in the recognition of base-base and small insertion/deletion mismatches. In human the complex consists of two subunits, MLH1 and PMS1.
A heterodimer involved in the recognition of base-base and small insertion/deletion mismatches. In human the complex consists of two subunits, MLH1 and PMS1.
The portion of the photoreceptor cell cilium linking the photoreceptor inner and outer segments. It's considered to be equivalent to the ciliary transition zone.
The process in which a transformation is induced in the geometry of a DNA double helix, resulting in a change in twist, writhe, or both, but with no change in linking number. Includes the unwinding of double-stranded DNA by helicases.
Combining with a MHC class I protein complex to mediate signaling that inhibits activation of a lymphocyte.
Combining with a MHC class I protein complex to mediate signaling that activates a lymphocyte.
A transmembrane protein complex composed of a MHC class Ib alpha chain and, in most cases, an invariant beta2-microglobin chain, and with or without a bound peptide or lipid antigen. Class Ib here refers to non-classical class I molecules, such as those of the CD1 or HLA-E gene families.
Interacting selectively and non-covalently with a HECT, 'Homologous to the E6-AP Carboxyl Terminus', domain of a protein.
Any process in which a melanosome is transported to, and/or maintained in, a specific location within the cell.
The directed movement of a melanosome to a specific location.
The directed movement of melanosomes into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Interacting selectively and non-covalently with a mismatch repair complex.
Interacting selectively and non-covalently with the mismatch repair complex MutLalpha.
Interacting selectively and non-covalently with the mismatch repair complex MutLbeta.
Interacting selectively and non-covalently with the mismatch repair complex MutSalpha.
Interacting selectively and non-covalently with the mismatch repair complex MutSbeta.
Any process that modulates the activity of a transporter.
Any process that stops or reduces the activity of a transporter.
Any process that stops or reduces the activity of a transporter.
Any process that stops or reduces the activity of a transporter.
Any process that stops or reduces the activity of a transporter.
Any process that activates or increases the activity of a transporter.
Any process that activates or increases the activity of a transporter.
Any process that activates or increases the activity of a transporter.
Any process that activates or increases the activity of a transporter.
Any process that activates or increases the activity of a transporter.
Any process that modulates the activity of an ion transporter.
Any process that stops or reduces the activity of an ion transporter.
Any process that stops or reduces the activity of an ion transporter.
Any process that stops or reduces the activity of an ion transporter.
Any process that stops or reduces the activity of an ion transporter.
Any process that stops or reduces the activity of an ion transporter.
Any process that activates or increases the activity of an ion transporter.
Any process that activates or increases the activity of an ion transporter.
Any process that activates or increases the activity of an ion transporter.
Any process that activates or increases the activity of an ion transporter.
Any process that activates or increases the activity of an ion transporter.
Any process that activates or increases the activity of an ion transporter.
Any process that modulates the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process that stops or reduces the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process that stops or reduces the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process that stops or reduces the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process that stops or reduces the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process that stops or reduces the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process that activates or increases the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process that activates or increases the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process that activates or increases the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process that activates or increases the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process that activates or increases the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process that activates or increases the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
Any process in which a lysosome is transported to, and/or maintained in, a specific location.
The component of an lysosome membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
The component of an lysosome membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
An actin-based protrusion from the apical surface of auditory and vestibular hair cells and of neuromast cells. These protrusions are supported by a bundle of cross-linked actin filaments (an actin cable), oriented such that the plus (barbed) ends are at the tip of the protrusion, capped by a tip complex which bridges to the plasma. Bundles of stereocilia act as mechanosensory organelles.
A bundle of cross-linked stereocilia, arranged around a kinocilium on the apical surface of a sensory hair cell (e.g. a neuromast, auditory or vestibular hair cell). Stereocilium bundles act as mechanosensory organelles by responding to fluid motion or fluid pressure changes.
Interacting selectively and non-covalently with a 30-bp purine-rich negative regulatory element; the best characterized such element is found in the first intronic region of the rat cardiac alpha-myosin heavy chain gene, and contains two palindromic high-affinity Ets-binding sites (CTTCCCTGGAAG). The presence of this element restricts expression of the gene containing it to cardiac myocytes.
Any process that modulates the frequency, rate or extent of mismatch repair.
Any process that stops, prevents, or reduces the frequency, rate or extent of mismatch repair.
Any process that stops, prevents, or reduces the frequency, rate or extent of mismatch repair.
Any process that stops, prevents, or reduces the frequency, rate or extent of mismatch repair.
Any process that stops, prevents, or reduces the frequency, rate or extent of mismatch repair.
Any process that activates or increases the frequency, rate or extent of mismatch repair.
Any process that activates or increases the frequency, rate or extent of mismatch repair.
Any process that activates or increases the frequency, rate or extent of mismatch repair.
Any process that activates or increases the frequency, rate or extent of mismatch repair.
Any process that activates or increases the frequency, rate or extent of mismatch repair.
A distinct compartment at the tip of a stereocilium, distal to the site of attachment to the apical cell surface. It consists of a dense matrix bridging the barbed ends of the stereocilium actin filaments with the overlying plasma membrane, is dynamic compared to the shaft, and is required for stereocilium elongation.
Interacting selectively and non-covalently with the GTPase protein binding domain (GDB) domain of a protein. The GBD is a short motif, including a minimum region of 16 amino acids, identified in proteins that bind to small GTPases such as Cdc42 and Rac.
Interacting selectively and non-covalently with the GTPase protein binding domain (GDB) domain of a protein. The GBD is a short motif, including a minimum region of 16 amino acids, identified in proteins that bind to small GTPases such as Cdc42 and Rac.
Interacting selectively and non-covalently with the GTPase protein binding domain (GDB) domain of a protein. The GBD is a short motif, including a minimum region of 16 amino acids, identified in proteins that bind to small GTPases such as Cdc42 and Rac.
Interacting selectively and non-covalently with the GTPase protein binding domain (GDB) domain of a protein. The GBD is a short motif, including a minimum region of 16 amino acids, identified in proteins that bind to small GTPases such as Cdc42 and Rac.
Catalysis of the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-beta-D-galactosaminides.
Any process that modulates the activity of the enzyme phospholipase A2.
Any process that activates or increases the activity of the enzyme phospholipase A2.
Any process that activates or increases the activity of the enzyme phospholipase A2.
Any process that activates or increases the activity of the enzyme phospholipase A2.
Any process that activates or increases the activity of the enzyme phospholipase A2.
Any process that activates or increases the activity of the enzyme phospholipase A2.
Any process that initiates the activity of the inactive enzyme phospholipase A2.
An assembly of actin filaments that are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
An assembly of actin filaments that are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
An assembly of actin filaments that are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
The end of a filopodium distal to the body of the cell.
Any process that modulates the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
Any process that stops, prevents, or reduces the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
Any process that stops, prevents, or reduces the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
Any process that stops, prevents, or reduces the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
Any process that stops, prevents, or reduces the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
A dense network of actin filaments found beneath the apical cell surface of hair cells, and into which stereocilia are inserted.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a melanosome. A melanosome is a tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a melanosome. A melanosome is a tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored.
Catalysis of the reaction: n-alkanal + NAD(P)+ = alk-2-enal + NAD(P)H + H+.
Catalysis of the reaction: n-alkanal + NAD(P)+ = alk-2-enal + NAD(P)H + H+.
Catalysis of the reaction: pheophorbide a + reduced ferredoxin + 2 O2 = red chlorophyll catabolite + oxidized ferredoxin + H2O.
Catalysis of the NADPH-dependent 7-O-4' reduction of phenylcoumaran lignans to the corresponding diphenols; for example, catalysis of the reaction: dehydrodiconiferyl alcohol + NADPH + H+ = isodihydrodehydrodiconiferyl alcohol + NADP+.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ergosterol.
A transcriptionally active complex that binds to an activin response element (ARE) in the promoter of target genes, and is composed of two SMAD2 proteins, one SMAD4 protein and a Forkhead activin signal transducer (FAST) transcription factor.
The directed movement of the hexose monosaccharide fructose into a cell or organelle.
A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to a target protein.
Covalent attachment of the ubiquitin-like protein URM1 to another protein.
Interacting selectively and non-covalently with DNA containing a hairpin. A hairpin structure forms when a DNA strand folds back on itself and intrachain base pairing occurs between inverted repeat sequences.
A protein complex comprising Carma1, Bcl10 and MALT1; plays a role in signal transduction during NF-kappaB activation.
Catalysis of the reaction: alpha-maltose + H2O = 2 alpha-D-glucose.
Catalysis of the removal of a methyl group from a substrate.
Catalysis of the removal of a methyl group from a histone.
Catalysis of the removal of a methyl group from lysine at position 4 of the histone H3 protein.
Catalysis of the reaction: histone H3 N6-methyl-L-lysine (position 9) + alpha-ketoglutarate + O2 = succinate + CO2 + formaldehyde + lysine. This reaction is the removal of a methyl group from lysine at position 9 of the histone H3 protein.
The generation of a mature nerve growth factor (NGF) by proteolysis of a precursor.
The generation of a mature nerve growth factor (NGF) by proteolysis of a precursor.
The directed movement of membrane-bounded vesicles from recycling endosomes back to the plasma membrane where they are recycled for further rounds of transport.
The directed movement of membrane-bounded vesicles from peripheral endocytic compartments back to the plasma membrane where they are recycled for further rounds of transport.
The directed movement of membrane-bounded vesicles from deep (non-peripheral) compartments endocytic compartments back to the plasma membrane where they are recycled for further rounds of transport.
Any process that modulates the frequency, rate or extent of protein oligomerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein oligomerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein oligomerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein oligomerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein oligomerization.
Any process that activates or increases the frequency, rate or extent of protein oligomerization.
Any process that activates or increases the frequency, rate or extent of protein oligomerization.
Any process that activates or increases the frequency, rate or extent of protein oligomerization.
Any process that activates or increases the frequency, rate or extent of protein oligomerization.
Any process that activates or increases the frequency, rate or extent of protein oligomerization.
Any process that activates or increases the frequency, rate or extent of protein oligomerization.
Any process that modulates the frequency, rate or extent of protein homooligomerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein homooligomerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein homooligomerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein homooligomerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein homooligomerization.
Any process that activates or increases the frequency, rate or extent of protein homooligomerization.
Any process that activates or increases the frequency, rate or extent of protein homooligomerization.
Any process that activates or increases the frequency, rate or extent of protein homooligomerization.
Any process that activates or increases the frequency, rate or extent of protein homooligomerization.
Any process that activates or increases the frequency, rate or extent of protein homooligomerization.
Any process that activates or increases the frequency, rate or extent of protein homooligomerization.
Any process that modulates the frequency, rate or extent of the division of the cytoplasm of a cell and its separation into two daughter cells.
Any process that modulates the frequency, rate or extent of the division of the cytoplasm of a cell and its separation into two daughter cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that activates or increases the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that activates or increases the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that activates or increases the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that activates or increases the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that activates or increases the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that activates or increases the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process that activates or increases the frequency, rate or extent of the division of the cytoplasm of a cell, and its separation into two daughter cells.
Any process involved in the maintenance of an internal steady state of calcium ions within the Golgi apparatus of a cell or between the Golgi and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the Golgi apparatus of a cell or between the Golgi and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the Golgi apparatus of a cell or between the Golgi and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the Golgi apparatus of a cell or between the Golgi and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the endoplasmic reticulum of a cell or between the endoplasmic reticulum and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the endoplasmic reticulum of a cell or between the endoplasmic reticulum and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the endoplasmic reticulum of a cell or between the endoplasmic reticulum and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the endoplasmic reticulum of a cell or between the endoplasmic reticulum and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the endoplasmic reticulum of a cell or between the endoplasmic reticulum and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the endoplasmic reticulum of a cell or between the endoplasmic reticulum and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the endoplasmic reticulum of a cell or between the endoplasmic reticulum and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the endoplasmic reticulum of a cell or between the endoplasmic reticulum and its surroundings.
Any process involved in the maintenance of an internal steady state of calcium ions within the endoplasmic reticulum of a cell or between the endoplasmic reticulum and its surroundings.
Any process that increases the concentration of calcium ions in the endoplasmic reticulum.
Any process that increases the concentration of calcium ions in the endoplasmic reticulum.
Any process that increases the concentration of calcium ions in the endoplasmic reticulum.
Any process that increases the concentration of calcium ions in the endoplasmic reticulum.
Any process that decreases the concentration of calcium ions in the endoplasmic reticulum.
Any process that decreases the concentration of calcium ions in the endoplasmic reticulum.
Any process that decreases the concentration of calcium ions in the endoplasmic reticulum.
Any process that decreases the concentration of calcium ions in the endoplasmic reticulum.
Any process that decreases the concentration of calcium ions in the endoplasmic reticulum.
Any process that decreases the concentration of calcium ions in the endoplasmic reticulum.
The directed movement of calcium ions (Ca2+) into, out of or within the Golgi apparatus.
The external (cytoplasmic) face of the mitochondrial outer membrane.
The external (cytoplasmic) face of the mitochondrial outer membrane.
The external (cytoplasmic) face of the mitochondrial outer membrane.
The external (cytoplasmic) face of the mitochondrial outer membrane.
The process in which the anatomical structures of an otolith are generated and organized.
The process that gives rise to an otolith. This process pertains to the initial formation of a structure from unspecified parts.
A complex that possesses di-trans,poly-cis-decaprenylcistransferase activity; involved in ubiquinone biosynthesis.
A homodimeric complex that possesses di-trans,poly-cis-decaprenylcistransferase activity; involved in ubiquinone biosynthesis.
A heterotetrameric complex located in the mitochondrial inner membrane that possesses di-trans,poly-cis-decaprenylcistransferase activity; involved in ubiquinone biosynthesis. In S. pombe it is a heterotetramer of Dlp1 and Dps1.
Any process that modulates the frequency, rate, or extent of interferon type I production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that stops, prevents, or reduces the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that stops, prevents, or reduces the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that stops, prevents, or reduces the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that stops, prevents, or reduces the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that stops, prevents, or reduces the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that activates or increases the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that activates or increases the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that activates or increases the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that activates or increases the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that activates or increases the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that activates or increases the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
A series of molecular signals within the cell that are mediated by a member of the Rab family of proteins switching to a GTP-bound active state.
Any process that modulates the frequency, rate or extent of Rab protein signal transduction.
A series of molecular signals within the cell that are mediated by a member of the Ral family of proteins switching to a GTP-bound active state.
Any process that modulates the frequency, rate or extent of Ral protein signal transduction.
A series of molecular signals within the cell that are mediated by a member of the Rap family of proteins switching to a GTP-bound active state.
Any process that modulates the frequency, rate or extent of Rap protein signal transduction.
A series of molecular signals within the cell that are mediated by the Cdc42 protein switching to a GTP-bound active state.
A series of molecular signals within the cell that are mediated by the Cdc42 protein switching to a GTP-bound active state.
A series of molecular signals within the cell that are mediated by the Cdc42 protein switching to a GTP-bound active state.
Any process that modulates the frequency, rate or extent of Cdc42 protein signal transduction.
The series of events in which a stimulus from a molecule of bacterial origin is received and converted into a molecular signal.
The series of events in which a stimulus from a molecule of bacterial origin is received and converted into a molecular signal.
The series of events in which a stimulus from a molecule of bacterial origin is received and converted into a molecular signal.
The series of events in which a stimulus from a molecule of fungal origin is received and converted into a molecular signal.
The series of events in which a stimulus from a molecule of fungal origin is received and converted into a molecular signal.
The series of events in which a stimulus from a molecule of oomycetes origin is received and converted into a molecular signal.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a bacterial lipoprotein stimulus.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a peptidoglycan stimulus. Peptidoglycan is a bacterial cell wall macromolecule.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a muramyl dipeptide stimulus. Muramyl dipeptide is derived from peptidoglycan.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria.
The series of events in which a lipopolysaccharide stimulus is received by a cell and converted into a molecular signal. Lipopolysaccharide is a major component of the cell wall of gram-negative bacteria.
The series of events in which a muramyl dipeptide stimulus is received by a cell and converted into a molecular signal. Muramyl dipeptide is derived from peptidoglycan.
The series of events in which a peptidoglycan stimulus is received by a cell and converted into a molecular signal. Peptidoglycan is a bacterial cell wall macromolecule.
Interacting selectively and non-covalently, in a non-covalent manner, with muramyl dipeptide; muramyl dipeptide is derived from peptidoglycan.
Any biological process, occurring at the level of a multicellular organism, pertinent to its function.
Any biological process, occurring at the level of a multicellular organism, pertinent to its function.
Any biological process, occurring at the level of a multicellular organism, pertinent to its function.
Any biological process, occurring at the level of a multicellular organism, pertinent to its function.
A biological process whose specific outcome is the progression of an integrated living unit: an anatomical structure (which may be a subcellular structure, cell, tissue, or organ), or organism over time from an initial condition to a later condition.
A biological process whose specific outcome is the progression of an integrated living unit: an anatomical structure (which may be a subcellular structure, cell, tissue, or organ), or organism over time from an initial condition to a later condition.
A biological process whose specific outcome is the progression of an integrated living unit: an anatomical structure (which may be a subcellular structure, cell, tissue, or organ), or organism over time from an initial condition to a later condition.
The biological process in which new individuals are produced by one or two multicellular organisms. The new individuals inherit some proportion of their genetic material from the parent or parents.
The biological process in which new individuals are produced by one or two single-celled organisms. The new individuals inherit some proportion of their genetic material from the parent or parents.
A cellular process that is involved in cytokinesis (the division of the cytoplasm of a cell and its separation into two daughter cells).
Any process in which a protein is maintained in a specific location within, or in the membrane of, a cell, and is prevented from moving elsewhere.
The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating a region of unpaired single strands.
The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating a region of unpaired single strands.
The directed movement of substances from endosomes to lysosomes or vacuoles by a pathway in which molecules are sorted into multivesicular bodies, which then fuse with the target compartment.
The directed movement of substances from endosomes to lysosomes by a pathway in which molecules are sorted into multivesicular bodies, which then fuse with the lysosome.
The directed movement of substances from endosomes to vacuoles by a pathway in which molecules are sorted into multivesicular bodies, which then fuse with the vacuole.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that stops or reduces the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
Any process that activates or increases the activity of a phosphoprotein phosphatase.
A protein complex formed by the association of superoxide dismutase 1 (SOD1) with calcineurin; complex formation is implicated in activation of calcineurin by SOD1.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + amino acid(in) -> ADP + phosphate + amino acid(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + cysteine(in) -> ADP + phosphate + cysteine(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + amino acid(out) -> ADP + phosphate + amino acid(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + D-methionine(in) -> ADP + phosphate + D-methionine(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + D-methionine(out) -> ADP + phosphate + D-methionine(in).
Enables the transfer of silicon from the inside of the cell to the outside of the cell across a membrane.
The establishment, maintenance and elaboration of the rostro-caudal axis of a somite, prior to the morphological formation of a somite boundary.
The establishment, maintenance and elaboration of the rostro-caudal axis of a somite, prior to the morphological formation of a somite boundary.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a retinoic acid stimulus.
The directed movement of proteins from the endoplasmic reticulum.
The directed movement of proteins from the endoplasmic reticulum.
The directed movement of proteins from the endoplasmic reticulum.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a microvillus, a thin cylindrical membrane-covered projection on the surface of a cell.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a microvillus, a thin cylindrical membrane-covered projection on the surface of a cell.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a microvillus on a follicle cell. A microvillus is a thin cylindrical membrane-covered projection on the surface of an animal cell containing a core bundle of actin filaments.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a microvillus on a follicle cell. A microvillus is a thin cylindrical membrane-covered projection on the surface of an animal cell containing a core bundle of actin filaments.
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a microvillus.
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a microvillus.
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a microvillus on a follicle cell.
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a microvillus on a follicle cell.
A process that modulates the length of a microvillus.
A process that modulates the length of a microvillus on a follicle cell.
A process that modulates the formation of a microvillus.
A process that modulates the size of a cellular component.
A process that modulates the size of a cell projection.
The specific behavior of an organism that are associated with finding a host organism; may include behavioral responses to light, temperature, or chemical emanations from the prospective host.
Any process that modulates the frequency, rate or extent of any behavior associated with finding a host organism.
Any process that stops, prevents, or reduces the frequency, rate or extent of any behavior associated with finding a host organism.
Any process that stops, prevents, or reduces the frequency, rate or extent of any behavior associated with finding a host organism.
Any process that stops, prevents, or reduces the frequency, rate or extent of any behavior associated with finding a host organism.
Any process that stops, prevents, or reduces the frequency, rate or extent of any behavior associated with finding a host organism.
Any process that stops, prevents, or reduces the frequency, rate or extent of any behavior associated with finding a host organism.
Any process that activates or increases the frequency, rate or extent of any behavior associated with finding a host organism.
Any process that activates or increases the frequency, rate or extent of any behavior associated with finding a host organism.
Any process that activates or increases the frequency, rate or extent of any behavior associated with finding a host organism.
Any process that activates or increases the frequency, rate or extent of any behavior associated with finding a host organism.
Any process that activates or increases the frequency, rate or extent of any behavior associated with finding a host organism.
Any process that activates or increases the frequency, rate or extent of any behavior associated with finding a host organism.
A cortical network of highly dynamic tubules that are juxtaposed to the plasma membrane and undergo ring closure and tubule-branching movements.
A cortical network of highly dynamic tubules that are juxtaposed to the plasma membrane and undergo ring closure and tubule-branching movements.
A cortical network of highly dynamic tubules that are juxtaposed to the plasma membrane and undergo ring closure and tubule-branching movements.
A cortical network of highly dynamic tubules that are juxtaposed to the plasma membrane and undergo ring closure and tubule-branching movements.
Catalysis of the reaction: peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R.
Catalysis of the reaction: peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R.
Catalysis of the reaction: peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R.
Catalysis of the reaction: peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R.
The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.
The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.
The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.
The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.
The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.
The chemical reactions and pathways resulting in the formation of a protein in a plastid. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the plastid has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.
The chemical reactions and pathways resulting in the formation of a protein in a plastid. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the plastid has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.
The chemical reactions and pathways resulting in the formation of a protein in a plastid. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the plastid has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.
The chemical reactions and pathways resulting in the formation of a protein in a plastid. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the plastid has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.
The chemical reactions and pathways resulting in the formation of a protein in a plastid. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the plastid has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.
A protein complex that is involved in the transcription of ribosomal genes. In Saccharomyces this complex consists of Ckb2p, Utp22p, Rrp7p and Ifh1p.
Interacting selectively and non-covalently with a deoxyribonucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked to deoxyribose.
Interacting selectively and non-covalently with a purine deoxyribonucleoside, a compound consisting of a purine base linked to deoxyribose.
Interacting selectively and non-covalently with a pyrimidine deoxyribonucleoside, a compound consisting of a pyrimidine base linked to deoxyribose.
Interacting selectively and non-covalently with a ribonucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked to ribose.
Interacting selectively and non-covalently with a purine ribonucleoside, a compound consisting of a purine base linked to ribose.
Interacting selectively and non-covalently with a pyrimidine ribonucleoside, a compound consisting of a pyrimidine base linked to ribose.
Interacting selectively and non-covalently with a deoxyribonucleotide, any compound consisting of a deoxyribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the deoxyribose moiety.
Interacting selectively and non-covalently with a ribonucleotide, any compound consisting of a ribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety.
Interacting selectively and non-covalently with a purine deoxyribonucleotide, any compound consisting of a purine deoxyribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the deoxyribose moiety.
Interacting selectively and non-covalently with a purine ribonucleotide, any compound consisting of a purine ribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety.
Interacting selectively and non-covalently with a pyrimidine deoxyribonucleotide, any compound consisting of a pyrimidine deoxyribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the deoxyribose moiety.
Interacting selectively and non-covalently with a pyrimidine ribonucleotide, any compound consisting of a pyrimidine ribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety.
Interacting selectively and non-covalently with an adenyl deoxyribonucleotide, any compound consisting of adenosine esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the deoxyribose moiety.
Interacting selectively and non-covalently with an adenyl ribonucleotide, any compound consisting of adenosine esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety.
Interacting selectively and non-covalently with a guanyl deoxyribonucleotide, any compound consisting of guanosine esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the deoxyribose moiety.
Interacting selectively and non-covalently with a guanyl ribonucleotide, any compound consisting of guanosine esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety.
Interacting selectively and non-covalently with dAMP, deoxyadenosine monophosphate.
Interacting selectively and non-covalently with dADP, deoxyadenosine diphosphate.
Interacting selectively and non-covalently with dATP, deoxyadenosine triphosphate.
Interacting selectively and non-covalently with dGMP, deoxyguanosine monophosphate.
Interacting selectively and non-covalently with dGDP, deoxyguanosine diphosphate.
Interacting selectively and non-covalently with dGTP, deoxyguanosine triphosphate.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a progesterone stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin K stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a menaquinone (vitamin K2) stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a menaquinone (vitamin K2) stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a phylloquinone (vitamin K1) stimulus.
Catalysis of the unwinding of an RNA helix in the direction 5' to 3'.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction drives the unwinding of an RNA helix in the direction 5' to 3'.
Catalysis of the transfer of a linoleoyl ((9Z,12Z)-octadeca-9,12-dienoyl) group to an oxygen atom on the acceptor molecule.
Catalysis of the transfer of a linoleoyl ((9Z,12Z)-octadeca-9,12-dienoyl) group from phosphatidylcholine to an oxygen atom on a cardiolipin molecule.
The lipid bilayer surrounding an aleurone grain.
A fibrous network that is part of the hyalin layer extracellular matrix. The apical lamina is thought to be principally composed of the glycoproteins fibropellins. This matrix has been found in echinoderms.
The lipid bilayer surrounding any of the thin, flattened compartments that form the central portion of the Golgi complex.
A process of peroxisome organization in which assembly or arrangement of constituent parts takes place in the endoplasmic reticulum.
A process of peroxisome organization in which assembly or arrangement of constituent parts takes place in the endoplasmic reticulum.
A process of peroxisome organization in which assembly or arrangement of constituent parts takes place in the endoplasmic reticulum.
The portion of the plasma membrane surrounding a growth cone.
The lipid bilayer surrounding a multivesicular body.
The lipid bilayer surrounding a multivesicular body.
The lipid bilayer surrounding a multivesicular body.
The lipid bilayer surrounding a protein storage vacuole.
The portion of the plasma membrane surrounding a ruffle.
The lipid bilayer surrounding any of the compartments that make up the trans-Golgi network.
The lipid bilayer surrounding any of the compartments that make up the trans-Golgi network.
The portion of the plasma membrane surrounding a neuron projection.
The portion of the plasma membrane surrounding a dendrite.
The portion of the plasma membrane surrounding a dendritic spine.
The component of the mitochondrial membrane consisting of the gene products having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
A small membrane-bounded vesicle that releases its contents by exocytosis in response to insulin stimulation; the contents are enriched in GLUT4, IRAP and VAMP2.
A small membrane-bounded vesicle that releases its contents by exocytosis in response to insulin stimulation; the contents are enriched in GLUT4, IRAP and VAMP2.
A small membrane-bounded vesicle that releases its contents by exocytosis in response to insulin stimulation; the contents are enriched in GLUT4, IRAP and VAMP2.
The directed movement of a protein from one location to another within a lipid bilayer.
The directed movement of a protein from one location to another within a lipid bilayer.
The directed movement of a protein from one location to another within a lipid bilayer.
The directed movement of a B cell receptor within a lipid bilayer.
The directed movement of a B cell receptor within a lipid bilayer.
The directed movement of a B cell receptor within a lipid bilayer.
The directed movement of a protein into a membrane raft. Membrane rafts are small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes.
The directed movement of a protein into a membrane raft. Membrane rafts are small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes.
The directed movement of a protein into a membrane raft. Membrane rafts are small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes.
The directed movement of a protein into a membrane raft. Membrane rafts are small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes.
The directed movement of a B cell receptor into a membrane raft.
The directed movement of a B cell receptor into a membrane raft.
The directed movement of a B cell receptor into a membrane raft.
The directed movement of a B cell receptor into a membrane raft.
The directed movement of a B cell receptor into an immunological synapse.
The directed movement of a B cell receptor into an immunological synapse.
The directed movement of a B cell receptor into an immunological synapse.
The directed movement of a protein out of a membrane raft. Membrane rafts are small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes.
The directed movement of a protein out of a membrane raft. Membrane rafts are small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes.
The directed movement of a protein out of a membrane raft. Membrane rafts are small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes.
The directed movement of a protein out of a membrane raft. Membrane rafts are small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes.
The directed movement of a chemokine receptor out of a membrane raft.
The directed movement of a chemokine receptor out of a membrane raft.
The appearance of connective tissue growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of connective tissue growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of connective tissue growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of connective tissue growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of connective tissue growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of connective tissue growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of a chemokine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of fractalkine due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of granulocyte macrophage colony-stimulating factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of granulocyte macrophage colony-stimulating factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of hepatocyte growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
The appearance of type I interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
The appearance of interferon-alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interferon-alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interferon-beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interferon-beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon.
The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon.
The appearance of interferon-gamma due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon-gamma is also known as type II interferon.
The appearance of interleukin-1 alpha due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-1 beta due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-1 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-10 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-11 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-12 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-13 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-14 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-15 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-16 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of any member of the interleukin-17 family of cytokines due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-18 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-19 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-20 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-21 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-22 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-23 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-24 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-25 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-26 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-27 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-3 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-4 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-5 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-6 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-7 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-8 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-9 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of TRAIL due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of tumor necrosis factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of lymphotoxin A due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of lymphotoxin A due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of lymphotoxin A due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of lymphotoxin A due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
Any process that modulates the frequency, rate, or extent of chemokine production.
Any process that modulates the frequency, rate, or extent of connective tissue growth factor production.
Any process that modulates the frequency, rate, or extent of connective tissue growth factor production.
Any process that modulates the frequency, rate, or extent of connective tissue growth factor production.
Any process that modulates the frequency, rate, or extent of connective tissue growth factor production.
Any process that modulates the frequency, rate, or extent of connective tissue growth factor production.
Any process that modulates the frequency, rate, or extent of connective tissue growth factor production.
Any process that modulates the frequency, rate, or extent of fractalkine production.
Any process that modulates the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that modulates the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that modulates the frequency, rate, or extent of hepatocyte growth factor production.
Any process that modulates the frequency, rate, or extent of interferon-alpha production.
Any process that modulates the frequency, rate, or extent of interferon-beta production.
Any process that modulates the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that modulates the frequency, rate, or extent of interleukin-1 alpha production.
Any process that modulates the frequency, rate, or extent of interleukin-1 beta production.
Any process that modulates the frequency, rate, or extent of interleukin-1 production.
Any process that modulates the frequency, rate, or extent of interleukin-10 production.
Any process that modulates the frequency, rate, or extent of interleukin-11 production.
Any process that modulates the frequency, rate, or extent of interleukin-12 production.
Any process that modulates the frequency, rate, or extent of interleukin-13 production.
Any process that modulates the frequency, rate, or extent of interleukin-14 production.
Any process that modulates the frequency, rate, or extent of interleukin-15 production.
Any process that modulates the frequency, rate, or extent of interleukin-16 production.
Any process that modulates the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that modulates the frequency, rate, or extent of interleukin-18 production.
Any process that modulates the frequency, rate, or extent of interleukin-19 production.
Any process that modulates the frequency, rate, or extent of interleukin-2 production.
Any process that modulates the frequency, rate, or extent of interleukin-20 production.
Any process that modulates the frequency, rate, or extent of interleukin-21 production.
Any process that modulates the frequency, rate, or extent of interleukin-22 production.
Any process that modulates the frequency, rate, or extent of interleukin-23 production.
Any process that modulates the frequency, rate, or extent of interleukin-24 production.
Any process that modulates the frequency, rate, or extent of interleukin-25 production.
Any process that modulates the frequency, rate, or extent of interleukin-26 production.
Any process that modulates the frequency, rate, or extent of interleukin-27 production.
Any process that modulates the frequency, rate, or extent of interleukin-3 production.
Any process that modulates the frequency, rate, or extent of interleukin-4 production.
Any process that modulates the frequency, rate, or extent of interleukin-5 production.
Any process that modulates the frequency, rate, or extent of interleukin-6 production.
Any process that modulates the frequency, rate, or extent of interleukin-7 production.
Any process that modulates the frequency, rate, or extent of interleukin-8 production.
Any process that modulates the frequency, rate, or extent of interleukin-9 production.
Any process that modulates the frequency, rate, or extent of TRAIL production.
Any process that modulates the frequency, rate, or extent of tumor necrosis factor production.
Any process that modulates the frequency, rate, or extent of tumor necrosis factor production.
Any process that modulates the frequency, rate, or extent of tumor necrosis factor production.
Any process that modulates the frequency, rate, or extent of lymphotoxin A production.
Any process that modulates the frequency, rate, or extent of lymphotoxin A production.
Any process that modulates the frequency, rate, or extent of lymphotoxin A production.
Any process that modulates the frequency, rate, or extent of lymphotoxin A production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of chemokine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of chemokine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of chemokine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of chemokine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of connective tissue growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of connective tissue growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of connective tissue growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of connective tissue growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of connective tissue growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of connective tissue growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of connective tissue growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of connective tissue growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of connective tissue growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of connective tissue growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of fractalkine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of fractalkine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of fractalkine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of fractalkine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of hepatocyte growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of hepatocyte growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of hepatocyte growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of hepatocyte growth factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-alpha production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-alpha production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-alpha production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-alpha production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 alpha production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 alpha production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 alpha production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 alpha production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 alpha production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 beta production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 beta production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 beta production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 beta production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 beta production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-1 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-10 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-10 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-10 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-10 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-10 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-11 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-11 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-11 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-11 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-11 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-12 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-12 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-12 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-12 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-12 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-13 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-13 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-13 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-13 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-13 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-14 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-14 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-14 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-14 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-14 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-15 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-15 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-15 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-15 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-15 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-16 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-16 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-16 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-16 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-16 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-18 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-18 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-18 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-18 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-18 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-19 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-19 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-19 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-19 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-19 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-2 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-2 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-2 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-2 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-2 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-20 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-20 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-20 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-20 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-20 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-21 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-21 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-21 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-21 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-21 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-22 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-22 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-22 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-22 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-22 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-23 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-23 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-23 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-23 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-23 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-24 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-24 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-24 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-24 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-24 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-25 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-25 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-25 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-25 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-25 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-26 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-26 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-26 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-26 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-26 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-27 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-27 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-27 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-27 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-27 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-3 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-3 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-3 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-3 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-3 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-4 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-4 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-4 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-4 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-4 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-5 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-5 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-5 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-5 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-5 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-6 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-6 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-6 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-6 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-6 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-7 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-7 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-7 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-7 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-7 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-8 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-8 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-8 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-8 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-8 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-9 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-9 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-9 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-9 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-9 production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of TRAIL production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of TRAIL production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of TRAIL production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of TRAIL production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of tumor necrosis factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of tumor necrosis factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of tumor necrosis factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of tumor necrosis factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of tumor necrosis factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of tumor necrosis factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of tumor necrosis factor production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of lymphotoxin A production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of lymphotoxin A production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of lymphotoxin A production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of lymphotoxin A production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of lymphotoxin A production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of lymphotoxin A production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of lymphotoxin A production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of lymphotoxin A production.
Any process that activates or increases the frequency, rate, or extent of chemokine production.
Any process that activates or increases the frequency, rate, or extent of chemokine production.
Any process that activates or increases the frequency, rate, or extent of chemokine production.
Any process that activates or increases the frequency, rate, or extent of chemokine production.
Any process that activates or increases the frequency, rate, or extent of chemokine production.
Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production.
Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production.
Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production.
Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production.
Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production.
Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production.
Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production.
Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production.
Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production.
Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production.
Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production.
Any process that activates or increases the frequency, rate, or extent of fractalkine production.
Any process that activates or increases the frequency, rate, or extent of fractalkine production.
Any process that activates or increases the frequency, rate, or extent of fractalkine production.
Any process that activates or increases the frequency, rate, or extent of fractalkine production.
Any process that activates or increases the frequency, rate, or extent of fractalkine production.
Any process that activates or increases the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that activates or increases the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that activates or increases the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that activates or increases the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that activates or increases the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that activates or increases the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that activates or increases the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production.
Any process that activates or increases the frequency, rate, or extent of hepatocyte growth factor production.
Any process that activates or increases the frequency, rate, or extent of hepatocyte growth factor production.
Any process that activates or increases the frequency, rate, or extent of hepatocyte growth factor production.
Any process that activates or increases the frequency, rate, or extent of hepatocyte growth factor production.
Any process that activates or increases the frequency, rate, or extent of hepatocyte growth factor production.
Any process that activates or increases the frequency, rate, or extent of interferon-alpha production.
Any process that activates or increases the frequency, rate, or extent of interferon-alpha production.
Any process that activates or increases the frequency, rate, or extent of interferon-alpha production.
Any process that activates or increases the frequency, rate, or extent of interferon-alpha production.
Any process that activates or increases the frequency, rate, or extent of interferon-alpha production.
Any process that activates or increases the frequency, rate, or extent of interferon-beta production.
Any process that activates or increases the frequency, rate, or extent of interferon-beta production.
Any process that activates or increases the frequency, rate, or extent of interferon-beta production.
Any process that activates or increases the frequency, rate, or extent of interferon-beta production.
Any process that activates or increases the frequency, rate, or extent of interferon-beta production.
Any process that activates or increases the frequency, rate, or extent of interferon-beta production.
Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 alpha production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 alpha production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 alpha production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 alpha production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 alpha production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 alpha production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-1 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-10 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-10 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-10 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-10 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-10 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-10 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-11 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-11 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-11 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-11 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-11 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-11 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-12 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-12 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-12 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-12 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-12 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-12 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-13 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-13 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-13 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-13 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-13 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-13 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-14 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-14 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-14 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-14 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-14 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-14 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-15 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-15 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-15 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-15 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-15 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-15 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-16 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-16 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-16 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-16 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-16 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-16 production.
Any process that activates or increases the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that activates or increases the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that activates or increases the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that activates or increases the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that activates or increases the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that activates or increases the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
Any process that activates or increases the frequency, rate, or extent of interleukin-18 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-18 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-18 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-18 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-18 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-18 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-19 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-19 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-19 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-19 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-19 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-19 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-2 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-2 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-2 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-2 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-2 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-2 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-20 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-20 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-20 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-20 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-20 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-20 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-21 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-21 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-21 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-21 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-21 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-21 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-22 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-22 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-22 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-22 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-22 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-22 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-23 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-23 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-23 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-23 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-23 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-23 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-24 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-24 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-24 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-24 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-24 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-24 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-25 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-25 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-25 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-25 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-25 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-25 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-26 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-26 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-26 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-26 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-26 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-26 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-27 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-27 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-27 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-27 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-27 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-27 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-3 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-3 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-3 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-3 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-3 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-3 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-4 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-4 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-4 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-4 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-4 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-4 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-5 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-5 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-5 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-5 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-5 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-5 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-6 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-6 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-6 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-6 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-6 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-6 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-7 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-7 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-7 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-7 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-7 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-7 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-8 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-9 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-9 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-9 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-9 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-9 production.
Any process that activates or increases the frequency, rate, or extent of interleukin-9 production.
Any process that activates or increases the frequency, rate, or extent of TRAIL production.
Any process that activates or increases the frequency, rate, or extent of TRAIL production.
Any process that activates or increases the frequency, rate, or extent of TRAIL production.
Any process that activates or increases the frequency, rate, or extent of TRAIL production.
Any process that activates or increases the frequency, rate, or extent of TRAIL production.
Any process that activates or increases the frequency, rate, or extent of tumor necrosis factor production.
Any process that activates or increases the frequency, rate, or extent of tumor necrosis factor production.
Any process that activates or increases the frequency, rate, or extent of tumor necrosis factor production.
Any process that activates or increases the frequency, rate, or extent of tumor necrosis factor production.
Any process that activates or increases the frequency, rate, or extent of tumor necrosis factor production.
Any process that activates or increases the frequency, rate, or extent of tumor necrosis factor production.
Any process that activates or increases the frequency, rate, or extent of tumor necrosis factor production.
Any process that activates or increases the frequency, rate, or extent of tumor necrosis factor production.
Any process that activates or increases the frequency, rate, or extent of lymphotoxin A production.
Any process that activates or increases the frequency, rate, or extent of lymphotoxin A production.
Any process that activates or increases the frequency, rate, or extent of lymphotoxin A production.
Any process that activates or increases the frequency, rate, or extent of lymphotoxin A production.
Any process that activates or increases the frequency, rate, or extent of lymphotoxin A production.
Any process that activates or increases the frequency, rate, or extent of lymphotoxin A production.
Any process that activates or increases the frequency, rate, or extent of lymphotoxin A production.
Any process that activates or increases the frequency, rate, or extent of lymphotoxin A production.
Any process that activates or increases the frequency, rate, or extent of lymphotoxin A production.
Any process that contributes to cytokine production by a mast cell.
Any process that modulates the frequency, rate, or extent of mast cell cytokine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mast cell cytokine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mast cell cytokine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mast cell cytokine production.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mast cell cytokine production.
Any process that activates or increases the frequency, rate, or extent of mast cell cytokine production.
Any process that activates or increases the frequency, rate, or extent of mast cell cytokine production.
Any process that activates or increases the frequency, rate, or extent of mast cell cytokine production.
Any process that activates or increases the frequency, rate, or extent of mast cell cytokine production.
Any process that activates or increases the frequency, rate, or extent of mast cell cytokine production.
A heterotrimeric protein complex formed by the association of NHE3, E3KARP and alpha-actinin upon an increase in calcium ion concentration; found in clusters localized on plasma membrane and in intracellular compartments.
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules), in the presence of copper.
Any process that modulates the activity of a monooxygenase.
Any process that stops or reduces the activity of a monooxygenase.
Any process that stops or reduces the activity of a monooxygenase.
Any process that stops or reduces the activity of a monooxygenase.
Any process that stops or reduces the activity of a monooxygenase.
Any process that activates or increases the activity of a monooxygenase.
Any process that activates or increases the activity of a monooxygenase.
Any process that activates or increases the activity of a monooxygenase.
Any process that activates or increases the activity of a monooxygenase.
Any process that activates or increases the activity of a monooxygenase.
Any process that modulates the activity of the enzyme monophenol monooxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
Any process that stops or reduces the activity of the enzyme monophenol monooxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
Any process that stops or reduces the activity of the enzyme monophenol monooxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
Any process that stops or reduces the activity of the enzyme monophenol monooxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
Any process that stops or reduces the activity of the enzyme monophenol monooxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
Any process that stops or reduces the activity of the enzyme monophenol monooxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
Any process that activates or increases the activity of the enzyme monophenol oxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
Any process that activates or increases the activity of the enzyme monophenol oxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
Any process that activates or increases the activity of the enzyme monophenol oxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
Any process that activates or increases the activity of the enzyme monophenol oxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
Any process that activates or increases the activity of the enzyme monophenol oxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
Any process that activates or increases the activity of the enzyme monophenol oxygenase. Monophenol monooxygenase catalyzes the reaction: L-tyrosine + L-DOPA + O2 = L-DOPA + DOPAquinone + H2O.
The chemical reactions and pathways resulting in the formation of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. Includes polymerization of ribonucleotide monomers. Refers not only to transcription but also to e.g. viral RNA replication.
The chemical reactions and pathways resulting in the formation of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. Includes polymerization of ribonucleotide monomers. Refers not only to transcription but also to e.g. viral RNA replication.
The chemical reactions and pathways resulting in the formation of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. Includes polymerization of ribonucleotide monomers. Refers not only to transcription but also to e.g. viral RNA replication.
The chemical reactions and pathways resulting in the formation of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. Includes polymerization of ribonucleotide monomers. Refers not only to transcription but also to e.g. viral RNA replication.
The covalent transfer of a methyl group to N-6 of adenine in a DNA molecule.
The covalent transfer of a methyl group to C-5 or N-4 of cytosine in a DNA molecule.
A heterotrimeric H4/H2A histone acetyltransferase complex with a substrate preference of chromatin over free histones. It contains a subset of the proteins found in the larger NuA4 histone acetyltransferase complex; for example, the S. cerevisiae complex contains Esa1p, Yng2p, and Epl1p.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + cobalt(out) = ADP + phosphate + cobalt(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + cobalt(out) = ADP + phosphate + cobalt(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + cobalt(out) = ADP + phosphate + cobalt(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + cobalt(out) = ADP + phosphate + cobalt(in).
Any process that stops or reduces the rate of ATP hydrolysis by an ATPase.
Any process that stops or reduces the rate of ATP hydrolysis by an ATPase.
Any process that stops or reduces the rate of ATP hydrolysis by an ATPase.
Any process that stops or reduces the rate of ATP hydrolysis by an ATPase.
Any process that stops or reduces the rate of ATP hydrolysis by an ATPase.
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
Any process that activates or increases the rate of ATP hydrolysis by an ATPase.
The regulated release of bile acid, composed of any of a group of steroid carboxylic acids occurring in bile, by a cell or a tissue.
A heterodimeric protein complex that acts as an RNA polymerase II elongation factor; the complex is conserved from yeast to humans, and is present in S. pombe, but absent from S. cerevisiae.
Any process that modulates the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that modulates the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that modulates the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that modulates the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
Any process that modulates the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides catalyzed by a DNA-dependent RNA polymerase.
The chemical reactions and pathways involving monocarboxylic acids, any organic acid containing one carboxyl (COOH) group or anion (COO-).
The chemical reactions and pathways involving monocarboxylic acids, any organic acid containing one carboxyl (COOH) group or anion (COO-).
The chemical reactions and pathways involving saturated monocarboxylic acids, any organic acid containing one carboxyl (COOH) group or anion (COO-) and fully saturated C-C bonds.
The chemical reactions and pathways involving saturated monocarboxylic acids, any organic acid containing one carboxyl (COOH) group or anion (COO-) and fully saturated C-C bonds.
The chemical reactions and pathways involving unsaturated monocarboxylic acids, any organic acid containing one carboxyl (COOH) group or anion (COO-) and one or more unsaturated C-C bonds.
The chemical reactions and pathways involving unsaturated monocarboxylic acids, any organic acid containing one carboxyl (COOH) group or anion (COO-) and one or more unsaturated C-C bonds.
The disaggregation of a ribosome into its constituent components; includes the dissociation of ribosomal subunits.
The disaggregation of a ribosome into its constituent components; includes the dissociation of ribosomal subunits.
Interacting selectively and non-covalently with lead (Pb) ions.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the transcription factor CREB.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the transcription factor CREB.
Any process that activates or increases the frequency, rate or extent of activity of the transcription factor CREB.
Any process that activates or increases the frequency, rate or extent of activity of the transcription factor CREB.
Any process that activates or increases the frequency, rate or extent of activity of the transcription factor CREB.
Interacting selectively and non-covalently with a GTPase activating protein.
Interacting selectively and non-covalently with a heterotrimeric G-protein.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a uropod, a rigid membrane projection with related cytoskeletal components at the trailing edge of a lymphocyte or other cell in the process of migrating or being activated.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a uropod, a rigid membrane projection with related cytoskeletal components at the trailing edge of a lymphocyte or other cell in the process of migrating or being activated.
A protein complex that contains the survival motor neuron (SMN) protein and at least eight additional integral components, including the Gemin2-8 and Unrip proteins; the complex is found in the cytoplasm and in nuclear Gems, and is involved in spliceosomal snRNP assembly in the cytoplasm and in pre-mRNA splicing in the nucleus.
A protein complex that contains the survival motor neuron (SMN) protein and at least eight additional integral components, including the Gemin2-8 and Unrip proteins; the complex is found in the cytoplasm and in nuclear Gems, and is involved in spliceosomal snRNP assembly in the cytoplasm and in pre-mRNA splicing in the nucleus.
A conserved DNA recombinase mediator complex that contains two Swi5 monomers and one Sfr1 monomer in Schizosaccharomyces, or orthologs thereof (e.g. Sae3p and Mei5p in Saccharomyces).
A conserved DNA recombinase mediator complex that contains two Swi5 monomers and one Sfr1 monomer in Schizosaccharomyces, or orthologs thereof (e.g. Sae3p and Mei5p in Saccharomyces).
The chemical reactions and pathways involving low-density lipoprotein receptors.
The chemical reactions and pathways involving low-density lipoprotein receptors.
The chemical reactions and pathways involving low-density lipoprotein receptors.
The chemical reactions and pathways resulting in the formation of a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the formation of a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the formation of a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the formation of a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the breakdown of a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the breakdown of a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the breakdown of a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the breakdown of a low-density lipoprotein particle receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the breakdown of a low-density lipoprotein particle receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the breakdown of a low-density lipoprotein particle receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the breakdown of a low-density lipoprotein particle receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the breakdown of a low-density lipoprotein particle receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the breakdown of a low-density lipoprotein particle receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the breakdown of a low-density lipoprotein particle receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
The chemical reactions and pathways resulting in the breakdown of a low-density lipoprotein particle receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein particle receptors.
A protein complex that phosphorylates amino acid residues of RNA polymerase II C-terminal domain repeats; phosphorylation occurs mainly on Ser2 and Ser5.
A eukaryotically conserved protein complex that contains DNA ligase IV and is involved in DNA repair by non-homologous end joining; in addition to the ligase, the complex also contains XRCC4 or a homolog, e.g. Saccharomyces Lif1p.
The process whose specific outcome is the progression of the lacrimal gland over time, from its formation to the mature structure. The lacrimal gland produces secretions that lubricate and protect the cornea of the eye.
The plasma membrane of a neuron cell body - excludes the plasma membrane of cell projections such as axons and dendrites.
The plasma membrane of a neuron cell body - excludes the plasma membrane of cell projections such as axons and dendrites.
Interacting selectively and non-covalently with the sterol response element (SRE), a nonpalindromic sequence found in the promoters of genes involved in lipid metabolism.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of epinephrine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of epinephrine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of epinephrine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of epinephrine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of epinephrine.
Any process that activates or increases the frequency, rate or extent of the regulated release of epinephrine.
Any process that activates or increases the frequency, rate or extent of the regulated release of epinephrine.
Any process that activates or increases the frequency, rate or extent of the regulated release of epinephrine.
Any process that activates or increases the frequency, rate or extent of the regulated release of epinephrine.
Any process that activates or increases the frequency, rate or extent of the regulated release of epinephrine.
Any process that activates or increases the frequency, rate or extent of the regulated release of epinephrine.
Interacting selectively and non-covalently with any member of the tumor necrosis factor receptor superfamily.
Any process that modulates the frequency, rate or extent of natural killer cell activation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell activation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell activation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell activation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell activation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell activation.
Any process that activates or increases the frequency, rate or extent of natural killer cell activation.
Any process that activates or increases the frequency, rate or extent of natural killer cell activation.
Any process that activates or increases the frequency, rate or extent of natural killer cell activation.
Any process that activates or increases the frequency, rate or extent of natural killer cell activation.
Any process that activates or increases the frequency, rate or extent of natural killer cell activation.
Any process that activates or increases the frequency, rate or extent of natural killer cell activation.
Any process that modulates the frequency, rate or extent of natural killer cell proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell proliferation.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation.
Any process that modulates the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that modulates the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation as part of an immune response.
Any process that modulates the frequency, rate or extent of natural killer cell differentiation.
Any process that modulates the frequency, rate or extent of natural killer cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation.
Any process that modulates the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that modulates the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that modulates the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that activates or increases the frequency, rate or extent of natural killer cell differentiation as part of an immune response.
Any process that modulates the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that modulates the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that modulates the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that modulates the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells.
Any process that modulates the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that modulates the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that modulates the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that modulates the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that modulates the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
Any process that activates or increases the frequency, rate or extent of differentiation of CD4-positive, CD25-positive, alpha-beta regulatory T cells as part of an immune response.
The progression of the glomerulus over time from its initial formation until its mature state. The glomerulus is a capillary tuft which forms a close network with the visceral epithelium (podocytes) and the mesangium to form the filtration barrier and is surrounded by Bowman's capsule in nephrons of the vertebrate kidney. The glomerulus is part of the nephron and is restricted to one body segment.
The process whose specific outcome is the progression of the glomerular basement membrane over time, from its formation to the mature structure. The glomerular basement membrane is the basal laminal portion of the glomerulus which performs the actual filtration.
The cell cycle process in which genetic material, in the form of chromosomes, is organized and then physically separated and apportioned to two or more sets during a normally chiasmate meiosis under the condition that chiasma have not occurred between a particular pair of homologs. Distributive segregation is a "backup" mechanism to ensure the segregation of homologs that have failed to cross over - either as a consequence of mutation or not, as, for example, the 4th chromosome of Drosophila melanogaster (which never exchanges, presumably due to its small size) - but nevertheless segregate normally.
All of the contents of a plasma membrane bounded cell projection, excluding the plasma membrane surrounding the projection.
All of the contents of a dendrite, excluding the surrounding plasma membrane.
Interacting selectively and non-covalently with a proline-rich region within the same polypeptide.
Interacting selectively and non-covalently with calcitonin, a peptide hormone responsible for reducing serum calcium levels by inhibiting osteoclastic bone reabsorption and promoting renal calcium excretion. It is synthesized and released by the C cells of the thyroid.
Catalysis of the reaction: 2 RSH + ROOH = RSSR + ROH + H2O. This reaction is the thiol-dependent conversion of an organic hydroperoxide to the corresponding alcohol.
Any process that modulates the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that modulates the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that modulates the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that modulates the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that modulates the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that modulates the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that activates or increases the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that activates or increases the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that activates or increases the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that activates or increases the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that activates or increases the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that activates or increases the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that activates or increases the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that activates or increases the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that activates or increases the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that activates or increases the frequency, rate, or extent of a process that reduces the internal pH of a cell.
Any process that activates or increases the frequency, rate, or extent of a process that reduces the internal pH of a cell.
A protein complex that links the endoplasmic reticulum with mitochondria and may have a role in promoting exchange of calcium and phospholipids between the two organelles. The complex is also associated with actively replicating mitochondrial DNA nucleoids, and may further coordinate mitochondrial genome replication and membrane growth.
A protein complex that links the endoplasmic reticulum with mitochondria and may have a role in promoting exchange of calcium and phospholipids between the two organelles. The complex is also associated with actively replicating mitochondrial DNA nucleoids, and may further coordinate mitochondrial genome replication and membrane growth.
A protein complex that links the endoplasmic reticulum with mitochondria and may have a role in promoting exchange of calcium and phospholipids between the two organelles. The complex is also associated with actively replicating mitochondrial DNA nucleoids, and may further coordinate mitochondrial genome replication and membrane growth.
A protein complex that links the endoplasmic reticulum with mitochondria and may have a role in promoting exchange of calcium and phospholipids between the two organelles. The complex is also associated with actively replicating mitochondrial DNA nucleoids, and may further coordinate mitochondrial genome replication and membrane growth.
Catalysis of the reaction: D-xylitol + NADP+ = D-xylose + NADPH + H+.
Catalysis of the reaction: D-xylitol + NADP+ = D-xylose + NADPH + H+.
Catalysis of the reaction: L-arabitol + NADP+ = L-arabinose + NADPH + H+.
Catalysis of the reaction: L-arabitol + NADP+ = L-arabinose + NADPH + H+.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hormone stimulus.
Any process that modulates the frequency, rate or extent of karyogamy, the creation of a single nucleus from multiple nuclei as a result of membrane fusion.
Any process that modulates the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that modulates the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that modulates the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that modulates the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that modulates the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that modulates the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that modulates the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
Any process that modulates the frequency, rate or extent of DNA endoreduplication.
Any process that modulates the frequency, rate or extent of DNA endoreduplication.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA endoreduplication.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA endoreduplication.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA endoreduplication.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA endoreduplication.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA endoreduplication.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA endoreduplication.
Any process that activates or increases the frequency, rate or extent of DNA endoreduplication.
Any process that activates or increases the frequency, rate or extent of DNA endoreduplication.
Any process that activates or increases the frequency, rate or extent of DNA endoreduplication.
Any process that activates or increases the frequency, rate or extent of DNA endoreduplication.
Any process that activates or increases the frequency, rate or extent of DNA endoreduplication.
Any process that activates or increases the frequency, rate or extent of DNA endoreduplication.
Any process that activates or increases the frequency, rate or extent of DNA endoreduplication.
Any process that modulates the frequency, rate or extent of the specification, formation or maintenance of anisotropic intracellular organization or cell growth patterns.
Any process that modulates the frequency, rate or extent of any process in which a cell, a substance, or a cellular entity is transported to, or maintained in, a specific location.
Any process that modulates the frequency, rate or extent of any process in which a protein is transported to, or maintained in, a specific location.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving polysaccharides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cell wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cell wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cell wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cell wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of polysaccharides.
Any process that modulates the frequency, rate or extent of any cellular process that depends upon or alters the microtubule cytoskeleton.
Any process that modulates the frequency, rate or extent of the cell cycle process in which the distance is lengthened between poles of the spindle.
Any process that modulates the frequency, rate or extent of the cell cycle process in which the distance is lengthened between poles of the mitotic spindle.
Any process that modulates the frequency, rate or extent of the fusion of two vacuole membranes to form a single vacuole.
Any process that modulates the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Catalysis of the reaction: palmitoyl-CoA + AH2 + O2 = palmitoleic acid (16:1delta9) + A + 2 H2O.
Any process that stops, prevents, or reduces the frequency, rate or extent of viral transcription.
Any process that stops, prevents, or reduces the frequency, rate or extent of viral transcription.
Any process that stops, prevents, or reduces the frequency, rate or extent of viral transcription.
Any process that stops, prevents, or reduces the frequency, rate or extent of viral transcription.
The appearance of a neurotrophin due to biosynthesis or secretion by cells in a neuron's target field, resulting in an increase in its intracellular or extracellular levels. A neurotrophin is any of a family of growth factors that prevent apoptosis in neurons and promote nerve growth.
Any process that modulates the frequency, rate, or extent of production of a neurotrophin.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of a neurotrophin.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of a neurotrophin.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of a neurotrophin.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of a neurotrophin.
Any process that activates or increases the frequency, rate, or extent of production of a neurotrophin.
Any process that activates or increases the frequency, rate, or extent of production of a neurotrophin.
Any process that activates or increases the frequency, rate, or extent of production of a neurotrophin.
Any process that activates or increases the frequency, rate, or extent of production of a neurotrophin.
Any process that activates or increases the frequency, rate, or extent of production of a neurotrophin.
The appearance of nerve growth factor (NGF) due to biosynthesis or secretion by cells in a neuron's target field, resulting in an increase in its intracellular or extracellular levels.
The appearance of nerve growth factor (NGF) due to biosynthesis or secretion by cells in a neuron's target field, resulting in an increase in its intracellular or extracellular levels.
Any process that modulates the frequency, rate, or extent of production of nerve growth factor (NGF).
Any process that modulates the frequency, rate, or extent of production of nerve growth factor (NGF).
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of nerve growth factor (NGF).
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of nerve growth factor (NGF).
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of nerve growth factor (NGF).
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of nerve growth factor (NGF).
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of nerve growth factor (NGF).
The appearance of transforming growth factor-beta1 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of transforming growth factor-beta1 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of transforming growth factor-beta1 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of transforming growth factor-beta2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of transforming growth factor-beta2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of transforming growth factor-beta2 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of transforming growth factor-beta3 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of transforming growth factor-beta3 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of transforming growth factor-beta3 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
Any process that modulates the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that modulates the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that modulates the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that modulates the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that modulates the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that modulates the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that modulates the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that modulates the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that modulates the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta1.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta2.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta3.
Any process that activates or increases the frequency, rate, or extent of production of transforming growth factor-beta3.
The modification of polyamines by addition of acetyl groups.
The modification of spermidine by addition of acetyl groups.
The modification of spermine by addition of acetyl groups.
The modification of putrescine by addition of acetyl groups.
A complex consisting of 4 protein subunits as a heterotetramer, that possesses sarcosine oxidase activity.
Any process that modulates the frequency, rate or extent of gene expression such that an expression pattern recurs with a regularity of approximately 24 hours.
Any process that modulates the frequency, rate or extent of gene expression such that an expression pattern recurs with a regularity of approximately 24 hours.
Any process that modulates the frequency, rate or extent of gene expression such that an expression pattern recurs with a regularity of approximately 24 hours.
The chemical reactions and pathways resulting in the formation of phosphonates, any organic compound containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Synthesis of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included.
A series of molecular signals initiated by the binding of an extracellular ligand to an activin receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any process that modulates the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that modulates the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that modulates the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of any activin receptor signaling pathway.
Any process that modulates the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Any process that activates or increases the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Any process that activates or increases the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Any process that activates or increases the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Any process that activates or increases the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Any process that activates or increases the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Any process that activates or increases the frequency, rate or extent of enzymatic generation of superoxide by a cell.
Catalysis of the reaction: acetyl-CoA + histone H3 L-lysine (position 56) = CoA + histone H3 N6-acetyl-L-lysine (position 56).
Any process that stops, prevents, or reduces the frequency, rate or extent of the depolymerization of astral microtubules.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
A series of molecular signals from the endoplasmic reticulum to the nucleus generated as a consequence of decreased levels of one or more sterols (and in some yeast, changes in oxygen levels) and which proceeds through activation of a sterol response element binding transcription factor (SREBP) to result in up-regulation of target gene transcription.
Interacting selectively and non-covalently with a sterol, any steroid containing a hydroxy group in the 3 position, closely related to cholestan-3-ol.
Interacting selectively and non-covalently with a sterol, any steroid containing a hydroxy group in the 3 position, closely related to cholestan-3-ol.
Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of a sterol.
A protein complex formed by the association of sterol regulatory element binding protein (SREBP) and SREBP-cleavage-activating protein (SCAP) in the ER membrane; in the absence of sterols, the SREBP-SCAP complex is packaged into COPII vesicles and travels to the Golgi apparatus to be processed.
A protein complex formed by the association of sterol regulatory element binding protein (SREBP), SREBP-cleavage-activating protein (SCAP), and an Insig protein (Insig-1 or Insig-2) in the ER membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of translation as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
Any process that activates or increases the frequency, rate or extent of translation as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
Any process that activates or increases the frequency, rate or extent of translation as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
Any process that activates or increases the frequency, rate or extent of translation as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
Any process that activates or increases the frequency, rate or extent of translation as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
Any process that activates or increases the frequency, rate or extent of translation as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
The controlled release of a substance by a cell.
The controlled release of a substance by a tissue.
The controlled release of a substance by a tissue.
Catalysis of the reaction: 1D-myo-inositol tetrakisphosphate + ATP = 1D-myo-inositol pentakisphosphate (containing 2-phosphate) + ADP.
Catalysis of the reaction: 1D-myo-inositol tetrakisphosphate + ATP = 1D-myo-inositol pentakisphosphate (containing 2-phosphate) + ADP.
Catalysis of the reaction: 1D-myo-inositol tetrakisphosphate + ATP = 1D-myo-inositol pentakisphosphate (containing 2-phosphate) + ADP.
The expansion of a mononuclear cell population by cell division. A mononuclear cell is a leukocyte with a single non-segmented nucleus in the mature form.
The expansion of a mononuclear cell population by cell division. A mononuclear cell is a leukocyte with a single non-segmented nucleus in the mature form.
Any process that modulates the frequency, rate or extent of mononuclear cell proliferation.
Any process that modulates the frequency, rate or extent of mononuclear cell proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of mononuclear cell proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of mononuclear cell proliferation.
Any process that activates or increases the frequency, rate or extent of mononuclear cell proliferation.
Any process that activates or increases the frequency, rate or extent of mononuclear cell proliferation.
Any process that activates or increases the frequency, rate or extent of mononuclear cell proliferation.
Any process that activates or increases the frequency, rate or extent of mononuclear cell proliferation.
Any process that activates or increases the frequency, rate or extent of mononuclear cell proliferation.
Any process that activates or increases the frequency, rate or extent of mononuclear cell proliferation.
Any process that activates or increases the frequency, rate or extent of mononuclear cell proliferation.
A structural molecule activity that provides a physical support for the assembly of a multiprotein complex. The scaffold may or may not be part of the final complex.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving alpha-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways relusting in the formation of alpha-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways relusting in the formation of alpha-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways relusting in the formation of alpha-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways relusting in the formation of alpha-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving beta-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways relusting in the formation of beta-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways relusting in the formation of beta-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways relusting in the formation of beta-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways relusting in the formation of beta-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving (1->3)-beta-D-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving (1->3)-beta-D-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving (1->3)-beta-D-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving (1->3)-beta-D-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans.
Any process that modulates the frequency, rate or extent of a cytokinetic process.
Any process that modulates the frequency, rate or extent of division septum formation. division septum formation is the assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis.
Any process that modulates the frequency, rate or extent of division septum formation. division septum formation is the assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis.
Any process that modulates the frequency, rate or extent of division septum formation. division septum formation is the assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis.
Any process that modulates the frequency, rate or extent of division septum formation. division septum formation is the assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis.
Any process that modulates the frequency, rate or extent of division septum formation. division septum formation is the assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis.
Any process that modulates the frequency, rate or extent of division septum formation. division septum formation is the assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis.
Any process that modulates the frequency, rate or extent of division septum formation. division septum formation is the assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis.
Any process that modulates the frequency, rate or extent of division septum formation. division septum formation is the assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis.
Any process that modulates the frequency, rate or extent of division septum formation. division septum formation is the assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis.
Any process that modulates the frequency, rate or extent of division septum formation. division septum formation is the assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis.
Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
The chemical reactions and pathways involving myo-inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
The chemical reactions and pathways involving myo-inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
The chemical reactions and pathways involving myo-inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
The chemical reactions and pathways involving myo-inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
The chemical reactions and pathways resulting in the formation of an inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with one or more phosphate groups attached.
The chemical reactions and pathways resulting in the formation of an inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with one or more phosphate groups attached.
The chemical reactions and pathways resulting in the formation of an inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with one or more phosphate groups attached.
The chemical reactions and pathways resulting in the formation of an inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with one or more phosphate groups attached.
The chemical reactions and pathways resulting in the formation of an inositol phosphate, 1,2,3,4,5,6-cyclohexanehexol, with one or more phosphate groups attached.
The chemical reactions and pathways resulting in the formation of inositol trisphosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
The chemical reactions and pathways resulting in the formation of inositol trisphosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
The chemical reactions and pathways resulting in the formation of inositol trisphosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
The chemical reactions and pathways resulting in the formation of inositol trisphosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
The chemical reactions and pathways resulting in the formation of inositol trisphosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
The chemical reactions and pathways resulting in the formation of inositol trisphosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
The chemical reactions and pathways resulting in the formation of inositol trisphosphate, 1,2,3,4,5,6-cyclohexanehexol, with three phosphate groups attached.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of inositol trisphosphate.
The chemical reactions and pathways involving collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%).
The chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%).
The chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%).
The chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%).
The chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%).
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II.
Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II.
A protein complex that contains MAPKSP1 (MP1, Map2k1ip1) and ROBLD3 (p14, Mapbpip), is anchored to late endosomes, and is involved in selective activation of the ERK1 in ERK/MAPK signaling.
A protein complex that contains MAPKSP1 (MP1, Map2k1ip1) and ROBLD3 (p14, Mapbpip), is anchored to late endosomes, and is involved in selective activation of the ERK1 in ERK/MAPK signaling.
Any process that modulates the frequency, rate or extent of any cellular process that depends upon or alters the actin cytoskeleton.
Any process that modulates the frequency, rate or extent of muscle filament sliding.
Any process that modulates the velocity of muscle filament sliding.
The directed movement of amino acids from inside of a cell, across the plasma membrane and into the extracellular region.
The directed movement of amino acids from inside of a cell, across the plasma membrane and into the extracellular region.
The directed movement of amino acids from inside of a cell, across the plasma membrane and into the extracellular region.
The directed movement of amino acids from inside of a cell, across the plasma membrane and into the extracellular region.
The directed movement of amino acids out of the vacuole, across the vacuolar membrane.
The directed movement of amino acids out of the vacuole, across the vacuolar membrane.
The directed movement of amino acids into the vacuole across the vacuolar membrane.
The process in which enzymes, such as aspartate aminotransferase, are enabled to move from the mitochondrial matrix into the cytosol, as part of the apoptotic process.
The process in which enzymes, such as aspartate aminotransferase, are enabled to move from the mitochondrial matrix into the cytosol, as part of the apoptotic process.
Mediates the integration of proteins into a membrane from the inner side of the membrane. Membrane insertases are highly conserved and include the bacterial YidC family, the plant chloroplast Alb3 family, and the fungal and animal mitochondrial Oxa1/Cox18 family.
The process in which a protein is incorporated into a lipid bilayer, e.g., the prokaryotic, mitochondrial, or chloroplast inner membrane, from the inner side.
The process in which a protein is incorporated into the mitochondrial inner membrane from the matrix side. This includes membrane insertion of newly synthesized mitochondrially-encoded proteins, and insertion of nuclear-encoded proteins after their import into the mitochondrial matrix.
The process in which a protein is incorporated into the mitochondrial inner membrane from the matrix side. This includes membrane insertion of newly synthesized mitochondrially-encoded proteins, and insertion of nuclear-encoded proteins after their import into the mitochondrial matrix.
A change in the morphology or behavior of a keratinocyte resulting from exposure to an activating factor such as a cellular or soluble ligand. Upon activation, keratinocytes become migratory and hyperproliferative, and produce growth factors and cytokines.
The aggregation, arrangement and bonding together of a set of components to form mitochondrial respiratory chain complex I.
The aggregation, arrangement and bonding together of a set of components to form mitochondrial respiratory chain complex I.
A protein complex containing myosin heavy chains, plus associated light chains and other proteins, in which the myosin heavy chains are arranged into a filament.
A protein complex containing myosin heavy chains, plus associated light chains and other proteins, in which the myosin heavy chains are arranged into a filament.
An assembly of four or five subunits which form a structure with an extracellular N-terminus and a large loop that together form the ligand binding domain. The C-terminus is intracellular. The ionotropic glutamate receptor complex itself acts as a ligand gated ion channel; on binding glutamate, charged ions pass through a channel in the center of the receptor complex. Kainate receptors are multimeric assemblies of GluK1-3 (also called GluR5-7), GluK4 (KA1) and GluK5 (KA2) subunits.
The disaggregation of a protein-containing macromolecular complex into its constituent components.
The disaggregation of a protein-containing macromolecular complex into its constituent components.
The disaggregation of a protein-containing macromolecular complex into its constituent components.
The disaggregation of a protein-containing macromolecular complex into its constituent components.
The disaggregation of a protein-containing macromolecular complex into its constituent components.
The disaggregation of a protein-carbohydrate complex into its constituent components.
The disaggregation of a protein-DNA complex into its constituent components.
The disaggregation of a protein-lipid complex into its constituent components.
The disaggregation of a protein-RNA complex into its constituent components.
The disaggregation of a protein-RNA complex into its constituent components.
The disaggregation of a protein-RNA complex into its constituent components.
The process in which cellular structures, including whole cells or cell parts, are generated and organized.
The process in which the anatomical structures of a cell part are generated and organized.
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
A macromolecular complex containing separate protein and carbohydrate molecules.  Separate in this context means not covalently bound to each other.
A macromolecular complex containing both protein and DNA molecules.
A macromolecular complex containing separate protein and lipid molecules.  Separate in this context means not covalently bound to each other.
Any process that modulates the process in which a cell wall is synthesized, aggregates, and bonds together. The fungal-type cell wall contains beta-glucan and may contain chitin.
A protein complex containing Bcl3 and Bcl10, which forms when Akt1 is activated by TNF-alpha to phosphorylate Bcl10; the Bcl3-Bcl10 complex is translocated to the nucleus.
A protein complex composed of a subunit or subunits capable of binding the Fc portion of an immunoglobulin with additional signaling components. The complex functions as a receptor for immunoglobulin.
A protein complex composed of a subunit or subunits capable of binding the Fc portion of an immunoglobulin with additional signaling components. The complex functions as a receptor for immunoglobulin.
A protein complex composed of a subunit or subunits capable of binding the Fc portion of an immunoglobulin with additional signaling components. The complex functions as a receptor for immunoglobulin.
A protein complex composed of an Fc-epsilon RI alpha chain and an Fc-epsilon RI gamma chain dimer with or without an Fc-episilon RI beta chain and additional signaling components. The complex functions primarily as an activating receptor for IgE.
A protein complex composed of an Fc-epsilon RI alpha chain and an Fc-epsilon RI gamma chain dimer with or without an Fc-episilon RI beta chain and additional signaling components. The complex functions primarily as an activating receptor for IgE.
A protein complex composed of an Fc-epsilon RI alpha chain and an Fc-epsilon RI gamma chain dimer with or without an Fc-episilon RI beta chain and additional signaling components. The complex functions primarily as an activating receptor for IgE.
A protein complex composed of an Fc-alpha R alpha chain and an Fc-epsilon RI gamma chain dimer with or without additional signaling components. The complex functions primarily as an activating receptor for IgA.
A protein complex composed of an Fc-alpha R alpha chain and an Fc-epsilon RI gamma chain dimer with or without additional signaling components. The complex functions primarily as an activating receptor for IgA.
A protein complex composed of an Fc-alpha R alpha chain and an Fc-epsilon RI gamma chain dimer with or without additional signaling components. The complex functions primarily as an activating receptor for IgA.
A protein complex composed of an Fc-gamma RI alpha chain and an Fc-epsilon RI gamma chain dimer with or without additional signaling components. The complex functions primarily as an activating receptor for IgG.
A protein complex composed of an Fc-gamma RI alpha chain and an Fc-epsilon RI gamma chain dimer with or without additional signaling components. The complex functions primarily as an activating receptor for IgG.
A protein complex composed of an Fc-gamma RI alpha chain and an Fc-epsilon RI gamma chain dimer with or without additional signaling components. The complex functions primarily as an activating receptor for IgG.
A protein complex composed of an Fc-gamma RIII alpha chain and an Fc-epsilon RI gamma chain dimer with or without an Fc-epsilon RI beta chain and additional signaling components. The complex functions primarily as an activating receptor for IgG.
A protein complex composed of an Fc-gamma RIII alpha chain and an Fc-epsilon RI gamma chain dimer with or without an Fc-epsilon RI beta chain and additional signaling components. The complex functions primarily as an activating receptor for IgG.
A protein complex composed of an Fc-gamma RIII alpha chain and an Fc-epsilon RI gamma chain dimer with or without an Fc-epsilon RI beta chain and additional signaling components. The complex functions primarily as an activating receptor for IgG.
The expansion of a muscle cell population by cell division.
Any process that modulates the frequency, rate, or extent of mast cell activation.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mast cell activation.
Any process that activates or increases the frequency, rate, or extent of mast cell activation.
Any process that modulates the frequency, rate, or extent of mast cell activation as part of an immune response.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mast cell activation as part of an immune response.
Any process that activates or increases the frequency, rate, or extent of mast cell activation as part of an immune response.
A small, vestigial nucleus found in some plastids that derive from a eukaryotic endosymbiont. Observed in chlorarachniophytes and cryptomonads, which acquired their plastids from a green and red alga respectively.
A highly specialized cell-cell junction found in vertebrates, which forms between a neuron and a glial cell, and has structural similarity to Drosophila septate junctions. It flanks the node of Ranvier in myelinated nerve and electrically isolates the myelinated from unmyelinated nerve segments and physically separates the voltage-gated sodium channels at the node from the cluster of potassium channels underneath the myelin sheath.
A highly specialized cell-cell junction found in vertebrates, which forms between a neuron and a glial cell, and has structural similarity to Drosophila septate junctions. It flanks the node of Ranvier in myelinated nerve and electrically isolates the myelinated from unmyelinated nerve segments and physically separates the voltage-gated sodium channels at the node from the cluster of potassium channels underneath the myelin sheath.
A highly specialized cell-cell junction found in vertebrates, which forms between a neuron and a glial cell, and has structural similarity to Drosophila septate junctions. It flanks the node of Ranvier in myelinated nerve and electrically isolates the myelinated from unmyelinated nerve segments and physically separates the voltage-gated sodium channels at the node from the cluster of potassium channels underneath the myelin sheath.
A condensed cytoplasmic structure that covers the nucleus of mammalian spermatozoa except for a narrow zone around the insertion of the tail. It shows two distinct regions, a subacrosomal layer and, continuing caudally beyond the acrosomic system, the postacrosomal sheath. The perinuclear theca has been considered a cytoskeletal scaffold responsible for maintaining the overall architecture of the mature sperm head; however, recent studies indicate that the bulk of its constituent proteins are not traditional cytoskeletal proteins but rather a variety of cytosolic proteins.
A permanent cup-shaped structure at the cell plasma membrane in secretory cells. Following a secretory stimulus, secretory vesicles transiently dock and fuse at the base of porosomes and release intravesicular contents dictated by the turgor pressure generated from the swelling of secretory vesicles.
The chemical reactions and pathways involving tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next.
The chemical reactions and pathways leading to the breakdown of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next.
The chemical reactions and pathways leading to the breakdown of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next.
The chemical reactions and pathways leading to the breakdown of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next.
The lipid bilayer surrounding a rhoptry.
The lipid bilayer surrounding the sarcoplasmic reticulum.
The volume enclosed by the membranes of the sarcoplasmic reticulum.
Catalysis of the reaction: 5-hydroxyvalerate + NAD+ = 5-oxovalerate + NADH.
The chemical reactions and pathways involving cyclopentanol.
The chemical reactions and pathways resulting in the formation of cyclopentanol.
The chemical reactions and pathways resulting in the formation of cyclopentanol.
The chemical reactions and pathways resulting in the formation of cyclopentanol.
The chemical reactions and pathways resulting in the formation of cyclopentanol.
The chemical reactions and pathways resulting in the breakdown of cyclopentanol.
The chemical reactions and pathways resulting in the breakdown of cyclopentanol.
The chemical reactions and pathways resulting in the breakdown of cyclopentanol.
The process of regulating the proliferation and elimination of mast cells such that the total number of mast cells within a whole or part of an organism is stable over time in the absence of an outside stimulus.
Any apoptotic process in a mast cell, a cell that is found in almost all tissues containing numerous basophilic granules and capable of releasing large amounts of histamine and heparin upon activation.
Any apoptotic process in a mast cell, a cell that is found in almost all tissues containing numerous basophilic granules and capable of releasing large amounts of histamine and heparin upon activation.
Any process that modulates the frequency, rate, or extent of mast cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mast cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mast cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mast cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mast cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mast cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of mast cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of mast cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of mast cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of mast cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of mast cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of mast cell apoptotic process.
Any apoptotic process in a myeloid cell, a cell of the monocyte, granulocyte, mast cell, megakaryocyte, or erythroid lineage.
Any apoptotic process in a myeloid cell, a cell of the monocyte, granulocyte, mast cell, megakaryocyte, or erythroid lineage.
Any process that modulates the frequency, rate, or extent of neutrophil apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of neutrophil apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of neutrophil apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of neutrophil apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of neutrophil apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of neutrophil apoptotic process.
Any process that activates or increases the frequency, rate, or extent of neutrophil apoptotic process.
Any process that activates or increases the frequency, rate, or extent of neutrophil apoptotic process.
Any process that activates or increases the frequency, rate, or extent of neutrophil apoptotic process.
Any process that activates or increases the frequency, rate, or extent of neutrophil apoptotic process.
Any process that activates or increases the frequency, rate, or extent of neutrophil apoptotic process.
Any process that activates or increases the frequency, rate, or extent of neutrophil apoptotic process.
Any process that modulates the frequency, rate, or extent of myeloid cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a myeloid cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a myeloid cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a myeloid cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a myeloid cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of a myeloid cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of myeloid cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of myeloid cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of myeloid cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of myeloid cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of myeloid cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of myeloid cell apoptotic process.
Any process in which a macromolecule is transported to, or maintained in, a specific location.
Any process in which a polysaccharide is transported to, or maintained in, a specific location.
Combining with soluble bitter compounds to initiate a change in cell activity. These receptors are responsible for the sense of bitter taste.
Combining with soluble salty compounds to initiate a change in cell activity. These receptors are responsible for the sense of salty taste.
Combining with soluble sour compounds to initiate a change in cell activity. These receptors are responsible for the sense of sour taste.
Combining with soluble sweet compounds to initiate a change in cell activity. These receptors are responsible for the sense of sweet taste.
Combining with soluble umami compounds to initiate a change in cell activity. These receptors are responsible for the sense of umami taste, the savory taste of meats and other foods that are rich in glutamates.
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of an organelle.
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of an organelle.
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a chromosome.
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a chromosome.
Any process that modulates the frequency, rate or extent of sister chromatid segregation.
Any process that stops, prevents, or reduces the frequency, rate or extent of sister chromatid segregation.
Any process that modulates the frequency, rate or extent of sister chromatid segregation during mitosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of sister chromatid segregation during mitosis.
The chemical reactions and pathways involving clavulanic acid, (2R,3Z,5R)-3-(2-hydroxyethylidene)-7-oxo-4-oxa-1-azabicyclo[3.2.0]heptane-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of clavulanic acid, (2R,3Z,5R)-3-(2-hydroxyethylidene)-7-oxo-4-oxa-1-azabicyclo[3.2.0]heptane-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of clavulanic acid, (2R,3Z,5R)-3-(2-hydroxyethylidene)-7-oxo-4-oxa-1-azabicyclo[3.2.0]heptane-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of clavulanic acid, (2R,3Z,5R)-3-(2-hydroxyethylidene)-7-oxo-4-oxa-1-azabicyclo[3.2.0]heptane-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of clavulanic acid, (2R,3Z,5R)-3-(2-hydroxyethylidene)-7-oxo-4-oxa-1-azabicyclo[3.2.0]heptane-2-carboxylic acid.
The chemical reactions and pathways involving aminophosphonates, phosphonic acid derivatives that contain an amino group.
The chemical reactions and pathways involving cyanoamino acids, amino acid derivatives that contain a cyanide group.
The chemical reactions and pathways involving D-glutamine, the D-enantiomer of the amino acid glutamine, i.e. (2R)-2,5-diamino-5-oxopentanoic acid.
The chemical reactions and pathways involving D-glutamate, the D-enantiomer of the amino acid glutamate, i.e. (2R)-2-aminopentanedioic acid.
The chemical reactions and pathways involving D-arginine, the D-enantiomer of the amino acid arginine, i.e. (2R)-2-amino-5-(carbamimidamido)pentanoic acid.
The chemical reactions and pathways involving D-ornithine, the D-enantiomer of the amino acid ornithine, i.e. (2R)-2,5-diaminopentanoic acid.
Self-propelled movement of a cell or organism from one location to another along an axis.
The deposition or aggregation of coloring matter in a cell.
The deposition or aggregation of coloring matter in an ocellus, a minute simple eye found in many invertebrates.
A protein complex containing accessory proteins which bind a recombinase (e.g. Rad51) and bind single-stranded DNA (ssDNA), and promote nucleation of the recombinase onto ssDNA.
A conserved heterodimeric DNA recombinase mediator complex that contains the RecA family proteins Rhp55p and Rph57 in Schizosaccharomyces, or orthologs thereof (e.g. Rad55p and Rad57p in Saccharomyces).
A DNA recombinase mediator complex that contains the Rad51 paralogs RAD51B, RAD51C, RAD51D, and XRCC2, or orthologs thereof.
A heterodimeric DNA recombinase mediator complex that contains the Rad51 paralogs RAD51D and XRCC2, or orthologs thereof; conserved from fission yeast to human but absent from budding yeast.
A DNA recombinase mediator complex that contains the Rad51 paralogs RAD51C and XRCC3, or orthologs thereof.
A DNA recombinase mediator complex that contains the Rad51 paralogs RAD51B and RAD51C, or orthologs thereof.
The chemical reactions and pathways involving macrolides, any of a large group of polyketide compounds that contain a large lactone ring with few or no double bonds and no nitrogen atoms, linked glycosidically to one or more sugar groups. The macrolides include the carbomycins, the erythromycins, oleandomycin, oligomycins, and the spiramycins, and act as antibiotics, mainly against Gram-positive bacteria.
The chemical reactions and pathways leading to the formation of macrolides, any of a large group of polyketide compounds that contain a large lactone ring with few or no double bonds and no nitrogen atoms, linked glycosidically to one or more sugar groups. The macrolides include the carbomycins, the erythromycins, oleandomycin, oligomycins, and the spiramycins, and act as antibiotics, mainly against Gram-positive bacteria.
The chemical reactions and pathways leading to the formation of macrolides, any of a large group of polyketide compounds that contain a large lactone ring with few or no double bonds and no nitrogen atoms, linked glycosidically to one or more sugar groups. The macrolides include the carbomycins, the erythromycins, oleandomycin, oligomycins, and the spiramycins, and act as antibiotics, mainly against Gram-positive bacteria.
The chemical reactions and pathways leading to the formation of macrolides, any of a large group of polyketide compounds that contain a large lactone ring with few or no double bonds and no nitrogen atoms, linked glycosidically to one or more sugar groups. The macrolides include the carbomycins, the erythromycins, oleandomycin, oligomycins, and the spiramycins, and act as antibiotics, mainly against Gram-positive bacteria.
The chemical reactions and pathways leading to the formation of macrolides, any of a large group of polyketide compounds that contain a large lactone ring with few or no double bonds and no nitrogen atoms, linked glycosidically to one or more sugar groups. The macrolides include the carbomycins, the erythromycins, oleandomycin, oligomycins, and the spiramycins, and act as antibiotics, mainly against Gram-positive bacteria.
The chemical reactions and pathways involving ansamycins, any of a group of complex macrolactam compounds characterized by a cyclic structure in which an aliphatic ansa chain forms a bridge between two non-adjacent positions of a cyclic p-system; many exhibit antibacterial, antifungal or antitumor activity.
The chemical reactions and pathways leading to the formation of ansamycins, any of a group of complex macrolactam compounds characterized by a cyclic structure in which an aliphatic ansa chain forms a bridge between two non-adjacent positions of a cyclic p-system; many exhibit antibacterial, antifungal or antitumor activity.
The chemical reactions and pathways leading to the formation of ansamycins, any of a group of complex macrolactam compounds characterized by a cyclic structure in which an aliphatic ansa chain forms a bridge between two non-adjacent positions of a cyclic p-system; many exhibit antibacterial, antifungal or antitumor activity.
The chemical reactions and pathways leading to the formation of ansamycins, any of a group of complex macrolactam compounds characterized by a cyclic structure in which an aliphatic ansa chain forms a bridge between two non-adjacent positions of a cyclic p-system; many exhibit antibacterial, antifungal or antitumor activity.
The chemical reactions and pathways leading to the formation of ansamycins, any of a group of complex macrolactam compounds characterized by a cyclic structure in which an aliphatic ansa chain forms a bridge between two non-adjacent positions of a cyclic p-system; many exhibit antibacterial, antifungal or antitumor activity.
The chemical reactions and pathways involving vancomycin, (3S,6R,7R,11R,23S,26S,30aS,36R,38aR)-44-[2-O-(3-amino-2,3,6-trideoxy-3-C-methyl-alpha-L-lyxo-hexopyranosyl)-beta-D-glucopyranosyloxy]-3-(carbamoylmethyl)-10,19-dichloro-2,3,4,5,6,7,23,25,26,36,37,38,38a-tetradecahydro-7,22,28,30,32-pentahydroxy-6-(N-methyl-D-leucyl)-2,5,24,38,39-pentaoxo-1H,22H-23,36-(epiminomethano)-8,11:18,21-dietheno-13,16:31,35-di(metheno)[1,6,9]oxadiazacyclohexadecino[4,5-m][10,2,16]benzoxadiazacyclotetracosine-26-carboxylic acid, a complex glycopeptide from Streptomyces orientalis that inhibits a specific step in the synthesis of the peptidoglycan layer in Gram-positive bacteria.
The chemical reactions and pathways leading to the formation of vancomycin, (3S,6R,7R,11R,23S,26S,30aS,36R,38aR)-44-[2-O-(3-amino-2,3,6-trideoxy-3-C-methyl-alpha-L-lyxo-hexopyranosyl)-beta-D-glucopyranosyloxy]-3-(carbamoylmethyl)-10,19-dichloro-2,3,4,5,6,7,23,25,26,36,37,38,38a-tetradecahydro-7,22,28,30,32-pentahydroxy-6-(N-methyl-D-leucyl)-2,5,24,38,39-pentaoxo-1H,22H-23,36-(epiminomethano)-8,11:18,21-dietheno-13,16:31,35-di(metheno)[1,6,9]oxadiazacyclohexadecino[4,5-m][10,2,16]benzoxadiazacyclotetracosine-26-carboxylic acid, a complex glycopeptide from Streptomyces orientalis that inhibits a specific step in the synthesis of the peptidoglycan layer in Gram-positive bacteria.
The chemical reactions and pathways leading to the formation of vancomycin, (3S,6R,7R,11R,23S,26S,30aS,36R,38aR)-44-[2-O-(3-amino-2,3,6-trideoxy-3-C-methyl-alpha-L-lyxo-hexopyranosyl)-beta-D-glucopyranosyloxy]-3-(carbamoylmethyl)-10,19-dichloro-2,3,4,5,6,7,23,25,26,36,37,38,38a-tetradecahydro-7,22,28,30,32-pentahydroxy-6-(N-methyl-D-leucyl)-2,5,24,38,39-pentaoxo-1H,22H-23,36-(epiminomethano)-8,11:18,21-dietheno-13,16:31,35-di(metheno)[1,6,9]oxadiazacyclohexadecino[4,5-m][10,2,16]benzoxadiazacyclotetracosine-26-carboxylic acid, a complex glycopeptide from Streptomyces orientalis that inhibits a specific step in the synthesis of the peptidoglycan layer in Gram-positive bacteria.
The chemical reactions and pathways leading to the formation of vancomycin, (3S,6R,7R,11R,23S,26S,30aS,36R,38aR)-44-[2-O-(3-amino-2,3,6-trideoxy-3-C-methyl-alpha-L-lyxo-hexopyranosyl)-beta-D-glucopyranosyloxy]-3-(carbamoylmethyl)-10,19-dichloro-2,3,4,5,6,7,23,25,26,36,37,38,38a-tetradecahydro-7,22,28,30,32-pentahydroxy-6-(N-methyl-D-leucyl)-2,5,24,38,39-pentaoxo-1H,22H-23,36-(epiminomethano)-8,11:18,21-dietheno-13,16:31,35-di(metheno)[1,6,9]oxadiazacyclohexadecino[4,5-m][10,2,16]benzoxadiazacyclotetracosine-26-carboxylic acid, a complex glycopeptide from Streptomyces orientalis that inhibits a specific step in the synthesis of the peptidoglycan layer in Gram-positive bacteria.
The chemical reactions and pathways leading to the formation of vancomycin, (3S,6R,7R,11R,23S,26S,30aS,36R,38aR)-44-[2-O-(3-amino-2,3,6-trideoxy-3-C-methyl-alpha-L-lyxo-hexopyranosyl)-beta-D-glucopyranosyloxy]-3-(carbamoylmethyl)-10,19-dichloro-2,3,4,5,6,7,23,25,26,36,37,38,38a-tetradecahydro-7,22,28,30,32-pentahydroxy-6-(N-methyl-D-leucyl)-2,5,24,38,39-pentaoxo-1H,22H-23,36-(epiminomethano)-8,11:18,21-dietheno-13,16:31,35-di(metheno)[1,6,9]oxadiazacyclohexadecino[4,5-m][10,2,16]benzoxadiazacyclotetracosine-26-carboxylic acid, a complex glycopeptide from Streptomyces orientalis that inhibits a specific step in the synthesis of the peptidoglycan layer in Gram-positive bacteria.
The chemical reactions and pathways involving the monoterpenoid pinene; alpha-pinene is (1S,5S)-2,6,6-trimethylbicyclo[3.1.1]hept-2-ene, and beta-pinene is (1S,5S)-6,6-dimethyl-2-methylenebicyclo[3.1.1]heptane.
The chemical reactions and pathways leading to the breakdown of the monoterpenoid pinene; alpha-pinene is (1S,5S)-2,6,6-trimethylbicyclo[3.1.1]hept-2-ene, and beta-pinene is (1S,5S)-6,6-dimethyl-2-methylenebicyclo[3.1.1]heptane.
The chemical reactions and pathways leading to the breakdown of the monoterpenoid pinene; alpha-pinene is (1S,5S)-2,6,6-trimethylbicyclo[3.1.1]hept-2-ene, and beta-pinene is (1S,5S)-6,6-dimethyl-2-methylenebicyclo[3.1.1]heptane.
The chemical reactions and pathways leading to the breakdown of the monoterpenoid pinene; alpha-pinene is (1S,5S)-2,6,6-trimethylbicyclo[3.1.1]hept-2-ene, and beta-pinene is (1S,5S)-6,6-dimethyl-2-methylenebicyclo[3.1.1]heptane.
The chemical reactions and pathways resulting in the formation of isoquinoline alkaloids, alkaloid compounds that contain bicyclic N-containing aromatic rings and are derived from a 3,4-dihydroxytyramine (dopamine) precursor that undergoes a Schiff base addition with aldehydes of different origin.
The chemical reactions and pathways resulting in the formation of isoquinoline alkaloids, alkaloid compounds that contain bicyclic N-containing aromatic rings and are derived from a 3,4-dihydroxytyramine (dopamine) precursor that undergoes a Schiff base addition with aldehydes of different origin.
The chemical reactions and pathways resulting in the formation of isoquinoline alkaloids, alkaloid compounds that contain bicyclic N-containing aromatic rings and are derived from a 3,4-dihydroxytyramine (dopamine) precursor that undergoes a Schiff base addition with aldehydes of different origin.
The chemical reactions and pathways resulting in the formation of isoquinoline alkaloids, alkaloid compounds that contain bicyclic N-containing aromatic rings and are derived from a 3,4-dihydroxytyramine (dopamine) precursor that undergoes a Schiff base addition with aldehydes of different origin.
The chemical reactions and pathways resulting in the formation of isoquinoline alkaloids, alkaloid compounds that contain bicyclic N-containing aromatic rings and are derived from a 3,4-dihydroxytyramine (dopamine) precursor that undergoes a Schiff base addition with aldehydes of different origin.
The chemical reactions and pathways involving isoquinoline alkaloids, alkaloid compounds that contain bicyclic N-containing aromatic rings and are derived from a 3,4-dihydroxytyramine (dopamine) precursor that undergoes a Schiff base addition with aldehydes of different origin.
The chemical reactions and pathways involving isoquinoline alkaloids, alkaloid compounds that contain bicyclic N-containing aromatic rings and are derived from a 3,4-dihydroxytyramine (dopamine) precursor that undergoes a Schiff base addition with aldehydes of different origin.
The process in which a precursor cell type acquires the specialized features of a T cell via a differentiation pathway dependent upon transit through the thymus.
The process in which a precursor cell type acquires the specialized features of a T cell via a differentiation pathway dependent upon transit through the thymus.
The process in which a precursor cell type acquires the specialized features of a T cell via a differentiation pathway dependent upon transit through the thymus.
The process in which a precursor cell type acquires the specialized features of a T cell via a differentiation pathway dependent upon transit through the thymus.
The process in which a precursor cell type acquires the specialized features of a T cell via a differentiation pathway independent of the thymus.
The expansion of an immature T cell population by cell division.
The expansion of an immature T cell population by cell division in the thymus.
The expansion of an immature T cell population by cell division in the thymus.
The expansion of an immature T cell population by cell division in the thymus.
Any process that modulates the frequency, rate or extent of T cell differentiation in the thymus.
Any process that modulates the frequency, rate or extent of T cell differentiation in the thymus.
Any process that modulates the frequency, rate or extent of T cell differentiation in the thymus.
Any process that modulates the frequency, rate or extent of T cell differentiation in the thymus.
Any process that modulates the frequency, rate or extent of extrathymic T cell differentiation.
Any process that modulates the frequency, rate or extent of immature T cell proliferation.
Any process that modulates the frequency, rate or extent of immature T cell proliferation in the thymus.
Any process that modulates the frequency, rate or extent of immature T cell proliferation in the thymus.
Any process that modulates the frequency, rate or extent of immature T cell proliferation in the thymus.
Any process that stops, prevents, or reduces the frequency, rate or extent of T cell differentiation in the thymus.
Any process that stops, prevents, or reduces the frequency, rate or extent of T cell differentiation in the thymus.
Any process that stops, prevents, or reduces the frequency, rate or extent of T cell differentiation in the thymus.
Any process that stops, prevents, or reduces the frequency, rate or extent of T cell differentiation in the thymus.
Any process that stops, prevents, or reduces the frequency, rate or extent of extrathymic T cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of immature T cell proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of immature T cell proliferation in the thymus.
Any process that stops, prevents, or reduces the frequency, rate or extent of immature T cell proliferation in the thymus.
Any process that stops, prevents, or reduces the frequency, rate or extent of immature T cell proliferation in the thymus.
Any process that activates or increases the frequency, rate or extent of T cell differentiation in the thymus.
Any process that activates or increases the frequency, rate or extent of T cell differentiation in the thymus.
Any process that activates or increases the frequency, rate or extent of T cell differentiation in the thymus.
Any process that activates or increases the frequency, rate or extent of T cell differentiation in the thymus.
Any process that activates or increases the frequency, rate or extent of extrathymic T cell differentiation.
Any process that activates or increases the frequency, rate or extent of immature T cell proliferation.
Any process that activates or increases the frequency, rate or extent of immature T cell proliferation in the thymus.
Any process that activates or increases the frequency, rate or extent of immature T cell proliferation in the thymus.
Any process that activates or increases the frequency, rate or extent of immature T cell proliferation in the thymus.
A large, elongated, rod-shaped secretory granule characteristic of vascular endothelial cells that contain a number of structurally and functionally distinct proteins, of which the best characterized are von Willebrand factor (VWF) and P-selectin. Weibel-Palade bodies are formed from the trans-Golgi network in a process that depends on VWF, which is densely packed in a highly organized manner, and on coat proteins that remain associated with the granules. Upon cell stimulation, regulated exocytosis releases the contained proteins to the cell surface, where they act in the recruitment of platelets and leukocytes and in inflammatory and vasoactive responses.
Catalysis of the reaction: putrescine + 2-oxoglutarate = L-glutamate + 1-pyrroline + H2O.
Catalysis of the reaction: putrescine + 2-oxoglutarate = L-glutamate + 1-pyrroline + H2O.
Catalysis of the reaction: putrescine + 2-oxoglutarate = L-glutamate + 1-pyrroline + H2O.
Catalysis of the reaction: putrescine + 2-oxoglutarate = L-glutamate + 1-pyrroline + H2O.
Catalysis of the reaction: putrescine + 2-oxoglutarate = L-glutamate + 1-pyrroline + H2O.
Catalysis of the reaction: putrescine + 2-oxoglutarate = L-glutamate + 1-pyrroline + H2O.
Catalysis of the reaction: putrescine + 2-oxoglutarate = L-glutamate + 1-pyrroline + H2O.
A membrane-bounded storage granule found in cells of the aleurone layer in plants; contains either a protein matrix, protein-carbohydrate bodies and/or globoids. Aleurone grains are formed by the vacuole, rough endoplasmic reticulum and dictyosomes.
The double lipid bilayer enclosing the amyloplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
Either of the lipid bilayers that surround an amyloplast and form the amyloplast envelope.
The inner, i.e. lumen-facing, lipid bilayer of the amyloplast envelope; also faces the amyloplast stroma.
A membrane-bounded extension of the cell, originally characterized in Mycoplasma species, that contains an electron-dense core that is part of the cytoskeleton and is oriented lengthwise and ends distally in a bulbous knob (terminal button). Required for adherence to host cells and involved in gliding motility and cell division.
A Gcn5-independent multisubunit complex that catalyzes the acetylation of histone H3. The budding yeast complex includes Sas3p, Taf30p, and Yng1p.
The portion of the plasma membrane surrounding a cellular bud.
The lipid bilayer surrounding an acidocalcisome.
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the type VI secretion system. Proteins secreted by this system do not require an N-terminal signal sequence.
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the type VI secretion system. Proteins secreted by this system do not require an N-terminal signal sequence.
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the type VI secretion system. Proteins secreted by this system do not require an N-terminal signal sequence.
A complex of proteins that permits the transfer of proteins into the extracellular milieu or directly into host cells via the type VI secretion system. Proteins secreted by this complex do not require an N-terminal signal sequence.
The structure, composed of a monolayer of glycolipids with embedded proteins, that encloses the pigments and other contents of the chlorosome.
The lipid bilayer surrounding any of the compartments that make up the cis-Golgi network.
The lipid bilayer surrounding any of the compartments that make up the cis-Golgi network.
A cytosolic vesicle that is enclosed by a double membrane and is implicated in the cytoplasm to vacuole targeting pathway. These vesicles are found in the yeast S. cerevisiae, and contain vacuolar hydrolases, aminopeptidase I (Ape1p) and alpha-mannosidase (Ams1p).
A cytosolic vesicle that is enclosed by a double membrane and is implicated in the cytoplasm to vacuole targeting pathway. These vesicles are found in the yeast S. cerevisiae, and contain vacuolar hydrolases, aminopeptidase I (Ape1p) and alpha-mannosidase (Ams1p).
The aggregation, arrangement and bonding together of a set of components to form a mitochondrial respiratory chain complex.
Either of the two lipid bilayers surrounding a Cvt vesicle, a vesicle that functions in the cytoplasm-to-vacuole targeting (Cvt) pathway.
Either of the two lipid bilayers surrounding a Cvt vesicle, a vesicle that functions in the cytoplasm-to-vacuole targeting (Cvt) pathway.
The lipid bilayer surrounding an attachment organelle.  This is a region of the cell membrane facing the environment - in mycoplasma, part of the mycolate outer membrane.
The double lipid bilayer enclosing the cyanelle and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
Either of the lipid bilayers that surround a cyanelle and form the cyanelle envelope.
The volume enclosed by a cyanelle thylakoid membrane.
The lipid bilayer membrane of any thylakoid within a cyanelle.
The lipid bilayer surrounding any of the compartments of the endoplasmic reticulum (ER)-Golgi intermediate compartment system.
A vesicle filled with crystalline protein that shows sequence similarities with various esterases.
The lipid bilayer surrounding an esterosome. This membrane has characteristics of rough endoplasmic reticulum (RER) membranes.
Any process that stops, prevents, or reduces the frequency, rate or extent of RNA splicing.
Any process that activates or increases the frequency, rate or extent of RNA splicing.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of purine nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of purine nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of purine nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of purine nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of purine nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of purine nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of purine nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of purine nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of purine nucleotides.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that modulates the rate of GTP hydrolysis by a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that activates or increases the activity of a GTPase.
Any process that modulates the frequency, rate or extent of the addition of one or more phosphate groups to a histone protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of one or more phosphate groups to a histone protein.
Any process that activates or increases the frequency, rate or extent of the addition of one or more phosphate groups to a histone protein.
Interacting selectively and non-covalently with an acetylcholine receptor.
Any process that modulates the frequency, rate or extent of glucokinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a glucose molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of glucokinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a glucose molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of glucokinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a glucose molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of glucokinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a glucose molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of glucokinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a glucose molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of glucokinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a glucose molecule.
Any process that activates or increases the frequency, rate or extent of glucokinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a glucose molecule.
Any process that activates or increases the frequency, rate or extent of glucokinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a glucose molecule.
Any process that activates or increases the frequency, rate or extent of glucokinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a glucose molecule.
Any process that activates or increases the frequency, rate or extent of glucokinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a glucose molecule.
Any process that activates or increases the frequency, rate or extent of glucokinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a glucose molecule.
Interacting selectively and non-covalently with a ubiquitin activating enzyme, any of the E1 proteins.
Any process that modulates the frequency, rate or extent of the phosphorylation of peptidyl-serine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the phosphorylation of peptidyl-serine.
Any process that activates or increases the frequency, rate or extent of the phosphorylation of peptidyl-serine.
Any process that modulates the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the phosphorylation of a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Interacting selectively and non-covalently with a progesterone receptor.
Any process that modulates the frequency, rate or extent of the activity of any intracellular steroid hormone receptor signaling pathway.
Any process that modulates the frequency, rate or extent of the activity of any intracellular steroid hormone receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of any intracellular steroid hormone receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of any intracellular steroid hormone receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of any intracellular steroid hormone receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of any intracellular steroid hormone receptor signaling pathway.
Any process that modulates the frequency, rate or extent of the activity of an intracellular estrogen receptor signaling pathway.
Any process that modulates the frequency, rate or extent of the activity of an intracellular estrogen receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of an intracellular estrogen receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of an intracellular estrogen receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of an intracellular estrogen receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the activity of an intracellular estrogen receptor signaling pathway.
Interacting selectively and non-covalently with the FFAT motif, a short motif containing diphenylalanine in an acidic tract that targets proteins to the cytosolic surface of the ER and to the nuclear membrane by binding directly to members of the VAP (VAMP-associated protein) protein family.
A large cytoskeletal structure located at the posterior end of the perinuclear theca of a mammalian sperm head. The nucleus is tightly associated with the calyx, which contains calicin and basic cylicin proteins.
The process in which immune receptor V, D, and J, or V and J gene segments, depending on the specific receptor, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
The process in which immune receptor V, D, and J, or V and J gene segments, depending on the specific receptor, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
The process in which immune receptor V, D, and J, or V and J gene segments, depending on the specific receptor, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
The process in which immune receptor V, D, and J, or V and J gene segments, depending on the specific receptor, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
The process in which immune receptor V, D, and J, or V and J gene segments, depending on the specific receptor, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
The process in which immunoglobulin gene segments are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS). For immunoglobulin heavy chains V, D, and J gene segments are joined, and for immunoglobulin light chains V and J gene segments are joined.
The process in which immunoglobulin gene segments are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS). For immunoglobulin heavy chains V, D, and J gene segments are joined, and for immunoglobulin light chains V and J gene segments are joined.
The process in which immunoglobulin gene segments are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS). For immunoglobulin heavy chains V, D, and J gene segments are joined, and for immunoglobulin light chains V and J gene segments are joined.
The process in which immunoglobulin gene segments are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS). For immunoglobulin heavy chains V, D, and J gene segments are joined, and for immunoglobulin light chains V and J gene segments are joined.
The process in which immunoglobulin gene segments are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS). For immunoglobulin heavy chains V, D, and J gene segments are joined, and for immunoglobulin light chains V and J gene segments are joined.
The process in which T cell receptor V, D, and J, or V and J gene segments, depending on the specific locus, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
The process in which T cell receptor V, D, and J, or V and J gene segments, depending on the specific locus, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
The process in which T cell receptor V, D, and J, or V and J gene segments, depending on the specific locus, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
The process in which T cell receptor V, D, and J, or V and J gene segments, depending on the specific locus, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
The process in which T cell receptor V, D, and J, or V and J gene segments, depending on the specific locus, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
The process in which T cell receptor V, D, and J, or V and J gene segments, depending on the specific locus, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
The process in which T cell receptor V, D, and J, or V and J gene segments, depending on the specific locus, are recombined within a single locus utilizing the conserved heptamer and nonomer recombination signal sequences (RSS).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + oligogalacturonide(out) = ADP + phosphate + oligogalacturonide(in).
Enables the transfer of oligogalacturonide from one side of a membrane to the other.
The directed movement of oligogalacturonides into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of proteins within cells.
Any process that modulates the vectorial transfer of a protein from the cytoplasm into the nucleus, across the nuclear membrane.
Any process that stops, prevents or reduces the vectorial transfer of a protein from the cytoplasm into the nucleus, across the nuclear membrane.
Any process that activates or increases the vectorial transfer of a protein from the cytoplasm into the nucleus, across the nuclear membrane.
Interacting selectively and non-covalently with a mitogen-activated protein kinase kinase kinase kinase, any protein that can phosphorylate a MAP kinase kinase kinase.
The lipid bilayer surrounding a melanosome.
The lipid bilayer surrounding a microneme.
Catalysis of the transfer of an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-mannose linkage.
Catalysis of the transfer of an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-mannose linkage.
Catalysis of the transfer of an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-mannose linkage.
Catalysis of the transfer of an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-mannose linkage.
A specialized extracellularc matrix that surrounds the photoreceptors of the retina and lies between them and the apical surface of the retinal pigment epithelium. The IPM has been implicated in several important activities required for photoreceptor function and maintenance.
A multilayered extraembryonic matrix that functions as a substrate for cell adhesion through early development. It is thought to protect and lubricate the embryo, stabilize the blastomeres during morphogenesis, and regulate nutrient intake. The major constituent of the hyaline layer is the protein hyalin. This matrix has been found in echinoderms.
A ribonucleoprotein complex that contains members of the Argonaute family of proteins, additional protein subunits, and duplex siRNA; required for heterochromatin assembly and siRNA generation. Possibly involved in the conversion of ds siRNA to ss siRNA.
The process in which double-stranded siRNA molecules are converted to single-stranded siRNAs; required for the formation of a mature RITS complex during RNA interference.
The modification of histone H3 by the removal of a methyl group from lysine at position 9 of the histone.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the assembly of a protein or protein complex onto a DNA molecule.
The proteinaceous structure surrounding a gas vesicle.
The proteinaceous structure surrounding a gas vesicle.
Any intracellular signal transduction in which the signal is passed on within the cell by activation of a member of the NFAT protein family as a consequence of NFAT dephosphorylation by Ca(2+)-activated calcineurin. The cascade begins with calcium-dependent activation of the phosphatase calcineurin. Calcineurin dephosphorylates multiple phosphoserine residues on NFAT, resulting in the translocation of NFAT to the nucleus. The cascade ends with regulation of transcription by NFAT. The calcineurin-NFAT cascade lies downstream of many cell surface receptors, including G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs) that signal to mobilize calcium ions (Ca2+).
Any intracellular signal transduction in which the signal is passed on within the cell by activation of a member of the NFAT protein family as a consequence of NFAT dephosphorylation by Ca(2+)-activated calcineurin. The cascade begins with calcium-dependent activation of the phosphatase calcineurin. Calcineurin dephosphorylates multiple phosphoserine residues on NFAT, resulting in the translocation of NFAT to the nucleus. The cascade ends with regulation of transcription by NFAT. The calcineurin-NFAT cascade lies downstream of many cell surface receptors, including G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs) that signal to mobilize calcium ions (Ca2+).
The catalytic sector of the mitochondrial hydrogen-transporting ATP synthase; it comprises the catalytic core and central stalk, and is peripherally associated with the chloroplast thylakoid membrane when the entire ATP synthase is assembled. The chloroplast F0 domain contains three alpha, three beta, one gamma, one delta, and one epsilon subunits.
All non-F1 subunits of the chloroplast hydrogen-transporting ATP synthase, including integral and peripheral chloroplast thylakoid membrane proteins.
All non-F1 subunits of the chloroplast hydrogen-transporting ATP synthase, including integral and peripheral chloroplast thylakoid membrane proteins.
A proton-transporting two-sector ATPase complex that couples ATP hydrolysis to the transport of protons across a concentration gradient. The resulting transmembrane electrochemical potential of H+ is used to drive a variety of (i) secondary active transport systems via H+-dependent symporters and antiporters and (ii) channel-mediated transport systems. The complex comprises a membrane sector (V0) that carries out proton transport and a cytoplasmic compartment sector (V1) that catalyzes ATP hydrolysis. V-type ATPases are found in the membranes of organelles such as vacuoles, endosomes, and lysosomes, and in the plasma membrane.
A protein complex that forms part of a proton-transporting two-sector ATPase complex and carries out proton transport across a membrane. The proton-transporting domain (F0, V0, or A0) includes integral and peripheral membrane proteins.
A protein complex that forms part of a proton-transporting two-sector ATPase complex and catalyzes ATP hydrolysis or synthesis. The catalytic domain (F1, V1, or A1) comprises a hexameric catalytic core and a central stalk, and is peripherally associated with the membrane when the two-sector ATPase is assembled.
A protein complex that forms part of a proton-transporting V-type ATPase and mediates proton transport across a membrane. The V0 complex consists of at least four different subunits (a,c,d and e); six or more c subunits form a proton-binding rotor ring.
A protein complex that forms part of a proton-transporting V-type ATPase and catalyzes ATP hydrolysis. The V1 complex consists of: (1) a globular headpiece with three alternating copies of subunits A and B that form a ring, (2) a central rotational stalk composed of single copies of subunits D and F, and (3) a peripheral stalk made of subunits C, E, G and H. Subunits A and B mediate the hydrolysis of ATP at three reaction sites associated with subunit A.
A proton-transporting two-sector ATPase complex found in the plasma membrane.
Any process that modulates the frequency, rate or extent of the addition of a ubiquitin group to a histone protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of a ubiquitin group to a histone protein.
Any process that activates or increases the frequency, rate or extent of the addition of a ubiquitin group to a histone protein.
A protein complex that possesses dolichyl-phosphate beta-D-mannosyltransferase activity; contains a catalytic subunit, a regulatory subunit, and a third subunit that stabilizes the complex. In human and several other metazoa, the subunits are named DPM1, DPM2 and DPM3, respectively.
A protein complex that possesses dolichyl-phosphate beta-D-mannosyltransferase activity; contains a catalytic subunit, a regulatory subunit, and a third subunit that stabilizes the complex. In human and several other metazoa, the subunits are named DPM1, DPM2 and DPM3, respectively.
A conserved heterotrimeric protein complex that promotes histone H3 and H4 deposition onto newly synthesized DNA during replication or DNA repair; specifically facilitates replication-dependent nucleosome assembly with the major histone H3 (H3.1). In many species the CAF-1 subunits are designated p150, p60, and p48.
Catalysis of the reaction: 1,2-diacyl-sn-glycero-3-phosphocholine + ceramide = 1,2-diacyl-sn-glycerol + sphingomyelin.
Catalysis of the reaction: 1,2-diacyl-sn-glycero-3-phosphocholine + ceramide = 1,2-diacyl-sn-glycerol + sphingomyelin.
Catalysis of the reaction: 1,2-diacyl-sn-glycero-3-phosphocholine + ceramide = 1,2-diacyl-sn-glycerol + sphingomyelin.
Catalysis of the reaction: 1,2-diacyl-sn-glycero-3-phosphocholine + ceramide = 1,2-diacyl-sn-glycerol + sphingomyelin.
Catalysis of the reaction: 1,2-diacyl-sn-glycero-3-phosphocholine + ceramide = 1,2-diacyl-sn-glycerol + sphingomyelin.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin A stimulus.
Catalysis of the cyclization of double bonds in prosolanapyrone II to form (-)-solanapyrone A.
Catalysis of the reaction: a 2-pyrone + oxalacetate = macrophomate.
Catalysis of the reaction: protein serine/threonine phosphate + H2O = protein serine/threonine + phosphate, dependent on the presence of calcium-bound calmodulin.
Catalysis of the reaction: protein serine/threonine phosphate + H2O = protein serine/threonine + phosphate, dependent on the presence of calcium-bound calmodulin.
Catalysis of the reaction: protein serine/threonine phosphate + H2O = protein serine/threonine + phosphate, dependent on the presence of calcium-bound calmodulin.
Catalysis of the reaction: protein serine/threonine phosphate + H2O = protein serine/threonine + phosphate, dependent on the presence of calcium-bound calmodulin.
A nucleosome-binding protein complex that comprises two SWIRM domain histone demethylases and two PHD finger proteins. The complex is involved in transcriptional regulation via heterochromatic silencing and the regulation of chromatin boundary formation, and was first identified in fission yeast.
A nucleosome-binding protein complex that comprises two SWIRM domain histone demethylases and two PHD finger proteins. The complex is involved in transcriptional regulation via heterochromatic silencing and the regulation of chromatin boundary formation, and was first identified in fission yeast.
A nucleosome-binding protein complex that comprises two SWIRM domain histone demethylases and two PHD finger proteins. The complex is involved in transcriptional regulation via heterochromatic silencing and the regulation of chromatin boundary formation, and was first identified in fission yeast.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydroperoxide stimulus. Hydroperoxides are monosubstitution products of hydrogen peroxide, HOOH.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an alkyl hydroperoxide stimulus. Alkyl hydroperoxides are monosubstitution products of hydrogen peroxide, HOOH, where the substituent is an alkyl group.
Catalysis of the reaction: tryparedoxin + hydrogen peroxide = tryparedoxin disulfide + H2O.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin E stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin E stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin E stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ATP (adenosine 5'-triphosphate) stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ATP (adenosine 5'-triphosphate) stimulus.
Catalysis of the reaction: ATP + 4-diphospho-1D-myo-inositol (1,2,3,5,6)pentakisphosphate = 4,5-bisdiphosphoinositol-1D-myoinositol (1,2,3,6)tetrakisphosphate, and ATP + 6-diphospho-1D-myo-inositol (1,2,3,4,5)pentakisphosphate = 5,6-bisdiphosphoinositol-1D-myoinositol (1,2,3,4)tetrakisphosphate.
Catalysis of the reaction: ATP + 4-diphospho-1D-myo-inositol (1,2,3,5,6)pentakisphosphate = 4,5-bisdiphosphoinositol-1D-myoinositol (1,2,3,6)tetrakisphosphate, and ATP + 6-diphospho-1D-myo-inositol (1,2,3,4,5)pentakisphosphate = 5,6-bisdiphosphoinositol-1D-myoinositol (1,2,3,4)tetrakisphosphate.
Catalysis of the reaction: RDP-glucose + [alpha-D-glucosyl-(1,4)]n = RDP + [alpha-D-glucosyl-(1,4)]n+1, where RDP is ADP or UDP.
A protein complex that possesses DNA helicase activity.
A homohexameric protein complex that possesses DNA helicase activity; associates with DNA polymerase alpha-primase and translocates in the 5' to 3' direction.
Interacting selectively and non-covalently with the RNA subunit of ribonuclease P.
A cell cycle process that results in the division of the cytoplasm of a cell after meiosis, resulting in the separation of the original cell into two daughter cells.
Catalysis of the transfer of an N-acetylgalactosaminyl residue from UDP-N-acetyl-galactosamine to an acceptor molecule, forming a beta-1,4 linkage.
Catalysis of the reaction: UDP-N-acetylgalactosamine + N-acetylneuraminyl-alpha-2,3-galactosyl-beta-oligosaccharide = UDP + N-acetylgalactosaminyl-N-acetylneuraminyl-alpha-2,3-galactosyl-beta-oligosaccharide.
Catalysis of the reaction: UDP-N-acetylgalactosamine + N-acetylneuraminyl-alpha-2,3-galactosyl-beta-oligosaccharide = UDP + N-acetylgalactosaminyl-N-acetylneuraminyl-alpha-2,3-galactosyl-beta-oligosaccharide.
A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of leptin to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. Leptin is a hormone manufactured primarily in the adipocytes of white adipose tissue, and the level of circulating leptin is directly proportional to the total amount of fat in the body.
A series of molecular signals initiated by the binding of leptin to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. Leptin is a hormone manufactured primarily in the adipocytes of white adipose tissue, and the level of circulating leptin is directly proportional to the total amount of fat in the body.
A series of molecular signals initiated by the binding of adiponectin to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of adiponectin to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of adiponectin to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A process in which iron is solubilized and transported into a cell.
A process in which iron (Fe3+) is solubilized by binding to a receptor or transport protein and transported into a cell.
A process in which iron (Fe3+) is solubilized by ferric iron-specific chelators, known as siderophores, excreted by a cell; the iron-siderophore complex is then transported into the cell by specific cell surface receptors.
A process in which iron is solubilized by reduction from Fe3+ to Fe2+ via a cell surface reductase and subsequent transport of the iron across the membrane by iron uptake proteins.
The directed movement of ferric iron (Fe(III) or Fe3+) ions into a cell or organelle.
The directed movement of ferric iron (Fe(III) or Fe3+) ions into a cell or organelle.
Modulation of the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of deprivation of iron ions.
Interacting selectively and non-covalently with an amide, any derivative of an oxoacid in which an acidic hydroxy group has been replaced by an amino or substituted amino group.
Interacting selectively and non-covalently with urea, a water-soluble carboxamide with the structure H2N-CO-NH2.
Catalysis of the reaction: ATP + H2O + amide(out) = ADP + phosphate + amide(in).
Catalysis of the reaction: ATP + H2O + urea(out) = ADP + phosphate + urea(in).
Interacting selectively and non-covalently with the D- or L-enantiomer of xylose.
The directed movement of 2-aminoethylphosphonate, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of 2-aminoethylphosphonate, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Enables the directed movement of 2-aminoethylphosphonate from one side of a membrane to the other.
Enables the directed movement of 2-aminoethylphosphonate from one side of a membrane to the other.
Enables the directed movement of 2-aminoethylphosphonate from one side of a membrane to the other by catalysis of the reaction: ATP + H2O + 2-aminoethylphosphonate(out) = ADP + phosphate + 2-aminoethylphosphonate(in).
Enables the directed movement of 2-aminoethylphosphonate from one side of a membrane to the other by catalysis of the reaction: ATP + H2O + 2-aminoethylphosphonate(out) = ADP + phosphate + 2-aminoethylphosphonate(in).
Enables the directed movement of 2-aminoethylphosphonate from one side of a membrane to the other by catalysis of the reaction: ATP + H2O + 2-aminoethylphosphonate(out) = ADP + phosphate + 2-aminoethylphosphonate(in).
Interacting selectively and non-covalently with 2-aminoethylphosphonate.
Interacting selectively and non-covalently with 2-aminoethylphosphonate.
The directed movement of dsRNA, double-stranded ribonucleic acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of cysteine from inside of a cell, across the plasma membrane and into the extracellular region.
Enables the transfer of cysteine from one side of a membrane to the other.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + cysteine(out/in) = ADP + phosphate + cysteine(in/out).
The directed movement of carbohydrates out of a cell or organelle.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + D-methionine(out/in) = ADP + phosphate + D-methionine(in/out).
Any process that modulates the frequency, rate or extent of the addition of SUMO groups to a protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of SUMO groups to a protein.
Any process that activates or increases the frequency, rate or extent of the addition of SUMO groups to a protein.
Catalysis of the reaction: an 11-beta-hydroxysteroid + NAD+ = an 11-oxosteroid + NADH + H+.
Catalysis of the reaction: an 11-beta-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH + H+.
Catalysis of the reaction: an 11-beta-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH + H+.
Catalysis of the reaction: an 11-beta-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH + H+.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform amines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving amines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving amines.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of amines.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of amines.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of amines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of amines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of amines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of amines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of amines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of amines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of amines.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways leading to the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Catalysis of the reaction: a penicillin + H2O = a substituted beta-amino acid derivative of the penicillin.
Catalysis of the reaction: a cephalosporin + H2O = a substituted beta-amino acid derivative of the cephalosporin.
Any process that modulates the frequency, rate or extent of beta-lactamase activity, the hydrolysis of a beta-lactam to yield a substituted beta-amino acid.
Any process that modulates the frequency, rate or extent of nuclease activity, the hydrolysis of a penicillin to yield a substituted beta-amino acid derivative.
A protein complex that contains four related proteins that have been implicated in several membrane-related processes, such as sorting of H+-translocating ATPases, endocytosis, ER-Golgi trafficking, vacuole fusion, vacuolar polyphosphate homeostasis and the microautophagic scission of vesicles into the vacuolar lumen. The complex is enriched at the vacuolar membrane, but also found in other cellular compartments, including the ER and the cell periphery. In Saccharomyces, the subunits are Vtc1p, Vtc2p, Vtc3p and Vtc4p.
A protein complex that possesses histone acetyltransferase activity and links histone acetylation to the assembly of transcriptionally silent chromatin. In vitro, the complex acetylates lysine 16 of histone H4 and lysine 14 of histone H3, although the latter may not be relevant in vivo. The complex contains a catalytic subunit and at least two other subunits; in Saccharomyces, the catalytic subunit is Sas2p and additional subunits are Sas4p and Sas5p.
A protein complex containing an inhibitory-kappaB (I-kappaB/IKB) protein and one or more copies of an NF-kappaB protein. In the resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm.
A protein complex containing one Bcl protein and one or more copies of NF-kappaB2; formation of complexes of different stoichiometry depends on the Bcl3:NF-kappaB2 ratio, and allow Bcl3 to exert different regulatory effects on NF-kappaB2-dependent transcription.
A protein complex containing one Bcl protein and one or more copies of NF-kappaB2; formation of complexes of different stoichiometry depends on the Bcl3:NF-kappaB2 ratio, and allow Bcl3 to exert different regulatory effects on NF-kappaB2-dependent transcription.
The chemical reactions and pathways involving plastid DNA.
The process in which new strands of DNA are synthesized in a plastid.
The process in which new strands of DNA are synthesized in a plastid.
The DNA-dependent DNA replication that occurs in the nucleus of eukaryotic organisms as part of the cell cycle.
The DNA-dependent DNA replication that occurs in the nucleus of eukaryotic organisms as part of the cell cycle.
The DNA-dependent DNA replication that occurs in the nucleus of eukaryotic organisms as part of the cell cycle.
The DNA-dependent DNA replication that occurs in the nucleus of eukaryotic organisms as part of the cell cycle.
The cell cycle process by which a cell commits to entering the next cell cycle phase.
Any process that modulates the frequency, rate or extent of The DNA-dependent DNA replication that occurs in the nucleus of eukaryotic organisms as part of the cell cycle.
Any process that modulates the frequency, rate or extent of The DNA-dependent DNA replication that occurs in the nucleus of eukaryotic organisms as part of the cell cycle.
Any process that modulates the frequency, rate or extent of The DNA-dependent DNA replication that occurs in the nucleus of eukaryotic organisms as part of the cell cycle.
A multimeric protein complex that acts as an endosomal tethering complex (CORVET = class C core vacuole/endosome tethering) by cooperating with Rab GTPases to capture endosomal vesicles and trap them prior to the action of SNAREs; the complex is involved in endo-lysosomal biogenesis and required for transport between endosome and vacuole. The Saccharomyces cerevisiae complex contains Vps8p, Vps3p, Pep5p, Vps16p, Pep3p, and Vps33p.
Interacting selectively and non-covalently with choline, the amine 2-hydroxy-N,N,N-trimethylethanaminium.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of choline across a membrane.
A part of an axon, a cell projection of a neuron.
An axon part that is a gap in the myelin where voltage-gated sodium channels cluster and saltatory conduction is executed.
An axon part that is located between the nodes of Ranvier and surrounded by compact myelin sheath.
An axon part that is located adjacent to the nodes of Ranvier and surrounded by lateral loop portions of myelin sheath.
The directed movement of any phosphorylated myo-inositol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of myo-inositol hexakisphosphate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin B2 stimulus.
The sliding movement of actin thin filaments and myosin thick filaments past each other.
A protein complex that does not contain either a TATA-binding protein (TBP) or a TBP-like factor, but is composed of several TAFIIs and other proteins, including a histone acetyltransferase. This complex is able to nucleate transcription initiation by RNA polymerase II, can mediate transcriptional activation, and has histone acetyltransferase activity.
A cell cycle in which mitosis is begun and progresses normally through the end of anaphase, but not completed, resulting in a cell with increased ploidy.
The multiplication or reproduction of cells, resulting in the expansion of a cell population in the midbrain.
The multiplication or reproduction of cells, resulting in the expansion of a cell population in the midbrain.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin D stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin D stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin D stimulus.
A complex of three proteins integral to the cytoplasmic membrane of bacteria and membranes of organelles derived from bacteria (chloroplasts and mitochondria) involved in membrane transport of folded proteins.
A complex of three proteins integral to the cytoplasmic membrane of bacteria and membranes of organelles derived from bacteria (chloroplasts and mitochondria) involved in membrane transport of folded proteins.
A complex of three proteins integral to the cytoplasmic membrane of bacteria and membranes of organelles derived from bacteria (chloroplasts and mitochondria) involved in membrane transport of folded proteins.
A heterodimeric protein complex of protein C inhibitor (SERPINA5) and acrosin; formation of the complex inhibits the protease activity of acrosin.
A heterodimeric protein complex of protein C inhibitor (SERPINA5) and acrosin; formation of the complex inhibits the protease activity of acrosin.
A heterodimeric protein complex of protein C inhibitor (SERPINA5) and acrosin; formation of the complex inhibits the protease activity of acrosin.
A heterodimeric protein complex of protein C inhibitor (SERPINA5) and acrosin; formation of the complex inhibits the protease activity of acrosin.
A heterodimeric protein complex of protein C inhibitor (SERPINA5) and acrosin; formation of the complex inhibits the protease activity of acrosin.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + organic acid(out/in) = ADP + phosphate + organic acid(in/out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + carboxylic acid(out/in) = ADP + phosphate + carboxylic acid(in/out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + monocarboxylic acid(out/in) = ADP + phosphate + monocarboxylic acid(in/out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + ectoine(out/in) = ADP + phosphate + ectoine(in/out).
Enables the transfer of hydroxyectoine from one side of a membrane to the other.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + hydroxyectoine(out/in) = ADP + phosphate + hydroxyectoine(in/out).
A microtubule located such that it threads through the conoid and projects through the polar ring.
A protein complex composed of the small ribosomal subunit, eIF3, eIF1A, methionyl-initiatior methionine and a capped mRNA. The complex is initially positioned at the 5'-end of the capped mRNA.
A protein complex composed of the small ribosomal subunit, eIF3, eIF1A, methionyl-initiatior methionine and a capped mRNA. The complex is initially positioned at the 5'-end of the capped mRNA.
A protein complex composed of the small ribosomal subunit, eIF3, eIF1A, methionyl-initiatior methionine and a capped mRNA. The complex is initially positioned at the 5'-end of the capped mRNA.
A protein complex composed of the large and small ribosomal subunits, methionyl-initiatior tRNA, and the capped mRNA. The initiator tRNA is positioned at the ribosomal P site at the AUG codon corresponding to the beginning of the coding region.
A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of the T-tubule. A T-tubule is an invagination of the plasma membrane of a muscle cell that extends inward from the cell surface around each myofibril.
A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of the T-tubule. A T-tubule is an invagination of the plasma membrane of a muscle cell that extends inward from the cell surface around each myofibril.
A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of the T-tubule. A T-tubule is an invagination of the plasma membrane of a muscle cell that extends inward from the cell surface around each myofibril.
Interacting selectively and non-covalently with a monocarboxylic acid, any organic acid containing one carboxyl (COOH) group or anion (COO-).
Interacting selectively and non-covalently with ectoine, 1,4,5,6-tetrahydro-2-methyl-4-pyrimidinecarboxylic acid.
Interacting selectively and non-covalently with hydroxyectoine.
Interacting selectively and non-covalently with the D- or L-enantiomer of rhamnose.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + rhamnose(out/in) = ADP + phosphate + rhamnose(in/out).
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a contractile vacuole. A specialized vacuole that fills with water from the cytoplasm and then discharges this externally by the opening of contractile vacuole pores.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a contractile vacuole. A specialized vacuole that fills with water from the cytoplasm and then discharges this externally by the opening of contractile vacuole pores.
The controlled release of lysosomal enzymes by a cell.
Enables the transfer of dehydroascorbate, 5-(1,2-dihydroxyethyl)furan-2,3,4(5H)-trione, from one side of a membrane to the other.
Enables the transfer of dehydroascorbate, 5-(1,2-dihydroxyethyl)furan-2,3,4(5H)-trione, from one side of a membrane to the other.
A mitotic cell cycle in which mitosis is completed but cytokinesis does not occur, resulting in a cell containing multiple nuclei each with a chromosomal complement of the original ploidy (usually 2N).
The chemical reactions and pathways involving O-glucosylated derivatives of quercetin.
The chemical reactions and pathways leading to the formation of O-glucosylated derivatives of quercetin.
The chemical reactions and pathways leading to the formation of O-glucosylated derivatives of quercetin.
The chemical reactions and pathways leading to the formation of O-glucosylated derivatives of quercetin.
The chemical reactions and pathways leading to the formation of O-glucosylated derivatives of quercetin.
The chemical reactions and pathways involving chlorophyll a.
The chemical reactions and pathways leading to the formation of chlorophyll a.
The chemical reactions and pathways leading to the formation of chlorophyll a.
The chemical reactions and pathways leading to the formation of chlorophyll a.
The chemical reactions and pathways leading to the formation of chlorophyll a.
The chemical reactions and pathways involving phytol, (2E,7R,11R)-3,7,11,15-tetramethylhexadec-2-en-1-ol.
A process that generates phytol, (2E,7R,11R)-3,7,11,15-tetramethylhexadec-2-en-1-ol, from derivatives of it without de novo synthesis.
The directed movement of hydroxyectoine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
A protein complex that binds to the Swi4/6 cell cycle box (SCB) promoter element, consensus sequence CRCGAAA, and activates transcription during the G1/S transition of the cell cycle. In Saccharomyces, the complex contains a heterodimer of the DNA binding protein Swi4p and the activator Swi6p, and is associated with additional proteins known as Whi5p and Msa1p.
The chemical reactions and pathways leading to the breakdown of chlorophyll a.
The chemical reactions and pathways leading to the breakdown of chlorophyll a.
The chemical reactions and pathways leading to the breakdown of chlorophyll a.
The chemical reactions and pathways leading to the formation of chlorophyll a, via the intermediate phytyl diphosphate.
The chemical reactions and pathways leading to the formation of chlorophyll a, via the intermediate phytyl diphosphate.
The chemical reactions and pathways leading to the formation of chlorophyll a, via the intermediate phytyl diphosphate.
The chemical reactions and pathways leading to the formation of chlorophyll a, via the intermediate phytyl diphosphate.
The chemical reactions and pathways leading to the formation of chlorophyll a, via the intermediate phytyl diphosphate.
The chemical reactions and pathways leading to the formation of chlorophyll a, via the intermediate geranylgeranyl-chlorophyll a.
The chemical reactions and pathways leading to the formation of chlorophyll a, via the intermediate geranylgeranyl-chlorophyll a.
The chemical reactions and pathways leading to the formation of chlorophyll a, via the intermediate geranylgeranyl-chlorophyll a.
The chemical reactions and pathways leading to the formation of chlorophyll a, via the intermediate geranylgeranyl-chlorophyll a.
A cell cycle checkpoint that ensures accurate chromosome replication and segregation by preventing progression through a meiotic cell cycle until conditions are suitable for the cell to proceed to the next stage.
A cell cycle checkpoint that acts during a mitotic cell cycle and prevents the initiation of mitosis until DNA replication is complete, thereby ensuring that progeny inherit a full complement of the genome.
A cell cycle checkpoint that acts during a mitotic cell cycle and prevents the initiation of mitosis until DNA replication is complete, thereby ensuring that progeny inherit a full complement of the genome.
A cell cycle checkpoint that acts during a mitotic cell cycle and prevents the initiation of mitosis until DNA replication is complete, thereby ensuring that progeny inherit a full complement of the genome.
A cell cycle checkpoint that acts during a mitotic cell cycle and prevents the initiation of mitosis until DNA replication is complete, thereby ensuring that progeny inherit a full complement of the genome.
A cell cycle checkpoint that acts during a mitotic cell cycle and prevents the initiation of mitosis until DNA replication is complete, thereby ensuring that progeny inherit a full complement of the genome.
A DNA integrity checkpoint that acts to inhibit the G2/M1 transition of the meiotic cell cycle and prevents the initiation of nuclear division until DNA replication is complete.
A cell cycle checkpoint that delays the metaphase/anaphase transition of a meiotic cell cycle until the spindle is correctly assembled and chromosomes are attached to the spindle.
The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid, from other compounds, including valine.
The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid, from other compounds, including valine.
The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid, from other compounds, including valine.
The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid, from other compounds, including valine.
The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid, from other compounds, including 2-dehydropantolactone.
The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid, from other compounds, including 2-dehydropantolactone.
The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid, from other compounds, including 2-dehydropantolactone.
The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid, from other compounds, including 2-dehydropantolactone.
The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid, from other compounds, including 2-dehydropantolactone.
The chemical reactions and pathways involving UDP-D-xylose, uridinediphosphoxylose, a substance composed of xylose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-xylose, uridinediphosphoxylose, a substance composed of xylose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-xylose, uridinediphosphoxylose, a substance composed of xylose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-xylose, uridinediphosphoxylose, a substance composed of xylose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-xylose, uridinediphosphoxylose, a substance composed of xylose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways involving homomethionine, a non-protein amino acid synthesized from methionine via chain elongation.
The chemical reactions and pathways resulting in the formation of homomethionine, a non-protein amino acid synthesized from methionine via chain elongation.
The chemical reactions and pathways resulting in the formation of homomethionine, a non-protein amino acid synthesized from methionine via chain elongation.
The chemical reactions and pathways resulting in the formation of homomethionine, a non-protein amino acid synthesized from methionine via chain elongation.
The chemical reactions and pathways resulting in the formation of homomethionine, a non-protein amino acid synthesized from methionine via chain elongation.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate CDP-choline.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate CDP-choline.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate CDP-choline.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate CDP-choline.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate N-monomethylethanolamine.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate N-monomethylethanolamine.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate N-monomethylethanolamine.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate N-monomethylethanolamine.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate phosphoryl-ethanolamine.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate phosphoryl-ethanolamine.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate phosphoryl-ethanolamine.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), via the intermediate phosphoryl-ethanolamine.
The regulated release of cerebrospinal fluid (CSF) from the choroid plexus of the lateral, third and fourth ventricles. The cerebrospinal fluid is a clear liquid that located within the ventricles, spinal canal, and subarachnoid spaces.
The process in which a relatively unspecialized cell acquires specialized structural and/or functional features of a Leydig cell. A Leydig cell is a testosterone-secreting cell in the interstitial area, between the seminiferous tubules, in the testis.
Interacting selectively and non-covalently with a peroxisomal membrane targeting sequence, any of several sequences of amino acids within a protein that can act as a signal for the localization of the protein into the peroxisome membrane.
Interacting selectively and non-covalently with a peroxisomal membrane targeting sequence, any of several sequences of amino acids within a protein that can act as a signal for the localization of the protein into the peroxisome membrane.
Interacting selectively and non-covalently with a peroxisomal membrane targeting sequence, any of several sequences of amino acids within a protein that can act as a signal for the localization of the protein into the peroxisome membrane.
Interacting selectively and non-covalently with a peroxisomal membrane targeting sequence, any of several sequences of amino acids within a protein that can act as a signal for the localization of the protein into the peroxisome membrane.
The chemical reactions and pathways involving O-glucosylated derivatives of kaempferol.
The chemical reactions and pathways leading to the formation of O-glucosylated derivatives of kaempferol.
The chemical reactions and pathways leading to the formation of O-glucosylated derivatives of kaempferol.
The chemical reactions and pathways leading to the formation of O-glucosylated derivatives of kaempferol.
The chemical reactions and pathways leading to the formation of O-glucosylated derivatives of kaempferol.
The chemical reactions and pathways involving ent-kaur-16-ene. Ent-kaurene is a tetracyclic diterpenoid that is a precursor of several plant isoprenoids, including gibberellins.
The chemical reactions and pathways resulting in the formation of ent-kaurene. Ent-kaurene is a tetracyclic diterpenoid that is a precursor of several plant isoprenoids, including gibberellins.
The chemical reactions and pathways resulting in the formation of ent-kaurene. Ent-kaurene is a tetracyclic diterpenoid that is a precursor of several plant isoprenoids, including gibberellins.
The chemical reactions and pathways resulting in the formation of ent-kaurene. Ent-kaurene is a tetracyclic diterpenoid that is a precursor of several plant isoprenoids, including gibberellins.
The chemical reactions and pathways resulting in the formation of ent-kaurene. Ent-kaurene is a tetracyclic diterpenoid that is a precursor of several plant isoprenoids, including gibberellins.
The process whose specific outcome is the progression of a fin over time, from its formation to the mature structure.
The process in which the anatomical structures of a fin are generated and organized.
The process whose specific outcome is the progression of the anal fin over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the caudal fin over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the dorsal fin over time, from its formation to the mature structure.
The process whose specific outcome is the progression of a medial fin over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the pectoral fin over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the pelvic fin over time, from its formation to the mature structure.
Any process that modulates the frequency, rate or extent of collagen binding.
Any process that stops, prevents, or reduces the frequency, rate or extent of collagen binding.
Any process that stops, prevents, or reduces the frequency, rate or extent of collagen binding.
Any process that stops, prevents, or reduces the frequency, rate or extent of collagen binding.
Any process that stops, prevents, or reduces the frequency, rate or extent of collagen binding.
Any process that activates or increases the frequency, rate or extent of collagen binding.
Any process that activates or increases the frequency, rate or extent of collagen binding.
Any process that activates or increases the frequency, rate or extent of collagen binding.
Any process that activates or increases the frequency, rate or extent of collagen binding.
Any process that activates or increases the frequency, rate or extent of collagen binding.
The directed movement of cholesterol, cholest-5-en-3-beta-ol, out of a cell or organelle.
The chemical reactions and pathways resulting in the breakdown of glutamate, via the intermediate L-aspartate.
The chemical reactions and pathways resulting in the breakdown of glutamate, via the intermediate 2-oxosuccinamate.
The chemical reactions and pathways involving a tetrose, any monosaccharide with a chain of four carbon atoms in the molecule.
The chemical reactions and pathways resulting in the formation of a tetrose, any monosaccharide with a chain of four carbon atoms in the molecule.
The chemical reactions and pathways resulting in the formation of a tetrose, any monosaccharide with a chain of four carbon atoms in the molecule.
The chemical reactions and pathways resulting in the formation of a tetrose, any monosaccharide with a chain of four carbon atoms in the molecule.
The chemical reactions and pathways resulting in the formation of a tetrose, any monosaccharide with a chain of four carbon atoms in the molecule.
The chemical reactions and pathways involving apiose, the branched tetrose 3-C-(hydroxymethyl)-D-glycero-tetrose.
The chemical reactions and pathways resulting in the formation of apiose, the branched tetrose 3-C-(hydroxymethyl)-D-glycero-tetrose.
The chemical reactions and pathways resulting in the formation of apiose, the branched tetrose 3-C-(hydroxymethyl)-D-glycero-tetrose.
The chemical reactions and pathways resulting in the formation of apiose, the branched tetrose 3-C-(hydroxymethyl)-D-glycero-tetrose.
The chemical reactions and pathways resulting in the formation of apiose, the branched tetrose 3-C-(hydroxymethyl)-D-glycero-tetrose.
The chemical reactions and pathways involving UDP-D-apiose, uridinediphosphoapiose, a substance composed of apiose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-apiose, uridinediphosphoapicose, a substance composed of apiose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-apiose, uridinediphosphoapicose, a substance composed of apiose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-apiose, uridinediphosphoapicose, a substance composed of apiose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-apiose, uridinediphosphoapicose, a substance composed of apiose in glycosidic linkage with uridine diphosphate.
A cyclic series of interconversions involving S-adenosylmethionine, S-adenosyl-L-homocysteine, L-cysteine, and L-methionine. Couples utilization of the methyl group of SAM with recycling of the homocysteinyl group and regeneration of methionine.
A cyclic series of interconversions involving S-adenosylmethionine, S-adenosyl-L-homocysteine, L-cysteine, and L-methionine. Couples utilization of the methyl group of SAM with recycling of the homocysteinyl group and regeneration of methionine.
A cyclic series of interconversions involving chlorophyll a, chlorophyll b and several chlorophyllide intermediates.
A cyclic series of interconversions involving L-ascorbate and glutathione that scavenges hydrogen peroxide and reduces it to water, with concomitant oxidation of NADPH.
The chemical reactions and pathways involving UDP-L-arabinose, uridinediphosphoarabinose, a substance composed of arabinose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of L-arabinose, arabino-pentose.
The chemical reactions and pathways resulting in the formation of L-arabinose, arabino-pentose.
The chemical reactions and pathways resulting in the formation of L-arabinose, arabino-pentose.
The chemical reactions and pathways resulting in the formation of L-arabinose, arabino-pentose.
The chemical reactions and pathways resulting in the formation of UDP-L-arabinose, uridinediphosphoarabinose, a substance composed of arabinose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-L-arabinose, uridinediphosphoarabinose, a substance composed of arabinose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-L-arabinose, uridinediphosphoarabinose, a substance composed of arabinose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-L-arabinose, uridinediphosphoarabinose, a substance composed of arabinose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediates diaminopimelate and N-succinyl-2-amino-6-ketopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in four enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediates diaminopimelate and N-succinyl-2-amino-6-ketopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in four enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediates diaminopimelate and N-succinyl-2-amino-6-ketopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in four enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediates diaminopimelate and N-succinyl-2-amino-6-ketopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in four enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediates diaminopimelate and N-succinyl-2-amino-6-ketopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in four enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediates diaminopimelate and L-2-acetamido-6-oxoheptanedioate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in four enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediates diaminopimelate and L-2-acetamido-6-oxoheptanedioate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in four enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediates diaminopimelate and L-2-acetamido-6-oxoheptanedioate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in four enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediates diaminopimelate and L-2-acetamido-6-oxoheptanedioate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in four enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediates diaminopimelate and L-2-acetamido-6-oxoheptanedioate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in four enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in a single enzymatic step.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in a single enzymatic step.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in a single enzymatic step.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in a single enzymatic step.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in two enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in two enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in two enzymatic steps.
The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate; in this pathway tetrahydrodipicolinate is converted to meso-diaminopimelate in two enzymatic steps.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a secretory granule. A secretory granule is a small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a secretory granule. A secretory granule is a small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a secretory granule in a mast cell. A secretory granule is a small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a secretory granule in a mast cell. A secretory granule is a small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a secretory granule in a mast cell. A secretory granule is a small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion.
A process in which a protein is transported to, or maintained in, a location within an organelle.
A process in which a protein is transported to, or maintained in, a location within an organelle.
A process in which a protein is transported to, or maintained in, a location within a secretory granule.
A process in which a protein is transported to, or maintained in, a location within a secretory granule.
A process in which a protein is transported to, or maintained in, a location within a secretory granule in a mast cell.
A process in which a protein is transported to, or maintained in, a location within a secretory granule in a mast cell.
Any process in which a protease is transported to, or maintained in, a location within a secretory granule in a mast cell.
Any process in which a protease is transported to, or maintained in, a location within a secretory granule in a mast cell.
The directed movement of a protein to a location within a secretory granule in a mast cell.
The directed movement of a protein to a location within a secretory granule in a mast cell.
A process in which a protein is maintained in a secretory granule in a mast cell and prevented from moving elsewhere.
A process in which a protein is maintained in a secretory granule in a mast cell and prevented from moving elsewhere.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a secretory granule in a T cell. A secretory granule is a small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a secretory granule in a T cell. A secretory granule is a small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a secretory granule in a T cell. A secretory granule is a small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a secretory granule in a T cell. A secretory granule is a small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a secretory granule in a T cell. A secretory granule is a small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a secretory granule in a T cell. A secretory granule is a small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion.
The directed movement of a protease to a location within a secretory granule in a mast cell.
The directed movement of a protease to a location within a secretory granule in a mast cell.
A process in which a protease is maintained in a secretory granule in a mast cell and prevented from moving elsewhere.
A process in which a protease is maintained in a secretory granule in a mast cell and prevented from moving elsewhere.
A process in which a protein is transported to, or maintained in, a location within a secretory granule in a T cell.
A process in which a protein is transported to, or maintained in, a location within a secretory granule in a T cell.
A process in which a protein is transported to, or maintained in, a location within a secretory granule in a T cell.
A process in which a protein is transported to, or maintained in, a location within a secretory granule in a T cell.
A process in which a protein is transported to, or maintained in, a location within a secretory granule in a T cell.
Any process in which a protease is transported to, or maintained in, a location within a secretory granule in a T cell.
Any process in which a protease is transported to, or maintained in, a location within a secretory granule in a T cell.
Any process in which a protease is transported to, or maintained in, a location within a secretory granule in a T cell.
Any process in which a protease is transported to, or maintained in, a location within a secretory granule in a T cell.
Any process in which a protease is transported to, or maintained in, a location within a secretory granule in a T cell.
The directed movement of a protein to a location within a secretory granule in a T cell.
The directed movement of a protein to a location within a secretory granule in a T cell.
The directed movement of a protein to a location within a secretory granule in a T cell.
The directed movement of a protein to a location within a secretory granule in a T cell.
The directed movement of a protein to a location within a secretory granule in a T cell.
A process in which a protein is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
A process in which a protein is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
A process in which a protein is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
A process in which a protein is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
The directed movement of a protease to a location within a secretory granule in a T cell.
The directed movement of a protease to a location within a secretory granule in a T cell.
The directed movement of a protease to a location within a secretory granule in a T cell.
The directed movement of a protease to a location within a secretory granule in a T cell.
The directed movement of a protease to a location within a secretory granule in a T cell.
A process in which a protease is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
A process in which a protease is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
A process in which a protease is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
A process in which a protease is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
Any process in which the protease granzyme B is transported to, or maintained in, a location within a secretory granule in a T cell.
Any process in which the protease granzyme B is transported to, or maintained in, a location within a secretory granule in a T cell.
Any process in which the protease granzyme B is transported to, or maintained in, a location within a secretory granule in a T cell.
Any process in which the protease granzyme B is transported to, or maintained in, a location within a secretory granule in a T cell.
Any process in which the protease granzyme B is transported to, or maintained in, a location within a secretory granule in a T cell.
The directed movement of the protease granzyme B to a location within a secretory granule in a T cell.
The directed movement of the protease granzyme B to a location within a secretory granule in a T cell.
The directed movement of the protease granzyme B to a location within a secretory granule in a T cell.
The directed movement of the protease granzyme B to a location within a secretory granule in a T cell.
The directed movement of the protease granzyme B to a location within a secretory granule in a T cell.
The directed movement of the protease granzyme B to a location within a secretory granule in a T cell.
A process in which the protease granyme B is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
A process in which the protease granyme B is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
A process in which the protease granyme B is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
A process in which the protease granyme B is maintained in a secretory granule in a T cell and prevented from moving elsewhere.
The chemical reactions and pathways involving geranyl diphosphate, the universal precursor of the monoterpenes.
The chemical reactions and pathways involving geranyl diphosphate, the universal precursor of the monoterpenes.
The chemical reactions and pathways resulting in the formation of geranyl diphosphate.
The chemical reactions and pathways resulting in the formation of geranyl diphosphate.
The chemical reactions and pathways resulting in the formation of geranyl diphosphate.
The chemical reactions and pathways resulting in the formation of geranyl diphosphate.
The chemical reactions and pathways resulting in the formation of geranyl diphosphate.
The chemical reactions and pathways involving geranylgeranyl diphosphate, a polyprenol compound involved in the biosynthesis of a variety of terpenoids including chlorophylls, carotenoids, tocopherols, plastoquinones, and the plant hormones gibberellins.
The chemical reactions and pathways involving geranylgeranyl diphosphate, a polyprenol compound involved in the biosynthesis of a variety of terpenoids including chlorophylls, carotenoids, tocopherols, plastoquinones, and the plant hormones gibberellins.
The chemical reactions and pathways resulting in the formation of geranylgeranyl diphosphate.
The chemical reactions and pathways resulting in the formation of geranylgeranyl diphosphate.
The chemical reactions and pathways resulting in the formation of geranylgeranyl diphosphate.
The chemical reactions and pathways resulting in the formation of geranylgeranyl diphosphate.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane by decarboxylation of ornithine.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane by decarboxylation of ornithine.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane by decarboxylation of ornithine.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane by decarboxylation of ornithine.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine; in this pathway, arginine is converted to agmatine, and agmatine is converted to putrescine in a single enzymatic step.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine; in this pathway, arginine is converted to agmatine, and agmatine is converted to putrescine in a single enzymatic step.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine; in this pathway, arginine is converted to agmatine, and agmatine is converted to putrescine in a single enzymatic step.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine; in this pathway, arginine is converted to agmatine, and agmatine is converted to putrescine in a single enzymatic step.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine, via the intermediate N-carbamoylputrescine; in this pathway, arginine is converted to agmatine, and agmatine is converted to putrescine in two single enzymatic steps.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine, via the intermediate N-carbamoylputrescine; in this pathway, arginine is converted to agmatine, and agmatine is converted to putrescine in two single enzymatic steps.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine, via the intermediate N-carbamoylputrescine; in this pathway, arginine is converted to agmatine, and agmatine is converted to putrescine in two single enzymatic steps.
The chemical reactions and pathways resulting in the formation of putrescine, 1,4-diaminobutane, from other compounds, including arginine, via the intermediate N-carbamoylputrescine; in this pathway, arginine is converted to agmatine, and agmatine is converted to putrescine in two single enzymatic steps.
A ribonucleoprotein complex found in the cytoplasm of male germ cells, composed of exceedingly thin filaments that are consolidated into a compact mass or into dense strands of varying thickness that branch to form an irregular network. Contains mRNAs, miRNAs, and protein components involved in miRNA processing (such as Argonaute proteins and the endonuclease Dicer) and in RNA decay (such as the decapping enzyme DCP1a and GW182).
The chemical reactions and pathways resulting in the breakdown of homogalacturonan, a pectidic polymer, characterized by a backbone of 1,4-linked alpha-D-GalpA residues that can be methyl-esterified at C-6 and carry acetyl groups on O-2 and O-3.
The chemical reactions and pathways resulting in the breakdown of homogalacturonan, a pectidic polymer, characterized by a backbone of 1,4-linked alpha-D-GalpA residues that can be methyl-esterified at C-6 and carry acetyl groups on O-2 and O-3.
The chemical reactions and pathways resulting in the breakdown of homogalacturonan, a pectidic polymer, characterized by a backbone of 1,4-linked alpha-D-GalpA residues that can be methyl-esterified at C-6 and carry acetyl groups on O-2 and O-3.
The chemical reactions and pathways resulting in the formation of beta-alanine via the intermediate 1,3 diaminopropane.
The chemical reactions and pathways resulting in the formation of beta-alanine via the intermediate 1,3 diaminopropane.
The chemical reactions and pathways resulting in the formation of beta-alanine via the intermediate 1,3 diaminopropane.
The chemical reactions and pathways resulting in the formation of beta-alanine via the intermediate 1,3 diaminopropane.
The chemical reactions and pathways resulting in the formation of beta-alanine via the intermediate 3-hydroxypropionate.
The chemical reactions and pathways resulting in the formation of beta-alanine via the intermediate 3-hydroxypropionate.
The chemical reactions and pathways resulting in the formation of beta-alanine via the intermediate 3-hydroxypropionate.
The chemical reactions and pathways resulting in the formation of beta-alanine via the intermediate 3-hydroxypropionate.
The chemical reactions and pathways resulting in the formation of beta-alanine via the intermediate 3-ureidopropionate.
The chemical reactions and pathways resulting in the formation of beta-alanine via the intermediate 3-ureidopropionate.
The chemical reactions and pathways resulting in the formation of beta-alanine via the intermediate 3-ureidopropionate.
The chemical reactions and pathways involving zeatin, 2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of zeatin, 2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of zeatin, 2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of zeatin, 2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of zeatin, 2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways involving cis-zeatin, (2Z)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways involving trans-zeatin, (2E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
A triplet codon-amino acid adaptor activity that recognizes a UUU codon.
A triplet codon-amino acid adaptor activity that recognizes a UUU codon.
A triplet codon-amino acid adaptor activity that recognizes a UUC codon.
A triplet codon-amino acid adaptor activity that recognizes a UUC codon.
A triplet codon-amino acid adaptor activity that recognizes a UUA codon.
A triplet codon-amino acid adaptor activity that recognizes a UUA codon.
A triplet codon-amino acid adaptor activity that recognizes a UUG codon.
A triplet codon-amino acid adaptor activity that recognizes a UUG codon.
A triplet codon-amino acid adaptor activity that recognizes a UCU codon.
A triplet codon-amino acid adaptor activity that recognizes a UCU codon.
A triplet codon-amino acid adaptor activity that recognizes a UCC codon.
A triplet codon-amino acid adaptor activity that recognizes a UCC codon.
A triplet codon-amino acid adaptor activity that recognizes a UCA codon.
A triplet codon-amino acid adaptor activity that recognizes a UCA codon.
A triplet codon-amino acid adaptor activity that recognizes a UCG codon.
A triplet codon-amino acid adaptor activity that recognizes a UCG codon.
A triplet codon-amino acid adaptor activity that recognizes a UAU codon.
A triplet codon-amino acid adaptor activity that recognizes a UAU codon.
A triplet codon-amino acid adaptor activity that recognizes a UAC codon.
A triplet codon-amino acid adaptor activity that recognizes a UAC codon.
A triplet codon-amino acid adaptor activity that recognizes a UAA codon.
A triplet codon-amino acid adaptor activity that recognizes a UAG codon.
A triplet codon-amino acid adaptor activity that recognizes a UGU codon.
A triplet codon-amino acid adaptor activity that recognizes a UGU codon.
A triplet codon-amino acid adaptor activity that recognizes a UGC codon.
A triplet codon-amino acid adaptor activity that recognizes a UGC codon.
A triplet codon-amino acid adaptor activity that recognizes a UGA codon.
A triplet codon-amino acid adaptor activity that recognizes a UGG codon.
A triplet codon-amino acid adaptor activity that recognizes a UGG codon.
A triplet codon-amino acid adaptor activity that recognizes a CUU codon.
A triplet codon-amino acid adaptor activity that recognizes a CUU codon.
A triplet codon-amino acid adaptor activity that recognizes a CUC codon.
A triplet codon-amino acid adaptor activity that recognizes a CUC codon.
A triplet codon-amino acid adaptor activity that recognizes a CUA codon.
A triplet codon-amino acid adaptor activity that recognizes a CUA codon.
A triplet codon-amino acid adaptor activity that recognizes a CUG codon.
A triplet codon-amino acid adaptor activity that recognizes a CUG codon.
A triplet codon-amino acid adaptor activity that recognizes a CCU codon.
A triplet codon-amino acid adaptor activity that recognizes a CCU codon.
A triplet codon-amino acid adaptor activity that recognizes a CCC codon.
A triplet codon-amino acid adaptor activity that recognizes a CCA codon.
A triplet codon-amino acid adaptor activity that recognizes a CCG codon.
A triplet codon-amino acid adaptor activity that recognizes a CAU codon.
A triplet codon-amino acid adaptor activity that recognizes a CAU codon.
A triplet codon-amino acid adaptor activity that recognizes a CAC codon.
A triplet codon-amino acid adaptor activity that recognizes a CAA codon.
A triplet codon-amino acid adaptor activity that recognizes a CAG codon.
A triplet codon-amino acid adaptor activity that recognizes a CGU codon.
A triplet codon-amino acid adaptor activity that recognizes a CGU codon.
A triplet codon-amino acid adaptor activity that recognizes a CGC codon.
A triplet codon-amino acid adaptor activity that recognizes a CGA codon.
A triplet codon-amino acid adaptor activity that recognizes a CGG codon.
A triplet codon-amino acid adaptor activity that recognizes an AUU codon.
A triplet codon-amino acid adaptor activity that recognizes an AUU codon.
A triplet codon-amino acid adaptor activity that recognizes an AUC codon.
A triplet codon-amino acid adaptor activity that recognizes an AUC codon.
A triplet codon-amino acid adaptor activity that recognizes an AUA codon.
A triplet codon-amino acid adaptor activity that recognizes an AUA codon.
A triplet codon-amino acid adaptor activity that recognizes an AUG codon.
A triplet codon-amino acid adaptor activity that recognizes an AUG codon.
A triplet codon-amino acid adaptor activity that recognizes an AUG codon.
A triplet codon-amino acid adaptor activity that recognizes an ACU codon.
A triplet codon-amino acid adaptor activity that recognizes an ACU codon.
A triplet codon-amino acid adaptor activity that recognizes an ACC codon.
A triplet codon-amino acid adaptor activity that recognizes an ACA codon.
A triplet codon-amino acid adaptor activity that recognizes an ACG codon.
A triplet codon-amino acid adaptor activity that recognizes an AAU codon.
A triplet codon-amino acid adaptor activity that recognizes an AAU codon.
A triplet codon-amino acid adaptor activity that recognizes an AAC codon.
A triplet codon-amino acid adaptor activity that recognizes an AAA codon.
A triplet codon-amino acid adaptor activity that recognizes an AAG codon.
A triplet codon-amino acid adaptor activity that recognizes an AGU codon.
A triplet codon-amino acid adaptor activity that recognizes an AGU codon.
A triplet codon-amino acid adaptor activity that recognizes an AGC codon.
A triplet codon-amino acid adaptor activity that recognizes an AGA codon.
A triplet codon-amino acid adaptor activity that recognizes an AGG codon.
A triplet codon-amino acid adaptor activity that recognizes a GUU codon.
A triplet codon-amino acid adaptor activity that recognizes a GUU codon.
A triplet codon-amino acid adaptor activity that recognizes a GUC codon.
A triplet codon-amino acid adaptor activity that recognizes a GUC codon.
A triplet codon-amino acid adaptor activity that recognizes a GUA codon.
A triplet codon-amino acid adaptor activity that recognizes a GUA codon.
A triplet codon-amino acid adaptor activity that recognizes a GUG codon.
A triplet codon-amino acid adaptor activity that recognizes a GUG codon.
A triplet codon-amino acid adaptor activity that recognizes a GCU codon.
A triplet codon-amino acid adaptor activity that recognizes a GCU codon.
A triplet codon-amino acid adaptor activity that recognizes a GCC codon.
A triplet codon-amino acid adaptor activity that recognizes a GCA codon.
A triplet codon-amino acid adaptor activity that recognizes a GCG codon.
A triplet codon-amino acid adaptor activity that recognizes a GAU codon.
A triplet codon-amino acid adaptor activity that recognizes a GAU codon.
A triplet codon-amino acid adaptor activity that recognizes a GAC codon.
A triplet codon-amino acid adaptor activity that recognizes a GAA codon.
A triplet codon-amino acid adaptor activity that recognizes a GAG codon.
A triplet codon-amino acid adaptor activity that recognizes a GGU codon.
A triplet codon-amino acid adaptor activity that recognizes a GGU codon.
A triplet codon-amino acid adaptor activity that recognizes a GGC codon.
A triplet codon-amino acid adaptor activity that recognizes a GGA codon.
A triplet codon-amino acid adaptor activity that recognizes a GGG codon.
The chemical reactions and pathways resulting in the formation of cis-zeatin, (2Z)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of cis-zeatin, (2Z)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of cis-zeatin, (2Z)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of cis-zeatin, (2Z)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of trans-zeatin, (2E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of trans-zeatin, (2E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of trans-zeatin, (2E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of trans-zeatin, (2E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol.
The chemical reactions and pathways involving CMP-keto-3-deoxy-D-manno-octulosonic acid, a substance composed of the acidic sugar 3-deoxy-D-manno-octulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways involving CMP-keto-3-deoxy-D-manno-octulosonic acid, a substance composed of the acidic sugar 3-deoxy-D-manno-octulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways involving CMP-keto-3-deoxy-D-manno-octulosonic acid, a substance composed of the acidic sugar 3-deoxy-D-manno-octulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways resulting in the formation of CMP-keto-3-deoxy-D-manno-octulosonic acid, a substance composed of the acidic sugar 3-deoxy-D-manno-octulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways resulting in the formation of CMP-keto-3-deoxy-D-manno-octulosonic acid, a substance composed of the acidic sugar 3-deoxy-D-manno-octulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways resulting in the formation of CMP-keto-3-deoxy-D-manno-octulosonic acid, a substance composed of the acidic sugar 3-deoxy-D-manno-octulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways resulting in the formation of CMP-keto-3-deoxy-D-manno-octulosonic acid, a substance composed of the acidic sugar 3-deoxy-D-manno-octulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways resulting in the formation of CMP-keto-3-deoxy-D-manno-octulosonic acid, a substance composed of the acidic sugar 3-deoxy-D-manno-octulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways resulting in the formation of CMP-keto-3-deoxy-D-manno-octulosonic acid, a substance composed of the acidic sugar 3-deoxy-D-manno-octulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways resulting in the formation of CMP-keto-3-deoxy-D-manno-octulosonic acid, a substance composed of the acidic sugar 3-deoxy-D-manno-octulosonic acid in glycosidic linkage with cytidine monophosphate.
The chemical reactions and pathways involving gibberellin 12, (1R,2S,3S,4R,8S,9S,12R)-4,8-dimethyl-13-methylidenetetracyclo[10.2.1.01,9.03,8]pentadecane-2,4-dicarboxylic acid 1meta,4a-dimethyl-8-methylidene-4aalpha,4bbeta-gibbane-1alpha,10beta-dicarboxylic acid.
The chemical reactions and pathways involving gibberellin 12, (1R,2S,3S,4R,8S,9S,12R)-4,8-dimethyl-13-methylidenetetracyclo[10.2.1.01,9.03,8]pentadecane-2,4-dicarboxylic acid 1meta,4a-dimethyl-8-methylidene-4aalpha,4bbeta-gibbane-1alpha,10beta-dicarboxylic acid.
The chemical reactions and pathways involving gibberellin 12, (1R,2S,3S,4R,8S,9S,12R)-4,8-dimethyl-13-methylidenetetracyclo[10.2.1.01,9.03,8]pentadecane-2,4-dicarboxylic acid 1meta,4a-dimethyl-8-methylidene-4aalpha,4bbeta-gibbane-1alpha,10beta-dicarboxylic acid.
The chemical reactions and pathways resulting in the formation of gibberellin 12, (1R,2S,3S,4R,8S,9S,12R)-4,8-dimethyl-13-methylidenetetracyclo[10.2.1.01,9.03,8]pentadecane-2,4-dicarboxylic acid 1meta,4a-dimethyl-8-methylidene-4aalpha,4bbeta-gibbane-1alpha,10beta-dicarboxylic acid.
The chemical reactions and pathways resulting in the formation of gibberellin 12, (1R,2S,3S,4R,8S,9S,12R)-4,8-dimethyl-13-methylidenetetracyclo[10.2.1.01,9.03,8]pentadecane-2,4-dicarboxylic acid 1meta,4a-dimethyl-8-methylidene-4aalpha,4bbeta-gibbane-1alpha,10beta-dicarboxylic acid.
The chemical reactions and pathways resulting in the formation of gibberellin 12, (1R,2S,3S,4R,8S,9S,12R)-4,8-dimethyl-13-methylidenetetracyclo[10.2.1.01,9.03,8]pentadecane-2,4-dicarboxylic acid 1meta,4a-dimethyl-8-methylidene-4aalpha,4bbeta-gibbane-1alpha,10beta-dicarboxylic acid.
The chemical reactions and pathways resulting in the formation of gibberellin 12, (1R,2S,3S,4R,8S,9S,12R)-4,8-dimethyl-13-methylidenetetracyclo[10.2.1.01,9.03,8]pentadecane-2,4-dicarboxylic acid 1meta,4a-dimethyl-8-methylidene-4aalpha,4bbeta-gibbane-1alpha,10beta-dicarboxylic acid.
The chemical reactions and pathways resulting in the formation of gibberellin 12, (1R,2S,3S,4R,8S,9S,12R)-4,8-dimethyl-13-methylidenetetracyclo[10.2.1.01,9.03,8]pentadecane-2,4-dicarboxylic acid 1meta,4a-dimethyl-8-methylidene-4aalpha,4bbeta-gibbane-1alpha,10beta-dicarboxylic acid.
The chemical reactions and pathways resulting in the formation of gibberellin 12, (1R,2S,3S,4R,8S,9S,12R)-4,8-dimethyl-13-methylidenetetracyclo[10.2.1.01,9.03,8]pentadecane-2,4-dicarboxylic acid 1meta,4a-dimethyl-8-methylidene-4aalpha,4bbeta-gibbane-1alpha,10beta-dicarboxylic acid.
The chemical reactions and pathways involving GDP-L-galactose, a substance composed of L-galactose in glycosidic linkage with guanosine diphosphate.
The chemical reactions and pathways resulting in the formation of GDP-L-galactose, a substance composed of L-galactose in glycosidic linkage with guanosine diphosphate.
The chemical reactions and pathways resulting in the formation of GDP-L-galactose, a substance composed of L-galactose in glycosidic linkage with guanosine diphosphate.
The chemical reactions and pathways resulting in the formation of GDP-L-galactose, a substance composed of L-galactose in glycosidic linkage with guanosine diphosphate.
The chemical reactions and pathways resulting in the formation of GDP-L-galactose, a substance composed of L-galactose in glycosidic linkage with guanosine diphosphate.
The chemical reactions and pathways involving any indole-3-acetic acid conjugate, a form of indoleacetic acid covalently bound to another molecule.
The chemical reactions and pathways involving any indole-3-acetic acid conjugate, a form of indoleacetic acid covalently bound to another molecule.
The chemical reactions and pathways involving any indole-3-acetic acid conjugate, a form of indoleacetic acid covalently bound to another molecule.
The chemical reactions and pathways involving any indole-3-acetic acid conjugate, a form of indoleacetic acid covalently bound to another molecule.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid conjugate, a form of indoleacetic acid covalently bound to another molecule.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid conjugate, a form of indoleacetic acid covalently bound to another molecule.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid conjugate, a form of indoleacetic acid covalently bound to another molecule.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid conjugate, a form of indoleacetic acid covalently bound to another molecule.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid conjugate, a form of indoleacetic acid covalently bound to another molecule.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid conjugate, a form of indoleacetic acid covalently bound to another molecule.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid conjugate, a form of indoleacetic acid covalently bound to another molecule.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an amino acid or polypeptide through an amide bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an amino acid or polypeptide through an amide bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an amino acid or polypeptide through an amide bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an amino acid or polypeptide through an amide bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an amino acid or polypeptide through an amide bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an amino acid or polypeptide through an amide bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an amino acid or polypeptide through an amide bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an a sugar or polyol through an ester bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an a sugar or polyol through an ester bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an a sugar or polyol through an ester bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an a sugar or polyol through an ester bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an a sugar or polyol through an ester bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an a sugar or polyol through an ester bond.
The chemical reactions and pathways resulting in the formation of an indole-3-acetic acid amide conjugate, a form of indoleacetic acid covalently bound to an a sugar or polyol through an ester bond.
The chemical reactions and pathways involving S-methyl-methionine (SMM). SMM can be converted to methionine by donating a methyl group to homocysteine, and concurrent operation of this reaction and that mediated by MMT sets up the SMM cycle.
The chemical reactions and pathways involving UDP-L-rhamnose, a substance composed of rhamnose in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways involving UDP-D-galacturonate, a substance composed of galacturonic acid in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-galacturonate, a substance composed of galacturonic acid in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-galacturonate, a substance composed of galacturonic acid in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-galacturonate, a substance composed of galacturonic acid in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of UDP-D-galacturonate, a substance composed of galacturonic acid in glycosidic linkage with uridine diphosphate.
The chemical reactions and pathways resulting in the formation of galacturonate, the anion of galacturonic acid.
The chemical reactions and pathways resulting in the formation of galacturonate, the anion of galacturonic acid.
The chemical reactions and pathways resulting in the formation of galacturonate, the anion of galacturonic acid.
The chemical reactions and pathways resulting in the formation of galacturonate, the anion of galacturonic acid.
The chemical reactions and pathways resulting in the formation of D-galacturonate, the D-enantiomer of galacturonate, the anion of galacturonic acid.
The chemical reactions and pathways resulting in the formation of D-galacturonate, the D-enantiomer of galacturonate, the anion of galacturonic acid.
The chemical reactions and pathways resulting in the formation of D-galacturonate, the D-enantiomer of galacturonate, the anion of galacturonic acid.
The chemical reactions and pathways resulting in the formation of D-galacturonate, the D-enantiomer of galacturonate, the anion of galacturonic acid.
A homeostatic process involved in the maintenance of an internal steady state of a gas within an organism or cell.
A homeostatic process involved in the maintenance of an internal steady state of nitric oxide within an organism or cell.
The chemical reactions and pathways resulting in the formation of cyanidin 3-O-glucoside, a basic anthocyanin responsible for red to magenta coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of cyanidin 3-O-glucoside, a basic anthocyanin responsible for red to magenta coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of cyanidin 3-O-glucoside, a basic anthocyanin responsible for red to magenta coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of cyanidin 3-O-glucoside, a basic anthocyanin responsible for red to magenta coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of delphinidin 3-O-glucoside, a basic, water-soluble anthocyanin responsible for blue coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of delphinidin 3-O-glucoside, a basic, water-soluble anthocyanin responsible for blue coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of delphinidin 3-O-glucoside, a basic, water-soluble anthocyanin responsible for blue coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of delphinidin 3-O-glucoside, a basic, water-soluble anthocyanin responsible for blue coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of pelargonidin 3-O-glucoside, a basic anthocyanin responsible for red to magenta coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of pelargonidin 3-O-glucoside, a basic anthocyanin responsible for red to magenta coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of pelargonidin 3-O-glucoside, a basic anthocyanin responsible for red to magenta coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of pelargonidin 3-O-glucoside, a basic anthocyanin responsible for red to magenta coloration of flowers and fruits.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate 24,25-dihydrolanosterol.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate 24,25-dihydrolanosterol.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate 24,25-dihydrolanosterol.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate 24,25-dihydrolanosterol.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate desmosterol.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate desmosterol.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate desmosterol.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate desmosterol.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate lathosterol.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate lathosterol.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate lathosterol.
The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate lathosterol.
The chemical reactions and pathways involving coniferin, 4-(3-hydroxyprop-1-en-1-yl)-2-methoxyphenyl beta-D-glucopyranoside.
The chemical reactions and pathways involving esculetin, 6,7-dihydroxycoumarin.
The chemical reactions and pathways resulting in the formation of esculetin, 6,7-dihydroxycoumarin.
The chemical reactions and pathways resulting in the formation of esculetin, 6,7-dihydroxycoumarin.
The chemical reactions and pathways resulting in the formation of esculetin, 6,7-dihydroxycoumarin.
The chemical reactions and pathways resulting in the formation of esculetin, 6,7-dihydroxycoumarin.
The chemical reactions and pathways involving ferulate, (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of ferulate, (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of ferulate, (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of ferulate, (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of ferulate, (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoate.
The chemical reactions and pathways involving sinapate, (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of sinapate, (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of sinapate, (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of sinapate, (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of sinapate, (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the breakdown of galactose, via the intermediate D-galactonate.
The chemical reactions and pathways resulting in the breakdown of galactose, via the intermediate D-galactonate.
The chemical reactions and pathways resulting in the breakdown of galactose, via the intermediate D-galactonate.
The chemical reactions and pathways resulting in the breakdown of galactose, via the intermediate UDP-galactose.
The chemical reactions and pathways resulting in the breakdown of galactose, via the intermediate UDP-galactose.
The chemical reactions and pathways resulting in the breakdown of galactose, via the intermediate UDP-galactose.
The chemical reactions and pathways resulting in the breakdown of galactose, via the intermediate UDP-galactose.
A homeostatic process involved in the maintenance of an internal steady state of a carbohydrate within an organism or cell.
A homeostatic process involved in the maintenance of an internal steady state of galactose within an organism or cell.
A cellular homeostatic process involved in the maintenance of an internal steady state of galactose within a cell or between a cell and its external environment.
A ubiquitin-conjugating enzyme complex that contains two RING finger proteins, which have ubiquitin ligase activity, in addition to a protein with ubiquitin-conjugating enzyme activity; catalyzes the ubiquitination of histone H2B at lysine 119 (or the equivalent residue). In Schizosaccharomyces the subunits are Rhp1, Brl2/Rfp1 and Brl1/Rfp2.
The progression of the floor plate over time from its initial formation until its mature state.
The process in which the anatomical structure of the floor plate is generated and organized.
The chemical reactions and pathways resulting in the formation of glucosinolates from other compounds including homomethionine.
The chemical reactions and pathways resulting in the formation of glucosinolates from other compounds including homomethionine.
The chemical reactions and pathways resulting in the formation of glucosinolates from other compounds including homomethionine.
The chemical reactions and pathways resulting in the formation of glucosinolates from other compounds including homomethionine.
The chemical reactions and pathways resulting in the formation of glucosinolates from other compounds including phenylalanine.
The chemical reactions and pathways resulting in the formation of glucosinolates from other compounds including phenylalanine.
The chemical reactions and pathways resulting in the formation of glucosinolates from other compounds including phenylalanine.
The chemical reactions and pathways resulting in the formation of glucosinolates from other compounds including phenylalanine.
The chemical reactions and pathways resulting in the breakdown of glutamate into other compounds, including butyrate.
The chemical reactions and pathways resulting in the breakdown of glutamate into other compounds, including butyrate.
The chemical reactions and pathways resulting in the breakdown of glutamate into other compounds, including propionate.
The chemical reactions and pathways resulting in the breakdown of glutamate into other compounds, including propionate.
The chemical reactions and pathways involving luteolin, 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one.
The chemical reactions and pathways resulting in the formation of luteolin, 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one.
The chemical reactions and pathways resulting in the formation of luteolin, 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one.
The chemical reactions and pathways resulting in the formation of luteolin, 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one.
The chemical reactions and pathways resulting in the formation of luteolin, 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one.
The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including acetyl-CoA, via the intermediate saccharopine.
The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including acetyl-CoA, via the intermediate saccharopine.
The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including acetyl-CoA, via the intermediate 5-aminopentanamide.
The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including acetyl-CoA, via the intermediate 5-aminopentanamide.
The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including acetyl-CoA, via the intermediate L-pipecolate.
The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including acetyl-CoA, via the intermediate L-pipecolate.
The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including alpha-aminoadipate; in this pathway, L-lysine is converted to 2-aminoadipate-6-semialdehyde by lysine 6-aminotransferase.
The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including alpha-aminoadipate; in this pathway, L-lysine is converted to 2-aminoadipate-6-semialdehyde by lysine 6-aminotransferase.
The chemical reactions and pathways resulting in the formation of L-methionine from other compounds, including homoserine, via the intermediates O-phospho-L-homoserine and cystathionine.
The chemical reactions and pathways resulting in the formation of L-methionine from other compounds, including homoserine, via the intermediates O-phospho-L-homoserine and cystathionine.
The chemical reactions and pathways resulting in the formation of L-methionine from other compounds, including homoserine, via the intermediates O-phospho-L-homoserine and cystathionine.
The chemical reactions and pathways resulting in the formation of L-methionine from other compounds, including homoserine, via the intermediates O-phospho-L-homoserine and cystathionine.
The chemical reactions and pathways involving phytic acid, myo-inositol hexakisphosphate, a regulator of intracellular signaling, a highly abundant animal anti-nutrient and a phosphate and mineral storage compound in plant seeds.
The chemical reactions and pathways involving phytic acid, myo-inositol hexakisphosphate, a regulator of intracellular signaling, a highly abundant animal anti-nutrient and a phosphate and mineral storage compound in plant seeds.
The chemical reactions and pathways involving phytic acid, myo-inositol hexakisphosphate, a regulator of intracellular signaling, a highly abundant animal anti-nutrient and a phosphate and mineral storage compound in plant seeds.
The process of removing one or more phosphate group from myo-inositol hexakisphosphate.
The chemical reactions and pathways involving phytyl diphosphate, (2E)-3,7,11,15-tetramethylhexadec-2-en-1-yl trihydrogen diphosphate.
The chemical reactions and pathways resulting in the formation of phytol, (2E,7R,11R)-3,7,11,15-tetramethylhexadec-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of phytol, (2E,7R,11R)-3,7,11,15-tetramethylhexadec-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of phytol, (2E,7R,11R)-3,7,11,15-tetramethylhexadec-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of phytol, (2E,7R,11R)-3,7,11,15-tetramethylhexadec-2-en-1-ol.
The chemical reactions and pathways resulting in the formation of phytyl diphosphate, (2E)-3,7,11,15-tetramethylhexadec-2-en-1-yl trihydrogen diphosphate.
The chemical reactions and pathways resulting in the formation of phytyl diphosphate, (2E)-3,7,11,15-tetramethylhexadec-2-en-1-yl trihydrogen diphosphate.
The chemical reactions and pathways resulting in the formation of phytyl diphosphate, (2E)-3,7,11,15-tetramethylhexadec-2-en-1-yl trihydrogen diphosphate.
The chemical reactions and pathways resulting in the formation of phytyl diphosphate, (2E)-3,7,11,15-tetramethylhexadec-2-en-1-yl trihydrogen diphosphate.
The modification of histone H2A by addition of one or more ubiquitin groups.
The modification of histone H2B by addition of ubiquitin groups.
The chemical reactions and pathways involving ester derivatives of sinapate, (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of ester derivates of sinapate, (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of ester derivates of sinapate, (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of ester derivates of sinapate, (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate.
The chemical reactions and pathways resulting in the formation of ester derivates of sinapate, (2E)-3-(4-hydroxy-3,5-dimethoxyphenyl)prop-2-enoate.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next, from other compounds, including L-glutamate.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next, from other compounds, including L-glutamate.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next, from other compounds, including L-glutamate.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next, from other compounds, including L-glutamate.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next, from other compounds, including glycine and succinyl-CoA.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next, from other compounds, including glycine and succinyl-CoA.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next, from other compounds, including glycine and succinyl-CoA.
The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next, from other compounds, including glycine and succinyl-CoA.
A cyclic series of interconversions involving S-methyl-L-methionine, S-adenosyl-L-homocysteine, S-adenosyl-L-methionine, L-homocysteine, and L-methionine. Converts the methionine group of adenosylmethionine back to free methionine, and may serve regulate the cellular adenosylmethionine level.
The chemical reactions and pathways resulting in the formation of raffinose, the trisaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of raffinose, the trisaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of raffinose, the trisaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of raffinose, the trisaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways involving raffinose, the trisaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways involving stachyose, the tetrasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of stachyose, the tetrasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of stachyose, the tetrasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of stachyose, the tetrasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of stachyose, the tetrasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways involving verbascose, the pentasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of verbascose, the pentasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of verbascose, the pentasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of verbascose, the pentasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of verbascose, the pentasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways involving ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside, by a pathway in which galactinol:raffinose galactosyltransferase catalyzes chain elongation by transferring the alpha-galactosyl residue of galactinol to the oligosaccharide.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside, by a pathway in which galactinol:raffinose galactosyltransferase catalyzes chain elongation by transferring the alpha-galactosyl residue of galactinol to the oligosaccharide.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside, by a pathway in which galactinol:raffinose galactosyltransferase catalyzes chain elongation by transferring the alpha-galactosyl residue of galactinol to the oligosaccharide.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside, by a pathway in which galactinol:raffinose galactosyltransferase catalyzes chain elongation by transferring the alpha-galactosyl residue of galactinol to the oligosaccharide.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside, by a pathway in which galactan:galactan galactosyltransferase catalyzes chain elongation by transferring the alpha-galactosyl residue of one raffinose-family oligosaccharide to another.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside, by a pathway in which galactan:galactan galactosyltransferase catalyzes chain elongation by transferring the alpha-galactosyl residue of one raffinose-family oligosaccharide to another.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside, by a pathway in which galactan:galactan galactosyltransferase catalyzes chain elongation by transferring the alpha-galactosyl residue of one raffinose-family oligosaccharide to another.
The chemical reactions and pathways resulting in the formation of ajugose, the hexasaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside, by a pathway in which galactan:galactan galactosyltransferase catalyzes chain elongation by transferring the alpha-galactosyl residue of one raffinose-family oligosaccharide to another.
A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
A fatty acid beta-oxidation pathway in which the initial step, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA oxidase; the electrons removed by oxidation pass directly to oxygen and produce hydrogen peroxide, which is cleaved by peroxisomal catalases. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
A fatty acid beta-oxidation pathway by which fatty acids having cis-double bonds on odd-numbered carbons are degraded. In this pathway, a cis-3-enoyl-CoA is generated by the core beta-oxidation pathway, and then converted to a trans-2-enoyl-CoA, which can return to the core beta-oxidation pathway for complete degradation. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
A fatty acid beta-oxidation pathway by which fatty acids having cis-double bonds on even-numbered carbons are degraded. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
A fatty acid beta-oxidation pathway by which fatty acids having cis-double bonds on even-numbered carbons are degraded. In this pathway, the intermediate 2,4-dienoyl-CoA is converted to trans-2-enoyl-CoA by 2,4-dienoyl-CoA reductase and delta3-delta2-enoyl-CoA isomerase; trans-2-enoyl-CoA returns to the core beta-oxidation pathway for further degradation. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
A fatty acid beta-oxidation pathway by which fatty acids having cis-double bonds on even-numbered carbons are degraded. In this pathway, the intermediate 2,4-dienoyl-CoA is converted to cis-2-enoyl-CoA through one more cycle of the core beta-oxidation pathway. Cis-2-enoyl-CoA cannot be completely degraded via the core beta-oxidation pathway because hydratation of cis-2-enoyl-CoA yields D-3-hydroxyacyl-CoA, which is not a substrate for 3-hydroxylacyl-CoA dehydrogenase. Cis-2-enoyl-CoA must enter the so-called epimerase pathway, which involves converting D-3-hydroxyacyl-CoA to L-3-hydroxyacyl-CoA by 3-hydroxylacyl-CoA epimerase or by two stereo-specific enoyl-CoA hydratases. L-3-hydroxyacyl-CoA then returns to the core beta-oxidation pathway. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C.
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C.
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C.
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C.
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C.
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C.
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C; in this pathway, inositol 1,4,5-trisphosphate is first converted to inositol 1,3,4-trisphosphate, and then phosphorylated further.
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C; in this pathway, inositol 1,4,5-trisphosphate is first converted to inositol 1,3,4-trisphosphate, and then phosphorylated further.
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C; in this pathway, inositol 1,4,5-trisphosphate is first converted to inositol 1,3,4-trisphosphate, and then phosphorylated further.
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C; in this pathway, inositol 1,4,5-trisphosphate is first converted to inositol 1,3,4-trisphosphate, and then phosphorylated further.
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C; in this pathway, inositol 1,4,5-trisphosphate is first converted to inositol 1,3,4-trisphosphate, and then phosphorylated further.
The chemical reactions and pathways resulting in the formation of 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate, phytate, by a pathway using inositol 1,4,5-trisphosphate produced from phosphatidylinositol 4,5-biphosphate hydrolysis by phospholipase C; in this pathway, inositol 1,4,5-trisphosphate is first converted to inositol 1,3,4-trisphosphate, and then phosphorylated further.
The chemical reactions and pathways resulting in the formation of phytic acid, myo-inositol hexakisphosphate, by the successively phosphorylation of myo-inositol or an inositol trisphosphate; the inositol trisphosphates that may be used by this pathway are inositol 3,4,5-trisphosphate and inositol 3,4,6trisphosphate.
The chemical reactions and pathways resulting in the formation of phytic acid, myo-inositol hexakisphosphate, by the successively phosphorylation of myo-inositol or an inositol trisphosphate; the inositol trisphosphates that may be used by this pathway are inositol 3,4,5-trisphosphate and inositol 3,4,6trisphosphate.
The chemical reactions and pathways resulting in the formation of phytic acid, myo-inositol hexakisphosphate, by the successively phosphorylation of myo-inositol or an inositol trisphosphate; the inositol trisphosphates that may be used by this pathway are inositol 3,4,5-trisphosphate and inositol 3,4,6trisphosphate.
The chemical reactions and pathways resulting in the formation of phytic acid, myo-inositol hexakisphosphate, by the successively phosphorylation of myo-inositol or an inositol trisphosphate; the inositol trisphosphates that may be used by this pathway are inositol 3,4,5-trisphosphate and inositol 3,4,6trisphosphate.
The chemical reactions and pathways resulting in the formation of phytic acid, myo-inositol hexakisphosphate, by the successively phosphorylation of myo-inositol or an inositol trisphosphate; the inositol trisphosphates that may be used by this pathway are inositol 3,4,5-trisphosphate and inositol 3,4,6trisphosphate.
The chemical reactions and pathways resulting in the formation of phytic acid, myo-inositol hexakisphosphate, by the successively phosphorylation of myo-inositol or an inositol trisphosphate; the inositol trisphosphates that may be used by this pathway are inositol 3,4,5-trisphosphate and inositol 3,4,6trisphosphate.
Catalysis of the reaction: a phosphorylated MAP kinase + H2O = a MAP kinase + phosphate.
Catalysis of the reaction: MAP kinase tyrosine phosphate + H2O = MAP kinase tyrosine + phosphate.
A protein complex required for clamping microtubule binding sites, ensuring orientation of sister kinetochores to the same pole (mono-orientation) during meiosis I. In the yeast S. cerevisiae this complex consists of Csm1p, Lrs4p, Hrr25p and Mam1p; in S. pombe Psc1 and Mde4 have been identified as subunits.
A protein complex required for clamping microtubule binding sites, ensuring orientation of sister kinetochores to the same pole (mono-orientation) during meiosis I. In the yeast S. cerevisiae this complex consists of Csm1p, Lrs4p, Hrr25p and Mam1p; in S. pombe Psc1 and Mde4 have been identified as subunits.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin B3 stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin B3 stimulus.
A region of heterochromatin located at the rDNA repeats in a chromosome.
Any process that results in a change in state or activity of a multicellular organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).
Catalysis of the addition of a glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation; the transfer of glucose from dolichyl phosphate glucose (Dol-P-Glc) on to the lipid-linked oligosaccharide Man(7)GlcNAc(2)-PP-Dol.
A heterodimeric protein complex that possesses an endonuclease activity that specifically cleaves certain types of branched DNA structures; because such structures often form during the replication ribosomal DNA (rDNA) repeats, the complex plays a role in the maintenance of rDNA. The subunits are known as Slx1 and Slx 4 in budding and fission yeasts, and are conserved in eukaryotes.
Catalysis of the hydrolysis of an acetyl group or groups from a protein substrate.
The chemical reactions and pathways involving an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms.
Catalysis of the reaction: 7,8-dihydrofolate + NADP+ = folate + NADPH + H+.
A process that modulates the rate or extent of water loss from an organism via the skin.
A process in which the RNAi machinery mediates the degradation of nascent transcripts in association with chromatin.
A process in which the RNAi machinery mediates the degradation of nascent transcripts in association with chromatin.
A process in which the RNAi machinery mediates the degradation of nascent transcripts in association with chromatin.
A process in which the RNAi machinery mediates the degradation of nascent transcripts in association with chromatin.
A process in which the RNAi machinery mediates the degradation of nascent transcripts in association with chromatin.
The process in which the migration of an axon growth cone is directed to a specific target site along the dorsal-ventral body axis in response to a combination of attractive and repulsive cues. The dorsal/ventral axis is defined by a line that runs orthogonal to both the anterior/posterior and left/right axes. The dorsal end is defined by the upper or back side of an organism. The ventral end is defined by the lower or front side of an organism.
The process in which the migration of an axon growth cone is directed to a specific target site along the dorsal-ventral body axis in response to a combination of attractive and repulsive cues. The dorsal/ventral axis is defined by a line that runs orthogonal to both the anterior/posterior and left/right axes. The dorsal end is defined by the upper or back side of an organism. The ventral end is defined by the lower or front side of an organism.
The process in which the migration of an axon growth cone is directed to a specific target site along the dorsal-ventral body axis in response to a combination of attractive and repulsive cues. The dorsal/ventral axis is defined by a line that runs orthogonal to both the anterior/posterior and left/right axes. The dorsal end is defined by the upper or back side of an organism. The ventral end is defined by the lower or front side of an organism.
The process in which the migration of an axon growth cone is directed to a specific target site along the anterior-posterior body axis in response to a combination of attractive and repulsive cues. The anterior-posterior axis is defined by a line that runs from the head or mouth of an organism to the tail or opposite end of the organism.
The process in which the migration of an axon growth cone is directed to a specific target site along the anterior-posterior body axis in response to a combination of attractive and repulsive cues. The anterior-posterior axis is defined by a line that runs from the head or mouth of an organism to the tail or opposite end of the organism.
A protein complex required for the recycling of Golgi proteins, formation of lumenal membranes and sorting of ubiquitinated proteins into those membranes. This complex includes Vps1p and Hse1p in yeast and the Hrs and STAM proteins in mammals.
A protein complex required for the recycling of Golgi proteins, formation of lumenal membranes and sorting of ubiquitinated proteins into those membranes. This complex includes Vps1p and Hse1p in yeast and the Hrs and STAM proteins in mammals.
Any process in which a gamma-tubulin complex is transported to, or maintained in, a specific location.
Any process in which a gamma-tubulin complex is transported to, or maintained in, a specific location.
The DNA metabolic process, occurring during lagging strand synthesis, by which RNA primers are removed from Okazaki fragments, the resulting gaps filled by DNA polymerization, and the ends ligated to form a continuous strand.
Combining with lactoferrin and delivering lactoferrin into the cell via endocytosis. Lactoferrin is an iron-binding glycoprotein which binds ferric iron most efficiently at low pH.
Enables the transfer of lactoferrin from one side of a membrane to the other.
Enables the transfer of transferrin from one side of a membrane to the other.
The directed movement of lactoferrin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of transferrin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
A protein complex composed of a multicopper ferroxidase that oxidizes Fe(II) to Fe(III), and a ferric iron permease that transports the produced Fe(III) into the cell. In high-affinity transport the transporter is able to bind the solute even if it is only present at very low concentrations.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a testosterone stimulus.
The addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid at the surface of a cell.
The addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid in the cytosol.
The addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid in the endoplasmic reticulum.
The addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid in the endoplasmic reticulum.
The addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid in the endoplasmic reticulum.
The addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid in any compartment of the Golgi apparatus.
The addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid in any compartment of the Golgi apparatus.
The addition of a galactose unit to a protein amino acid in the endoplasmic reticulum.
The addition of a galactose unit to a protein amino acid in the endoplasmic reticulum.
The addition of a galactose unit to a protein amino acid at the surface of a cell.
The addition of a galactose unit to a protein amino acid in any compartment of the Golgi apparatus.
The addition of a galactose unit to a protein amino acid in the cytosol.
The portion of the plasma membrane surrounding the rhabdomere.
The chemical reactions and pathways resulting in the formation of tyrosine from other compounds, including chorismate, via the intermediate L-arogenate.
The chemical reactions and pathways resulting in the formation of tyrosine from other compounds, including chorismate, via the intermediate L-arogenate.
The chemical reactions and pathways resulting in the formation of tyrosine from other compounds, including chorismate, via the intermediate L-arogenate.
The chemical reactions and pathways resulting in the formation of L-phenylalanine from other compounds, including chorismate, via the intermediate phenylpyruvate.
The chemical reactions and pathways resulting in the formation of L-phenylalanine from other compounds, including chorismate, via the intermediate phenylpyruvate.
The chemical reactions and pathways resulting in the formation of L-phenylalanine from other compounds, including chorismate, via the intermediate phenylpyruvate.
The chemical reactions and pathways resulting in the formation of L-phenylalanine from other compounds, including chorismate, via the intermediate phenylpyruvate.
The chemical reactions and pathways resulting in the formation of L-phenylalanine from other compounds, including chorismate, via the intermediate L-arogenate.
The chemical reactions and pathways resulting in the formation of L-phenylalanine from other compounds, including chorismate, via the intermediate L-arogenate.
The chemical reactions and pathways resulting in the formation of L-phenylalanine from other compounds, including chorismate, via the intermediate L-arogenate.
The chemical reactions and pathways resulting in the formation of L-phenylalanine from other compounds, including chorismate, via the intermediate L-arogenate.
The chemical reactions and pathways resulting in the formation of shikimate, (3R,4S,5R)--3,4,5-trihydroxycyclohex-1-ene-1-carboxylate, the anion of shikimic acid.
The chemical reactions and pathways resulting in the formation of shikimate, (3R,4S,5R)--3,4,5-trihydroxycyclohex-1-ene-1-carboxylate, the anion of shikimic acid.
The chemical reactions and pathways resulting in the formation of shikimate, (3R,4S,5R)--3,4,5-trihydroxycyclohex-1-ene-1-carboxylate, the anion of shikimic acid.
The chemical reactions and pathways resulting in the formation of shikimate, (3R,4S,5R)--3,4,5-trihydroxycyclohex-1-ene-1-carboxylate, the anion of shikimic acid.
A heterohexameric protein complex that is involved in modification of wobble nucleosides in tRNA. The complex can associate physically with hyperphosphorylated RNA polymerase II; it contains two discrete heterotrimeric subcomplexes.
A heterohexameric protein complex that is involved in modification of wobble nucleosides in tRNA. The complex can associate physically with hyperphosphorylated RNA polymerase II; it contains two discrete heterotrimeric subcomplexes.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cobalamin (vitamin B12) stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an L-ascorbic acid (vitamin C) stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an L-ascorbic acid (vitamin C) stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an L-ascorbic acid (vitamin C) stimulus.
Facilitates the base-pairing of complementary single-stranded RNA.
A heterodimeric protein complex formed of BRCA2 and MAGE-D1; may mediate the synergistic activities of the two proteins in regulating cell growth.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydroxyisoflavone stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a genistein stimulus.
A protein complex consisting of at least tumerin and hamartin; its formation may regulate hamartin homomultimer formation. The complex acts as a GTPase activating protein (GAP) for the small GTPase (Rheb), and inhibits the TOR signaling pathway.
A protein complex consisting of at least tumerin and hamartin; its formation may regulate hamartin homomultimer formation. The complex acts as a GTPase activating protein (GAP) for the small GTPase (Rheb), and inhibits the TOR signaling pathway.
A multiprotein complex that functions as a mitotic checkpoint inhibitor of the anaphase-promoting complex/cyclosome (APC/C). In budding yeast this complex consists of Mad2p, Mad3p, Bub3p and Cdc20p, and in mammalian cells it consists of MAD2, BUBR1, BUB3, and CDC20.
The multiplication or reproduction of mammary gland epithelial cells, resulting in the expansion of a cell population. Mammary gland epithelial cells make up the covering of surfaces of the mammary gland. The mammary gland is a large compound sebaceous gland that in female mammals is modified to secrete milk.
Any process that modulates the frequency, rate or extent of mammary gland epithelial cell proliferation.
Any process that stops, prevents or reduces the rate or extent of mammary gland epithelial cell proliferation.
Any process that stops, prevents or reduces the rate or extent of mammary gland epithelial cell proliferation.
Any process that stops, prevents or reduces the rate or extent of mammary gland epithelial cell proliferation.
Any process that stops, prevents or reduces the rate or extent of mammary gland epithelial cell proliferation.
Any process that activates or increases the rate or extent of mammary gland epithelial cell proliferation.
Any process that activates or increases the rate or extent of mammary gland epithelial cell proliferation.
Any process that activates or increases the rate or extent of mammary gland epithelial cell proliferation.
Any process that activates or increases the rate or extent of mammary gland epithelial cell proliferation.
Any process that activates or increases the rate or extent of mammary gland epithelial cell proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of dopamine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of dopamine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of dopamine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of dopamine.
Any process that activates or increases the frequency, rate or extent of the regulated release of dopamine.
Any process that activates or increases the frequency, rate or extent of the regulated release of dopamine.
Any process that activates or increases the frequency, rate or extent of the regulated release of dopamine.
Any process that activates or increases the frequency, rate or extent of the regulated release of dopamine.
Any process that activates or increases the frequency, rate or extent of the regulated release of dopamine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a catecholamine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a catecholamine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a catecholamine.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a catecholamine.
Any process that activates or increases the frequency, rate or extent of the regulated release of a catecholamine.
Any process that activates or increases the frequency, rate or extent of the regulated release of a catecholamine.
Any process that activates or increases the frequency, rate or extent of the regulated release of a catecholamine.
Any process that activates or increases the frequency, rate or extent of the regulated release of a catecholamine.
Any process that activates or increases the frequency, rate or extent of the regulated release of a catecholamine.
The directed movement of a chemokine receptor within a lipid bilayer.
A heterodimeric protein complex formed of superoxide dismutase 1 and Bcl-2. Complex formation is thought to link superoxide dismutase to an apoptotic pathway.
Catalysis of the reaction: formyl-CoA + oxalate = formate + oxalyl-CoA.
Catalysis of the reaction: formyl-CoA + oxalate = formate + oxalyl-CoA.
Catalysis of the reaction: formyl-CoA + oxalate = formate + oxalyl-CoA.
The chemical reactions and pathways involving oxalate, the organic acid ethanedioate.
The chemical reactions and pathways involving oxalate, the organic acid ethanedioate.
The chemical reactions and pathways involving oxalate, the organic acid ethanedioate.
The chemical reactions and pathways involving oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the formation of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the formation of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the formation of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the formation of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the formation of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the formation of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the formation of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the breakdown of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the breakdown of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the breakdown of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the breakdown of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the breakdown of oxalate, the organic acid ethanedioate.
The chemical reactions and pathways resulting in the breakdown of oxalate, the organic acid ethanedioate.
Interacting selectively and non-covalently with a receptor that possesses protein serine/threonine kinase activity.
Interacting selectively and non-covalently with an activating transcription factor, any protein whose activity is required to initiate or upregulate transcription.
Interacting selectively and non-covalently with an activating transcription factor, any protein whose activity is required to initiate or upregulate transcription.
The aggregation, arrangement and bonding together of a proton-transporting ATP synthase in the chloroplast thylakoid membrane.
The aggregation, arrangement and bonding together of a proton-transporting ATP synthase in the mitochondrial inner membrane.
The aggregation, arrangement and bonding together of a proton-transporting ATP synthase in the plasma membrane.
The aggregation, arrangement and bonding together of a set of components to form respiratory chain complex IV (also known as cytochrome c oxidase) in the mitochondrial inner membrane.
The aggregation, arrangement and bonding together of a set of components to form respiratory chain complex IV (also known as cytochrome c oxidase) in the mitochondrial inner membrane.
The aggregation, arrangement and bonding together of a set of components to form respiratory chain complex IV (also known as cytochrome c oxidase) in the plasma membrane.
The aggregation, arrangement and bonding together of a set of components to form respiratory chain complex IV (also known as cytochrome c oxidase) in the plasma membrane.
The proteolytic cleavage of a transmembrane protein leading to the release of its intracellular or ecto-domains.
A ribonucleoprotein complex that forms during meiotic prophase in a fixed position in the horsetail nucleus; contains Mei2 and meiRNA. May play a role in the progression of meiosis I.
A ribonucleoprotein complex that forms during meiotic prophase in a fixed position in the horsetail nucleus; contains Mei2 and meiRNA. May play a role in the progression of meiosis I.
A ribonucleoprotein complex that forms during meiotic prophase in a fixed position in the horsetail nucleus; contains Mei2 and meiRNA. May play a role in the progression of meiosis I.
The chemical reactions and pathways resulting in the selective degradation of meiosis-specific transcripts during vegetative growth, by a mechanism that requires determinant of selective removal (DSR) sequences in the targeted mRNAs and involves a YTH family protein.
The chemical reactions and pathways resulting in the selective degradation of meiosis-specific transcripts during vegetative growth, by a mechanism that requires determinant of selective removal (DSR) sequences in the targeted mRNAs and involves a YTH family protein.
The chemical reactions and pathways resulting in the selective degradation of meiosis-specific transcripts during vegetative growth, by a mechanism that requires determinant of selective removal (DSR) sequences in the targeted mRNAs and involves a YTH family protein.
The chemical reactions and pathways resulting in the selective degradation of meiosis-specific transcripts during vegetative growth, by a mechanism that requires determinant of selective removal (DSR) sequences in the targeted mRNAs and involves a YTH family protein.
The chemical reactions and pathways resulting in the selective degradation of meiosis-specific transcripts during vegetative growth, by a mechanism that requires determinant of selective removal (DSR) sequences in the targeted mRNAs and involves a YTH family protein.
The aggregation, arrangement and bonding together of an integrin, a heterodimeric adhesion receptor formed by the non-covalent association of particular alpha and beta subunits, that lead to the increased affinity of the integrin for its extracellular ligands.
The aggregation, arrangement and bonding together of an integrin, a heterodimeric adhesion receptor formed by the non-covalent association of particular alpha and beta subunits, that lead to the increased affinity of the integrin for its extracellular ligands.
Any process that modulates the frequency, rate, or extent of integrin activation.
Any process that stops, prevents, or reduces the frequency, rate, or extent of integrin activation.
Any process that activates or increases the frequency, rate, or extent of integrin activation.
Any series of molecular signals initiated by the binding of an extracellular ligand to a receptor on the surface of the target cell that lead to the increased affinity of an integrin, a heterodimeric adhesion receptor formed by the non-covalent association of particular alpha and beta subunits, for its extracellular ligands.
Any series of molecular signals initiated by the binding of an extracellular ligand to a receptor on the surface of the target cell that lead to the increased affinity of an integrin, a heterodimeric adhesion receptor formed by the non-covalent association of particular alpha and beta subunits, for its extracellular ligands.
The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via an integrin, a heterodimeric adhesion receptor formed by the non-covalent association of particular alpha and beta subunits.
Any process that modulates the frequency, rate, or extent of cell adhesion mediated by integrin.
Any process that stops, prevents, or reduces the frequency, rate, or extent of cell adhesion mediated by integrin.
Any process that activates or increases the frequency, rate, or extent of cell adhesion mediated by integrin.
The attachment of one cell to another cell via an integrin, a heterodimeric adhesion receptor formed by the non-covalent association of particular alpha and beta subunits.
Any process that modulates the frequency, rate, or extent of cell-cell adhesion mediated by integrin.
Any process that stops, prevents, or reduces the frequency, rate, or extent of cell-cell adhesion mediated by integrin.
Any process that activates or increases the frequency, rate, or extent of cell-cell adhesion mediated by integrin.
Any process in which an organism modulates a change in the state or activity of a host cell or organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an abiotic (non-living) stimulus. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism modulates a change in state or activity of a host cell or organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a temperature stimulus. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism modulates a change in state or activity of a host cell or organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism modulates a change in state or activity of a host cell or organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism modulates a change in state or activity of a host cell or organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a water stimulus. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism modulates a change in state or activity of a host cell or organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism modulates a change in state or activity of a host cell or organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism modulates a change in state or activity of a host cell or organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gravitational stimulus. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any constituent part of a host cell. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Double layer of lipid molecules as it encloses host cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins. The host is defined as the larger of the organisms involved in a symbiotic interaction.
A collection of membranous structures involved in transport within the host cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any constituent part of the living contents of a host cell; the matter contained within (but not including) the plasma membrane, usually taken to exclude large vacuoles and masses of secretory or ingested material. In eukaryotes it includes the nucleus and cytoplasm. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Organized structure of distinctive morphology and function, occurring within the host cell. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma membrane. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Organized structure of distinctive morphology and function, as found in host cells, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. The host is defined as the larger of the organisms involved in a symbiotic interaction.
A semiautonomous, self replicating organelle as found in host cells that occurs in varying numbers, shapes, and sizes in the cell cytoplasm. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any member of a family of organelles as found in the cytoplasm of host cells, which are membrane-bounded and contain DNA. The host is defined as the larger of the organisms involved in a symbiotic interaction.
A chlorophyll-containing plastid as found within host cells with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any constituent part of a chloroplast as it is found in host cells and which are a chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any sac-like membranous structures (cisternae) in a chloroplast found in host cells, combined into stacks (grana) and present singly in the stroma (stroma thylakoids or frets) as interconnections between grana. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any constituent part of the host cell cytoplasm, all of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The process in which an organism effects a change in the structure or function of host cell chloroplasts. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The process in which an organism effects a change in the structure or function of a component of the host cell chloroplast. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The process in which an organism effects a change in the structure or function of the host cell chloroplast thylakoid. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The process in which an organism effects a change in the structure or function of host cell mitochondria. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the resistance gene-dependent defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the resistance gene-dependent defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the resistance gene-dependent defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the resistance gene-dependent defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the resistance gene-dependent defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the production of reactive oxygen species as part of the defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the production of reactive oxygen species as part of the defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the production of reactive oxygen species as part of the defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the production of reactive oxygen species as part of the defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the production of reactive oxygen species as part of the defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the production of reactive oxygen species as part of the defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the production of reactive oxygen species as part of the defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the production of reactive oxygen species as part of the defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the production of reactive oxygen species as part of the defense response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The alternation by a symbiont of the levels of defense-related proteins in its host. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which the symbiont stops or reduces of the levels of defense-related proteins in its host. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which the symbiont activates, maintains or increases levels of defense-related proteins in its host. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which the symbiont regulates the increase in its size or mass within the cells or tissues of the host organism. This may (but not necessarily) include a filamentous growth form, and also can include secretion of proteases and lipases to break down. The host is defined as the larger of the organisms involved in the symbiotic interaction.
Any process in which the symbiont regulates its progression from an initial condition to a later condition, within the cells or tissues of the host organism. This may (but not necessarily) include a filamentous growth form, and also can include secretion of proteases and lipases to break down. The host is defined as the larger of the organisms involved in the symbiotic interaction.
Any process in which the symbiont activates, maintains or increases its size or mass within the cells or tissues of the host organism. The host is defined as the larger of the organisms involved in the symbiotic interaction.
Any process in which the symbiont activates or maintains its progression from an initial condition to a later condition, within the cells or tissues of the host organism. The host is defined as the larger of the organisms involved in the symbiotic interaction.
Any process in which the symbiont stops, prevents or reduces its increase in size or mass within the cells or tissues of the host organism. The host is defined as the larger of the organisms involved in the symbiotic interaction.
Any process in which the symbiont stops, prevents or reduces its progression from an initial condition to a later condition, within the cells or tissues of the host organism. The host is defined as the larger of the organisms involved in the symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of programmed cell death in the host, where programmed cell death proceeds by apoptosis. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of programmed cell death in the host, where programmed cell death proceeds by apoptosis. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of programmed cell death in the host, where programmed cell death proceeds by apoptosis. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of programmed cell death in the host, where programmed cell death proceeds by apoptosis. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of programmed cell death in the host, where programmed cell death proceeds by apoptosis. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process that modulates the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that modulates the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that activates or increases the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that activates or increases the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that activates or increases the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that activates or increases the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that activates or increases the frequency, rate or extent of NAD kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to an NAD molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
Any process that activates or increases the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
Any process that activates or increases the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
Any process that activates or increases the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
Any process that activates or increases the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
Any process that activates or increases the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
A membrane-bounded vesicle found near the apical, or pericanalicular, membrane of a hepatocyte; contains proteins involved in bile salt transport and other fluid and solute transport processes.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction requires the presence of double-stranded DNA, and it drives another reaction.
Catalysis of the reaction: NTP + H2O = NDP + phosphate; this reaction drives the unwinding of a DNA/RNA duplex, i.e. a double helix in which a strand of DNA pairs with a complementary strand of RNA.
Catalysis of the unwinding of a DNA/RNA duplex in the direction 5' to 3'.
Catalysis of the unwinding of a DNA/RNA duplex in the direction 3' to 5'.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction drives the unwinding of a DNA/RNA duplex.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction drives the unwinding of a DNA/RNA duplex in the direction 3' to 5'.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction drives the unwinding of a DNA/RNA duplex in the direction 5' to 3'.
A process that results in the endonucleolytic cleavage of the damaged strand of DNA. The incision occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound.
A process that results in the endonucleolytic cleavage of the damaged strand of DNA. The incision occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound.
Any process that modulates the frequency, rate or extent of the regulated release of luteinizing hormone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of luteinizing hormone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of luteinizing hormone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of luteinizing hormone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of luteinizing hormone.
Any process that activates or increases the frequency, rate or extent of the regulated release of luteinizing hormone.
Any process that activates or increases the frequency, rate or extent of the regulated release of luteinizing hormone.
Any process that activates or increases the frequency, rate or extent of the regulated release of luteinizing hormone.
Any process that activates or increases the frequency, rate or extent of the regulated release of luteinizing hormone.
Any process that activates or increases the frequency, rate or extent of the regulated release of luteinizing hormone.
The multiplication or reproduction of osteoblasts, resulting in the expansion of an osteoblast cell population. An osteoblast is a bone-forming cell which secretes an extracellular matrix. Hydroxyapatite crystals are then deposited into the matrix to form bone.
Any process that modulates the frequency, rate or extent of osteoblast proliferation.
Any process that stops, prevents or reduces the rate or extent of osteoblast proliferation.
Any process that stops, prevents or reduces the rate or extent of osteoblast proliferation.
Any process that stops, prevents or reduces the rate or extent of osteoblast proliferation.
Any process that stops, prevents or reduces the rate or extent of osteoblast proliferation.
Any process that activates or increases the rate or extent of osteoblast proliferation.
Any process that activates or increases the rate or extent of osteoblast proliferation.
Any process that activates or increases the rate or extent of osteoblast proliferation.
Any process that activates or increases the rate or extent of osteoblast proliferation.
Any process that activates or increases the rate or extent of osteoblast proliferation.
Interacting selectively and non-covalently with sialic acid, any of a variety of N- or O- substituted derivatives of neuraminic acid, a nine carbon monosaccharide. Sialic acids often occur in polysaccharides, glycoproteins, and glycolipids in animals and bacteria.
The chemical reactions and pathways resulting in the formation of polysaccharides, polymers of many (typically more than 10) monosaccharide residues linked glycosidically, occurring at the level of an individual cell.
The chemical reactions and pathways resulting in the formation of polysaccharides, polymers of many (typically more than 10) monosaccharide residues linked glycosidically, occurring at the level of an individual cell.
The chemical reactions and pathways resulting in the formation of polysaccharides, polymers of many (typically more than 10) monosaccharide residues linked glycosidically, occurring at the level of an individual cell.
The chemical reactions and pathways resulting in the formation of polysaccharides, polymers of many (typically more than 10) monosaccharide residues linked glycosidically, occurring at the level of an individual cell.
The chemical reactions and pathways resulting in the formation of polysaccharides, polymers of many (typically more than 10) monosaccharide residues linked glycosidically, occurring at the level of an individual cell.
The chemical reactions and pathways resulting in the formation of polysaccharides, polymers of many (typically more than 10) monosaccharide residues linked glycosidically, occurring at the level of an individual cell.
The assembly of neurofilaments into bundles, in which the filaments are longitudinally oriented, with numerous crossbridges between them. Neurofilament bundles may be cross-linked to each other, to membrane-bounded organelles or other cytoskeletal structures such as microtubules.
Catalysis of an oxidation-reduction (redox) reaction in which a CH-NH group acts as a hydrogen or electron donor and reduces an iron-sulfur protein.
Catalysis of an oxidation-reduction (redox) reaction in which a CH2 group acts as a hydrogen or electron donor and reduces a quinone or similar acceptor molecule.
Any process that reduces the extent of heterochromatin formation; reduces the size of a chromosomal region converted to heterochromatin.
Any process that reduces the extent of heterochromatin formation; reduces the size of a chromosomal region converted to heterochromatin.
Any process that reduces the extent of heterochromatin formation; reduces the size of a chromosomal region converted to heterochromatin.
Any process that increases the extent of heterochromatin formation; increases the size of a chromosomal region converted to heterochromatin.
Any process that increases the extent of heterochromatin formation; increases the size of a chromosomal region converted to heterochromatin.
A histone deacetylase complex which deacetylates histones across gene coding regions. Composed of a catalytic histone deacetylase subunit, an Sds-3 family protein, a SIN3 family co-repressor, a WD repeat protein, and a zf- PHD finger (Clr6, Sds3, Pst1, Prw1, Png2 in Schizosaccharomyces pombe; Rpd3p, Sin3p, Ume1p, Pho23p, Sap30p, Sds3p, Cti6p, Rxt2p, Rxt3p, Dep1p, Ume6p and Ash1p in Saccharomyces cerevisiae).
A histone deacetylase complex which deacetylates histones across gene coding regions. Composed of a catalytic histone deacetylase subunit, an Sds-3 family protein, a SIN3 family co-repressor, a WD repeat protein, and a zf- PHD finger (Clr6, Sds3, Pst1, Prw1, Png2 in Schizosaccharomyces pombe; Rpd3p, Sin3p, Ume1p, Pho23p, Sap30p, Sds3p, Cti6p, Rxt2p, Rxt3p, Dep1p, Ume6p and Ash1p in Saccharomyces cerevisiae).
A histone deacetylase complex which deacetylates histones across gene coding regions. Composed of a catalytic histone deacetylase subunit, an Sds-3 family protein, a SIN3 family co-repressor, a WD repeat protein, and a zf- PHD finger (Clr6, Sds3, Pst1, Prw1, Png2 in Schizosaccharomyces pombe; Rpd3p, Sin3p, Ume1p, Pho23p, Sap30p, Sds3p, Cti6p, Rxt2p, Rxt3p, Dep1p, Ume6p and Ash1p in Saccharomyces cerevisiae).
A histone deacetylase complex which deacetylates histones across gene coding regions. Composed of a catalytic histone deacetylase subunit, an Sds-3 family protein, a SIN3 family co-repressor, a WD repeat protein, and a zf- PHD finger (Clr6, Sds3, Pst1, Prw1, Png2 in Schizosaccharomyces pombe; Rpd3p, Sin3p, Ume1p, Pho23p, Sap30p, Sds3p, Cti6p, Rxt2p, Rxt3p, Dep1p, Ume6p and Ash1p in Saccharomyces cerevisiae).
Catalysis of the reaction: 5'-AMP-DNA + H2O = AMP + DNA; nucleophilic release of a covalently linked adenylate residue from a DNA strand, leaving a 5' phosphate terminus.
Catalysis of the reaction: 5'-AMP-DNA + H2O = AMP + DNA; nucleophilic release of a covalently linked adenylate residue from a DNA strand, leaving a 5' phosphate terminus.
Catalysis of the reaction: 5'-AMP-DNA + H2O = AMP + DNA; nucleophilic release of a covalently linked adenylate residue from a DNA strand, leaving a 5' phosphate terminus.
Catalysis of the reaction: 5'-AMP-DNA + H2O = AMP + DNA; nucleophilic release of a covalently linked adenylate residue from a DNA strand, leaving a 5' phosphate terminus.
Catalysis of the reaction: 5'-AMP-DNA + H2O = AMP + DNA; nucleophilic release of a covalently linked adenylate residue from a DNA strand, leaving a 5' phosphate terminus.
The directed movement of a phospholipid out of a cell or organelle.
Catalysis of the reaction: dTDP-D-galactose + 2 NADP+ + H2O = dTDP-D-galacturonate + 2 NADPH + 2 H+.
Catalysis of the reaction: dTDP-D-galactose + 2 NADP+ + H2O = dTDP-D-galacturonate + 2 NADPH + 2 H+.
Catalysis of the reaction: dTDP-D-galactose + 2 NADP+ + H2O = dTDP-D-galacturonate + 2 NADPH + 2 H+.
Catalysis of the reaction: (1R,5S)-carveol + NAD(+) = (S)-carvone + H(+) + NADH.
Catalysis of the reaction: 3beta-hydroxy-5beta-pregnane-20-one + NADP(+) = 5beta-pregnan-3,20-dione + H(+) + NADPH.
Catalysis of the reaction: 3beta-hydroxy-5beta-pregnane-20-one + NADP(+) = 5beta-pregnan-3,20-dione + H(+) + NADPH.
Catalysis of the reaction: 3beta-hydroxy-5beta-pregnane-20-one + NADP(+) = 5beta-pregnan-3,20-dione + H(+) + NADPH.
Catalysis of the reaction: 3beta-hydroxy-5alpha-pregnane-20-one + NADP(+) = 5alpha-pregnane-3,20-dione + H(+) + NADPH.
Catalysis of the reaction: GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+.
Catalysis of the reaction: GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+.
Catalysis of the reaction: GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+.
Catalysis of the reaction: GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+.
Catalysis of the reaction: quinate + NADP+ = 3-dehydroquinate + NADPH + H+.
Catalysis of the reaction: quinate + NADP+ = 3-dehydroquinate + NADPH + H+.
Catalysis of the reaction: quinate + NADP+ = 3-dehydroquinate + NADPH + H+.
Catalysis of the reaction: shikimate + NAD+ = 3-dehydroshikimate + NADH + H+.
Catalysis of the reaction: shikimate + NAD+ = 3-dehydroshikimate + NADH + H+.
Catalysis of the reaction: shikimate + NAD+ = 3-dehydroshikimate + NADH + H+.
Catalysis of the reaction: shikimate + NAD+ = 3-dehydroshikimate + NADH + H+.
Catalysis of the reaction: shikimate + NAD+ = 3-dehydroshikimate + NADH + H+.
Catalysis of the reaction: shikimate + NAD+ = 3-dehydroshikimate + NADH + H+.
Catalysis of the reaction: shikimate + NAD+ = 3-dehydroshikimate + NADH + H+.
Catalysis of the reaction: 2'-deoxymugineic acid + NAD(P)+ = 3''-deamino-3''-oxonicotianamine + NAD(P)H + H+.
Catalysis of the reactions: isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH, and (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+.
Catalysis of the reactions: isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH, and (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+.
Catalysis of the reactions: isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH, and (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+.
Catalysis of the reaction: D-arabinitol + NADP+ = D-ribulose + NADPH + H+.
Catalysis of the reaction: D-arabinitol + NADP+ = D-ribulose + NADPH + H+.
Catalysis of the reaction: D-arabinitol + NADP+ = D-ribulose + NADPH + H+.
Catalysis of the reaction: D-arabinitol + NADP+ = D-ribulose + NADPH + H+.
Catalysis of the reaction: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + H(+) + NADH.
Catalysis of the reaction: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + H(+) + NADH.
Catalysis of the reaction: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + H(+) + NADH.
Catalysis of the reaction: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + H(+) + NADH.
Catalysis of the reaction: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + H(+) + NADH.
Catalysis of the reaction: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + H(+) + NADH.
Catalysis of the reaction: 1,5-anhydro-D-mannitol + NADP(+) = 1,5-anhydro-D-fructose + H(+) + NADPH.
Catalysis of the reaction: 1,5-anhydro-D-mannitol + NADP(+) = 1,5-anhydro-D-fructose + H(+) + NADPH.
Catalysis of the reaction: choline + O2 = betaine aldehyde + hydrogen peroxide.
Catalysis of the reaction: O(2) + secondary alcohol = H(2)O(2) + ketone.
Catalysis of the reaction: O(2) + secondary alcohol = H(2)O(2) + ketone.
Catalysis of the reaction: O(2) + secondary alcohol = H(2)O(2) + ketone.
Catalysis of the reactions: inosine + O2 = 9-riburonosylhypoxanthine + 2 H2O; (1a) 2 inosine + O2 = 2 5'-dehydroinosine + 2 H2O, and (1b) 2 5'-dehydroinosine + O2 = 2 9-riburonosylhypoxanthine + 2 H2O.
Catalysis of the reactions: adenosine + 2 O2 = 9-riburonosyladenine + 2 hydrogen peroxide; (1a) adenosine + O2 = 5'-dehydroadenosine + hydrogen peroxide, and (1b) 5'-dehydroadenosine + O2 = 9-riburonosyladenine + hydrogen peroxide.
Catalysis of the reaction: D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor.
Catalysis of the reaction: D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor.
Catalysis of the reaction: D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor.
Catalysis of the reaction: D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor.
Catalysis of the reaction: D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor.
Catalysis of the reaction: D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor.
Catalysis of the reaction: D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor.
Catalysis of the reaction: D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor.
Catalysis of the reactions: pyranose + acceptor = 2-dehydropyranose (or 3-dehydropyranose or 2,3-didehydropyranose) + reduced acceptor, and a pyranoside + acceptor = a 3-dehydropyranoside (or 3,4-didehydropyranoside) + reduced acceptor.
Catalysis of the reactions: pyranose + acceptor = 2-dehydropyranose (or 3-dehydropyranose or 2,3-didehydropyranose) + reduced acceptor, and a pyranoside + acceptor = a 3-dehydropyranoside (or 3,4-didehydropyranoside) + reduced acceptor.
Catalysis of the reactions: pyranose + acceptor = 2-dehydropyranose (or 3-dehydropyranose or 2,3-didehydropyranose) + reduced acceptor, and a pyranoside + acceptor = a 3-dehydropyranoside (or 3,4-didehydropyranoside) + reduced acceptor.
Catalysis of the reactions: pyranose + acceptor = 2-dehydropyranose (or 3-dehydropyranose or 2,3-didehydropyranose) + reduced acceptor, and a pyranoside + acceptor = a 3-dehydropyranoside (or 3,4-didehydropyranoside) + reduced acceptor.
Catalysis of the reactions: pyranose + acceptor = 2-dehydropyranose (or 3-dehydropyranose or 2,3-didehydropyranose) + reduced acceptor, and a pyranoside + acceptor = a 3-dehydropyranoside (or 3,4-didehydropyranoside) + reduced acceptor.
Catalysis of the reaction: a (2R)-hydroxy-carboxylate + acceptor = a 2-oxo-carboxylate + reduced acceptor.
Catalysis of the reaction: a (2R)-hydroxy-carboxylate + acceptor = a 2-oxo-carboxylate + reduced acceptor.
Catalysis of the reaction: a (2R)-hydroxy-carboxylate + acceptor = a 2-oxo-carboxylate + reduced acceptor.
Catalysis of the reaction: a (2R)-hydroxy-carboxylate + acceptor = a 2-oxo-carboxylate + reduced acceptor.
Catalysis of the reaction: (S)-2-hydroxy-2-phenylacetate + acceptor = 2-oxo-2-phenylacetate + reduced acceptor.
Catalysis of the reaction: (S)-2-hydroxy-2-phenylacetate + acceptor = 2-oxo-2-phenylacetate + reduced acceptor.
Catalysis of the reaction: (S)-2-hydroxy-2-phenylacetate + acceptor = 2-oxo-2-phenylacetate + reduced acceptor.
Catalysis of the reaction: an aldehyde + NADP+ + H2O = an acid + NADPH + H+.
Catalysis of the reaction: an aldehyde + NADP+ + H2O = an acid + NADPH + H+.
Catalysis of the reaction: an aldehyde + NADP+ + H2O = an acid + NADPH + H+.
Catalysis of the reaction: 3-oxopropanoate + NAD(P)+ + H2O = malonate + NAD(P)H + H+.
Catalysis of the reaction: 3-oxopropanoate + NAD(P)+ + H2O = malonate + NAD(P)H + H+.
Catalysis of the reaction: fluoroacetaldehyde + NAD+ + H2O = fluoroacetate + NADH + 2 H+.
Catalysis of the reaction: an aldehyde + H2O + 2 oxidized ferredoxin = an acid + 2 H+ + 2 reduced ferredoxin.
Catalysis of the reaction: an aldehyde + H2O + 2 oxidized ferredoxin = an acid + 2 H+ + 2 reduced ferredoxin.
Catalysis of the reaction: an aldehyde + H2O + 2 oxidized ferredoxin = an acid + 2 H+ + 2 reduced ferredoxin.
Catalysis of the reaction: an aldehyde + H2O + acceptor = a carboxylate + reduced acceptor.
Catalysis of the reaction: an aldehyde + H2O + acceptor = a carboxylate + reduced acceptor.
Catalysis of the reaction: an aldehyde + H2O + acceptor = a carboxylate + reduced acceptor.
Catalysis of the reaction: an aldehyde + H2O + acceptor = a carboxylate + reduced acceptor.
Catalysis of the reaction: chlorophyllide a + NADP+ = divinyl chlorophyllide a + NADPH + H+.
Catalysis of the reaction: chlorophyllide a + NADP+ = divinyl chlorophyllide a + NADPH + H+.
Catalysis of the reaction: chlorophyllide a + NADP+ = divinyl chlorophyllide a + NADPH + H+.
Catalysis of the reaction: a flavan-3-ol + 2 NAD(P)+ = an anthocyanidin + 2 NAD(P)H + H+.
Catalysis of the reaction: a flavan-3-ol + 2 NAD(P)+ = an anthocyanidin + 2 NAD(P)H + H+.
Catalysis of the reaction: a flavan-3-ol + 2 NAD(P)+ = an anthocyanidin + 2 NAD(P)H + H+.
Catalysis of the reaction: a flavan-3-ol + 2 NAD(P)+ = an anthocyanidin + 2 NAD(P)H + H+.
Catalysis of the reaction: L-arogenate + NADP+ = L-tyrosine + NADPH + CO2.
Catalysis of the reaction: L-arogenate + NADP+ = L-tyrosine + NADPH + CO2.
Catalysis of the reaction: L-arogenate + NADP+ = L-tyrosine + NADPH + CO2.
Catalysis of the reaction: L-arogenate + NADP+ = L-tyrosine + NADPH + CO2.
Catalysis of the reaction: L-arogenate + NADP+ = L-tyrosine + NADPH + CO2.
Catalysis of the reaction: L-arogenate + NADP+ = L-tyrosine + NADPH + CO2.
Catalysis of the reaction: L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + CO2.
Catalysis of the reaction: L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + CO2.
Catalysis of the reaction: L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + CO2.
Catalysis of the reaction: 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O(2) = 2 H(2)O + 2 H(2)O(2) + H(+) + pyrroloquinoline quinone.
Catalysis of the reaction: 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O(2) = 2 H(2)O + 2 H(2)O(2) + H(+) + pyrroloquinoline quinone.
Catalysis of the reaction: (R)-2-benzylsuccinyl-CoA + 2 electron-transferring flavoprotein = (E)-2-benzylidenesuccinyl-CoA + 2 reduced electron-transferring flavoprotein.
Catalysis of the reaction: (R)-2-benzylsuccinyl-CoA + 2 electron-transferring flavoprotein = (E)-2-benzylidenesuccinyl-CoA + 2 reduced electron-transferring flavoprotein.
Catalysis of the reaction: (R)-2-benzylsuccinyl-CoA + 2 electron-transferring flavoprotein = (E)-2-benzylidenesuccinyl-CoA + 2 reduced electron-transferring flavoprotein.
Catalysis of the reaction: L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+.
Catalysis of the reaction: L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+.
Catalysis of the reaction: L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+.
Catalysis of the reaction: L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+.
Catalysis of the reaction: L-lysine + H(2)O + O(2) = allysine + H(2)O(2) + NH(4)(+).
Catalysis of the reaction: L-lysine + H(2)O + O(2) = allysine + H(2)O(2) + NH(4)(+).
Catalysis of the reaction: L-lysine + H(2)O + O(2) = allysine + H(2)O(2) + NH(4)(+).
Catalysis of the reaction: L-lysine + H(2)O + O(2) = allysine + H(2)O(2) + NH(4)(+).
Catalysis of the reaction: L-lysine + H(2)O + O(2) = allysine + H(2)O(2) + NH(4)(+).
Catalysis of the reaction: 1-pyrroline + NAD+ + 2 H2O = 4-aminobutanoate + NADH + 2 H+.
Catalysis of the reaction: 1-pyrroline + NAD+ + 2 H2O = 4-aminobutanoate + NADH + 2 H+.
Catalysis of the reaction: 1-pyrroline + NAD+ + 2 H2O = 4-aminobutanoate + NADH + 2 H+.
Catalysis of the reaction: 1-pyrroline + NAD+ + 2 H2O = 4-aminobutanoate + NADH + 2 H+.
Catalysis of the reaction: 7-aminomethyl-7-deazaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH.
Catalysis of the reaction: 7-aminomethyl-7-deazaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH.
Catalysis of the reaction: 7-aminomethyl-7-deazaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH.
Catalysis of the reaction: 7-aminomethyl-7-deazaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH.
Catalysis of the reaction: 7-aminomethyl-7-deazaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH.
Catalysis of the reaction: 7-aminomethyl-7-deazaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH.
Catalysis of the reaction: 7-aminomethyl-7-deazaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH.
Catalysis of the reaction: 7-aminomethyl-7-deazaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH.
Catalysis of the reactions: hydroxylamine + NH3 = hydrazine + H2O, and hydrazine + acceptor = N2 + reduced acceptor.
Catalysis of the reaction: AMP + glutathione disulfide + H(+) + sulfite = 5'-adenylyl sulfate + 2 glutathione.
Catalysis of the reaction: AMP + glutathione disulfide + H(+) + sulfite = 5'-adenylyl sulfate + 2 glutathione.
Catalysis of the reaction: AMP + glutathione disulfide + H(+) + sulfite = 5'-adenylyl sulfate + 2 glutathione.
Catalysis of the reaction: AMP + glutathione disulfide + H(+) + sulfite = 5'-adenylyl sulfate + 2 glutathione.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (R)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (R)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (R)-S-oxide + thioredoxin.
Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (R)-S-oxide + thioredoxin.
Catalysis of the removal of a methyl group from arginine at position 2 of the histone H3 protein.
Catalysis of the reaction: reactive black 5 + hydrogen peroxide = oxidized reactive black 5 + 2 H2O.
Catalysis of the reaction: H2 + A = AH2.
Catalysis of the reaction: H2 + A = AH2.
Catalysis of the reaction: H2 + A = AH2.
Catalysis of the reaction: H2 + A = AH2.
Catalysis of the reaction: H2 + A = AH2.
Catalysis of the reaction: H2 + A = AH2.
Catalysis of the removal of a methyl group from arginine at position 3 of the histone H4 protein.
A process in which a ribosome is transported to, and/or maintained in, a specific location.
A process in which a ribosome is transported to, and/or maintained in, a specific location.
A process in which a ribosome is transported to, and/or maintained in, a specific location.
A process in which a ribosome is transported to, and/or maintained in, a specific location.
Catalysis of the reaction: linoleate + O2 = (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate.
Catalysis of the reaction: linoleate + O2 = (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate.
Catalysis of the reaction: linoleate + O2 = (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate.
Catalysis of the reaction: pentane-2,4-dione + O2 = acetate + 2-oxopropanal.
Catalysis of the reaction: pentane-2,4-dione + O2 = acetate + 2-oxopropanal.
Catalysis of the reaction: pentane-2,4-dione + O2 = acetate + 2-oxopropanal.
Catalysis of the reaction: pentane-2,4-dione + O2 = acetate + 2-oxopropanal.
Catalysis of the reaction: pentane-2,4-dione + O2 = acetate + 2-oxopropanal.
Catalysis of the reaction: pentane-2,4-dione + O2 = acetate + 2-oxopropanal.
Catalysis of the reaction: tryptophan + O2 = N-formylkynurenine. The product of the reaction depends on the substrate; D-tryptophan produces N-formyl-D-kynurenine, and L-tryptophan produces N-formyl-L-kynurenine.
Catalysis of the reaction: tryptophan + O2 = N-formylkynurenine. The product of the reaction depends on the substrate; D-tryptophan produces N-formyl-D-kynurenine, and L-tryptophan produces N-formyl-L-kynurenine.
Catalysis of the reaction: tryptophan + O2 = N-formylkynurenine. The product of the reaction depends on the substrate; D-tryptophan produces N-formyl-D-kynurenine, and L-tryptophan produces N-formyl-L-kynurenine.
Catalysis of the reaction: 4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 bisulfite + 2 H+.
Catalysis of the reaction: 4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 bisulfite + 2 H+.
Catalysis of the reaction: 4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 bisulfite + 2 H+.
Catalysis of the reaction: 4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 bisulfite + 2 H+.
Catalysis of the reaction: Oplophorus luciferin + O2 = oxidized Oplophorus luciferin + CO2 + hnu.
Catalysis of the reaction: Oplophorus luciferin + O2 = oxidized Oplophorus luciferin + CO2 + hnu.
Catalysis of the reaction: sucrose + acceptor = 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced acceptor.
Catalysis of the reaction: sucrose + acceptor = 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced acceptor.
Catalysis of the reaction: sucrose + acceptor = 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced acceptor.
Catalysis of the reaction: sucrose + acceptor = 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced acceptor.
Catalysis of the reaction: sucrose + acceptor = 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced acceptor.
Catalysis of the reactions: deoxyamidinoproclavaminate + 2-oxoglutarate + O2 = amidinoproclavaminate + succinate + CO2 + H2O; proclavaminate + 2-oxoglutarate + O2 = dihydroclavaminate + succinate + CO2 + 2 H2O; and dihydroclavaminate + 2-oxoglutarate + O2 = clavaminate + succinate + CO2 + 2 H2O.
Catalysis of the reactions: deoxyamidinoproclavaminate + 2-oxoglutarate + O2 = amidinoproclavaminate + succinate + CO2 + H2O; proclavaminate + 2-oxoglutarate + O2 = dihydroclavaminate + succinate + CO2 + 2 H2O; and dihydroclavaminate + 2-oxoglutarate + O2 = clavaminate + succinate + CO2 + 2 H2O.
Catalysis of the reactions: deoxyamidinoproclavaminate + 2-oxoglutarate + O2 = amidinoproclavaminate + succinate + CO2 + H2O; proclavaminate + 2-oxoglutarate + O2 = dihydroclavaminate + succinate + CO2 + 2 H2O; and dihydroclavaminate + 2-oxoglutarate + O2 = clavaminate + succinate + CO2 + 2 H2O.
Catalysis of the reaction: a flavanone + 2-oxoglutarate + O2 = a flavone + succinate + CO2 + H2O.
Catalysis of the reaction: a flavanone + 2-oxoglutarate + O2 = a flavone + succinate + CO2 + H2O.
Catalysis of the reaction: a flavanone + 2-oxoglutarate + O2 = a flavone + succinate + CO2 + H2O.
Catalysis of the reaction: 2'-deoxymugineate + 2-oxoglutarate + O(2) = CO(2) + H(+) + mugineate + succinate.
Catalysis of the reaction: 2'-deoxymugineate + 2-oxoglutarate + O(2) = CO(2) + H(+) + mugineate + succinate.
Catalysis of the reactions: mugineic acid + 2-oxoglutarate + O2 = 3-epihydroxymugineic acid + succinate + CO2.
Catalysis of the reactions: mugineic acid + 2-oxoglutarate + O2 = 3-epihydroxymugineic acid + succinate + CO2.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a glucagon stimulus.
Catalysis of the reaction: L-proline + 2-oxoglutarate + O2 = cis-3-hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: L-proline + 2-oxoglutarate + O2 = cis-3-hydroxy-L-proline + succinate + CO2.
Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP, and in which one substrate is a sterol derivative.
Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor, and in which one substrate is a sterol derivative.
Catalysis of the reaction: H(+) + NADH + O(2) + quinolin-2-ol = H(2)O + NAD(+) + quinoline-2,8-diol.
Catalysis of the reaction: H(+) + NADH + O(2) + quinolin-2-ol = H(2)O + NAD(+) + quinoline-2,8-diol.
Catalysis of the reaction: 4'-hydroxyacetophenone + H(+) + NADPH + O(2) = 4-hydroxyphenyl acetate + H(2)O + NADP(+).
Catalysis of the reaction: 4'-hydroxyacetophenone + H(+) + NADPH + O(2) = 4-hydroxyphenyl acetate + H(2)O + NADP(+).
A nuclear ubiquitin ligase complex that specifically targets SUMOylated proteins; the complex is formed of homodimers or heterodimers of RNF4 family ubiquitin ligases and is conserved in eukaryotes.
Catalysis of the reactions: 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADPH + H+ + O2 = glyceollin + NADP+ + 2 H2O, and 4-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADPH + H+ + O2 = glyceollin + NADP+ + 2 H2O.
Catalysis of the reactions: 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADPH + H+ + O2 = glyceollin + NADP+ + 2 H2O, and 4-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADPH + H+ + O2 = glyceollin + NADP+ + 2 H2O.
Catalysis of the reaction: apigenin + 2 NADPH + 2 H+ + O2 = 2-hydroxy-2,3-dihydrogenistein + 2 NADP+ + H2O.
Catalysis of the reaction: apigenin + 2 NADPH + 2 H+ + O2 = 2-hydroxy-2,3-dihydrogenistein + 2 NADP+ + H2O.
Catalysis of the reaction: H(+) + liquiritigenin + NADPH + O(2) = H(2)O + licodione + NADP(+).
Catalysis of the reaction: H(+) + liquiritigenin + NADPH + O(2) = H(2)O + licodione + NADP(+).
Catalysis of the reactions: a flavanone + NADPH + H+ + O2 = a 3'-hydroxyflavanone + NADP+ + H2O, and a 3'-hydroxyflavanone + NADPH + H+ + O2 = a 3',5'-dihydroxyflavanone + NADP+ + H2O.
Catalysis of the reactions: a flavanone + NADPH + H+ + O2 = a 3'-hydroxyflavanone + NADP+ + H2O, and a 3'-hydroxyflavanone + NADPH + H+ + O2 = a 3',5'-dihydroxyflavanone + NADP+ + H2O.
Catalysis of the reactions: a flavanone + NADPH + H+ + O2 = a 3'-hydroxyflavanone + NADP+ + H2O, and a 3'-hydroxyflavanone + NADPH + H+ + O2 = a 3',5'-dihydroxyflavanone + NADP+ + H2O.
Catalysis of the reaction: an isoflavone + NADPH + H+ + O2 = a 2'-hydroxyisoflavone + NADP+ + H2O.
Catalysis of the reaction: an isoflavone + NADPH + H+ + O2 = a 2'-hydroxyisoflavone + NADP+ + H2O.
Catalysis of the reaction: an isoflavone + NADPH + H+ + O2 = a 2'-hydroxyisoflavone + NADP+ + H2O.
Catalysis of the reaction: an isoflavone + NADPH + H+ + O2 = a 2'-hydroxyisoflavone + NADP+ + H2O.
A region in the lower half of some cells formed from extensive infoldings of the basal plasma membrane; includes cytoplasm adjacent to the infolded membrane.
Catalysis of the reaction: 10-deoxysarpagine + H(+) + NADPH + O(2) = H(2)O + NADP(+) + sarpagine.
Catalysis of the reaction: 10-deoxysarpagine + H(+) + NADPH + O(2) = H(2)O + NADP(+) + sarpagine.
Catalysis of the reaction: H(+) + NADPH + O(2) + phenylacetone = benzyl acetate + H(2)O + NADP(+).
Catalysis of the reaction: H(+) + NADPH + O(2) + phenylacetone = benzyl acetate + H(2)O + NADP(+).
Catalysis of the reaction: H(+) + lithocholate + NADPH + O(2) = 6-beta-hydroxylithocholate + H(2)O + NADP(+).
Catalysis of the reaction: H(+) + lithocholate + NADPH + O(2) = 6-beta-hydroxylithocholate + H(2)O + NADP(+).
Catalysis of the reaction: H(+) + lithocholate + NADPH + O(2) = 6-beta-hydroxylithocholate + H(2)O + NADP(+).
Catalysis of the reaction: H(+) + lithocholate + NADPH + O(2) = 6-beta-hydroxylithocholate + H(2)O + NADP(+).
Catalysis of the reaction: H(+) + lithocholate + NADPH + O(2) = 6-beta-hydroxylithocholate + H(2)O + NADP(+).
Catalysis of the reaction: 7alpha-hydroxycholest-4-en-3-one + H(+) + NADPH + O(2) = 7alpha,12alpha-dihydroxycholest-4-en-3-one + H(2)O + NADP(+).
Catalysis of the reaction: 7alpha-hydroxycholest-4-en-3-one + H(+) + NADPH + O(2) = 7alpha,12alpha-dihydroxycholest-4-en-3-one + H(2)O + NADP(+).
Catalysis of the reaction: 7alpha-hydroxycholest-4-en-3-one + H(+) + NADPH + O(2) = 7alpha,12alpha-dihydroxycholest-4-en-3-one + H(2)O + NADP(+).
Catalysis of the reaction: 7alpha-hydroxycholest-4-en-3-one + H(+) + NADPH + O(2) = 7alpha,12alpha-dihydroxycholest-4-en-3-one + H(2)O + NADP(+).
Catalysis of the reaction: 7alpha-hydroxycholest-4-en-3-one + H(+) + NADPH + O(2) = 7alpha,12alpha-dihydroxycholest-4-en-3-one + H(2)O + NADP(+).
Catalysis of the reaction: 5beta-cholestane-3alpha,7alpha-diol + H(+) + NADPH + O(2) = 5beta-cholestane-3alpha,7alpha,12alpha-triol + H(2)O + NADP(+).
Catalysis of the reaction: 5beta-cholestane-3alpha,7alpha-diol + H(+) + NADPH + O(2) = 5beta-cholestane-3alpha,7alpha,12alpha-triol + H(2)O + NADP(+).
Catalysis of the reaction: 5beta-cholestane-3alpha,7alpha-diol + H(+) + NADPH + O(2) = 5beta-cholestane-3alpha,7alpha,12alpha-triol + H(2)O + NADP(+).
Catalysis of the reaction: 5beta-cholestane-3alpha,7alpha-diol + H(+) + NADPH + O(2) = 5beta-cholestane-3alpha,7alpha,12alpha-triol + H(2)O + NADP(+).
Catalysis of the reaction: 5beta-cholestane-3alpha,7alpha-diol + H(+) + NADPH + O(2) = 5beta-cholestane-3alpha,7alpha,12alpha-triol + H(2)O + NADP(+).
Catalysis of the reactions: taurochenodeoxycholate + NADPH + H+ + O2 = taurohyocholate + NADP+ + H2O, and lithocholate + NADPH + H+ + O2 = hyodeoxycholate + NADP+ + H2O.
Catalysis of the reactions: taurochenodeoxycholate + NADPH + H+ + O2 = taurohyocholate + NADP+ + H2O, and lithocholate + NADPH + H+ + O2 = hyodeoxycholate + NADP+ + H2O.
Catalysis of the reactions: taurochenodeoxycholate + NADPH + H+ + O2 = taurohyocholate + NADP+ + H2O, and lithocholate + NADPH + H+ + O2 = hyodeoxycholate + NADP+ + H2O.
Catalysis of the reactions: taurochenodeoxycholate + NADPH + H+ + O2 = taurohyocholate + NADP+ + H2O, and lithocholate + NADPH + H+ + O2 = hyodeoxycholate + NADP+ + H2O.
Catalysis of the reaction: cholesterol + H(+) + NADPH + O(2) = (24S)-24-hydroxycholesterol + H(2)O + NADP(+).
Catalysis of the reaction: cholesterol + H(+) + NADPH + O(2) = (24S)-24-hydroxycholesterol + H(2)O + NADP(+).
Catalysis of the reaction: cholesterol + H(+) + NADPH + O(2) = (24S)-24-hydroxycholesterol + H(2)O + NADP(+).
Catalysis of the reaction: cholesterol + H(+) + NADPH + O(2) = (24S)-24-hydroxycholesterol + H(2)O + NADP(+).
Catalysis of the reaction: cholesterol + H(+) + NADPH + O(2) = (24S)-24-hydroxycholesterol + H(2)O + NADP(+).
Catalysis of the reaction: cholesterol + H(+) + NADPH + O(2) = (24S)-24-hydroxycholesterol + H(2)O + NADP(+).
Catalysis of the reaction: (24R)-cholest-5-ene-3beta,24-diol + H(+) + NADPH + O(2) = (24R)-7alpha,24-dihydroxycholesterol + H(2)O + NADP(+).
Catalysis of the reaction: (24R)-cholest-5-ene-3beta,24-diol + H(+) + NADPH + O(2) = (24R)-7alpha,24-dihydroxycholesterol + H(2)O + NADP(+).
Catalysis of the reaction: (24R)-cholest-5-ene-3beta,24-diol + H(+) + NADPH + O(2) = (24R)-7alpha,24-dihydroxycholesterol + H(2)O + NADP(+).
Catalysis of the reaction: (24R)-cholest-5-ene-3beta,24-diol + H(+) + NADPH + O(2) = (24R)-7alpha,24-dihydroxycholesterol + H(2)O + NADP(+).
Catalysis of the reactions: cholest-5-ene-3beta,25-diol + NADPH + H+ + O2 = cholest-5-ene-3beta,7alpha,25-triol + NADP+ + H2O, and cholest-5-ene-3beta,27-diol + NADPH + H+ + O2 = cholest-5-ene-3beta,7alpha,27-triol + NADP+ + H2O.
Catalysis of the reactions: cholest-5-ene-3beta,25-diol + NADPH + H+ + O2 = cholest-5-ene-3beta,7alpha,25-triol + NADP+ + H2O, and cholest-5-ene-3beta,27-diol + NADPH + H+ + O2 = cholest-5-ene-3beta,7alpha,27-triol + NADP+ + H2O.
Catalysis of the reactions: cholest-5-ene-3beta,25-diol + NADPH + H+ + O2 = cholest-5-ene-3beta,7alpha,25-triol + NADP+ + H2O, and cholest-5-ene-3beta,27-diol + NADPH + H+ + O2 = cholest-5-ene-3beta,7alpha,27-triol + NADP+ + H2O.
Catalysis of the reactions: cholest-5-ene-3beta,25-diol + NADPH + H+ + O2 = cholest-5-ene-3beta,7alpha,25-triol + NADP+ + H2O, and cholest-5-ene-3beta,27-diol + NADPH + H+ + O2 = cholest-5-ene-3beta,7alpha,27-triol + NADP+ + H2O.
Catalysis of the reaction: H(+) + NADPH + O(2) + senecionine = H(2)O + NADP(+) + senecionine N-oxide.
Catalysis of the reaction: H(+) + NADPH + O(2) + senecionine = H(2)O + NADP(+) + senecionine N-oxide.
Catalysis of the reaction: H(+) + NADPH + O(2) + senecionine = H(2)O + NADP(+) + senecionine N-oxide.
Catalysis of the reaction: cob(I)alamin + hydrogen cyanide + NADP(+) = cyanocob(III)alamin + H(+) + NADPH.
Catalysis of the reaction: cob(I)alamin + hydrogen cyanide + NADP(+) = cyanocob(III)alamin + H(+) + NADPH.
Catalysis of the reaction: cob(I)alamin + hydrogen cyanide + NADP(+) = cyanocob(III)alamin + H(+) + NADPH.
Catalysis of the reaction: cob(I)alamin + hydrogen cyanide + NADP(+) = cyanocob(III)alamin + H(+) + NADPH.
Catalysis of the reaction: cob(I)alamin + hydrogen cyanide + NADP(+) = cyanocob(III)alamin + H(+) + NADPH.
Catalysis of the reaction: cob(I)alamin + hydrogen cyanide + NADP(+) = cyanocob(III)alamin + H(+) + NADPH.
Catalysis of the reaction: (2R,3S)-catechin + NADP+ + H2O = 2,3-trans-3,4-cis-leucocyanidin + NADPH + H+.
Catalysis of the reaction: (2R,3S)-catechin + NADP+ + H2O = 2,3-trans-3,4-cis-leucocyanidin + NADPH + H+.
Catalysis of the reaction: 2 1,4-benzoquinone + H(2)O + phenylacetyl-CoA = 2 hydroquinone + phenylglyoxylyl-CoA.
Catalysis of the reaction: 2 1,4-benzoquinone + H(2)O + phenylacetyl-CoA = 2 hydroquinone + phenylglyoxylyl-CoA.
Catalysis of the reaction: 5-hydroxymethylfurfural + NAD(P)H + H+ = 2,5-bis-hydroxymethylfuran + NAD(P)+.
Catalysis of the reaction: (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor.
Catalysis of the reaction: (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor.
Catalysis of the reaction: (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor.
Catalysis of the reaction: (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor.
Catalysis of the reaction: (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor.
Catalysis of the reaction: (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor.
Catalysis of the reactions: deoxycholate + FAD + H2O = cholate + FADH2, and lithocholate + FAD + H2O = chenodeoxycholate + FADH2.
Catalysis of the reactions: deoxycholate + FAD + H2O = cholate + FADH2, and lithocholate + FAD + H2O = chenodeoxycholate + FADH2.
Catalysis of the reactions: deoxycholate + FAD + H2O = cholate + FADH2, and lithocholate + FAD + H2O = chenodeoxycholate + FADH2.
Catalysis of the reactions: deoxycholate + FAD + H2O = cholate + FADH2, and lithocholate + FAD + H2O = chenodeoxycholate + FADH2.
Catalysis of the reactions: deoxycholate + FAD + H2O = cholate + FADH2, and lithocholate + FAD + H2O = chenodeoxycholate + FADH2.
Catalysis of the reactions: 2',4,4',6'-tetrahydroxychalcone + O2 = aureusidin + H2O, and 2',3,4,4',6'-pentahydroxychalcone + 1/2 O2 = aureusidin + H2O.
Catalysis of the reaction: acetyl phosphate + methylamine + thioredoxin disulfide = N-methylglycine + phosphate + thioredoxin.
Catalysis of the reaction: acetyl phosphate + trimethylamine + thioredoxin disulfide = N,N,N-trimethylglycine + phosphate + thioredoxin.
Catalysis of the reduction of elemental sulfur or polysulfide to hydrogen sulfide.
Catalysis of the reduction of elemental sulfur or polysulfide to hydrogen sulfide.
Catalysis of the reaction: 2 e(-) + 2 H(+) + selenate = H(2)O + selenite.
Catalysis of the reaction: 3,3',5'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2.
Catalysis of the reaction: 3,3',5'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2.
Catalysis of the reaction: 3,3',5'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2.
Catalysis of the reaction: 3,3',5'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2.
Catalysis of the reaction: 3,3',5'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2.
Catalysis of the reaction: 3,3',5'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2.
Catalysis of the reaction: S-adenosyl-L-methionine + myricetin = S-adenosyl-L-homocysteine + laricitrin.
Catalysis of the reaction: S-adenosyl-L-methionine + myricetin = S-adenosyl-L-homocysteine + laricitrin.
Catalysis of the reaction: S-adenosyl-L-methionine + myricetin = S-adenosyl-L-homocysteine + laricitrin.
Catalysis of the reaction: S-adenosyl-L-methionine + a 7-hydroxyisoflavone = S-adenosyl-L-homocysteine + a 7-methoxyisoflavone.
Catalysis of the reaction: S-adenosyl-L-methionine + vitexin 2''-O-beta-L-rhamnoside = S-adenosyl-L-homocysteine + 7-O-methylvitexin 2''-O-beta-L-rhamnoside.
Catalysis of the reaction: S-adenosyl-L-methionine + isoliquiritigenin = 2'-O-methylisoliquiritigenin + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + isoliquiritigenin = 2'-O-methylisoliquiritigenin + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + isoliquiritigenin = 2'-O-methylisoliquiritigenin + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + kaempferol = S-adenosyl-L-homocysteine + H(+) + kaempferide.
Catalysis of the reaction: S-adenosyl-L-methionine + kaempferol = S-adenosyl-L-homocysteine + H(+) + kaempferide.
Catalysis of the reaction: S-adenosyl-L-methionine + kaempferol = S-adenosyl-L-homocysteine + H(+) + kaempferide.
Catalysis of the reaction: S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine.
Catalysis of the reaction: S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine.
Catalysis of the reaction: S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine.
Catalysis of the reaction: S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine.
Catalysis of the reaction: L-threonine + fluoroacetaldehyde = acetaldehyde + 4-fluoro-L-threonine.
Catalysis of the reaction: stearoyl-CoA + malonyl-CoA + 2 NAD(P)H + 2 H+ = icosanoyl-CoA + CO2 + 2 NAD(P)+.
Catalysis of the reaction: stearoyl-CoA + malonyl-CoA + 2 NAD(P)H + 2 H+ = icosanoyl-CoA + CO2 + 2 NAD(P)+.
Catalysis of the reaction: stearoyl-CoA + malonyl-CoA + 2 NAD(P)H + 2 H+ = icosanoyl-CoA + CO2 + 2 NAD(P)+.
Catalysis of the reaction: stearoyl-CoA + malonyl-CoA + 2 NAD(P)H + 2 H+ = icosanoyl-CoA + CO2 + 2 NAD(P)+.
Catalysis of the reaction: 3 malonyl-CoA + 4-coumaroyl-CoA + NADPH + H+ = 4 CoA + isoliquiritigenin + 3 CO2 + NADP+ + H2O.
Catalysis of the reaction: malonyl-CoA + an anthocyanidin 3-O-beta-D-glucoside = CoA + an anthocyanidin 3-O-(6-O-malonyl-beta-D-glucoside).
Catalysis of the reaction: malonyl-CoA + an anthocyanidin 3-O-beta-D-glucoside = CoA + an anthocyanidin 3-O-(6-O-malonyl-beta-D-glucoside).
Catalysis of the reaction: malonyl-CoA + an anthocyanidin 3-O-beta-D-glucoside = CoA + an anthocyanidin 3-O-(6-O-malonyl-beta-D-glucoside).
Catalysis of the reaction: malonyl-CoA + an anthocyanidin 3-O-beta-D-glucoside = CoA + an anthocyanidin 3-O-(6-O-malonyl-beta-D-glucoside).
Catalysis of the reaction: malonyl-CoA + pelargonidin 3-O-(6-caffeoyl-beta-D-glucoside) 5-O-beta-D-glucoside = CoA + 4'''-demalonylsalvianin.
Catalysis of the reaction: malonyl-CoA + pelargonidin 3-O-(6-caffeoyl-beta-D-glucoside) 5-O-beta-D-glucoside = CoA + 4'''-demalonylsalvianin.
Catalysis of the reaction: 4-coumaroyl-CoA + a flavonol 3-O-[beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside] = CoA + a flavonol 3-O-[6-(4-coumaroyl)-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside].
Catalysis of the reaction: succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA.
Catalysis of the reaction: acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA.
Catalysis of the reaction: acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA.
Catalysis of the reaction: acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA.
Catalysis of the reaction: acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA.
Catalysis of the reaction: acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA.
Catalysis of the reaction: acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA.
Catalysis of the reaction: acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA.
Catalysis of the reaction: acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA.
Catalysis of the reaction: acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA.
Catalysis of the reaction: acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA.
Catalysis of the reaction: 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA.
Catalysis of the reaction: 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA.
Catalysis of the reaction: 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA.
Catalysis of the reaction: 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA.
Catalysis of the reaction: 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA.
Catalysis of the reaction: 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA.
Catalysis of the reaction: 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA.
Catalysis of the reaction: 3 malonyl-CoA + benzoyl-CoA = 4 CoA + 3,5-dihydroxybiphenyl + 4 CO2.
Catalysis of the reaction: 3 malonyl-CoA + benzoyl-CoA = 4 CoA + 3,5-dihydroxybiphenyl + 4 CO2.
Catalysis of the reaction: L-2,4-diaminobutyrate + acetyl-CoA = N(4)-acetyl-L-2,4-diaminobutyrate + CoA + H(+).
Catalysis of the reaction: L-2,4-diaminobutyrate + acetyl-CoA = N(4)-acetyl-L-2,4-diaminobutyrate + CoA + H(+).
Catalysis of the reaction: L-2,4-diaminobutyrate + acetyl-CoA = N(4)-acetyl-L-2,4-diaminobutyrate + CoA + H(+).
Catalysis of the reaction: L-2,4-diaminobutyrate + acetyl-CoA = N(4)-acetyl-L-2,4-diaminobutyrate + CoA + H(+).
Catalysis of the reaction: L-2,4-diaminobutyrate + acetyl-CoA = N(4)-acetyl-L-2,4-diaminobutyrate + CoA + H(+).
Catalysis of the reaction: L-2,4-diaminobutyrate + acetyl-CoA = N(4)-acetyl-L-2,4-diaminobutyrate + CoA + H(+).
Catalysis of the reaction: L-2,4-diaminobutyrate + acetyl-CoA = N(4)-acetyl-L-2,4-diaminobutyrate + CoA + H(+).
Catalysis of the reaction: L-2,4-diaminobutyrate + acetyl-CoA = N(4)-acetyl-L-2,4-diaminobutyrate + CoA + H(+).
Catalysis of the reaction: L-2,4-diaminobutyrate + acetyl-CoA = N(4)-acetyl-L-2,4-diaminobutyrate + CoA + H(+).
Catalysis of the reaction: L-2,4-diaminobutyrate + acetyl-CoA = N(4)-acetyl-L-2,4-diaminobutyrate + CoA + H(+).
Catalysis of the reaction: (Z)-hexadec-11-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
Catalysis of the reaction: (Z)-hexadec-11-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
Catalysis of the reaction: (Z)-hexadec-11-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
Catalysis of the reaction: (Z)-hexadec-11-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
Catalysis of the reaction: (Z)-hexadec-11-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
Catalysis of the reaction: (Z)-hexadec-11-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
Catalysis of the reaction: acetyl-CoA + malonyl-[acyl-carrier protein] = acetoacyl-[acyl-carrier protein] + CoA + CO2.
Catalysis of the reaction: acetyl-CoA + malonyl-[acyl-carrier protein] = acetoacyl-[acyl-carrier protein] + CoA + CO2.
Catalysis of the reaction: acetyl-CoA + malonyl-[acyl-carrier protein] = acetoacyl-[acyl-carrier protein] + CoA + CO2.
Catalysis of the reaction: acetyl-CoA + malonyl-[acyl-carrier protein] = acetoacyl-[acyl-carrier protein] + CoA + CO2.
Catalysis of the reaction: acetyl-CoA + malonyl-[acyl-carrier protein] = acetoacyl-[acyl-carrier protein] + CoA + CO2.
Catalysis of the reaction: acetyl-CoA + malonyl-[acyl-carrier protein] = acetoacyl-[acyl-carrier protein] + CoA + CO2.
Catalysis of the reaction: acetyl-CoA + malonyl-[acyl-carrier protein] = acetoacyl-[acyl-carrier protein] + CoA + CO2.
Catalysis of the reaction: acetyl-CoA + malonyl-[acyl-carrier protein] = acetoacyl-[acyl-carrier protein] + CoA + CO2.
Catalysis of the reaction: acetyl-CoA + malonyl-[acyl-carrier protein] = acetoacyl-[acyl-carrier protein] + CoA + CO2.
Catalysis of the reaction: octanoyl-[acyl-carrier protein] + protein = protein N6-(octanoyl)lysine + acyl-carrier protein.
Catalysis of the reaction: octanoyl-[acyl-carrier protein] + protein = protein N6-(octanoyl)lysine + acyl-carrier protein.
Catalysis of the reaction: octanoyl-[acyl-carrier protein] + protein = protein N6-(octanoyl)lysine + acyl-carrier protein.
Catalysis of the reaction: octanoyl-[acyl-carrier protein] + protein = protein N6-(octanoyl)lysine + acyl-carrier protein.
Catalysis of the reaction: octanoyl-[acyl-carrier protein] + protein = protein N6-(octanoyl)lysine + acyl-carrier protein.
Catalysis of the reaction: octanoyl-[acyl-carrier protein] + protein = protein N6-(octanoyl)lysine + acyl-carrier protein.
Catalysis of the reaction: octanoyl-[acyl-carrier protein] + protein = protein N6-(octanoyl)lysine + acyl-carrier protein.
Catalysis of the transfer of an alpha-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of an alpha-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of an alpha-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of an alpha-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of an alpha-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of an alpha-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a glucosylhydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a glucosylhydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a glucosylhydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a glucosylhydroxymethylcytosine residue in DNA.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose to a glucosylhydroxymethylcytosine residue in DNA.
Catalysis of the reaction: UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
Catalysis of the reaction: UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
Catalysis of the reaction: UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
Catalysis of the reaction: UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
Catalysis of the reaction: UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
Catalysis of the reaction: UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
Catalysis of the reaction: UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
Catalysis of the reaction: UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
Catalysis of the reaction: UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
Catalysis of the transfer of an alpha-D-glucosyl residue from sucrose to alternately the 6-position and the 3-position of the non-reducing terminal residue of an alpha-D-glucan, thus producing a glucan having alternating alpha-1,6- and alpha-1,3-linkages.
Catalysis of the transfer of an alpha-D-glucosyl residue from sucrose to alternately the 6-position and the 3-position of the non-reducing terminal residue of an alpha-D-glucan, thus producing a glucan having alternating alpha-1,6- and alpha-1,3-linkages.
Catalysis of the transfer of an alpha-D-glucosyl residue from sucrose to alternately the 6-position and the 3-position of the non-reducing terminal residue of an alpha-D-glucan, thus producing a glucan having alternating alpha-1,6- and alpha-1,3-linkages.
Catalysis of the transfer of the non-reducing terminal alpha-D-glucose residue from a 1,4-alpha-D-glucan to the 4-position of an alpha-D-glucan, thus bringing about the hydrolysis of oligosaccharides.
Catalysis of the transfer of the non-reducing terminal alpha-D-glucose residue from a 1,4-alpha-D-glucan to the 4-position of an alpha-D-glucan, thus bringing about the hydrolysis of oligosaccharides.
Catalysis of the transfer of the non-reducing terminal alpha-D-glucose residue from a 1,4-alpha-D-glucan to the 4-position of an alpha-D-glucan, thus bringing about the hydrolysis of oligosaccharides.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose on to a glucose residue in xyloglucan, forming a beta-1,4-D-glucosyl-D-glucose linkage.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose on to a glucose residue in xyloglucan, forming a beta-1,4-D-glucosyl-D-glucose linkage.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose on to a glucose residue in xyloglucan, forming a beta-1,4-D-glucosyl-D-glucose linkage.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose on to a glucose residue in xyloglucan, forming a beta-1,4-D-glucosyl-D-glucose linkage.
Catalysis of the transfer of a beta-D-glucosyl residue from UDP-glucose on to a glucose residue in xyloglucan, forming a beta-1,4-D-glucosyl-D-glucose linkage.
Catalysis of the transfer of an N-acetyl-D-glucosamine residue from UDP-N-acetyl-D-glucosamine to the 4-position of a mannose linked alpha-1,6 to the core mannose of high-mannose oligosaccharides produced by Dictyostelium discoideum.
Catalysis of the transfer of an N-acetyl-D-glucosamine residue from UDP-N-acetyl-D-glucosamine to the 4-position of a mannose linked alpha-1,6 to the core mannose of high-mannose oligosaccharides produced by Dictyostelium discoideum.
Catalysis of the transfer of an N-acetyl-D-glucosamine residue from UDP-N-acetyl-D-glucosamine to the 4-position of a mannose linked alpha-1,6 to the core mannose of high-mannose oligosaccharides produced by Dictyostelium discoideum.
Catalysis of the transfer of an N-acetyl-D-glucosamine residue from UDP-N-acetyl-D-glucosamine to the 4-position of a mannose linked alpha-1,6 to the core mannose of high-mannose oligosaccharides produced by Dictyostelium discoideum.
Catalysis of the reaction: sn-glycerol 3-phosphate + ADP-glucose = 2-O-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + ADP-glucose = 2-O-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + ADP-glucose = 2-O-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + ADP-glucose = 2-O-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP + H(+).
Catalysis of the reaction: sn-glycerol 3-phosphate + ADP-glucose = 2-O-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP + H(+).
Catalysis of the transfer of a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.
Catalysis of the transfer of a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.
Catalysis of the reaction: UDP-N-acetylglucosamine + Skp1-protein-hydroxyproline = UDP + Skp1-protein-O-(N-acetyl-D-glucosaminyl)hydroxyproline.
Catalysis of the reaction: UDP-N-acetylglucosamine + Skp1-protein-hydroxyproline = UDP + Skp1-protein-O-(N-acetyl-D-glucosaminyl)hydroxyproline.
Catalysis of the reaction: UDP-N-acetylglucosamine + Skp1-protein-hydroxyproline = UDP + Skp1-protein-O-(N-acetyl-D-glucosaminyl)hydroxyproline.
Catalysis of the reaction: UDP-N-acetylglucosamine + Skp1-protein-hydroxyproline = UDP + Skp1-protein-O-(N-acetyl-D-glucosaminyl)hydroxyproline.
Catalysis of the reaction: UDP-N-acetylglucosamine + Skp1-protein-hydroxyproline = UDP + Skp1-protein-O-(N-acetyl-D-glucosaminyl)hydroxyproline.
Catalysis of the reaction: kojibiose + phosphate = beta-D-glucose 1-phosphate + D-glucose.
Catalysis of the reaction: alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate.
Catalysis of the reaction: alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate.
Catalysis of the reaction: 5-hydroxymethylfurfural + NADH + H+ = 2,5-bis-hydroxymethylfuran + NAD+.
Catalysis of the reaction: UDP-galactose + kaempferol = UDP + kaempferol 3-O-beta-D-galactoside.
Catalysis of the reaction: UDP-galactose + kaempferol = UDP + kaempferol 3-O-beta-D-galactoside.
Catalysis of the reaction: UDP-L-rhamnose + a flavanone 7-O-glucoside = UDP + a flavanone 7-O-[beta-L-rhamnosyl-(1->2)-beta-D-glucoside].
Catalysis of the reaction: UDP-L-rhamnose + a flavanone 7-O-glucoside = UDP + a flavanone 7-O-[beta-L-rhamnosyl-(1->2)-beta-D-glucoside].
Catalysis of the reaction: UDP-L-rhamnose + a flavanone 7-O-glucoside = UDP + a flavanone 7-O-[beta-L-rhamnosyl-(1->2)-beta-D-glucoside].
Catalysis of the reaction: UDP-glucose + a flavonol = UDP + a flavonol 7-O-beta-D-glucoside.
Catalysis of the reaction: UDP-glucose + a flavonol = UDP + a flavonol 7-O-beta-D-glucoside.
Catalysis of the reaction: UDP-glucose + an anthocyanin = UDP + an anthocyanin 3'-O-beta-D-glucoside.
Catalysis of the reaction: UDP-glucose + an anthocyanin = UDP + an anthocyanin 3'-O-beta-D-glucoside.
Catalysis of the reaction: UDP-glucose + an anthocyanin = UDP + an anthocyanin 3'-O-beta-D-glucoside.
Catalysis of the reaction: UDP-glucose + a flavonol 3-O-beta-D-glucoside = UDP + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside.
Catalysis of the reaction: UDP-glucose + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside = UDP + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside.
Catalysis of the reaction: NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP + (1,4-alpha-D-glucosyl)n+1.
Catalysis of the reaction: NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP + (1,4-alpha-D-glucosyl)n+1.
Catalysis of the reaction: NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP + (1,4-alpha-D-glucosyl)n+1.
Catalysis of the reaction: NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP + (1,4-alpha-D-glucosyl)n+1.
Catalysis of the reaction: NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP + (1,4-alpha-D-glucosyl)n+1.
Catalysis of the reaction: NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP + (1,4-alpha-D-glucosyl)n+1.
Catalysis of the reaction: NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP + (1,4-alpha-D-glucosyl)n+1.
Catalysis of the reaction: NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP + (1,4-alpha-D-glucosyl)n+1.
Catalysis of the reaction: NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP + (1,4-alpha-D-glucosyl)n+1.
Catalysis of the reaction: NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP + (1,4-alpha-D-glucosyl)n+1.
Catalysis of the reaction: NDP-glucose + (1,4-alpha-D-glucosyl)n = NDP + (1,4-alpha-D-glucosyl)n+1.
Catalysis of the reaction: [1-beta-D-fructofuranosyl-(2->1)-]m+1 alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 alpha-D-glucopyranoside = [1-beta-D-fructofuranosyl-(2->1)-]m alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0; n >= 0).
Catalysis of the reaction: [1-beta-D-fructofuranosyl-(2->1)-]m+1 alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 alpha-D-glucopyranoside = [1-beta-D-fructofuranosyl-(2->1)-]m alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0; n >= 0).
Catalysis of the reaction: [1-beta-D-fructofuranosyl-(2->1)-]m+1 alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 alpha-D-glucopyranoside = [1-beta-D-fructofuranosyl-(2->1)-]m alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0; n >= 0).
Catalysis of the reaction: [1-beta-D-fructofuranosyl-(2->1)-]m+1 alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 alpha-D-glucopyranoside = [1-beta-D-fructofuranosyl-(2->1)-]m alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0; n >= 0).
Catalysis of the reaction: [1-beta-D-fructofuranosyl-(2->1)-]m+1 alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 alpha-D-glucopyranoside = [1-beta-D-fructofuranosyl-(2->1)-]m alpha-D-glucopyranoside + [1-beta-D-fructofuranosyl-(2->1)-]n+1 beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0; n >= 0).
Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + N-acetyl-beta-D-glucosaminyl group = UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group.
Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + N-acetyl-beta-D-glucosaminyl group = UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group.
Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + N-acetyl-beta-D-glucosaminyl group = UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group.
Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + N-acetyl-beta-D-glucosaminyl group = UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group.
Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + N-acetyl-beta-D-glucosaminyl group = UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group.
Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + N-acetyl-beta-D-glucosaminyl group = UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl group.
Catalysis of the transfer of an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an alpha-1,6-D-xylosyl-D-glucose linkage.
Catalysis of the transfer of an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an alpha-1,6-D-xylosyl-D-glucose linkage.
Catalysis of the transfer of an alpha-D-xylosyl residue from UDP-D-xylose to a glucose residue in xyloglucan, forming an alpha-1,6-D-xylosyl-D-glucose linkage.
Catalysis of the elimination of sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues.
Catalysis of the elimination of sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues.
Catalysis of the elimination of sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues.
Catalysis of the elimination of sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues.
Catalysis of the reaction: 5-hydroxymethylfurfural + NADPH + H+ = 2,5-bis-hydroxymethylfuran + NADP+.
Catalysis of the reaction: S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine.
Catalysis of the reaction: S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine.
Catalysis of the reaction: O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate.
Catalysis of the reaction: O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate.
Catalysis of the reaction: D-glyceraldehyde 3-phosphate + L-arginine = N(2)-(2-carboxyethyl)-L-arginine + H(+) + phosphate.
Catalysis of the reaction: D-glyceraldehyde 3-phosphate + L-arginine = N(2)-(2-carboxyethyl)-L-arginine + H(+) + phosphate.
Catalysis of the reaction: D-glyceraldehyde 3-phosphate + L-arginine = N(2)-(2-carboxyethyl)-L-arginine + H(+) + phosphate.
Catalysis of the reaction: D-glyceraldehyde 3-phosphate + L-arginine = N(2)-(2-carboxyethyl)-L-arginine + H(+) + phosphate.
Catalysis of the reaction: D-glyceraldehyde 3-phosphate + L-arginine = N(2)-(2-carboxyethyl)-L-arginine + H(+) + phosphate.
Catalysis of the reaction: 2 dimethylallyl diphosphate = (R,R)-chrysanthemyl diphosphate + diphosphate.
Catalysis of the reaction: 2 dimethylallyl diphosphate = (R,R)-chrysanthemyl diphosphate + diphosphate.
Catalysis of the reaction: geranyl diphosphate + isopentenyl diphosphate = 2-cis,6-trans-farnesyl diphosphate + diphosphate.
Catalysis of the reaction: geranyl diphosphate + isopentenyl diphosphate = 2-cis,6-trans-farnesyl diphosphate + diphosphate.
Catalysis of the reaction: 2 dimethylallyl diphosphate = diphosphate + lavandulyl diphosphate.
Catalysis of the reaction: 2 dimethylallyl diphosphate = diphosphate + lavandulyl diphosphate.
Catalysis of the reaction: 2-oxoglutarate + 3,5,3'-triiodo-L-thyronine = 3,5,3'-triiodothyropyruvate + L-glutamate.
Catalysis of the reaction: 2-oxoglutarate + 3,5,3'-triiodo-L-thyronine = 3,5,3'-triiodothyropyruvate + L-glutamate.
Catalysis of the reaction: 2-oxoglutarate + 3,5,3'-triiodo-L-thyronine = 3,5,3'-triiodothyropyruvate + L-glutamate.
Catalysis of the reaction: 2-oxoglutarate + 3,5,3'-triiodo-L-thyronine = 3,5,3'-triiodothyropyruvate + L-glutamate.
Catalysis of the reaction: 2-oxoglutarate + 3,5,3'-triiodo-L-thyronine = 3,5,3'-triiodothyropyruvate + L-glutamate.
Catalysis of the reaction: L-arogenate + oxaloacetate = prephenate + L-aspartate.
Catalysis of the reaction: L-arogenate + oxaloacetate = prephenate + L-aspartate.
Catalysis of the reaction: L-arogenate + oxaloacetate = prephenate + L-aspartate.
Catalysis of the reaction: L-arogenate + oxaloacetate = prephenate + L-aspartate.
Catalysis of the reaction: L-arogenate + oxaloacetate = prephenate + L-aspartate.
Catalysis of the reaction: 2-oxoglutarate + L-arogenate = L-glutamate + prephenate.
Catalysis of the reaction: 2-oxoglutarate + L-arogenate = L-glutamate + prephenate.
Catalysis of the reaction: 2-oxoglutarate + L-arogenate = L-glutamate + prephenate.
Catalysis of the reaction: 2-oxoglutarate + L-arogenate = L-glutamate + prephenate.
Catalysis of the reaction: 2-oxoglutarate + nicotianamine = 3''-deamino-3''-oxonicotianamine + L-glutamate.
Catalysis of the reaction: 2-oxoglutarate + nicotianamine = 3''-deamino-3''-oxonicotianamine + L-glutamate.
Catalysis of the reaction: 2-oxoglutarate + nicotianamine = 3''-deamino-3''-oxonicotianamine + L-glutamate.
Catalysis of the reaction: 2-oxoglutarate + nicotianamine = 3''-deamino-3''-oxonicotianamine + L-glutamate.
Catalysis of the reaction: 2-oxoglutarate + nicotianamine = 3''-deamino-3''-oxonicotianamine + L-glutamate.
Catalysis of the reaction: 2-oxoglutarate + nicotianamine = 3''-deamino-3''-oxonicotianamine + L-glutamate.
Catalysis of the reaction: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = 2 H(2)O + H(+) + phosphate + pyridoxine 5'-phosphate.
Catalysis of the reaction: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = 2 H(2)O + H(+) + phosphate + pyridoxine 5'-phosphate.
Catalysis of the reaction: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = 2 H(2)O + H(+) + phosphate + pyridoxine 5'-phosphate.
Catalysis of the reaction: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = 2 H(2)O + H(+) + phosphate + pyridoxine 5'-phosphate.
Catalysis of the reaction: ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate.
Catalysis of the reaction: ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate.
Catalysis of the reaction: ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate.
Catalysis of the reaction: ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate.
Catalysis of the reaction: ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate.
Catalysis of the reaction: ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate.
Catalysis of the reaction: ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate.
Catalysis of the reaction: ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate.
Catalysis of the reaction: ATP + N-acetyl-D-galactosamine = ADP + N-acetyl-alpha-D-galactosamine 1-phosphate.
Catalysis of the reaction: ATP + N-acetyl-D-galactosamine = ADP + N-acetyl-alpha-D-galactosamine 1-phosphate.
Catalysis of the reaction: ATP + N-acetyl-D-galactosamine = ADP + N-acetyl-alpha-D-galactosamine 1-phosphate.
Catalysis of the reaction: ATP + N-acetyl-D-galactosamine = ADP + N-acetyl-alpha-D-galactosamine 1-phosphate.
Catalysis of the reaction: ATP + N-acetyl-D-galactosamine = ADP + N-acetyl-alpha-D-galactosamine 1-phosphate.
The chemical reactions and pathways involving furaldehyde, a furan ring-containing aldehyde compound which can be formed from the thermal decomposition of biomass.
Any process that modulates the activity of the enzyme NAD(P)H oxidase.
Any process that stops or reduces the activity of the enzyme NAD(P)H oxidase.
Any process that stops or reduces the activity of the enzyme NAD(P)H oxidase.
Any process that stops or reduces the activity of the enzyme NAD(P)H oxidase.
Any process that stops or reduces the activity of the enzyme NAD(P)H oxidase.
Catalysis of the reaction: ATP + UMP = ADP + UDP.
Catalysis of the reaction: ATP + UMP = ADP + UDP.
Catalysis of the reaction: ATP + UMP = ADP + UDP.
Catalysis of the reaction: ATP + UMP = ADP + UDP.
Catalysis of the reaction: ATP + UMP = ADP + UDP.
Catalysis of the reaction: ATP + UMP = ADP + UDP.
Catalysis of the reaction: D-ribose 1,5-diphosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + ADP + H(+).
Catalysis of the reaction: D-ribose 1,5-diphosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + ADP + H(+).
Catalysis of the reaction: D-ribose 1,5-diphosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + ADP + H(+).
Any process that activates or increases the activity of the enzyme NAD(P)H oxidase.
Any process that activates or increases the activity of the enzyme NAD(P)H oxidase.
Any process that activates or increases the activity of the enzyme NAD(P)H oxidase.
Any process that activates or increases the activity of the enzyme NAD(P)H oxidase.
Any process that activates or increases the activity of the enzyme NAD(P)H oxidase.
The chemical reactions and pathways involving a nucleoside bisphosphate, a compound consisting of a nucleobase linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a nucleoside bisphosphate, a compound consisting of a nucleobase linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a nucleoside bisphosphate, a compound consisting of a nucleobase linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a nucleoside bisphosphate, a compound consisting of a nucleobase linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a nucleoside bisphosphate, a compound consisting of a nucleobase linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
Catalysis of the reaction: ATP + Fas-activated serine/threonine protein = ADP + Fas-activated serine/threonine phosphoprotein.
Catalysis of the reaction: ATP + Fas-activated serine/threonine protein = ADP + Fas-activated serine/threonine phosphoprotein.
Catalysis of the reaction: ATP + Fas-activated serine/threonine protein = ADP + Fas-activated serine/threonine phosphoprotein.
Catalysis of the reaction: ATP + Fas-activated serine/threonine protein = ADP + Fas-activated serine/threonine phosphoprotein.
Catalysis of the reaction: ATP + Goodpasture antigen-binding protein = ADP + Goodpasture antigen-binding phosphoprotein.
Catalysis of the reaction: ATP + Goodpasture antigen-binding protein = ADP + Goodpasture antigen-binding phosphoprotein.
Catalysis of the reaction: ATP + Goodpasture antigen-binding protein = ADP + Goodpasture antigen-binding phosphoprotein.
Catalysis of the reaction: ATP + Goodpasture antigen-binding protein = ADP + Goodpasture antigen-binding phosphoprotein.
Catalysis of the reaction: ATP + Goodpasture antigen-binding protein = ADP + Goodpasture antigen-binding phosphoprotein.
The chemical reactions and pathways resulting in the breakdown of a nucleoside bisphosphate, a compound consisting of a nucleobase linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the breakdown of a nucleoside bisphosphate, a compound consisting of a nucleobase linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the breakdown of a nucleoside bisphosphate, a compound consisting of a nucleobase linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + a thiol = adenosine 3',5'-bisphosphate + an S-alkyl thiosulfate.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + a thiol = adenosine 3',5'-bisphosphate + an S-alkyl thiosulfate.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + a thiol = adenosine 3',5'-bisphosphate + an S-alkyl thiosulfate.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate; modifies selected glucosamine residues preceded by GlcA2S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate; modifies selected glucosamine residues preceded by GlcA2S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate; modifies selected glucosamine residues preceded by GlcA2S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate; modifies selected glucosamine residues preceded by GlcA2S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate; modifies selected glucosamine residues preceded by GlcA2S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate; modifies selected glucosamine residues preceded by GlcA2S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate; modifies selected glucosamine residues preceded by GlcA2S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate; modifies selected glucosamine residues preceded by GlcA2S.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.
Catalysis of the reaction: 3'-phospho-5'-adenylyl sulfate + 5alpha-cholane-3alpha,7alpha,12alpha,24-tetrol = 3alpha,7alpha,12alpha-trihydroxy-5alpha-cholan-24-yl sulfate + adenosine 3',5'-diphosphate + H(+).
Catalysis of the reaction: 3'-phospho-5'-adenylyl sulfate + 5alpha-cholane-3alpha,7alpha,12alpha,24-tetrol = 3alpha,7alpha,12alpha-trihydroxy-5alpha-cholan-24-yl sulfate + adenosine 3',5'-diphosphate + H(+).
Catalysis of the reaction: 3'-phospho-5'-adenylyl sulfate + 5beta-scymnol = 5beta-scymnol sulfate + adenosine 3',5'-diphosphate + H(+).
The chemical reactions and pathways involving a ribonucleoside bisphosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
Catalysis of the reaction: 3'-phospho-5'-adenylyl sulfate + glycochenodeoxycholate = adenosine 3',5'-diphosphate + glycochenodeoxycholate 7-sulfate + H(+).
Catalysis of the reaction: 3'-phospho-5'-adenylyl sulfate + glycochenodeoxycholate = adenosine 3',5'-diphosphate + glycochenodeoxycholate 7-sulfate + H(+).
Catalysis of the reaction: 3'-phospho-5'-adenylyl sulfate + glycochenodeoxycholate = adenosine 3',5'-diphosphate + glycochenodeoxycholate 7-sulfate + H(+).
Catalysis of the reaction: 3'-phospho-5'-adenylyl sulfate + glycochenodeoxycholate = adenosine 3',5'-diphosphate + glycochenodeoxycholate 7-sulfate + H(+).
Catalysis of the reaction: (R)-2-benzylsuccinate + succinyl-CoA = (R)-2-benzylsuccinyl-CoA + succinate.
Catalysis of the reaction: (R)-2-benzylsuccinate + succinyl-CoA = (R)-2-benzylsuccinyl-CoA + succinate.
Catalysis of the reaction: (R)-2-benzylsuccinate + succinyl-CoA = (R)-2-benzylsuccinyl-CoA + succinate.
Catalysis of the reaction: (R)-2-benzylsuccinate + succinyl-CoA = (R)-2-benzylsuccinyl-CoA + succinate.
Catalysis of the reactions: diacylglycerol + H2O = monoacylglycerol + a carboxylate; triacylglycerol + H2O = diacylglycerol + a carboxylate; and monoacylglycerol + H2O = glycerol + a carboxylate.
Catalysis of the reactions: diacylglycerol + H2O = monoacylglycerol + a carboxylate; triacylglycerol + H2O = diacylglycerol + a carboxylate; and monoacylglycerol + H2O = glycerol + a carboxylate.
Catalysis of the reactions: 17-O-acetylajmaline + H2O = ajmaline + acetate, and 17-O-acetylnorajmaline + H2O = norajmaline + acetate.
Catalysis of the reactions: 17-O-acetylajmaline + H2O = ajmaline + acetate, and 17-O-acetylnorajmaline + H2O = norajmaline + acetate.
Catalysis of the reactions: 17-O-acetylajmaline + H2O = ajmaline + acetate, and 17-O-acetylnorajmaline + H2O = norajmaline + acetate.
Catalysis of the reactions: 17-O-acetylajmaline + H2O = ajmaline + acetate, and 17-O-acetylnorajmaline + H2O = norajmaline + acetate.
Catalysis of the reaction: H(2)O + phenylglyoxylyl-CoA = CoA + H(+) + phenylglyoxylate.
Catalysis of the reaction: deoxycholoyl-CoA + H(2)O = CoA + deoxycholate + H(+).
Catalysis of the reaction: deoxycholoyl-CoA + H(2)O = CoA + deoxycholate + H(+).
Catalysis of the reaction: choloyl-CoA + H2O = cholate + CoA.
Catalysis of the reaction: choloyl-CoA + H2O = cholate + CoA.
Catalysis of the reaction: choloyl-CoA + H2O = cholate + CoA.
Catalysis of the reaction: choloyl-CoA + H2O = cholate + CoA.
Catalysis of the reaction: pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.
Catalysis of the reaction: pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.
Catalysis of the reaction: pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.
Catalysis of the reaction: pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.
Catalysis of the reaction: pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.
Catalysis of the reaction: choline phosphate + H2O = choline + phosphate.
Catalysis of the reaction: choline phosphate + H2O = choline + phosphate.
Catalysis of the reaction: choline phosphate + H2O = choline + phosphate.
Catalysis of the reaction: O-phosphoethanolamine + H2O = ethanolamine + phosphate.
Catalysis of the reaction: O-phosphoethanolamine + H2O = ethanolamine + phosphate.
Catalysis of the reaction: O-phosphoethanolamine + H2O = ethanolamine + phosphate.
Catalysis of the reaction: (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.
Catalysis of the reaction: (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.
Catalysis of the reaction: (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.
Catalysis of the reaction: (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.
Catalysis of the reaction: (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.
Catalysis of the reaction: (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.
Catalysis of the reaction: (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.
Catalysis of the reaction: (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.
Catalysis of the hydrolysis of the 2- and 3-sulfate groups of the polysulfates of cellulose and charonin.
Catalysis of the reaction: 4-deoxy-beta-D-gluc-4-enuronosyl-(1->3)-N-acetyl-D-galactosamine 4-sulfate + H(2)O = 4-deoxy-beta-D-gluc-4-enuronosyl-(1->3)-N-acetyl-D-galactosamine + H(+) + sulfate.
Catalysis of the reaction: 4-deoxy-beta-D-gluc-4-enuronosyl-(1->3)-N-acetyl-D-galactosamine 6-sulfate + H(2)O = 4-deoxy-beta-D-gluc-4-enuronosyl-(1->3)-N-acetyl-D-galactosamine + H(+) + sulfate.
Catalysis of the hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin.
Catalysis of the hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin.
Catalysis of the exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
Catalysis of the endonucleolytic cleavage to give 5'-phosphooligonucleotide end-products, with a preference for cleavage within the sequence CC.
Catalysis of the endonucleolytic cleavage to give 5'-phosphooligonucleotide end-products, with a preference for cleavage within the sequence CC.
Catalysis of the endonucleolytic cleavage to give 5'-phosphooligonucleotide end-products, with a preference for cleavage within the sequence CC.
Catalysis of the endonucleolytic cleavage to give 5'-phosphooligonucleotide end-products, with a preference for cleavage within the sequence CC.
Catalysis of the endonucleolytic cleavage near pyrimidine dimers to products with 5'-phosphate.
Catalysis of the endonucleolytic cleavage near pyrimidine dimers to products with 5'-phosphate.
Catalysis of the endonucleolytic cleavage near pyrimidine dimers to products with 5'-phosphate.
Catalysis of the endonucleolytic cleavage of poly(A) to fragments terminated by 3'-hydroxy and 5'-phosphate groups.
Catalysis of the endonucleolytic cleavage of RNA, removing 3'-extranucleotides from tRNA precursor.
Catalysis of the endonucleolytic cleavage of poly(U) to fragments terminated by 3'-hydroxy and 5'-phosphate groups.
Catalysis of the endonucleolytic cleavage of poly(U) to fragments terminated by 3'-hydroxy and 5'-phosphate groups.
Catalysis of the endonucleolytic cleavage of poly(U) to fragments terminated by 3'-hydroxy and 5'-phosphate groups.
Catalysis of the endonucleolytic cleavage of poly(U) or poly(C) to fragments terminated by 3'-hydroxy and 5'-phosphate groups.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.
Catalysis of the endonucleolytic cleavage to 2',3'-cyclic nucleotides.
Catalysis of the endonucleolytic cleavage to 2',3'-cyclic nucleotides.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Ap or Gp with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Ap or Gp with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Ap or Gp with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Ap or Gp with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Ap or Gp with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Ap or Gp with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Ap or Gp with 2',3'-cyclic phosphate intermediates.
Catalysis of the two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Ap or Gp with 2',3'-cyclic phosphate intermediates.
Catalysis of the endonucleolytic cleavage of RNA precursor into two, leaving 5'-hydroxy and 3'-phosphate groups.
Catalysis of the endonucleolytic cleavage of RNA precursor into two, leaving 5'-hydroxy and 3'-phosphate groups.
Catalysis of the hydrolysis of poly(A), forming oligoribonucleotides and ultimately 3'-AMP.
Catalysis of the hydrolysis of the phosphodiester linkage between guanosine and adenosine residues at one specific position in 28S rRNA from rat ribosomes.
Catalysis of the endohydrolysis of (1->3)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3.
Catalysis of the endohydrolysis of (1->3)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3.
Catalysis of the endohydrolysis of (1->3)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3.
Catalysis of the endohydrolysis of (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3.
Catalysis of the endohydrolysis of (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3.
Catalysis of the endohydrolysis of (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3.
Catalysis of the endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran.
Catalysis of the endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran.
Catalysis of the endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran.
Catalysis of the endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran.
Catalysis of the endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran.
Catalysis of the endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran.
Catalysis of the endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran.
Catalysis of the endohydrolysis of 1,6-alpha-D-glucosidic linkages in dextran.
Catalysis of the random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.
Catalysis of the random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.
Catalysis of the random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.
Catalysis of the random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.
Catalysis of the random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.
Catalysis of the random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.
Catalysis of the random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.
Catalysis of the random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.
Catalysis of the random hydrolysis of 1,3-linkages between beta-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate.
Catalysis of the random hydrolysis of 1,3-linkages between beta-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate.
Catalysis of the random hydrolysis of 1,3-linkages between beta-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate.
Catalysis of the random hydrolysis of 1,3-linkages between beta-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate.
Catalysis of the hydrolysis of terminal non-reducing beta-D-fucose residues in beta-D-fucosides.
Catalysis of the hydrolysis of terminal non-reducing beta-D-fucose residues in beta-D-fucosides.
Catalysis of the hydrolysis of terminal, non-reducing beta-L-rhamnose residues in beta-L-rhamnosides.
Catalysis of the endohydrolysis of 1,2-alpha-L-fucoside linkages in fucoidan without release of sulfate.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.
Catalysis of the endohydrolysis of 1,4-alpha-D-glucosidic linkages in alpha-D-glucans containing both 1,3- and 1,4-bonds.
Catalysis of the hydrolysis of (2->6)-beta-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(beta-D-fructofuranosyl)-D-fructose, from the end of the chain.
Catalysis of the hydrolysis of (2->6)-beta-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(beta-D-fructofuranosyl)-D-fructose, from the end of the chain.
Catalysis of the hydrolysis of (2->6)-beta-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(beta-D-fructofuranosyl)-D-fructose, from the end of the chain.
Catalysis of the hydrolysis of (2->6)-beta-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(beta-D-fructofuranosyl)-D-fructose, from the end of the chain.
Catalysis of the hydrolysis of (2->6)-beta-D-fructofuranan, to remove successive disaccharide residues as levanbiose, i.e. 6-(beta-D-fructofuranosyl)-D-fructose, from the end of the chain.
Catalysis of the random hydrolysis of (1->2)-glucosidic linkages in (1->2)-beta-D-glucans.
Catalysis of the random hydrolysis of (1->2)-glucosidic linkages in (1->2)-beta-D-glucans.
Catalysis of the random hydrolysis of (1->2)-glucosidic linkages in (1->2)-beta-D-glucans.
Catalysis of the random hydrolysis of (1->2)-glucosidic linkages in (1->2)-beta-D-glucans.
Catalysis of the hydrolysis of successive xylose residues from the non-reducing termini of (1->3)-beta-D-xylans.
Catalysis of the hydrolysis of successive xylose residues from the non-reducing termini of (1->3)-beta-D-xylans.
Catalysis of the hydrolysis of successive xylose residues from the non-reducing termini of (1->3)-beta-D-xylans.
Catalysis of the hydrolysis of successive xylose residues from the non-reducing termini of (1->3)-beta-D-xylans.
Catalysis of the hydrolysis of successive xylose residues from the non-reducing termini of (1->3)-beta-D-xylans.
Catalysis of the hydrolysis of (1->2) and (1->3) linkages in mannan, releasing mannose.
Catalysis of the hydrolysis of (1->2) and (1->3) linkages in mannan, releasing mannose.
Catalysis of the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.
Catalysis of the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.
Catalysis of the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.
Catalysis of the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.
Catalysis of the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.
Catalysis of the hydrolysis of pectic acid from the non-reducing end, releasing digalacturonate.
Catalysis of the hydrolysis of pectic acid from the non-reducing end, releasing digalacturonate.
Catalysis of the endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans.
Catalysis of the endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans.
Catalysis of the hydrolysis of terminal (1->3)-alpha-D-glucosidic links in 1,3-alpha-D-glucans.
Catalysis of the hydrolysis of terminal (1->3)-alpha-D-glucosidic links in 1,3-alpha-D-glucans.
Catalysis of the hydrolysis of terminal (1->3)-alpha-D-glucosidic links in 1,3-alpha-D-glucans.
Catalysis of the reaction: a 6-phospho-beta-D-galactoside + H2O = 6-phospho-D-galactose + an alcohol.
Catalysis of the reaction: a 6-phospho-beta-D-galactoside + H2O = 6-phospho-D-galactose + an alcohol.
Catalysis of the reaction: a 6-phospho-beta-D-galactoside + H2O = 6-phospho-D-galactose + an alcohol.
Catalysis of the reaction: a 6-phospho-beta-D-galactoside + H2O = 6-phospho-D-galactose + an alcohol.
Catalysis of the reaction: a 6-phospho-beta-D-galactoside + H2O = 6-phospho-D-galactose + an alcohol.
Catalysis of the random hydrolysis of (1->3)-alpha-D-galactosidic linkages in Aerobacter aerogenes capsular polysaccharide.
Catalysis of the random hydrolysis of (1->3)-alpha-D-galactosidic linkages in Aerobacter aerogenes capsular polysaccharide.
Catalysis of the random hydrolysis of (1->3)-alpha-D-galactosidic linkages in Aerobacter aerogenes capsular polysaccharide.
Catalysis of the hydrolysis of terminal, non-reducing N-acetylmuramic residues.
Catalysis of the hydrolysis of terminal, non-reducing N-acetylmuramic residues.
Catalysis of the hydrolysis of terminal, non-reducing N-acetylmuramic residues.
Catalysis of the hydrolysis of terminal, non-reducing N-acetylmuramic residues.
Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains.
Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains.
Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains.
Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains.
Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains.
Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic linkages in dextrans, to remove successive isomaltotriose units from the non-reducing ends of the chains.
Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic linkages in dextrans, to remove successive isomaltotriose units from the non-reducing ends of the chains.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Catalysis of the reaction: D-galactosyl-3-(N-acetyl-alpha-D-galactosaminyl)-L-serine + H2O = D-galactosyl-3-N-acetyl-alpha-D-galactosamine + L-serine in mucin-type glycoproteins.
Catalysis of the reaction: D-galactosyl-3-(N-acetyl-alpha-D-galactosaminyl)-L-serine + H2O = D-galactosyl-3-N-acetyl-alpha-D-galactosamine + L-serine in mucin-type glycoproteins.
Catalysis of the reaction: D-galactosyl-3-(N-acetyl-alpha-D-galactosaminyl)-L-serine + H2O = D-galactosyl-3-N-acetyl-alpha-D-galactosamine + L-serine in mucin-type glycoproteins.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-beta-D-mannosidic linkages in (1->4)-beta-D-mannans, to remove successive mannobiose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-beta-D-mannosidic linkages in (1->4)-beta-D-mannans, to remove successive mannobiose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-beta-D-mannosidic linkages in (1->4)-beta-D-mannans, to remove successive mannobiose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-beta-D-mannosidic linkages in (1->4)-beta-D-mannans, to remove successive mannobiose residues from the non-reducing chain ends.
Catalysis of the endohydrolysis of (1->4)-beta-D-galactosidic linkages in blood group A and B substances.
Catalysis of the endohydrolysis of (1->4)-beta-D-galactosidic linkages in blood group A and B substances.
Catalysis of the endohydrolysis of (1->4)-beta-D-galactosidic linkages in keratan sulfate.
Catalysis of the endohydrolysis of (1->4)-beta-D-galactosidic linkages in keratan sulfate.
Catalysis of the endohydrolysis of (1->4)-beta-D-galactosidic linkages in keratan sulfate.
Catalysis of the endohydrolysis of (1->4)-beta-D-galactosidic linkages in keratan sulfate.
Catalysis of the endohydrolysis of (1->4)-alpha-D-galactosaminidic linkages in poly(D-galactosamine).
Catalysis of the hydrolysis of (1->3) linkages between alpha-L-fucose and N-acetylglucosamine residues in glycoproteins.
Catalysis of the hydrolysis of (1->3) linkages between alpha-L-fucose and N-acetylglucosamine residues in glycoproteins.
Catalysis of the hydrolysis of (1->2)-alpha-D-glucosidic linkages at the branch points of dextrans and related polysaccharides, producing free D-glucose.
Catalysis of the hydrolysis of (1->2)-alpha-D-glucosidic linkages at the branch points of dextrans and related polysaccharides, producing free D-glucose.
Catalysis of the hydrolysis of (1->2)-alpha-D-glucosidic linkages at the branch points of dextrans and related polysaccharides, producing free D-glucose.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotriose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotriose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotriose residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic links in oligoxyloglucans so as to remove successive isoprimeverose (i.e. alpha-xylo-1,6-beta-D-glucosyl-) residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic links in oligoxyloglucans so as to remove successive isoprimeverose (i.e. alpha-xylo-1,6-beta-D-glucosyl-) residues from the non-reducing chain ends.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic links in oligoxyloglucans so as to remove successive isoprimeverose (i.e. alpha-xylo-1,6-beta-D-glucosyl-) residues from the non-reducing chain ends.
Catalysis of the endohydrolysis of the D-mannuronide linkages of polymannuronate.
Catalysis of the endohydrolysis of the D-mannuronide linkages of polymannuronate.
Catalysis of the endohydrolysis of the beta-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonate in capsular polysaccharides.
Catalysis of the endohydrolysis of the beta-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonate in capsular polysaccharides.
Catalysis of the endohydrolysis of the beta-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonate in capsular polysaccharides.
Catalysis of the endohydrolysis of the beta-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonate in capsular polysaccharides.
Catalysis of the endohydrolysis of the beta-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonate in capsular polysaccharides.
Catalysis of the hydrolysis of (1->6) linkages between alpha-L-fucose and N-acetyl-D-glucosamine in glycopeptides such as immunoglobulin G glycopeptide and fucosyl-asialo-agalacto-fetuin.
Catalysis of the hydrolysis of alpha-D-(1->2)-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans.
Catalysis of the hydrolysis of alpha-D-(1->2)-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans.
Catalysis of the hydrolysis of alpha-D-(1->2)-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans.
Catalysis of the hydrolysis of (1->2)-alpha-D- and (1->6)-alpha-D- linkages in mannan, releasing D-mannose.
Catalysis of the hydrolysis of (1->2)-alpha-D- and (1->6)-alpha-D- linkages in mannan, releasing D-mannose.
Catalysis of the hydrolysis of alpha-(1->4)-D-glucosidic linkage in 4-alpha-D-{(1->4)-alpha-D-glucanosyl}n trehalose to yield trehalose and alpha-(1->4)-D-glucan.
Catalysis of the hydrolysis of alpha-(1->4)-D-glucosidic linkage in 4-alpha-D-{(1->4)-alpha-D-glucanosyl}n trehalose to yield trehalose and alpha-(1->4)-D-glucan.
Catalysis of the hydrolysis of alpha-(1->4)-D-glucosidic linkage in 4-alpha-D-{(1->4)-alpha-D-glucanosyl}n trehalose to yield trehalose and alpha-(1->4)-D-glucan.
Catalysis of the hydrolysis of alpha-(1->4)-D-glucosidic linkage in 4-alpha-D-{(1->4)-alpha-D-glucanosyl}n trehalose to yield trehalose and alpha-(1->4)-D-glucan.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-galactose residues in (1->3)-beta-D-galactopyranans.
Catalysis of the hydrolysis of terminal, non-reducing beta-D-galactose residues in (1->3)-beta-D-galactopyranans.
Catalysis of the hydrolysis of terminal non-reducing beta-D-galactofuranosides, releasing galactose.
Catalysis of the hydrolysis of terminal non-reducing beta-D-galactofuranosides, releasing galactose.
Catalysis of the hydrolysis of terminal non-reducing beta-D-galactofuranosides, releasing galactose.
Catalysis of the hydrolysis of terminal non-reducing beta-D-galactofuranosides, releasing galactose.
Catalysis of the hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a beta-(1->4) linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted.
Catalysis of the hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a beta-(1->4) linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted.
Catalysis of the reaction: xyloglucan + H2O = xyloglucan oligosaccharides. This reaction is the endohydrolysis of (1->4)-beta-D-glucosidic linkages in xyloglucan.
Catalysis of the reaction: xyloglucan + H2O = xyloglucan oligosaccharides. This reaction is the endohydrolysis of (1->4)-beta-D-glucosidic linkages in xyloglucan.
Catalysis of the reaction: xyloglucan + H2O = xyloglucan oligosaccharides. This reaction is the endohydrolysis of (1->4)-beta-D-glucosidic linkages in xyloglucan.
Catalysis of the reaction: xyloglucan + H2O = xyloglucan oligosaccharides. This reaction is the endohydrolysis of (1->4)-beta-D-glucosidic linkages in xyloglucan.
Catalysis of the reaction: xyloglucan + H2O = xyloglucan oligosaccharides. This reaction is the endohydrolysis of (1->4)-beta-D-glucosidic linkages in xyloglucan.
Catalysis of the reaction: xyloglucan + H2O = xyloglucan oligosaccharides. This reaction is the endohydrolysis of (1->4)-beta-D-glucosidic linkages in xyloglucan.
Catalysis of the reaction: xyloglucan + H2O = xyloglucan oligosaccharides. This reaction is the endohydrolysis of (1->4)-beta-D-glucosidic linkages in xyloglucan.
Catalysis of the hydrolysis of the alpha-D-mannosyl-(1->6)-beta-D-mannosyl-(1->4)-beta-D-N-acetylglucosaminyl-(1->4)-beta-D-N-acetylglucosaminyl sequence of glycoprotein to alpha-D-mannosyl-(1->6)-D-mannose and beta-D-N-acetylglucosaminyl-(1->4)-beta-D-N-acetylglucosaminyl sequences.
Catalysis of the hydrolysis of terminal, non-reducing (2->1) linked beta-D-fructofuranose residues in fructans.
Catalysis of the hydrolysis of terminal, non-reducing (2->1) linked beta-D-fructofuranose residues in fructans.
Catalysis of the hydrolysis of terminal, non-reducing (2->1) linked beta-D-fructofuranose residues in fructans.
Catalysis of the hydrolysis of terminal, non-reducing (2->1) linked beta-D-fructofuranose residues in fructans.
Catalysis of the hydrolysis of terminal, non-reducing (2->1) linked beta-D-fructofuranose residues in fructans.
Catalysis of the hydrolysis of terminal, non-reducing (2->1) linked beta-D-fructofuranose residues in fructans.
Catalysis of the hydrolysis of terminal, non-reducing (2->1) linked beta-D-fructofuranose residues in fructans.
Catalysis of the hydrolysis of terminal, non-reducing (2->6) linked beta-D-fructofuranose residues in fructans.
Catalysis of the hydrolysis of terminal, non-reducing (2->6) linked beta-D-fructofuranose residues in fructans.
Catalysis of the hydrolysis of terminal, non-reducing (2->6) linked beta-D-fructofuranose residues in fructans.
Catalysis of the reaction: xyloglucan + H2O = xyloglucan oligosaccharides. This reaction is the exohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan.
Catalysis of the reaction: xyloglucan + H2O = xyloglucan oligosaccharides. This reaction is the exohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan.
Catalysis of the hydrolysis of 1,4-beta-D-xylose residues from the reducing end of oligosaccharides.
Catalysis of the hydrolysis of 1,4-beta-D-xylose residues from the reducing end of oligosaccharides.
Catalysis of the hydrolysis of 1,4-beta-D-xylose residues from the reducing end of oligosaccharides.
Catalysis of the endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose-2-sulfate in iota-carrageenans.
Catalysis of the endohydrolysis of 1,3-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product.
Catalysis of the endohydrolysis of 1,3-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product.
Catalysis of the endohydrolysis of 1,3-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product.
Catalysis of the hydrolysis of the 1,3-alpha-L-galactosidic linkages of neoagaro-oligosaccharides that are smaller than a hexamer, yielding 3,6-anhydro-L-galactose and D-galactose.
Catalysis of the hydrolysis of the 1,3-alpha-L-galactosidic linkages of neoagaro-oligosaccharides that are smaller than a hexamer, yielding 3,6-anhydro-L-galactose and D-galactose.
Catalysis of the hydrolysis of the 1,3-alpha-L-galactosidic linkages of neoagaro-oligosaccharides that are smaller than a hexamer, yielding 3,6-anhydro-L-galactose and D-galactose.
The process in which copies of the mitochondrial genome are distributed into daughter mitochondria upon mitochondrial fission.
The process in which copies of the mitochondrial genome are distributed into daughter mitochondria upon mitochondrial fission.
The process in which copies of the mitochondrial genome are distributed into daughter mitochondria upon mitochondrial fission.
Catalysis of the reaction: 7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + beta-D-apiofuranosyl-(1->6)-D-glucose.
Catalysis of the reaction: 7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + beta-D-apiofuranosyl-(1->6)-D-glucose.
Catalysis of the reaction: 7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + beta-D-apiofuranosyl-(1->6)-D-glucose.
Catalysis of the reaction: 7-[beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + beta-D-apiofuranosyl-(1->6)-D-glucose.
Catalysis of the endohydrolysis of beta-1,4-linkages in the backbone of lambda-carrageenan, resulting in the tetrasaccharide alpha-D-Galp2,6S2-(1->3)-beta-D-Galp2S-(1->4)-alpha-D-Galp2,6S2-(1->3)-D-Galp2S.
Catalysis of the hydrolysis of DNA and polynucleotides, releasing free hypoxanthine.
Catalysis of the hydrolysis of DNA and polynucleotides, releasing free hypoxanthine.
Catalysis of the hydrolysis of DNA and polynucleotides, releasing free hypoxanthine.
Catalysis of the hydrolysis of DNA and polynucleotides, releasing free hypoxanthine.
Catalysis of the hydrolysis of DNA and polynucleotides, releasing free hypoxanthine.
Catalysis of the cleavage of the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue.
Catalysis of the cleavage of the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue.
Catalysis of the cleavage of the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue.
Catalysis of the cleavage of the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue.
Catalysis of the cleavage of the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue.
Catalysis of the cleavage of the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue.
Catalysis of the cleavage of the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue.
Catalysis of the reaction: 7-methylxanthosine + H(2)O = 7-methylxanthine + H(+) + ribofuranose.
Catalysis of the reaction: 7-methylxanthosine + H(2)O = 7-methylxanthine + H(+) + ribofuranose.
Catalysis of the reaction: 7-methylxanthosine + H(2)O = 7-methylxanthine + H(+) + ribofuranose.
Catalysis of the reaction: 7-methylxanthosine + H(2)O = 7-methylxanthine + H(+) + ribofuranose.
Catalysis of the reaction: 7-methylxanthosine + H(2)O = 7-methylxanthine + H(+) + ribofuranose.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
Catalysis of the reaction: cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.
The aggregation, arrangement and bonding together of proteins and RNA molecules to form a cytoplasmic mRNA processing body.
The aggregation, arrangement and bonding together of proteins and RNA molecules to form a cytoplasmic mRNA processing body.
The aggregation, arrangement and bonding together of proteins and RNA molecules to form a cytoplasmic mRNA processing body.
Catalysis of the reactions: 5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O = cholestane-3beta-5alpha,6beta-triol, and 5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O = cholestane-3beta-5alpha,6beta-triol.
Catalysis of the reactions: 5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O = cholestane-3beta-5alpha,6beta-triol, and 5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O = cholestane-3beta-5alpha,6beta-triol.
Catalysis of the reactions: 5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O = cholestane-3beta-5alpha,6beta-triol, and 5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O = cholestane-3beta-5alpha,6beta-triol.
Catalysis of the hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives.
Catalysis of the hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives.
Catalysis of the hydrolysis of the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side-chain.
Catalysis of the hydrolysis of the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side-chain.
Catalysis of the reaction: N-benzylformamide + H2O = formate + benzylamine.
Catalysis of the reaction: N-benzylformamide + H2O = formate + benzylamine.
The chemical reactions and pathways involving box C/D type small nucleolar RNA.
Catalysis of the reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.
Catalysis of the reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.
Catalysis of the reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.
Catalysis of the reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.
Catalysis of the reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.
Catalysis of the reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.
Catalysis of the reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.
Catalysis of the reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.
Catalysis of the reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.
Catalysis of the reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.
Catalysis of the reaction: 4-(L-gamma-glutamylamino)butanoate + H(2)O = 4-aminobutanoate + L-glutamate.
Catalysis of the reaction: 4-(L-gamma-glutamylamino)butanoate + H(2)O = 4-aminobutanoate + L-glutamate.
Catalysis of the reaction: 4-(L-gamma-glutamylamino)butanoate + H(2)O = 4-aminobutanoate + L-glutamate.
Catalysis of the reaction: 4-(L-gamma-glutamylamino)butanoate + H(2)O = 4-aminobutanoate + L-glutamate.
Catalysis of the reaction: 3-oxo-3-ureidopropanoate + H(2)O = H(+) + malonate + urea.
Catalysis of the reaction: 3-oxo-3-ureidopropanoate + H(2)O = H(+) + malonate + urea.
Catalysis of the reaction: 5-hydroxyisourate + H(2)O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+).
Catalysis of the reaction: 5-hydroxyisourate + H(2)O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+).
Catalysis of the reaction: 5-hydroxyisourate + H(2)O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+).
Catalysis of the reaction: amidinoproclavaminate + H(2)O = proclavaminate + urea.
Catalysis of the reaction: amidinoproclavaminate + H(2)O = proclavaminate + urea.
Catalysis of the reaction: amidinoproclavaminate + H(2)O = proclavaminate + urea.
Catalysis of the reaction: dCTP + 2 H(2)O = diphosphate + dUMP + H(+) + NH(4)(+).
Catalysis of the hydrolysis of mixed phospho-anhydride bonds.
Catalysis of the reaction: (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide.
Catalysis of the reaction: (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide.
Catalysis of the reaction: (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide.
Catalysis of the reaction: (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide.
Catalysis of the reaction: (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide.
Catalysis of the reactions: (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide, and (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide.
Catalysis of the reactions: (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide, and (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide.
Catalysis of the reactions: (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide, and (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide.
Catalysis of the reactions: (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide, and (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide.
Catalysis of the reactions: (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide, and (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide.
Catalysis of the reactions: (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide, and (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide.
Catalysis of the reactions: (S)-2-haloacid + H2O = (S)-2-hydroxyacid + halide, and (R)-2-haloacid + H2O = (R)-2-hydroxyacid + halide.
Catalysis of the reactions: (S)-2-haloacid + H2O = (S)-2-hydroxyacid + halide, and (R)-2-haloacid + H2O = (R)-2-hydroxyacid + halide.
Catalysis of the reactions: (S)-2-haloacid + H2O = (S)-2-hydroxyacid + halide, and (R)-2-haloacid + H2O = (R)-2-hydroxyacid + halide.
Catalysis of the reactions: (S)-2-haloacid + H2O = (S)-2-hydroxyacid + halide, and (R)-2-haloacid + H2O = (R)-2-hydroxyacid + halide.
Catalysis of the reaction: 3-phosphonopyruvate + H(2)O = phosphate + pyruvate.
The chemical reactions and pathways involving box H/ACA type small nucleolar RNA.
Catalysis of the reaction: 3-phosphonopyruvate + 2 H(+) = CO(2) + phosphonoacetaldehyde.
Catalysis of the reaction: 3-phosphonopyruvate + 2 H(+) = CO(2) + phosphonoacetaldehyde.
Catalysis of the reaction: D-dopachrome + H(+) = 5,6-dihydroxyindole + CO(2).
Catalysis of the reaction: D-dopachrome + H(+) = 5,6-dihydroxyindole + CO(2).
Catalysis of the reaction: D-dopachrome + H(+) = 5,6-dihydroxyindole + CO(2).
Catalysis of the reaction: D-dopachrome + H(+) = 5,6-dihydroxyindole + CO(2).
Catalysis of the reaction: D-dopachrome + H(+) = 5,6-dihydroxyindole + CO(2).
Catalysis of the reaction: D-dopachrome + H(+) = 5,6-dihydroxyindole + CO(2).
Catalysis of the reaction: D-dopachrome + H(+) = 5,6-dihydroxyindole + CO(2).
Catalysis of the reaction: D-dopachrome + H(+) = 5,6-dihydroxyindole + CO(2).
Catalysis of the reaction: 3-dehydro-L-gulonate 6-phosphate + H(+) = L-xylulose 5-phosphate + CO(2).
Catalysis of the reaction: 3-dehydro-L-gulonate 6-phosphate + H(+) = L-xylulose 5-phosphate + CO(2).
Catalysis of the reaction: 3-dehydro-L-gulonate 6-phosphate + H(+) = L-xylulose 5-phosphate + CO(2).
Catalysis of the reaction: 3-dehydro-L-gulonate 6-phosphate + H(+) = L-xylulose 5-phosphate + CO(2).
Catalysis of the reaction: 3-dehydro-L-gulonate 6-phosphate + H(+) = L-xylulose 5-phosphate + CO(2).
Catalysis of the reaction: 3-dehydro-L-gulonate 6-phosphate + H(+) = L-xylulose 5-phosphate + CO(2).
Catalysis of the reaction: 3-dehydro-L-gulonate 6-phosphate + H(+) = L-xylulose 5-phosphate + CO(2).
Catalysis of the reaction: L-2,4-diaminobutyrate + H(+) = 1,3-diaminopropane + CO(2).
Catalysis of the reaction: L-2,4-diaminobutyrate + H(+) = 1,3-diaminopropane + CO(2).
Catalysis of the reaction: L-2,4-diaminobutyrate + H(+) = 1,3-diaminopropane + CO(2).
Catalysis of the reaction: L-2,4-diaminobutyrate + H(+) = 1,3-diaminopropane + CO(2).
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
Catalysis of the reaction: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate.
The volume enclosed by the membranes of an acidocalcisome.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a methanol stimulus.
Catalysis of the reaction: 2,7,4'-trihydroxyisoflavanone = daidzein + H2O.
Catalysis of the reaction: 2,7,4'-trihydroxyisoflavanone = daidzein + H2O.
Catalysis of the reaction: 7alpha,12alpha-dihydroxy-3-oxochol-4-en-24-oate = 12alpha-hydroxy-3-oxochola-4,6-dien-24-oate + H(2)O.
Catalysis of the reaction: 7alpha,12alpha-dihydroxy-3-oxochol-4-en-24-oate = 12alpha-hydroxy-3-oxochola-4,6-dien-24-oate + H(2)O.
Catalysis of the reaction: 7alpha,12alpha-dihydroxy-3-oxochol-4-en-24-oate = 12alpha-hydroxy-3-oxochola-4,6-dien-24-oate + H(2)O.
Catalysis of the reaction: (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O.
Catalysis of the reaction: (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O.
Catalysis of the reaction: (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O.
Catalysis of the reaction: (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O.
Catalysis of the reaction: N(4)-acetyl-L-2,4-diaminobutyrate = ectoine + H(2)O.
Catalysis of the reaction: N(4)-acetyl-L-2,4-diaminobutyrate = ectoine + H(2)O.
Catalysis of the reaction: N(4)-acetyl-L-2,4-diaminobutyrate = ectoine + H(2)O.
Catalysis of the reaction: N(4)-acetyl-L-2,4-diaminobutyrate = ectoine + H(2)O.
Catalysis of the reaction: N(4)-acetyl-L-2,4-diaminobutyrate = ectoine + H(2)O.
Catalysis of the reaction: N(4)-acetyl-L-2,4-diaminobutyrate = ectoine + H(2)O.
Catalysis of the reactions: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O; (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O and (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one.
Catalysis of the reactions: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O; (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O and (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one.
Catalysis of the reactions: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O; (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O and (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one.
Catalysis of the reactions: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O; (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O and (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one.
Catalysis of the reaction: 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O.
Catalysis of the reaction: 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O.
Catalysis of the reaction: 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O.
Catalysis of the reaction: 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O.
Catalysis of the reaction: 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O.
Catalysis of the reaction: 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O.
Catalysis of the reaction: 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipid stimulus.
Catalysis of the reaction: (1->4)-beta-D-glucuronan = an oligosaccharide with 4-deoxy-beta-D-gluc-4-enuronosyl end + (1->4)-beta-D-glucuronan. This reaction is the eliminative cleavage of (1->4)-beta-D-glucuronans to give oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.
Catalysis of the reaction: an N-acetylneuraminate glycoside = 2,7-anhydro-alpha-N-acetylneuraminate + an alpha-sialyl group. This reaction is the elimination of alpha-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate.
Catalysis of the reaction: an N-acetylneuraminate glycoside = 2,7-anhydro-alpha-N-acetylneuraminate + an alpha-sialyl group. This reaction is the elimination of alpha-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate.
Catalysis of the reaction: an N-acetylneuraminate glycoside = 2,7-anhydro-alpha-N-acetylneuraminate + an alpha-sialyl group. This reaction is the elimination of alpha-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate.
Catalysis of the reaction: an N-acetylneuraminate glycoside = 2,7-anhydro-alpha-N-acetylneuraminate + an alpha-sialyl group. This reaction is the elimination of alpha-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate.
Catalysis of the reaction: beta-D-fructopyranosyl-(2->6)-[D-fructofuranosyl-(2->6)]n-D-fructofuranoside = beta-D-fructopyranosyl-(2->6)-[D-fructofuranosyl-(2->6)](n-1)-D-fructofuranoside + di-beta-D-fructofuranose 2,6':2',6-dianhydride. This reaction is the production of di-beta-D-fructofuranose 2,6':2',6-dianhydride (DFA IV) by successively eliminating the diminishing (2->6)-beta-D-fructan (levan) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: beta-D-fructopyranosyl-(2->6)-[D-fructofuranosyl-(2->6)]n-D-fructofuranoside = beta-D-fructopyranosyl-(2->6)-[D-fructofuranosyl-(2->6)](n-1)-D-fructofuranoside + di-beta-D-fructofuranose 2,6':2',6-dianhydride. This reaction is the production of di-beta-D-fructofuranose 2,6':2',6-dianhydride (DFA IV) by successively eliminating the diminishing (2->6)-beta-D-fructan (levan) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: beta-D-fructopyranosyl-(2->6)-[D-fructofuranosyl-(2->6)]n-D-fructofuranoside = beta-D-fructopyranosyl-(2->6)-[D-fructofuranosyl-(2->6)](n-1)-D-fructofuranoside + di-beta-D-fructofuranose 2,6':2',6-dianhydride. This reaction is the production of di-beta-D-fructofuranose 2,6':2',6-dianhydride (DFA IV) by successively eliminating the diminishing (2->6)-beta-D-fructan (levan) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose-beta-D-fructofuranose 1,2':1,2'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose-beta-D-fructofuranose 1,2':1,2'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose-beta-D-fructofuranose 1,2':1,2'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose-beta-D-fructofuranose 1,2':1,2'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose-beta-D-fructofuranose 1,2':1,2'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Catalysis of the reaction: dermatan sulfate = n 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 4-sulfate. This reaction is the eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (DeltaUA-GalNAC-4S). Chondroitin sulfate B is also known as dermatan sulfate.
Catalysis of the reaction: dermatan sulfate = n 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 4-sulfate. This reaction is the eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (DeltaUA-GalNAC-4S). Chondroitin sulfate B is also known as dermatan sulfate.
Catalysis of the reaction: dermatan sulfate = n 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 4-sulfate. This reaction is the eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (DeltaUA-GalNAC-4S). Chondroitin sulfate B is also known as dermatan sulfate.
Catalysis of the reaction: dermatan sulfate = n 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 4-sulfate. This reaction is the eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (DeltaUA-GalNAC-4S). Chondroitin sulfate B is also known as dermatan sulfate.
Catalysis of the endolytic cleavage of beta-1,4-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides.
Catalysis of the endolytic cleavage of beta-1,4-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides.
Catalysis of the endolytic cleavage of beta-1,4-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides.
Catalysis of the endolytic cleavage of beta-1,4-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides.
Catalysis of the endolytic cleavage of beta-1,4-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides.
Catalysis of the endolytic cleavage of beta-1,4-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides.
Catalysis of the endolytic cleavage of beta-1,4-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides.
Catalysis of the endolytic cleavage of beta-1,4-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides.
Catalysis of the exolytic cleavage of disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments.
Catalysis of the exolytic cleavage of disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments.
Catalysis of the exolytic cleavage of disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments.
Catalysis of the exolytic cleavage of disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments.
Catalysis of the exolytic cleavage of disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments.
Catalysis of the exolytic cleavage of disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments.
Catalysis of the exolytic cleavage of disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments.
Catalysis of the exolytic cleavage of disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments.
Catalysis of the reaction: geranyl diphosphate = (4R)-limonene + diphosphate.
Catalysis of the reaction: geranyl diphosphate = (4R)-limonene + diphosphate.
Catalysis of the reaction: geranyl diphosphate = (4R)-limonene + diphosphate.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = diphosphate + vetispiradiene.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = diphosphate + vetispiradiene.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = diphosphate + vetispiradiene.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = diphosphate + vetispiradiene.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = diphosphate + vetispiradiene.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate + H2O = (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = (+)-(R)-germacrene A + diphosphate.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = (+)-(R)-germacrene A + diphosphate.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = (+)-(R)-germacrene A + diphosphate.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = (+)-(R)-germacrene A + diphosphate.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = (+)-(R)-germacrene A + diphosphate.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = (+)-(R)-germacrene A + diphosphate.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = amorpha-4,11-diene + diphosphate.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = amorpha-4,11-diene + diphosphate.
Catalysis of the reaction: geranyl diphosphate + H(2)O = (S)-linalool + diphosphate.
Catalysis of the reaction: geranyl diphosphate + H(2)O = (S)-linalool + diphosphate.
Catalysis of the reaction: geranyl diphosphate + H(2)O = (S)-linalool + diphosphate.
Catalysis of the reaction: geranyl diphosphate + H(2)O = (R)-linalool + diphosphate.
Catalysis of the reaction: geranyl diphosphate + H(2)O = (R)-linalool + diphosphate.
Catalysis of the reaction: geranyl diphosphate + H(2)O = (R)-linalool + diphosphate.
Catalysis of the reaction: dimethylallyl diphosphate = diphosphate + isoprene.
Catalysis of the reaction: dimethylallyl diphosphate = diphosphate + isoprene.
Catalysis of the reaction: dimethylallyl diphosphate = diphosphate + isoprene.
Catalysis of the reaction: 3-sulfolactate = pyruvate + sulfite.
Catalysis of the reaction: 3-sulfolactate = pyruvate + sulfite.
Catalysis of the reaction: 3-sulfolactate = pyruvate + sulfite.
Catalysis of the reaction: 3-sulfolactate = pyruvate + sulfite.
Catalysis of the reaction: L-cysteate + H(2)O = NH(4)(+) + pyruvate + sulfite.
Catalysis of the reaction: L-cysteate + H(2)O = NH(4)(+) + pyruvate + sulfite.
Catalysis of the reaction: L-cysteate + H(2)O = NH(4)(+) + pyruvate + sulfite.
Catalysis of the reaction: FAD = AMP + riboflavin cyclic-4',5'-phosphate.
Catalysis of the reaction: FAD = AMP + riboflavin cyclic-4',5'-phosphate.
Catalysis of the reaction: FAD = AMP + riboflavin cyclic-4',5'-phosphate.
Catalysis of the reaction: an aliphatic aldoxime = an aliphatic nitrile + H2O.
Catalysis of the reaction: an aliphatic aldoxime = an aliphatic nitrile + H2O.
Catalysis of the reaction: an aliphatic aldoxime = an aliphatic nitrile + H2O.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a triglyceride stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a triglyceride stimulus.
Catalysis of the reaction: L-ribulose 5-phosphate = L-xylulose 5-phosphate.
Catalysis of the reaction: L-ribulose 5-phosphate = L-xylulose 5-phosphate.
Catalysis of the reaction: L-ribulose 5-phosphate = L-xylulose 5-phosphate.
Catalysis of the reaction: all-cis-icosa-5,8,11,14,17-pentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate.
Catalysis of the reaction: all-cis-icosa-5,8,11,14,17-pentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate.
Catalysis of the reaction: all-cis-icosa-5,8,11,14,17-pentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate.
Catalysis of the reaction: all-cis-icosa-5,8,11,14,17-pentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate.
Catalysis of the reaction: all-cis-icosa-5,8,11,14,17-pentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate.
Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein].
Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein].
Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein].
Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein].
Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein].
Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein].
Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein].
Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein].
Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein].
Catalysis of the reaction: 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose.
Catalysis of the reaction: 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose.
Catalysis of the reaction: 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose.
Catalysis of the reaction: 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose.
Catalysis of the reaction: 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose.
Catalysis of the reaction: 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose.
Catalysis of the reaction: 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose.
Catalysis of the reaction: antheraxanthin = capsanthin.
Catalysis of the reaction: antheraxanthin = capsanthin.
Catalysis of the reaction: antheraxanthin = capsanthin.
Catalysis of the reaction: violaxanthin = capsorubin.
Catalysis of the reaction: violaxanthin = capsorubin.
Catalysis of the reaction: violaxanthin = capsorubin.
Catalysis of the reaction: violaxanthin = capsorubin.
Catalysis of the reaction: all-trans-violaxanthin = all-trans-neoxanthin.
Catalysis of the reaction: all-trans-violaxanthin = all-trans-neoxanthin.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a silicon dioxide stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a silicon dioxide stimulus.
Catalysis of the reaction: 3-hydroxyaminophenol = aminohydroquinone.
Catalysis of the reaction: 3-hydroxyaminophenol = aminohydroquinone.
Catalysis of the reaction: 3-hydroxyaminophenol = aminohydroquinone.
Catalysis of the reaction: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
Catalysis of the reaction: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
Catalysis of the reaction: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
Catalysis of the reaction: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
Catalysis of the reaction: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
Catalysis of the reaction: L-glutamate + ATP + putrescine = gamma-L-glutamylputrescine + ADP + 2 H(+) + phosphate.
Catalysis of the reaction: L-glutamate + ATP + putrescine = gamma-L-glutamylputrescine + ADP + 2 H(+) + phosphate.
Catalysis of the reaction: L-glutamate + ATP + putrescine = gamma-L-glutamylputrescine + ADP + 2 H(+) + phosphate.
Catalysis of the reaction: ATP + D-aspartate + [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate.
Catalysis of the reaction: ATP + D-aspartate + [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate.
Catalysis of the reaction: ATP + D-aspartate + [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate.
Catalysis of the reaction: ATP + D-aspartate + [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + ADP + phosphate.
Catalysis of the reaction: ATP + an L-amino acid + an L-amino acid = ADP + phosphate + L-aminoacyl-L-amino acid.
Catalysis of the reaction: ATP + an L-amino acid + an L-amino acid = ADP + phosphate + L-aminoacyl-L-amino acid.
Catalysis of the reaction: ATP + an L-amino acid + an L-amino acid = ADP + phosphate + L-aminoacyl-L-amino acid.
Catalysis of the reaction: ATP + an L-amino acid + an L-amino acid = ADP + phosphate + L-aminoacyl-L-amino acid.
Catalysis of the reaction: N(2)-(2-carboxyethyl)-L-arginine + ATP = AMP + deoxyamidinoproclavaminate + diphosphate + 2 H(+).
Catalysis of the reaction: N(2)-(2-carboxyethyl)-L-arginine + ATP = AMP + deoxyamidinoproclavaminate + diphosphate + 2 H(+).
Catalysis of the reaction: N(2)-(2-carboxyethyl)-L-arginine + ATP = AMP + deoxyamidinoproclavaminate + diphosphate + 2 H(+).
Catalysis of the reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole + ATP + bicarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 3 H(+) + phosphate.
Catalysis of the reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole + ATP + bicarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 3 H(+) + phosphate.
Catalysis of the reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole + ATP + bicarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 3 H(+) + phosphate.
Catalysis of the reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole + ATP + bicarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 3 H(+) + phosphate.
Catalysis of the reaction: 2-oxoglutarate + ATP + bicarbonate = ADP + 2 H(+) + oxalosuccinate + phosphate.
Catalysis of the reaction: 2-oxoglutarate + ATP + bicarbonate = ADP + 2 H(+) + oxalosuccinate + phosphate.
Catalysis of the reaction: 2-oxoglutarate + ATP + bicarbonate = ADP + 2 H(+) + oxalosuccinate + phosphate.
Catalysis of the reaction: 2-oxoglutarate + ATP + bicarbonate = ADP + 2 H(+) + oxalosuccinate + phosphate.
The chemical reactions and pathways resulting in the formation of a ribonucleoside bisphosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a ribonucleoside bisphosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a ribonucleoside bisphosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a ribonucleoside bisphosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the breakdown of a ribonucleoside bisphosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the breakdown of a ribonucleoside bisphosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the breakdown of a ribonucleoside bisphosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways involving a purine nucleoside bisphosphate, a compound consisting of a purine base linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a purine nucleoside bisphosphate, a compound consisting of a purine base linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a purine nucleoside bisphosphate, a compound consisting of a purine base linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a purine nucleoside bisphosphate, a compound consisting of a purine base linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a purine nucleoside bisphosphate, a compound consisting of a purine base linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the breakdown of a purine nucleoside bisphosphate, a compound consisting of a purine base linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the breakdown of a purine nucleoside bisphosphate, a compound consisting of a purine base linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the breakdown of a purine nucleoside bisphosphate, a compound consisting of a purine base linked to a deoxyribose or ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways involving a purine ribonucleoside bisphosphate, a compound consisting of a purine base linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a purine ribonucleoside bisphosphate, a compound consisting of a purine base linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a purine ribonucleoside bisphosphate, a compound consisting of a purine base linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a purine ribonucleoside bisphosphate, a compound consisting of a purine base linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the formation of a purine ribonucleoside bisphosphate, a compound consisting of a purine base linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the breakdown of a purine ribonucleoside bisphosphate, a compound consisting of a purine base linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the breakdown of a purine ribonucleoside bisphosphate, a compound consisting of a purine base linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
The chemical reactions and pathways resulting in the breakdown of a purine ribonucleoside bisphosphate, a compound consisting of a purine base linked to a ribose sugar esterified with one phosphate group attached to each of two different hydroxyl groups on the sugar.
Catalysis of the removal of 8-oxo-7,8-dihydroguanine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + lipid(in) = ADP + phosphate + lipid(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + sterol(in) = ADP + phosphate + sterol(out).
Catalysis of the removal of 5-formyluracil bases by cleaving the N-C1' glycosidic bond between the oxidized pyrimidine and the deoxyribose sugar.
Catalysis of the removal of 5-hydroxymethyluracil bases by cleaving the N-C1' glycosidic bond between the oxidized pyrimidine and the deoxyribose sugar.
A protein complex that forms a coat structure on vesicles involved in exocytosis of proteins from the trans-Golgi network to the cell surface; in Saccharomyces, the complex contains Chs5p, Chs6p, and Chs6p paralogues.
A cellular membrane associated with the phagophore assembly site.
A cellular membrane associated with the phagophore assembly site.
A cellular membrane associated with the phagophore assembly site.
A cellular membrane associated with the phagophore assembly site.
Interacting selectively and non-covalently with a sequence of guanine residues in an RNA molecule.
Interacting selectively and non-covalently with a sequence of guanine residues in an RNA molecule.
Cell death in a host resulting from activation of host endogenous cellular processes after direct or indirect interaction with a symbiont (defined as the smaller of two, or more, organisms engaged in symbiosis, a close interaction encompassing mutualism through parasitism). An example of direct interaction is contact with penetrating hyphae of a fungus; an example of indirect interaction is encountering symbiont-secreted molecules.
Any process that stops, prevents, or reduces the frequency, rate or extent of the hypersensitive response in a plant.
Any process that stops, prevents, or reduces the frequency, rate or extent of the hypersensitive response in a plant.
Any process that stops, prevents, or reduces the frequency, rate or extent of the hypersensitive response in a plant.
Any process that stops, prevents, or reduces the frequency, rate or extent of the hypersensitive response in a plant.
Any process that stops, prevents, or reduces the frequency, rate or extent of the hypersensitive response in a plant.
Any process that stops, prevents, or reduces the frequency, rate or extent of the hypersensitive response in a plant.
Any process that stops, prevents, or reduces the frequency, rate or extent of the hypersensitive response in a plant.
Any process that activates or increases the frequency, rate or extent of the hypersensitive response in a plant.
Any process that activates or increases the frequency, rate or extent of the hypersensitive response in a plant.
Any process that activates or increases the frequency, rate or extent of the hypersensitive response in a plant.
Any process that activates or increases the frequency, rate or extent of the hypersensitive response in a plant.
Any process that activates or increases the frequency, rate or extent of the hypersensitive response in a plant.
Any process that activates or increases the frequency, rate or extent of the hypersensitive response in a plant.
Any process that activates or increases the frequency, rate or extent of the hypersensitive response in a plant.
Any process that activates or increases the frequency, rate or extent of the hypersensitive response in a plant.
Any process in which an organism modulates the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism modulates the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism modulates the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism modulates the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism modulates the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates or increases the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates or increases the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates or increases the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates or increases the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates or increases the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates or increases the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates or increases the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates or increases the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates or increases the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates or increases the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates or increases the frequency, rate or extent of defense-related programmed cell death in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Interacting selectively and non-covalently with the estrogen response element (ERE), a conserved sequence found in the promoters of genes whose expression is regulated in response to estrogen.
Facilitates the displacement of one strand of an RNA-RNA duplex and its replacement with a different strand of higher complementarity.
The homotypic fusion of endocytic vesicles to form or add to an early endosome.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating a decline in oxygen levels to trace amounts, <0.1%.
The space enclosed by the double membrane of a cyanelle.
Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a nucleic acid template and a 3'hydroxyl group.
Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a nucleic acid template and a 3'hydroxyl group.
Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a nucleic acid template and a 3'hydroxyl group.
Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a nucleic acid template and a 3'hydroxyl group.
Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a nucleic acid template and a 3'hydroxyl group.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
The aggregation, arrangement and bonding together of proteins and RNA molecules to form a stress granule.
A protein complex that contains the transcription factor Ste11 and the RNA binding protein Mei2; involved in regulation of conjugation in fission yeast.
A protein complex that acts as a nucleotide exchange factor for the GTPase Ypt6p, and is required for fusion of endosome-derived vesicles with the Golgi.
A process in which a protein is transported to, or maintained in, a location within the Golgi apparatus.
A process in which a protein is transported to, or maintained in, a location within the Golgi apparatus.
A process in which a protein is transported to, or maintained in, a location within the Golgi apparatus.
A process in which a protein is transported to, or maintained in, a location within the Golgi apparatus.
A process in which a protein is transported to, or maintained in, a location within the Golgi apparatus.
A process in which a protein is transported to, or maintained in, a location within the Golgi apparatus.
A process in which a protein is transported to, or maintained in, a location within the Golgi apparatus.
A process in which a protein is transported to, or maintained in, a location within the Golgi apparatus.
A process in which a protein is transported to, or maintained in, a location within the Golgi apparatus.
A process in which a protein is transported to, or maintained in, a location within the Golgi apparatus.
Catalysis of the reaction: nucleoside triphosphate + aminoglycoside = diphosphate + nucleotidylaminoglycoside.
Catalysis of the reaction: nucleoside triphosphate + aminoglycoside = diphosphate + nucleotidylaminoglycoside.
Catalysis of the reaction: nucleoside triphosphate + aminoglycoside = diphosphate + nucleotidylaminoglycoside.
Catalysis of the reaction: nucleoside triphosphate + aminoglycoside = diphosphate + nucleotidylaminoglycoside.
Catalysis of the reaction: nucleoside triphosphate + aminoglycoside = diphosphate + nucleotidylaminoglycoside.
Catalysis of the reaction: nucleoside triphosphate + aminoglycoside = diphosphate + nucleotidylaminoglycoside.
Catalysis of the reaction: acetyl-CoA + aminoglycoside = CoA + N-acetylaminoglycoside.
Catalysis of the reaction: acetyl-CoA + aminoglycoside = CoA + 1-N-acetylaminoglycoside. This is acetylation of the 1-amino group of the central deoxystreptamine ring.
Catalysis of the reaction: ATP + aminoglycoside = ADP + phosphoaminoglycoside.
Catalysis of the reaction: squalene = triterpene.
Catalysis of the reaction: squalene = tetrahymanol.
Catalysis of the reaction: oxidosqualene = marneral.
Catalysis of the reaction: oxidosqualene + H2O = arabidiol ((13R,14R,17E)-malabarica-17,21-diene-3beta,14-diol).
Catalysis of the reaction: oxidosqualene = cucurbitadienol.
The chemical reactions and pathways involving butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways involving butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways involving butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the breakdown of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the breakdown of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the breakdown of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the breakdown of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the breakdown of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the breakdown of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the formation of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the formation of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the formation of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the formation of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the formation of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The chemical reactions and pathways resulting in the formation of butanediol; the biologically relevant isomer is 2,3-butanediol, CH3CH(OH)CH(OH)CH3.
The formation of nucleosomes containing the histone H3 variant CENP-A to form centromeric chromatin. This specialised chromatin occurs at centromeric region in point centromeres,  and the central core in modular centromeres.
The formation of nucleosomes containing the histone H3 variant CENP-A to form centromeric chromatin. This specialised chromatin occurs at centromeric region in point centromeres,  and the central core in modular centromeres.
The formation of nucleosomes containing the histone H3 variant CENP-A to form centromeric chromatin. This specialised chromatin occurs at centromeric region in point centromeres,  and the central core in modular centromeres.
The formation of nucleosomes containing the histone H3 variant CENP-A to form centromeric chromatin. This specialised chromatin occurs at centromeric region in point centromeres,  and the central core in modular centromeres.
The formation of nucleosomes containing the histone H3 variant CENP-A to form centromeric chromatin. This specialised chromatin occurs at centromeric region in point centromeres,  and the central core in modular centromeres.
The formation of nucleosomes containing the histone H3 variant CENP-A to form centromeric chromatin. This specialised chromatin occurs at centromeric region in point centromeres,  and the central core in modular centromeres.
The formation of nucleosomes containing the histone H3 variant CENP-A to form centromeric chromatin. This specialised chromatin occurs at centromeric region in point centromeres,  and the central core in modular centromeres.
The formation of nucleosomes containing the histone H3 variant CENP-A to form centromeric chromatin. This specialised chromatin occurs at centromeric region in point centromeres,  and the central core in modular centromeres.
The formation of nucleosomes containing the histone H3 variant CENP-A to form centromeric chromatin. This specialised chromatin occurs at centromeric region in point centromeres,  and the central core in modular centromeres.
A polyketide synthase complex that consists of several different polypeptide chains, each of which catalyzes a single reaction.
A polyketide synthase complex that consists of several different polypeptide chains, each of which catalyzes a single reaction.
A polyketide synthase complex that consists of several different polypeptide chains, each of which catalyzes a single reaction.
A polyketide synthase complex that consists of two identical ketosynthase polypeptides.
A polyketide synthase complex that consists of two identical ketosynthase polypeptides.
A polyketide synthase complex that consists of two identical ketosynthase polypeptides.
Catalysis of the hydrolysis of an acetyl group or groups from an acetylated sterol.
The process in which the sister chromatids of a replicated chromosome become associated with each other during S phase.
The process in which the association between sister chromatids of a replicated chromosome is maintained as chromosomes condense, attach to the spindle in a bipolar orientation, and congress to the metaphase plate.
The process in which the sister chromatids of a replicated chromosome become joined along the entire length of the chromosome during S phase during a mitotic cell cycle.
The process in which the association between sister chromatids of a replicated chromosome is maintained as chromosomes condense, attach to the spindle in a bipolar orientation, and congress to the metaphase plate during a mitotic cell cycle.
The process in which the sister chromatids of a replicated chromosome become joined along the entire length of the chromosome during S phase during a meiotic cell cycle.
The process in which the association between sister chromatids of a replicated chromosome is maintained as chromosomes condense, attach to the spindle in a bipolar orientation, and congress to the metaphase plate during a meiotic cell cycle.
Any process that modulates the extent to which the association between sister chromatids of a replicated chromosome is maintained.
Any process that decreases the extent to which the association between sister chromatids of a replicated chromosome is maintained.
Any process that increases the extent to which the association between sister chromatids of a replicated chromosome is maintained.
Any process that modulates the extent to which the association between sister chromatids of a replicated chromosome is maintained during a meiotic cell cycle.
Any process that decreases the extent to which the association between sister chromatids of a replicated chromosome is maintained during a meiotic cell cycle.
Any process that increases the extent to which the association between sister chromatids of a replicated chromosome is maintained during a meiotic cell cycle.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cytokine stimulus.
A multiprotein ATPase complex required for the efficient dislocation of ER-lumenal degradation substrates, and their subsequent proteolysis by the proteasome. In budding yeast, this complex includes Cdc48p, Npl4p and Ufd1p proteins. In mammals, this complex includes a hexamer of VCP/p97 (a cytosolic ATPase) and trimers of each of its cofactors UFD1L and NPL4 (NPLOC4) (e.g. a 6:3:3 stoichiometry).
A multiprotein ATPase complex required for the efficient dislocation of ER-lumenal degradation substrates, and their subsequent proteolysis by the proteasome. In budding yeast, this complex includes Cdc48p, Npl4p and Ufd1p proteins. In mammals, this complex includes a hexamer of VCP/p97 (a cytosolic ATPase) and trimers of each of its cofactors UFD1L and NPL4 (NPLOC4) (e.g. a 6:3:3 stoichiometry).
A multiprotein complex that recognizes ERAD-luminal misfolded substrates and brings them to the ubiquitination/extraction machinery. In yeast, this complex consists of Yos9p, Kar2p and Hrd3p proteins.
Any process of regulating the production and elimination of erythrocytes within an organism.
Any process of regulating the production and elimination of erythrocytes within an organism.
The selective elimination of erythrocytes from the body by autoregulatory mechanisms.
The selective elimination of erythrocytes from the body by autoregulatory mechanisms.
The selective elimination of erythrocytes from the body by autoregulatory mechanisms.
Any process that modulates the frequency, rate, or extent of tissue remodeling.
Any process that stops, prevents, or reduces the frequency, rate, or extent of tissue remodeling.
Any process that activates or increases the frequency, rate, or extent of tissue remodeling.
Any process that modulates the frequency, rate, or extent of erythrocyte clearance.
Any process that modulates the frequency, rate, or extent of erythrocyte clearance.
Any process that modulates the frequency, rate, or extent of erythrocyte clearance.
Any process that stops, prevents, or reduces the frequency, rate, or extent of erythrocyte clearance.
Any process that stops, prevents, or reduces the frequency, rate, or extent of erythrocyte clearance.
Any process that stops, prevents, or reduces the frequency, rate, or extent of erythrocyte clearance.
Any process that activates or increases the frequency, rate, or extent of erythrocyte clearance.
Any process that activates or increases the frequency, rate, or extent of erythrocyte clearance.
Any process that activates or increases the frequency, rate, or extent of erythrocyte clearance.
The attachment of a cell to a second cell of the identical type via adhesion molecules.
Any process that modulates the frequency, rate, or extent of homotypic cell-cell adhesion.
Any process that stops, prevents, or reduces the frequency, rate, or extent of homotypic cell-cell adhesion.
Any process that activates or increases the frequency, rate, or extent of homotypic cell-cell adhesion.
The attachment of a cell to a cell of a different type via adhesion molecules.
Any process that modulates the frequency, rate, or extent of heterotypic cell-cell adhesion.
Any process that stops, prevents, or reduces the frequency, rate, or extent of heterotypic cell-cell adhesion.
Any process that activates or increases the frequency, rate, or extent of heterotypic cell-cell adhesion.
The adhesion of one erythrocyte to one or more other erythrocytes via adhesion molecules.
The adhesion of one erythrocyte to one or more other erythrocytes via adhesion molecules.
Any process that modulates the frequency, rate, or extent of erythrocyte aggregation.
Any process that modulates the frequency, rate, or extent of erythrocyte aggregation.
Any process that stops, prevents, or reduces the frequency, rate, or extent of erythrocyte aggregation.
Any process that stops, prevents, or reduces the frequency, rate, or extent of erythrocyte aggregation.
Any process that activates or increases the frequency, rate, or extent of erythrocyte aggregation.
Any process that activates or increases the frequency, rate, or extent of erythrocyte aggregation.
Any process that modulates the frequency, rate, or extent of toll-like receptor signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor signaling pathway.
Any process that modulates the frequency, rate, or extent of MyD88-dependent toll-like receptor signaling pathway.
Any process that modulates the frequency, rate, or extent of MyD88-dependent toll-like receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of MyD88-dependent toll-like receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of MyD88-dependent toll-like receptor signaling pathway.
Any process that activates or increases the frequency, rate, or extent of MyD88-dependent toll-like receptor signaling pathway.
Any process that activates or increases the frequency, rate, or extent of MyD88-dependent toll-like receptor signaling pathway.
Any process that modulates the frequency, rate, or extent of MyD88-independent toll-like receptor signaling pathway.
Any process that modulates the frequency, rate, or extent of MyD88-independent toll-like receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of MyD88-independent toll-like receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of MyD88-independent toll-like receptor signaling pathway.
Any process that activates or increases the frequency, rate, or extent of MyD88-independent toll-like receptor signaling pathway.
Any process that activates or increases the frequency, rate, or extent of MyD88-independent toll-like receptor signaling pathway.
Any process that activates or increases the frequency, rate, or extent of MyD88-independent toll-like receptor signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 1.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 1.
Any process that modulates the frequency, rate, or extent of toll-like receptor 1 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 1 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 1 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 1 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 1 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 1 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 2.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 2.
Any process that modulates the frequency, rate, or extent of toll-like receptor 2 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 2 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 2 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 2 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 2 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 2 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 3.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 3.
Any process that modulates the frequency, rate, or extent of toll-like receptor 3 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 3 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 3 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 3 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 3 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 3 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 4.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 4.
Any process that modulates the frequency, rate, or extent of toll-like receptor 4 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 4 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 4 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 4 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 4 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 4 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 5.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 5.
Any process that modulates the frequency, rate, or extent of toll-like receptor 5 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 5 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 5 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 5 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 5 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 5 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 6.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 6.
Any process that modulates the frequency, rate, or extent of toll-like receptor 6 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 6 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 6 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 6 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 6 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 6 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 7.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 7.
Any process that modulates the frequency, rate, or extent of toll-like receptor 7 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 7 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 7 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 7 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 7 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 7 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 8.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 8.
Any process that modulates the frequency, rate, or extent of toll-like receptor 8 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 8 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 8 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 8 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 8 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 8 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 9.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 9.
Any process that modulates the frequency, rate, or extent of toll-like receptor 9 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 9 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 9 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 9 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 9 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 9 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 10.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 10.
Any process that modulates the frequency, rate, or extent of toll-like receptor 10 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 10 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 10 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 10 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 10 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 10 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 11.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 11.
Any process that modulates the frequency, rate, or extent of toll-like receptor 11 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 11 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 11 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 11 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 11 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 11 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 12.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 12.
Any process that modulates the frequency, rate, or extent of toll-like receptor 12 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 12 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 12 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 12 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 12 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 12 signaling pathway.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 13.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 13.
Any process that modulates the frequency, rate, or extent of toll-like receptor 13 signaling pathway.
Any process that modulates the frequency, rate, or extent of toll-like receptor 13 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 13 signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate, or extent of toll-like receptor 13 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 13 signaling pathway.
Any process that activates or increases the frequency, rate, or extent of toll-like receptor 13 signaling pathway.
Any process that modulates the extent to which the association between sister chromatids of a replicated chromosome is maintained during a mitotic cell cycle.
Any process that decreases the extent to which the association between sister chromatids of a replicated chromosome is maintained during a mitotic cell cycle.
Any process that increases the extent to which the association between sister chromatids of a replicated chromosome is maintained during a mitotic cell cycle.
Interacting selectively and non-covalently with an apolipoprotein, the protein component of a lipoprotein complex.
Interacting selectively and non-covalently with apolipoprotein A-I.
Combining with apolipoprotein A-I and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Interacting selectively and non-covalently with a very-low-density lipoprotein particle, a triglyceride-rich lipoprotein particle that is typically composed of APOB100, APOE and APOCs and has a density of about 1.006 g/ml and a diameter of between 20-80 nm.
Interacting selectively and non-covalently with a very-low-density lipoprotein particle, a triglyceride-rich lipoprotein particle that is typically composed of APOB100, APOE and APOCs and has a density of about 1.006 g/ml and a diameter of between 20-80 nm.
Interacting selectively and non-covalently with an apolipoprotein receptor.
Interacting selectively and non-covalently with an apolipoprotein A-I receptor.
The chemical reactions and pathways involving D-galactonate, the anion of D-galactonic acid.
The chemical reactions and pathways involving L-galactonate, the anion of L-galactonic acid.
The chemical reactions and pathways resulting in the breakdown of D-galactonate, the anion of D-galactonic acid.
The chemical reactions and pathways resulting in the breakdown of D-galactonate, the anion of D-galactonic acid.
The chemical reactions and pathways resulting in the breakdown of D-galactonate, the anion of D-galactonic acid.
The chemical reactions and pathways resulting in the breakdown of L-galactonate, the anion of L-galactonic acid.
The chemical reactions and pathways resulting in the breakdown of L-galactonate, the anion of L-galactonic acid.
The chemical reactions and pathways resulting in the breakdown of L-galactonate, the anion of L-galactonic acid.
The directed movement of an acylglycerol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. An acylglycerol is any mono-, di- or triester of glycerol with (one or more) fatty acids.
The directed movement of triglyceride into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Triglycerides are important components of plant oils, animal fats and animal plasma lipoproteins.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of amino acids.
Any process that initiates the activity of the inactive enzyme protein kinase A.
Catalysis of the reaction: D-beta-D-heptose 1,7-bisphosphate + H2O = D-beta-D-heptose 1-phosphate + phosphate.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an oleic acid stimulus.
Catalysis of the movement of glycolipids from one membrane face to the other (glycolipid 'flippase' activity).
The translocation, or flipping, of glycolipid molecules from one monolayer of a membrane bilayer to the opposite monolayer.
The translocation, or flipping, of glycolipid molecules from one monolayer of a membrane bilayer to the opposite monolayer.
The translocation, or flipping, of lipid molecules from one monolayer of a membrane bilayer to the opposite monolayer.
The generation of amyloid-beta by cleavage of the amyloid precursor protein (APP).
The generation of amyloid-beta by cleavage of the amyloid precursor protein (APP).
The generation of amyloid-beta by cleavage of the amyloid precursor protein (APP).
A protein-DNA complex formed by the association of a distinct set of general and specific transcription factors with a region of enhancer DNA. The cooperative assembly of an enhanceosome confers specificity of transcriptional regulation.
The addition of an acetyl group to a steroid molecule. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid.
The removal of an acetyl group from a steroid molecule. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid.
The addition of an acetyl group to a sterol molecule. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid.
The removal of an acetyl group from a sterol molecule. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid.
Catalysis of the reaction: ATP + a protein serine/threonine = ADP + protein serine/threonine phosphate, dependent on the presence of GTP.
Catalysis of the acetylation of an amino acid residue of a peptide or protein, according to the reaction: acetyl-CoA + peptide = CoA + N-acetylpeptide.
The chemical reactions and pathways resulting in the breakdown of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.
The chemical reactions and pathways resulting in the breakdown of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.
The chemical reactions and pathways resulting in the breakdown of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.
The formation of a protein hexamer, a macromolecular structure consisting of six noncovalently associated identical or nonidentical subunits.
The formation of a protein hexamer, a macromolecular structure consisting of six noncovalently associated identical or nonidentical subunits.
The formation of a protein hexamer, a macromolecular structure consisting of six noncovalently associated identical or nonidentical subunits.
The formation of a protein hexamer, a macromolecular structure consisting of six noncovalently associated identical or nonidentical subunits.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: thiamine(out) + H+(out) = thiamine(in) + H+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: thiamine(out) + H+(out) = thiamine(in) + H+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: thiamine(out) + H+(out) = thiamine(in) + H+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: thiamine(out) + H+(out) = thiamine(in) + H+(in). In high-affinity transport the transporter is able to bind the solute even if it is only present at very low concentrations.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: thiamine(out) + H+(out) = thiamine(in) + H+(in). In high-affinity transport the transporter is able to bind the solute even if it is only present at very low concentrations.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: thiamine(out) + H+(out) = thiamine(in) + H+(in). In high-affinity transport the transporter is able to bind the solute even if it is only present at very low concentrations.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: thiamine(out) + H+(out) = thiamine(in) + H+(in). In high-affinity transport the transporter is able to bind the solute even if it is only present at very low concentrations.
The chemical reactions and pathways resulting in the formation of ascospore wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of ascospore wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of ascospore wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of ascospore wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of ascospores.
The chemical reactions and pathways involving ascospore wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of ascospores.
The process in which a carbohydrate is transported across a membrane.
The process in which a carbohydrate is transported across a membrane.
A process in which an ion is transported across a membrane.
A process in which an ion is transported across a membrane.
The chemical reactions and pathways resulting in the formation of cell wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of fungal cells.
The chemical reactions and pathways resulting in the formation of cell wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of fungal cells.
The chemical reactions and pathways resulting in the formation of cell wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of fungal cells.
The chemical reactions and pathways resulting in the formation of cell wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of fungal cells.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving chitin in a cell wall.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ascospore wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ascospore wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ascospore wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ascospore wall chitin.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of zinc ions.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of zinc ions.
Modulation of the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a stimulus indicating the organism is deprived of zinc ions.
Modulation of the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a stimulus indicating the organism is deprived of zinc ions.
Enables the transfer of ethanolamine from one side of a membrane to the other. Ethanolamine (2-aminoethanol, monoethanolamine) is an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids, such as phosphatidylethanolamine.
Enables the transfer of ethanolamine from one side of a membrane to the other. Ethanolamine (2-aminoethanol, monoethanolamine) is an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids, such as phosphatidylethanolamine.
Enables the transfer of ethanolamine from one side of a membrane to the other. Ethanolamine (2-aminoethanol, monoethanolamine) is an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids, such as phosphatidylethanolamine.
The directed movement of ethanolamine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Ethanolamine (2-aminoethanol, monoethanolamine) is an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids, such as phosphatidylethanolamine.
The directed movement of ethanolamine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Ethanolamine (2-aminoethanol, monoethanolamine) is an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids, such as phosphatidylethanolamine.
The formation of mature enkephalin, a pentapeptide hormone involved in regulating pain and nociception in the body by proteolytic processing of enkephalin propeptide.
The formation of mature enkephalin, a pentapeptide hormone involved in regulating pain and nociception in the body by proteolytic processing of enkephalin propeptide.
The formation of mature enkephalin, a pentapeptide hormone involved in regulating pain and nociception in the body by proteolytic processing of enkephalin propeptide.
The formation of mature islet amyloid polypeptide (IAPP) by posttranslational processing of pro-islet amyloid polypeptide (pro-IAPP).
The formation of mature islet amyloid polypeptide (IAPP) by posttranslational processing of pro-islet amyloid polypeptide (pro-IAPP).
The formation of mature islet amyloid polypeptide (IAPP) by posttranslational processing of pro-islet amyloid polypeptide (pro-IAPP).
The formation of mature islet amyloid polypeptide (IAPP) by posttranslational processing of pro-islet amyloid polypeptide (pro-IAPP).
The formation of mature islet amyloid polypeptide (IAPP) by posttranslational processing of pro-islet amyloid polypeptide (pro-IAPP).
The chemical reactions and pathways resulting in the breakdown of ascospore wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of ascospores.
The chemical reactions and pathways resulting in the breakdown of ascospore wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of ascospores.
The chemical reactions and pathways resulting in the breakdown of ascospore wall chitin, a linear polysaccharide consisting of P-1,4-linked N-acetyl-D-glucosamine residues, found in the walls of ascospores.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of cell wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of cell wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of cell wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of ascospore wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of ascospore wall chitin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of ascospore wall chitin.
Interacting selectively and non-covalently with any glycosylphosphatidylinositol anchor. GPI anchors serve to attach membrane proteins to the lipid bilayer of cell membranes.
Interacting selectively and non-covalently with one or both of the catalytic subunits of protein kinase A.
Interacting selectively and non-covalently with one or both of the regulatory subunits of protein kinase A.
Interacting selectively and non-covalently with one or both of the regulatory subunits of protein kinase A.
The binding and fusion of a macrophage to one or more other cells to form a multinucleated cell.
Any process that modulates the frequency, rate or extent of macrophage fusion.
Any process that stops, prevents, or decreases the frequency, rate or extent of macrophage fusion.
Any process that activates or increases the frequency, rate or extent of macrophage fusion.
Any process that decreases the frequency, rate or extent of the formation of a syncytium, a mass of cytoplasm containing several nuclei enclosed within a single plasma membrane, by the fusion of the plasma membranes of two or more individual cells.
Any process that modulates the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II.
Any process that modulates the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II.
Any process that modulates the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II.
A DNA-directed RNA polymerase complex located in the mitochondrion. Mitochondrial RNA polymerase is composed of two subunits, a catalytic core, which resembles the enzymes from bacteriophage T7 and T3, and a specificity factor required for promoter recognition, which is similar to members of the eubacterial sigma factor family. In S. cerevisiae, these are encoded by the nuclear genes RPO41 and MTF1 and the specificity factor, required for promoter recognition and initiation, is not present in the elongating form.
A DNA-directed RNA polymerase complex located in the mitochondrion. Mitochondrial RNA polymerase is composed of two subunits, a catalytic core, which resembles the enzymes from bacteriophage T7 and T3, and a specificity factor required for promoter recognition, which is similar to members of the eubacterial sigma factor family. In S. cerevisiae, these are encoded by the nuclear genes RPO41 and MTF1 and the specificity factor, required for promoter recognition and initiation, is not present in the elongating form.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by mitochondrial RNA polymerase.
The process of removing sections of a primary snoRNA transcript to remove sequences not present in the mature form of the snoRNA and joining the remaining sections to form the mature form of the snoRNA.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving amides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving amides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving amides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of amides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of amides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of amides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of amides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of amides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of amides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of amides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of amides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of amides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of urea.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of urea.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of urea.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving urea.
Catalysis of the reaction: 71-hydroxychlorophyll(ide) a + NAD(P)+ = chlorophyll(ide) b + NAD(P)H + H+.
Catalysis of the reaction: 71-hydroxychlorophyll(ide) a + NAD(P)+ = chlorophyll(ide) b + NAD(P)H + H+.
Catalysis of the reaction: 71-hydroxychlorophyll(ide) a + NAD(P)+ = chlorophyll(ide) b + NAD(P)H + H+.
Enables the transfer of nicotinamide riboside, which is a pyridine-3-carboxamide covalently bonded to a ribose sugar, from one side of a membrane to the other.
The directed movement of a nicotinamide riboside, which is a pyridine-3-carboxamide covalently bonded to a ribose sugar, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The process in which the accumulation of misfolded proteins in the endoplasmic reticulum triggers a response that positively regulates autophagy.
The process in which the accumulation of misfolded proteins in the endoplasmic reticulum triggers a response that positively regulates autophagy.
The chemical reactions and pathways involving the cytokinin 6-isopentenyladenine.
The chemical reactions and pathways involving the cytokinin 6-isopentenyladenine.
The chemical reactions and pathways resulting in the formation of the cytokinin 6-isopentenyladenine.
The chemical reactions and pathways resulting in the formation of the cytokinin 6-isopentenyladenine.
The chemical reactions and pathways resulting in the formation of the cytokinin 6-isopentenyladenine.
The chemical reactions and pathways resulting in the formation of the cytokinin 6-isopentenyladenine.
The chemical reactions and pathways resulting in the formation of the cytokinin 6-isopentenyladenine.
The chemical reactions and pathways resulting in the breakdown of the cytokinin 6-isopentenyladenine.
The chemical reactions and pathways resulting in the breakdown of the cytokinin 6-isopentenyladenine.
The chemical reactions and pathways resulting in the breakdown of the cytokinin 6-isopentenyladenine.
The chemical reactions and pathways resulting in the breakdown of the cytokinin 6-isopentenyladenine.
The chemical reactions and pathways involving discadenine, (2S)-2-amino-4-{6-[(3-methylbut-2-en-1-yl)amino]-3H-purin-3-yl}butanoic acid.
The chemical reactions and pathways resulting in the formation of discadenine, (2S)-2-amino-4-{6-[(3-methylbut-2-en-1-yl)amino]-3H-purin-3-yl}butanoic acid.
The chemical reactions and pathways resulting in the formation of discadenine, (2S)-2-amino-4-{6-[(3-methylbut-2-en-1-yl)amino]-3H-purin-3-yl}butanoic acid.
The chemical reactions and pathways resulting in the formation of discadenine, (2S)-2-amino-4-{6-[(3-methylbut-2-en-1-yl)amino]-3H-purin-3-yl}butanoic acid.
The chemical reactions and pathways resulting in the formation of discadenine, (2S)-2-amino-4-{6-[(3-methylbut-2-en-1-yl)amino]-3H-purin-3-yl}butanoic acid.
The chemical reactions and pathways resulting in the breakdown of discadenine, (2S)-2-amino-4-{6-[(3-methylbut-2-en-1-yl)amino]-3H-purin-3-yl}butanoic acid.
The chemical reactions and pathways resulting in the breakdown of discadenine, (2S)-2-amino-4-{6-[(3-methylbut-2-en-1-yl)amino]-3H-purin-3-yl}butanoic acid.
The chemical reactions and pathways resulting in the breakdown of discadenine, (2S)-2-amino-4-{6-[(3-methylbut-2-en-1-yl)amino]-3H-purin-3-yl}butanoic acid.
A protein complex that is involved in the Cvt pathway. In budding yeast, the Cvt complex consists of multimers of preApe1p.
A protein complex that is involved in the Cvt pathway. In budding yeast, the Cvt complex consists of multimers of preApe1p.
A class III phosphatidylinositol 3-kinase complex that is involved in autophagy. In budding yeast, this complex consists of Vps30p, Vps34p, Apg14p and Vps15p.
A class III phosphatidylinositol 3-kinase complex that is involved in autophagy. In budding yeast, this complex consists of Vps30p, Vps34p, Apg14p and Vps15p.
A class III phosphatidylinositol 3-kinase complex that is involved in vacuolar protein sorting (VPS) via endosomes. In budding yeast, this complex consists of Vps30p, Vps34p, Vps38 and Vps15p.
A class III phosphatidylinositol 3-kinase complex that is involved in vacuolar protein sorting (VPS) via endosomes. In budding yeast, this complex consists of Vps30p, Vps34p, Vps38 and Vps15p.
A protein complex required for the expansion of the autophagosomal membrane. In budding yeast, this complex consists of Atg12p, Atg5p and Atg16p.
The chemical reactions and pathways involving kynurenic acid, 4-hydroxyquinoline-2-carboxylic acid.
The chemical reactions and pathways involving kynurenic acid, 4-hydroxyquinoline-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of kynurenic acid, 4-hydroxyquinoline-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of kynurenic acid, 4-hydroxyquinoline-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of kynurenic acid, 4-hydroxyquinoline-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of kynurenic acid, 4-hydroxyquinoline-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of kynurenic acid, 4-hydroxyquinoline-2-carboxylic acid.
Catalysis of the reaction: ent-copalyl diphosphate = ent-cassa-12,15-diene + diphosphate.
Catalysis of the reaction: 9-alpha-copalyl diphosphate = stemar-13-ene + diphosphate.
Catalysis of the reaction: 9-alpha-copalyl diphosphate = 9-beta-pimara-7,15-diene + diphosphate.
Catalysis of the reaction: ent-copalyl diphosphate = ent-sandaracopimara-8(14),15-diene + diphosphate.
Catalysis of the reaction: ent-copalyl diphosphate = ent-sandaracopimara-8(14),15-diene + diphosphate.
Catalysis of the reaction: ent-copalyl diphosphate = ent-isokaurene + diphosphate.
Catalysis of the reaction: ent-copalyl diphosphate = ent-pimara-8(14),15-diene + diphosphate.
Catalysis of the reaction: ent-copalyl diphosphate = ent-pimara-8(14),15-diene + diphosphate.
Catalysis of the reaction: 9-alpha-copalyl diphosphate = stemod-13(17)-ene + diphosphate.
Catalysis of the reaction: 9-alpha-copalyl diphosphate = stemod-13(17)-ene + diphosphate.
Catalysis of the reaction: 9-alpha-copalyl diphosphate = stemod-13(17)-ene + diphosphate.
Catalysis of the reaction: 9-alpha-copalyl diphosphate = stemod-13(17)-ene + diphosphate.
Catalysis of the reaction: 9-alpha-copalyl diphosphate = stemod-13(17)-ene + diphosphate.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a monosaccharide stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a disaccharide stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a maltose stimulus.
The series of events in which a stimulus from a monosaccharide is received and converted into a molecular signal.
The series of events in which a stimulus from a disaccharide is received and converted into a molecular signal.
The series of events in which a maltose stimulus is received by a cell and converted into a molecular signal.
A compound function consisting of the regulated formation of a pore via oligomerisation of an existing pool of subunits in the plasma membrane.  The resulting channel activity directly or indirectly allows murein hydrolyases to access their cell wall substrate.
A compound function consisting of the regulated formation of a pore via oligomerisation of an existing pool of subunits in the plasma membrane.  The resulting channel activity directly allows release of a fully-folded phage-encoded endolysin (murein-degradase) from the cell.
A compound function consisting of the regulated formation of a pore via oligomerisation of an existing pool of subunits in the plasma membrane.  The resulting ion channel activity indirectly allows endolysin (murein hydrolyases) to access their cell wall substrate by collapsing the proton motive force (PMF) across the membrane, allowing the endolysin to fold to an active form and hydrolyze bonds in the peptidoglycan cell wall.
The formation of spores derived from the products of meiosis.
The formation of spores derived from the products of meiosis.
The formation of spores derived from the products of meiosis.
The aggregation, arrangement and bonding together of a set of components to form a sexual spore wall, the specialized envelope lying outside the cell membrane of a spore derived from a product of meiosis.
The process in which spores form outside a specialized end cell known as a basidium. Basidia are characteristic of the basidiomycete fungi (phylum Basidiomycota), and give rise to spores that each contain a haploid nucleus that is the product of meiosis. The spores are usually attached to the basidium by short spikes called sterigmata (singular: sterigma). In most basidiomycetes there are four sterigmata (and four spores) to a basidium.
The process in which zygospores are formed. Zygospores are characteristic of the zygomycete fungi (phylum Zygomycota) thick-walled and darkly colored, and usually heavily ornamented as well, with many spines or ridges. It is formed between two specialized organs called suspensors, which are themselves usually heavily ornamented, one from each mating partner. The zygospore forms between them and then breaks away.
The process in which oidia, a type of asexual spore found in fungi, are formed. Oidia are borne a few at a time on very simple hyphae that protrude a short distance into the substrate, and are usually presumed not to constitute the main reproductive strategy of the fungus.
The formation of conidia by the conversion of a pre-existing hypha. An arthrospore is produced by the last cell on a hypha breaking off and dispersing. Usually the walls thicken and the cell(s) separates before swelling of each spore. Sometimes further septa form in each cell prior to disarticulation.
The formation of a spore following the marked enlargement of part of a cell before separation by a septum. Blastospores are a type of asexual spore found in some fungi, most notably the class Glomeromycota.
The process in which sporangiospores, a type of asexual spore found in fungi, are formed. Sporangiospores are formed within sac-like structure, the sporangium, following the division of the cytoplasm.
The process in which a cell gives rise to an endospore, a dormant, highly resistant spore with a thick wall that forms within the mother cell. Endospores are produced by some low G+C Gram-positive bacteria in response to harsh conditions.
The process in which an akinete, a thick-walled (encysted) dormant cell derived from the enlargement of a vegetative cell, is formed. Akinetes typically have granular cytoplasm, are more resistant to environmental extremes than vegetative cells, and are characteristic of several groups of Cyanobacteria.
The process in which differentiated, resting cells are formed, usually within a fruiting body by Myxobacteria. The myxospore is more resistant to high temperature, dessication, and UV than vegetative myxobacteria.
The process in which differentiated, resting cells are formed from a substrate mycelium; characteristic of many members of the order Actinomycetales.
Any process that modulates the frequency, rate or extent of spore formation from the products of mitosis.
Any process that modulates the frequency, rate or extent of spore formation from the products of mitosis.
Any process that modulates the frequency, rate or extent of spore formation from the products of mitosis.
Any process that modulates the frequency, rate or extent of spore formation from the products of meiosis. An example of this is found in Saccharomyces cerevisiae.
Any process that modulates the frequency, rate or extent of spore formation from the products of meiosis. An example of this is found in Saccharomyces cerevisiae.
Any process that modulates the frequency, rate or extent of spore formation from the products of meiosis. An example of this is found in Saccharomyces cerevisiae.
Any process that modulates the frequency, rate or extent of spore formation from the products of meiosis. An example of this is found in Saccharomyces cerevisiae.
Any process that modulates the frequency, rate or extent of ascospore formation. An example of this process is found in Saccharomyces cerevisiae.
The chemical reactions and pathways involving primary alcohols. A primary alcohol is any alcohol in which a hydroxy group, -OH, is attached to a saturated carbon atom which has either three hydrogen atoms attached to it or only one other carbon atom and two hydrogen atoms attached to it.
The chemical reactions and pathways involving primary alcohols. A primary alcohol is any alcohol in which a hydroxy group, -OH, is attached to a saturated carbon atom which has either three hydrogen atoms attached to it or only one other carbon atom and two hydrogen atoms attached to it.
The chemical reactions and pathways resulting in the formation of primary alcohols. A primary alcohol is any alcohol in which a hydroxy group, -OH, is attached to a saturated carbon atom which has either three hydrogen atoms attached to it or only one other carbon atom and two hydrogen atoms attached to it.
The chemical reactions and pathways resulting in the formation of primary alcohols. A primary alcohol is any alcohol in which a hydroxy group, -OH, is attached to a saturated carbon atom which has either three hydrogen atoms attached to it or only one other carbon atom and two hydrogen atoms attached to it.
The chemical reactions and pathways resulting in the formation of primary alcohols. A primary alcohol is any alcohol in which a hydroxy group, -OH, is attached to a saturated carbon atom which has either three hydrogen atoms attached to it or only one other carbon atom and two hydrogen atoms attached to it.
The chemical reactions and pathways resulting in the formation of primary alcohols. A primary alcohol is any alcohol in which a hydroxy group, -OH, is attached to a saturated carbon atom which has either three hydrogen atoms attached to it or only one other carbon atom and two hydrogen atoms attached to it.
The chemical reactions and pathways resulting in the formation of primary alcohols. A primary alcohol is any alcohol in which a hydroxy group, -OH, is attached to a saturated carbon atom which has either three hydrogen atoms attached to it or only one other carbon atom and two hydrogen atoms attached to it.
The chemical reactions and pathways resulting in the breakdown of primary alcohols. A primary alcohol is any alcohol in which a hydroxy group, -OH, is attached to a saturated carbon atom which has either three hydrogen atoms attached to it or only one other carbon atom and two hydrogen atoms attached to it.
The chemical reactions and pathways resulting in the breakdown of primary alcohols. A primary alcohol is any alcohol in which a hydroxy group, -OH, is attached to a saturated carbon atom which has either three hydrogen atoms attached to it or only one other carbon atom and two hydrogen atoms attached to it.
The chemical reactions and pathways resulting in the breakdown of primary alcohols. A primary alcohol is any alcohol in which a hydroxy group, -OH, is attached to a saturated carbon atom which has either three hydrogen atoms attached to it or only one other carbon atom and two hydrogen atoms attached to it.
The chemical reactions and pathways resulting in the breakdown of primary alcohols. A primary alcohol is any alcohol in which a hydroxy group, -OH, is attached to a saturated carbon atom which has either three hydrogen atoms attached to it or only one other carbon atom and two hydrogen atoms attached to it.
The chemical reactions and pathways involving a diol, a compound that contains two hydroxy groups, generally assumed to be, but not necessarily, alcoholic.
The chemical reactions and pathways involving a diol, a compound that contains two hydroxy groups, generally assumed to be, but not necessarily, alcoholic.
The chemical reactions and pathways resulting in the formation of a diol, any alcohol containing two hydroxyl groups attached to saturated carbon atoms.
The chemical reactions and pathways resulting in the formation of a diol, any alcohol containing two hydroxyl groups attached to saturated carbon atoms.
The chemical reactions and pathways resulting in the formation of a diol, any alcohol containing two hydroxyl groups attached to saturated carbon atoms.
The chemical reactions and pathways resulting in the formation of a diol, any alcohol containing two hydroxyl groups attached to saturated carbon atoms.
The chemical reactions and pathways resulting in the formation of a diol, any alcohol containing two hydroxyl groups attached to saturated carbon atoms.
The chemical reactions and pathways resulting in the breakdown of a diol, any alcohol containing two hydroxyl groups attached to saturated carbon atoms.
The chemical reactions and pathways resulting in the breakdown of a diol, any alcohol containing two hydroxyl groups attached to saturated carbon atoms.
The chemical reactions and pathways resulting in the breakdown of a diol, any alcohol containing two hydroxyl groups attached to saturated carbon atoms.
The chemical reactions and pathways resulting in the breakdown of a diol, any alcohol containing two hydroxyl groups attached to saturated carbon atoms.
The actin nucleation process in which actin monomers combine to form a new branch on the side of an existing actin filament; mediated by the Arp2/3 protein complex and its interaction with other proteins.
The actin nucleation process in which actin monomers combine to form a new branch on the side of an existing actin filament; mediated by the Arp2/3 protein complex and its interaction with other proteins.
Any process that modulates the frequency, rate or extent of actin nucleation mediated by the Arp2/3 complex and interacting proteins.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin nucleation mediated by the Arp2/3 complex and interacting proteins.
Catalysis of the reaction: ATP + nicotinic acid riboside = ADP + nicotinic acid mononucleotide.
Catalysis of the transfer of an acyl group to an oxygen atom on an alcohol acceptor molecule.
Catalysis of the transfer of an acyl group to an oxygen atom on an alcohol acceptor molecule.
Catalysis of the transfer of an acyl group to an oxygen atom on an alcohol acceptor molecule.
Catalysis of the transfer of an acyl group to an oxygen atom on an alcohol acceptor molecule.
Catalysis of the transfer of an acyl group to an oxygen atom on an alcohol acceptor molecule.
Catalysis of the transfer of an acyl group to an oxygen atom on an alcohol acceptor molecule.
Catalysis of the reaction: butanoyl-CoA + an alcohol = CoA + a butyl ester.
Catalysis of the reaction: hexanoyl-CoA + an alcohol = CoA + a hexyl ester.
Catalysis of the reaction: octanoyl-CoA + an alcohol = CoA + an octyl ester.
Catalysis of the reaction: decanoyl-CoA + an alcohol = CoA + a decyl ester.
Catalysis of the transfer of a butyl group to an oxygen atom on the acceptor molecule.
Catalysis of the transfer of a hexyl group to an oxygen atom on the acceptor molecule.
Catalysis of the transfer of a decyl group to an oxygen atom on the acceptor molecule.
Catalysis of the transfer of a butanoyl (CH3-[CH2]2-CO-) group to an acceptor molecule.
Catalysis of the transfer of a hexanoyl (CH3-[CH2]4-CO-) group to an acceptor molecule.
Catalysis of the transfer of a decanoyl (CH3-[CH2]8-CO-) group to an acceptor molecule.
A cellular process that results in the aggregation, arrangement and bonding together of a set of components to form a cell junction.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a cell junction. A cell junction is a specialized region of connection between two cells or between a cell and the extracellular matrix.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a cell junction. A cell junction is a specialized region of connection between two cells or between a cell and the extracellular matrix.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a cell junction. A cell junction is a specialized region of connection between two cells or between a cell and the extracellular matrix.
The organization process that preserves a cell junction in a stable functional or structural state. A cell junction is a specialized region of connection between two cells or between a cell and the extracellular matrix.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an adherens junction. An adherens junction is a cell junction at which the cytoplasmic face of the plasma membrane is attached to actin filaments.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an adherens junction. An adherens junction is a cell junction at which the cytoplasmic face of the plasma membrane is attached to actin filaments.
The aggregation, arrangement and bonding together of a set of components to form an adherens junction. An adherens junction is a cell junction at which the cytoplasmic face of the plasma membrane is attached to actin filaments.
The maintenance of an adherens junction. An adherens junction is a cell junction at which the cytoplasmic face of the plasma membrane is attached to actin filaments.
Catalytic introduction of supercoils in a DNA molecule or region thereof. In bacteria, negative supercoils are only introduced by DNA gyrase, a type II topoisomerase, but not all DNA gyrases are capable of introducing supercoils. In bacteria, the level of supercoiling varies widely between species and has been characterized properly in only a handful of organisms. The best characterized enzyme, from E.coli, is exceptionally proficient at supercoiling and this ability is not representative of all bacteria.
Catalytic introduction of supercoils in a DNA molecule or region thereof. In bacteria, negative supercoils are only introduced by DNA gyrase, a type II topoisomerase, but not all DNA gyrases are capable of introducing supercoils. In bacteria, the level of supercoiling varies widely between species and has been characterized properly in only a handful of organisms. The best characterized enzyme, from E.coli, is exceptionally proficient at supercoiling and this ability is not representative of all bacteria.
Interacting selectively and non-covalently with an RNA molecule that has assumed an incorrect conformation.
The process of assisting in the covalent and noncovalent assembly of single or multimeric RNAs into the correct tertiary structure.
Catalysis of the reaction: a carboxylic ester + H2O = an alcohol + a carboxylic anion, where the carboxylic chain has 8 or fewer carbon atoms.
Catalysis of the reaction: a carboxylic ester + H2O = an alcohol + a carboxylic anion, where the carboxylic chain has 8 or fewer carbon atoms.
Catalysis of the reaction: a carboxylic ester + H2O = an alcohol + a carboxylic anion, where the carboxylic chain has 8 or fewer carbon atoms.
Catalysis of the reaction: a carboxylic ester + H2O = an alcohol + a carboxylic anion, where the carboxylic chain has 8 or fewer carbon atoms.
Catalysis of the reaction: a carboxylic ester + H2O = an alcohol + a carboxylic anion, where the carboxylic chain has 8 or fewer carbon atoms.
Catalysis of the reaction: a carboxylic ester + H2O = an alcohol + a carboxylic anion, where the carboxylic chain has 8 or fewer carbon atoms.
Catalysis of the reaction: a carboxylic ester + H2O = an alcohol + a carboxylic anion, where the carboxylic chain has 8 or fewer carbon atoms.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type I interferon stimulus. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interferon-gamma stimulus. Interferon-gamma is also known as type II interferon.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interferon-gamma stimulus. Interferon-gamma is also known as type II interferon.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interferon-gamma stimulus. Interferon-gamma is also known as type II interferon.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interferon-gamma stimulus. Interferon-gamma is also known as type II interferon.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type III interferon stimulus. Interferon lambda is the only member of the type III interferon found so far.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a type III interferon stimulus. Interferon lambda is the only member of the type III interferon found so far.
The appearance of type III interferon due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. Interferon lambda is the only member of the type III interferon found so far.
Any process that modulates the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Any process that stops, prevents, or reduces the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Any process that stops, prevents, or reduces the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Any process that stops, prevents, or reduces the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Any process that stops, prevents, or reduces the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Any process that stops, prevents, or reduces the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Any process that activates or increases the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Any process that activates or increases the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Any process that activates or increases the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Any process that activates or increases the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Any process that activates or increases the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Any process that activates or increases the frequency, rate, or extent of type III interferon production. Interferon lambda is the only member of the type III interferon found so far.
Interacting selectively and non-covalently with a type III interferon. Interferon lambda is the only member of the type III interferon found so far.
Combining with a type III interferon and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. Interferon lambda is the only member of the type III interferon found so far.
Any apoptotic process in a glial cell, a non-neuronal cell of the nervous system.
Any apoptotic process in a glial cell, a non-neuronal cell of the nervous system.
Any apoptotic process in a glial cell, a non-neuronal cell of the nervous system.
Any apoptotic process in a glial cell, a non-neuronal cell of the nervous system.
Any apoptotic process in a glial cell, a non-neuronal cell of the nervous system.
Any apoptotic process in a glial cell, a non-neuronal cell of the nervous system.
Any apoptotic process in a glial cell, a non-neuronal cell of the nervous system.
Any apoptotic process in a glial cell, a non-neuronal cell of the nervous system.
Any apoptotic process in a glial cell, a non-neuronal cell of the nervous system.
Any apoptotic process in a glial cell, a non-neuronal cell of the nervous system.
Any process that modulates the frequency, rate, or extent of glial cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of glial cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of glial cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of glial cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of glial cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of glial cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of glial cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of glial cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of glial cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of glial cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of glial cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of glial cell apoptotic process.
Catalysis of the removal of a 5' terminal pyrophosphate from the 5'-triphosphate end of an RNA, leaving a 5'-monophosphate end.
The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD), beginning with the synthesis of tryptophan from simpler precursors; biosynthesis may be of either the oxidized form, NAD, or the reduced form, NADH.
Any process that generates nicotinamide adenine dinucleotide (NAD) from derivatives of it, without de novo synthesis; salvage is usually from the degradation products nicotinic acid (Na) and nicotinamide (Nam).
The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD) from the vitamin precursor nicotinamide riboside.
The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD) from the vitamin precursor nicotinamide riboside.
A membrane enriched in complexes formed of reaction centers, accessory pigments and electron carriers, in which photosynthetic reactions take place.
A spherical particle with a hydrophobic core of triglycerides and/or cholesterol esters, surrounded by an amphipathic monolayer of phospholipids, cholesterol and apolipoproteins. Plasma lipoprotein particles transport lipids, which are non-covalently associated with the particles, in the blood or lymph.
A chylomicron that contains apolipoprotein C2 (APOC2), a cofactor for lipoprotein lipase (LPL) activity, and has a mean diameter of 500 nm and density of 0.95g/ml. Mature chylomicron particles transport exogenous (dietary) lipids from the intestines to other body tissues, via the blood and lymph.
A lipoprotein particle that is derived from a mature chylomicron particle by the removal of triglycerides from the chylomicron core by lipoprotein lipase and the subsequent loss of surface components. It characteristically contains apolipoprotein E (APOE) and is cleared from the blood by the liver.
A triglyceride-rich lipoprotein particle that is typically composed of APOB100, APOE and APOCs and has a density of about 1.006 g/ml and a diameter of between 20-80 nm. It is found in blood and transports endogenous products (newly synthesized cholesterol and triglycerides) from the liver.
A triglyceride-rich lipoprotein particle that is typically composed of APOB100, APOE and APOCs and has a density of about 1.006 g/ml and a diameter of between 20-80 nm. It is found in blood and transports endogenous products (newly synthesized cholesterol and triglycerides) from the liver.
A triglyceride-rich lipoprotein particle that is typically composed of APOB100, APOE and APOCs and has a density of about 1.006 g/ml and a diameter of between 20-80 nm. It is found in blood and transports endogenous products (newly synthesized cholesterol and triglycerides) from the liver.
A lipoprotein particle, rich in cholesterol esters and low in triglycerides that is typically composed of APOB100 and APOE and has a density of 1.02-1.06 g/ml and a diameter of between 20-25 nm. LDL particles are formed from VLDL particles (via IDL) by the loss of triglyceride and gain of cholesterol ester. They transport endogenous cholesterol (and to some extent triglycerides) from peripheral tissues back to the liver.
A lipoprotein particle, rich in cholesterol esters and low in triglycerides that is typically composed of APOB100 and APOE and has a density of 1.02-1.06 g/ml and a diameter of between 20-25 nm. LDL particles are formed from VLDL particles (via IDL) by the loss of triglyceride and gain of cholesterol ester. They transport endogenous cholesterol (and to some extent triglycerides) from peripheral tissues back to the liver.
A lipoprotein particle, rich in cholesterol esters and low in triglycerides that is typically composed of APOB100 and APOE and has a density of 1.02-1.06 g/ml and a diameter of between 20-25 nm. LDL particles are formed from VLDL particles (via IDL) by the loss of triglyceride and gain of cholesterol ester. They transport endogenous cholesterol (and to some extent triglycerides) from peripheral tissues back to the liver.
A triglyceride-rich lipoprotein particle that typically contains APOB100, APOE and APOCs and has a density of 1.006-1.019 g/ml and a diameter of between 25-30 nm. IDL particles are found in blood and are formed by the delipidation of very-low-density lipoprotein particles (VLDL). IDL particles are removed from blood by the liver, following binding to the APOE receptor, or are converted to low-density lipoprotein (LDL).
A triglyceride-rich lipoprotein particle that typically contains APOB100, APOE and APOCs and has a density of 1.006-1.019 g/ml and a diameter of between 25-30 nm. IDL particles are found in blood and are formed by the delipidation of very-low-density lipoprotein particles (VLDL). IDL particles are removed from blood by the liver, following binding to the APOE receptor, or are converted to low-density lipoprotein (LDL).
A triglyceride-rich lipoprotein particle that typically contains APOB100, APOE and APOCs and has a density of 1.006-1.019 g/ml and a diameter of between 25-30 nm. IDL particles are found in blood and are formed by the delipidation of very-low-density lipoprotein particles (VLDL). IDL particles are removed from blood by the liver, following binding to the APOE receptor, or are converted to low-density lipoprotein (LDL).
A lipoprotein particle with a high density (typically 1.063-1.21 g/ml) and a diameter of 5-10 nm that contains APOAs and may contain APOCs and APOE; found in blood and carries lipids from body tissues to the liver as part of the reverse cholesterol transport process.
A lipoprotein particle with a high density (typically 1.063-1.21 g/ml) and a diameter of 5-10 nm that contains APOAs and may contain APOCs and APOE; found in blood and carries lipids from body tissues to the liver as part of the reverse cholesterol transport process.
A lipoprotein particle with a high density (typically 1.063-1.21 g/ml) and a diameter of 5-10 nm that contains APOAs and may contain APOCs and APOE; found in blood and carries lipids from body tissues to the liver as part of the reverse cholesterol transport process.
A lipoprotein particle with a high density (typically 1.063-1.21 g/ml) and a diameter of 5-10 nm that contains APOAs and may contain APOCs and APOE; found in blood and carries lipids from body tissues to the liver as part of the reverse cholesterol transport process.
A lipoprotein particle with a high density (typically 1.063-1.21 g/ml) and a diameter of 5-10 nm that contains APOAs and may contain APOCs and APOE; found in blood and carries lipids from body tissues to the liver as part of the reverse cholesterol transport process.
A newly formed high-density lipoprotein particle; consists of a phospholipid bilayer surrounded by two or more APOA1 molecules. The discoidal HDL particle is formed when lipid-free or lipid-poor APOA1 acquires phospholipids and unesterified cholesterol from either cell membranes or triglyceride-rich lipoproteins (undergoing lipolysis by lipoprotein lipase).
A newly formed high-density lipoprotein particle; consists of a phospholipid bilayer surrounded by two or more APOA1 molecules. The discoidal HDL particle is formed when lipid-free or lipid-poor APOA1 acquires phospholipids and unesterified cholesterol from either cell membranes or triglyceride-rich lipoproteins (undergoing lipolysis by lipoprotein lipase).
A newly formed high-density lipoprotein particle; consists of a phospholipid bilayer surrounded by two or more APOA1 molecules. The discoidal HDL particle is formed when lipid-free or lipid-poor APOA1 acquires phospholipids and unesterified cholesterol from either cell membranes or triglyceride-rich lipoproteins (undergoing lipolysis by lipoprotein lipase).
A mature high-density lipoprotein (HDL) particle, converted from discoidal HDL particles following the esterification of cholesterol in the particle by phosphatidylcholine-sterol O-acyltransferase (lecithin cholesterol acyltransferase; LCAT).
A mature high-density lipoprotein (HDL) particle, converted from discoidal HDL particles following the esterification of cholesterol in the particle by phosphatidylcholine-sterol O-acyltransferase (lecithin cholesterol acyltransferase; LCAT).
A mature high-density lipoprotein (HDL) particle, converted from discoidal HDL particles following the esterification of cholesterol in the particle by phosphatidylcholine-sterol O-acyltransferase (lecithin cholesterol acyltransferase; LCAT).
The acquisition, loss, or modification of macromolecules within a complex, resulting in the alteration of an existing complex.
The acquisition, loss or modification of a protein or lipid within a protein-lipid complex.
The acquisition, loss or modification of a protein or lipid within a plasma lipoprotein particle, including the hydrolysis of triglyceride by hepatic lipase, with the subsequent loss of free fatty acid, and the esterification of cholesterol by phosphatidylcholine-sterol O-acyltransferase (lecithin cholesterol acyltransferase; LCAT).
The acquisition, loss or modification of a protein or lipid within a triglyceride-rich lipoprotein particle, including the hydrolysis of triglyceride by lipoprotein lipase, with the subsequent loss of free fatty acid, and the transfer of cholesterol esters to a triglyceride-rich lipoprotein particle by cholesteryl ester transfer protein (CETP), with the simultaneous transfer of triglyceride from a triglyceride-rich lipoprotein particle.
The acquisition, loss or modification of a protein or lipid within a chylomicron, including the hydrolysis of triglyceride by lipoprotein lipase and the subsequent loss of free fatty acid.
The acquisition, loss or modification of a protein or lipid within a very-low-density lipoprotein particle, including the hydrolysis of triglyceride by hepatic lipase or lipoprotein lipase and the subsequent loss of free fatty acid.
The acquisition, loss or modification of a protein or lipid within a very-low-density lipoprotein particle, including the hydrolysis of triglyceride by hepatic lipase or lipoprotein lipase and the subsequent loss of free fatty acid.
The acquisition, loss or modification of a protein or lipid within a very-low-density lipoprotein particle, including the hydrolysis of triglyceride by hepatic lipase or lipoprotein lipase and the subsequent loss of free fatty acid.
The acquisition, loss or modification of a protein or lipid within an intermediate-density lipoprotein particle.
The acquisition, loss or modification of a protein or lipid within an intermediate-density lipoprotein particle.
The acquisition, loss or modification of a protein or lipid within an intermediate-density lipoprotein particle.
The acquisition, loss or modification of a protein or lipid within a low-density lipoprotein particle, including the hydrolysis of triglyceride by hepatic lipase, with the subsequent loss of free fatty acid, and the transfer of cholesterol esters from LDL to a triglyceride-rich lipoprotein particle by cholesteryl ester transfer protein (CETP), with the simultaneous transfer of triglyceride to LDL.
The acquisition, loss or modification of a protein or lipid within a low-density lipoprotein particle, including the hydrolysis of triglyceride by hepatic lipase, with the subsequent loss of free fatty acid, and the transfer of cholesterol esters from LDL to a triglyceride-rich lipoprotein particle by cholesteryl ester transfer protein (CETP), with the simultaneous transfer of triglyceride to LDL.
The acquisition, loss or modification of a protein or lipid within a low-density lipoprotein particle, including the hydrolysis of triglyceride by hepatic lipase, with the subsequent loss of free fatty acid, and the transfer of cholesterol esters from LDL to a triglyceride-rich lipoprotein particle by cholesteryl ester transfer protein (CETP), with the simultaneous transfer of triglyceride to LDL.
The acquisition, loss or modification of a protein or lipid within a high-density lipoprotein particle, including the hydrolysis of triglyceride by hepatic lipase, with the subsequent loss of free fatty acid, and the transfer of cholesterol esters from LDL to a triglyceride-rich lipoprotein particle by cholesteryl ester transfer protein (CETP), with the simultaneous transfer of triglyceride to LDL.
The process in which a discoidal high-density lipoprotein (HDL) particle acquires additional lipid or protein molecules, and cholesterol in the particle is converted to tightly bound cholesterol esters by the action of phosphatidylcholine-sterol O-acyltransferase (lecithin cholesterol acyltransferase; LCAT), resulting in the formation of a spherical HDL particle.
The process in which a discoidal high-density lipoprotein (HDL) particle acquires additional lipid or protein molecules, and cholesterol in the particle is converted to tightly bound cholesterol esters by the action of phosphatidylcholine-sterol O-acyltransferase (lecithin cholesterol acyltransferase; LCAT), resulting in the formation of a spherical HDL particle.
The process in which a discoidal high-density lipoprotein (HDL) particle acquires additional lipid or protein molecules, and cholesterol in the particle is converted to tightly bound cholesterol esters by the action of phosphatidylcholine-sterol O-acyltransferase (lecithin cholesterol acyltransferase; LCAT), resulting in the formation of a spherical HDL particle.
The non-covalent aggregation and arrangement of proteins and lipids to form a plasma lipoprotein particle.
The non-covalent aggregation and arrangement of proteins and lipids in the intestine to form a chylomicron.
The non-covalent aggregation and arrangement of proteins and lipids in the liver to form a very-low-density lipoprotein particle.
The non-covalent aggregation and arrangement of proteins and lipids to form a high-density lipoprotein particle.
The process in which a lipoprotein particle is removed from the blood via receptor-mediated endocytosis and its constituent parts degraded.
The process in which a chylomicron remnant is removed from the blood via receptor-mediated endocytosis into liver cells and its constituent parts degraded.
The process in which a low-density lipoprotein particle is removed from the blood via receptor-mediated endocytosis and its constituent parts degraded.
The process in which a high-density lipoprotein particle is removed from the blood via receptor-mediated endocytosis and its constituent parts degraded.
A plasma lipoprotein particle that has a hydrophobic core enriched in triglycerides surrounded by an amphipathic monolayer of phospholipids, cholesterol and apolipoproteins. Triglyceride-rich lipoprotein particles transport lipids, which are non-covalently associated with the particles, in the blood.
A plasma lipoprotein particle that has a hydrophobic core enriched in triglycerides surrounded by an amphipathic monolayer of phospholipids, cholesterol and apolipoproteins. Triglyceride-rich lipoprotein particles transport lipids, which are non-covalently associated with the particles, in the blood.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
Catalysis of the reaction: 4-aminobutanoate + pyruvate = succinate semialdehyde + alanine.
A protein complex that forms a subcomplex of the 90S preribosome and can interact directly with the 5' External Transcribed Spacer (ETS) of the full length pre-rRNA transcript. In S. cerevisiae, it sediments at 25-30 S and is composed of Pwp2p, Dip2p, Utp21p, Utp13p, Utp18p, and Utp6p.
A protein complex that forms a subcomplex of the 90S preribosome and can interact directly with the 5' External Transcribed Spacer (ETS) of the full length pre-rRNA transcript. In S. cerevisiae, it sediments at 25-30 S and is composed of Pwp2p, Dip2p, Utp21p, Utp13p, Utp18p, and Utp6p.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lipid particle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lipid particle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lipid particle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lipid particle.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lipid particle.
Any apoptotic process in a smooth muscle cell. Smooth muscle consists of non-striated, elongated, spindle-shaped cell found lining the digestive tract, uterus, and blood vessels.
Any apoptotic process in a smooth muscle cell. Smooth muscle consists of non-striated, elongated, spindle-shaped cell found lining the digestive tract, uterus, and blood vessels.
Any apoptotic process in a smooth muscle cell. Smooth muscle consists of non-striated, elongated, spindle-shaped cell found lining the digestive tract, uterus, and blood vessels.
Any apoptotic process in a smooth muscle cell. Smooth muscle consists of non-striated, elongated, spindle-shaped cell found lining the digestive tract, uterus, and blood vessels.
Any apoptotic process in a smooth muscle cell. Smooth muscle consists of non-striated, elongated, spindle-shaped cell found lining the digestive tract, uterus, and blood vessels.
Any apoptotic process in a smooth muscle cell. Smooth muscle consists of non-striated, elongated, spindle-shaped cell found lining the digestive tract, uterus, and blood vessels.
Any process that modulates the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that modulates the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that stops, prevents, or reduces the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of smooth muscle cell apoptotic process.
Any process that activates or increases the frequency, rate, or extent of smooth muscle cell apoptotic process.
A process in which a protein is transported to, or maintained in, a location within the external part of the cell wall and/or plasma membrane.
A process in which a protein is transported to, or maintained in, a location within the external part of the cell wall and/or plasma membrane.
Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter in response to an iron stimulus.
Any process that stops, prevents or reduces the rate of transcription from an RNA polymerase II promoter in response to an iron stimulus.
Any process that stops, prevents or reduces the rate of transcription from an RNA polymerase II promoter in response to an iron stimulus.
Any process that stops, prevents or reduces the rate of transcription from an RNA polymerase II promoter in response to an iron stimulus.
Any process that stops, prevents or reduces the rate of transcription from an RNA polymerase II promoter in response to an iron stimulus.
Any process that stops, prevents or reduces the rate of transcription from an RNA polymerase II promoter in response to an iron stimulus.
Any process in which a telomere is transported to, and/or maintained in, a specific location.
The process in which a telomere is maintained in a specific location at the nuclear periphery.
The portion of the nuclear lumen proximal to the inner nuclear membrane.
A plastid found in senescing, formerly green tissues that is derived from a chloroplast that undergoes an organized developmental program of senescence.
Any cellular process that results in the specification, formation or maintenance of the physical structure of eukaryotic chromatin that modulates the rate, frequency or extent of DNA-dependent transcription.
Any cellular process that results in the specification, formation or maintenance of the physical structure of eukaryotic chromatin that modulates the rate, frequency or extent of DNA-dependent transcription.
Any cellular process that results in the specification, formation or maintenance of the physical structure of eukaryotic chromatin that modulates the rate, frequency or extent of DNA-dependent transcription.
The process in which proteins required for 3'-end transcript processing become associated with the RNA polymerase II holoenzyme complex and the 3' end of a transcript.
Recognition of both the 5' and 3'-splice sites and positioning them in the correct alignment with respect to each other so that the second catalytic step of nuclear mRNA splicing can occur.
The chemical reactions and pathways resulting in the formation of a nucleobase-containing small molecule: a nucleobase, a nucleoside, or a nucleotide.
The chemical reactions and pathways resulting in the formation of a nucleobase-containing small molecule: a nucleobase, a nucleoside, or a nucleotide.
The chemical reactions and pathways resulting in the formation of a nucleobase-containing small molecule: a nucleobase, a nucleoside, or a nucleotide.
The chemical reactions and pathways resulting in the formation of a nucleobase-containing small molecule: a nucleobase, a nucleoside, or a nucleotide.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a fluid shear stress stimulus. Fluid shear stress is the force acting on an object in a system where the fluid is moving across a solid surface.
The chemical reactions and pathways involving beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways involving beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways involving (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
The chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of ascospores.
Endonucleolytic cleavage of the 3'-end of the pre-tRNA as part of the process of generating the mature 3'-end of the tRNA.
Endonucleolytic cleavage of the 3'-end of the pre-tRNA as part of the process of generating the mature 3'-end of the tRNA.
Endonucleolytic cleavage of the 3'-end of the pre-tRNA as part of the process of generating the mature 3'-end of the tRNA.
Exonucleolytic cleavage of the 3'-end of the pre-tRNA as part of the process of generating the mature 3'-end of the tRNA.
Exonucleolytic cleavage of the 3'-end of the pre-tRNA as part of the process of generating the mature 3'-end of the tRNA.
Exonucleolytic cleavage of the 3'-end of the pre-tRNA as part of the process of generating the mature 3'-end of the tRNA.
Catalysis of the reaction: 2,3-diphosphoglycerate + H2O = phosphoglycerate + phosphate.
Catalysis of the reaction: 2,3-diphosphoglycerate + H2O = phosphoglycerate + phosphate.
Catalysis of the reaction: 2,3-diphosphoglycerate + H2O = phosphoglycerate + phosphate.
Catalysis of the reaction: 2,3-diphosphoglycerate + H2O = phosphoglycerate + phosphate.
Catalysis of the reaction: 2,3-diphosphoglycerate + H2O = phosphoglycerate + phosphate.
Catalysis of the reaction: 2,3-diphosphoglycerate + H2O = 2-phospho-D-glycerate + phosphate.
The chemical reactions and pathways resulting in the formation of urate, the anion of uric acid, 2,6,8-trioxypurine.
The chemical reactions and pathways resulting in the formation of urate, the anion of uric acid, 2,6,8-trioxypurine.
The chemical reactions and pathways resulting in the formation of urate, the anion of uric acid, 2,6,8-trioxypurine.
The chemical reactions and pathways resulting in the formation of urate, the anion of uric acid, 2,6,8-trioxypurine.
The chemical reactions and pathways resulting in the formation of urate, the anion of uric acid, 2,6,8-trioxypurine.
Catalysis of the reaction: L-2-hydroxyglutarate + O2 = 2-oxoglutarate + hydrogen peroxide.
The addition of an acetyl group to one or more amino acids in a protein, occurring before the protein has been completely translated and released from the ribosome.
The addition of an acetyl group to one or more amino acids in a protein, occurring before the protein has been completely translated and released from the ribosome.
The addition of an acetyl group to one or more amino acids in a protein, occurring after the protein has been completely translated and released from the ribosome.
The addition of an acetyl group to one or more amino acids in a protein, occurring after the protein has been completely translated and released from the ribosome.
The volume enclosed by the membrane of an aleurone grain.
The volume enclosed within the autophagosome double-membrane.
A membrane-associated protein complex that is required for a late stage of endosomal transport. In budding yeast, this complex consists of Vps55p and Vps68p proteins.
The double lipid bilayer enclosing the etioplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
Either of the lipid bilayers that surround a etioplast and form the etioplast envelope.
The chemical reactions and pathways resulting in the breakdown of the mRNA transcript body that occurs when the 3' end is not protected by a 3'-poly(A) tail; degradation proceeds in the 3' to 5' direction.
The chemical reactions and pathways resulting in the breakdown of the mRNA transcript body that occurs when the 5' end is not protected by a 5'-cap; degradation proceeds in the 5' to 3' direction.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in the optic tectum towards target cells in the premotor reticulospinal system in the hindbrain.
The single layer of phopholipids surrounding a lipid storage body.
The single layer of phopholipids surrounding a lipid storage body.
The single layer of phopholipids surrounding a lipid storage body.
The single layer of phopholipids surrounding a lipid storage body.
The single layer of phopholipids surrounding a lipid storage body.
Catalysis of the reaction: P1-P6-bis(5'-adenosyl) hexaphosphate + H2O = AMP + adenosine 5'-pentaphosphate.
Catalysis of the reaction: P1-P6-bis(5'-adenosyl) hexaphosphate + H2O = AMP + adenosine 5'-pentaphosphate.
Catalysis of the reaction: P1-P6-bis(5'-adenosyl) hexaphosphate + H2O = AMP + adenosine 5'-pentaphosphate.
Catalysis of the reaction: P1-P6-bis(5'-adenosyl) hexaphosphate + H2O = AMP + adenosine 5'-pentaphosphate.
Catalysis of the reaction: P1-P6-bis(5'-adenosyl) pentaphosphate + H2O = AMP + adenosine 5'-tetraphosphate.
Catalysis of the reaction: P1-P6-bis(5'-adenosyl) pentaphosphate + H2O = AMP + adenosine 5'-tetraphosphate.
Catalysis of the reaction: P1-P6-bis(5'-adenosyl) pentaphosphate + H2O = AMP + adenosine 5'-tetraphosphate.
Catalysis of the reaction: P1-P6-bis(5'-adenosyl) pentaphosphate + H2O = AMP + adenosine 5'-tetraphosphate.
Catalysis of the reaction: P1-P6-bis(5'-adenosyl) pentaphosphate + H2O = AMP + adenosine 5'-tetraphosphate.
A lipid modification process in which a steroid ester is formed by the combination of a carboxylic acid (often a fatty acid) and a steroid molecule (e.g. cholesterol).
A lipid modification process in which a sterol ester is formed by the combination of a carboxylic acid (often a fatty acid) and a sterol molecule (e.g. cholesterol).
A lipid modification process in which a sterol ester is formed by the combination of a carboxylic acid (often a fatty acid) and cholesterol. In the blood this process is associated with the conversion of free cholesterol into cholesteryl ester, which is then sequestered into the core of a lipoprotein particle.
The directed movement of a glycoprotein, any protein that contains covalently bound glycose (i.e. monosaccharide) residues, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Enables the directed movement of a glycoprotein, any protein that contains covalently bound glycose (i.e. monosaccharide) residues, into, out of or within a cell, or between cells.
The modification of a lipoprotein by oxidation of one or more amino acids in the protein.
The modification of a lipoprotein by oxidation of the lipid group.
The removal of one or more electrons from a lipid, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen.
The modification of a lipid or protein within a plasma lipoprotein particle by oxidation of the lipid or one or more amino acids.
Any process that modulates the frequency, rate or extent of lipoprotein oxidation.
Any process that stops, prevents, or reduces the frequency, rate or extent of lipoprotein oxidation.
Any process that modulates the frequency, rate or extent of lipoprotein oxidation, occurring in the blood plasma.
Any process that stops, prevents, or reduces the frequency, rate or extent of lipoprotein particle oxidation, occurring in the blood plasma.
Any process that stops, prevents, or reduces the frequency, rate or extent of lipoprotein particle oxidation, occurring in the blood plasma.
The morphogenetic process that results in flattening of a cell as a consequence of its adhesion to a substrate.
The morphogenetic process that results in flattening of a cell as a consequence of its adhesion to a substrate.
The process in which a very-low-density lipoprotein particle is removed from the blood via receptor-mediated endocytosis and its constituent parts degraded.
A vacuolar membrane-associated protein complex that is required for activation of microautophagy during exit from rapamycin-induced growth arrest. In budding yeast, S. cerevisiae, this complex includes Gtr1p, Gtr2p, Meh1p, and Slm4p.
A vacuolar membrane-associated protein complex that is required for activation of microautophagy during exit from rapamycin-induced growth arrest. In budding yeast, S. cerevisiae, this complex includes Gtr1p, Gtr2p, Meh1p, and Slm4p.
A vacuolar membrane-associated protein complex that is required for activation of microautophagy during exit from rapamycin-induced growth arrest. In budding yeast, S. cerevisiae, this complex includes Gtr1p, Gtr2p, Meh1p, and Slm4p.
A vacuolar membrane-associated protein complex that is required for activation of microautophagy during exit from rapamycin-induced growth arrest. In budding yeast, S. cerevisiae, this complex includes Gtr1p, Gtr2p, Meh1p, and Slm4p.
Isoenergetic transfer of ubiquitin from one protein to an existing ubiquitin chain via the reaction X-ubiquitin + Y-ubiquitin -> Y-ubiquitin-ubiquitin + X, where both the X-ubiquitin and Y-ubiquitin-ubiquitin linkages are thioester bonds between the C-terminal glycine of ubiquitin and a sulfhydryl side group of a cysteine residue.
A small (70-100 nm) cytoplasmic granule that contains a number of centrosomal proteins; centriolar satellites traffic toward microtubule minus ends and are enriched near the centrosome.
Interacting selectively and non-covalently with any part of a dynactin complex; dynactin is a large protein complex that activates dynein-based motor activity.
Any process in which a microtubule is maintained in a specific location in a cell.
Any process in which a microtubule is maintained in a specific location in a cell by attachment to a centrosome.
A protein complex that forms a subcomplex of the 90S preribosome and is required for the subsequent assembly of the rest of the preribosome. In S. cerevisiae, it is composed of Utp5p, Utp4p, Nan1p, Utp8p, Utp9p, Utp10 and Utp15p.
A protein complex that forms a subcomplex of the 90S preribosome. In S. cerevisiae, it is composed of Rrp7p, Utp22p, Ckb1p, Cka1p, Ckb2p and Cka2p.
A protein complex that forms a subcomplex of the 90S preribosome. In S. cerevisiae, it is composed of Mpp10p, Imp3p and Imp4p.
Catalysis of the unwinding of an RNA helix in the direction 3' to 5'.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction drives the unwinding of an RNA helix in the direction 3' to 5'.
The assembly of a uropod by rearrangement of the cytoskeleton and overlying membrane.
The process in which a uropod detaches from the cell substrate and retracts the rear of a migrating cell.
The aggregation, arrangement and bonding together of proteins and RNA molecules to form a small-subunit processome.
The aggregation, arrangement and bonding together of proteins and RNA molecules to form a small-subunit processome.
The aggregation, arrangement and bonding together of proteins and RNA molecules to form a 90S preribosome. The 90S preribosome represents the complex that forms on the primary rRNA transcript before it splits into the small subunit and large subunit portions.
A ciliary protein complex involved in cilium biogenesis. It consists of at least seven Bardet-Biedl syndrome (BBS) proteins and BBIP10. It moves in association with IFT trains through cilia (likely as an IFT-A/B adaptor or cargo), and is required for the integrity of IFT-A and IFT-B.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a carbon monoxide (CO) stimulus.
The volume enclosed by the membrane of a chromaffin granule.
The volume enclosed by the membrane of an esterosome.
The volume enclosed by the membrane of a glycosome.
The volume enclosed by any of the membranes of the thin, flattened cisternae that form the central portion of the Golgi complex.
Any process that results in the conversion of one or more primary non-coding RNA (ncRNA) transcripts into one or more mature ncRNA molecules.
Any process involved in forming the mature 5' end of a non-coding RNA molecule.
Any process involved in forming the mature 3' end of an snRNA molecule.
Any process involved in forming the mature 3' end of a U1 snRNA molecule.
Any process involved in forming the mature 3' end of a U2 snRNA molecule.
Any process involved in forming the mature 3' end of a U4 snRNA molecule.
Any process involved in forming the mature 3' end of a U5 snRNA molecule.
Any process involved in forming the mature 3' end of a U6 snRNA molecule.
The chemical reactions and pathways resulting in the breakdown of phosphatidylglycerols, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol.
The chemical reactions and pathways resulting in the breakdown of phosphatidylglycerols, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol.
The chemical reactions and pathways resulting in the breakdown of phosphatidylglycerols, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of glycerol.
Catalysis of the reaction: a phosphatidylglycerol + H2O = 1,2-diacylglycerol + glycerol 3-phosphate.
Catalysis of the reaction: phosphatidylcholine + H2O = 1,2-diacylglycerol + a choline phosphate.
Catalysis of the reaction: phosphatidylcholine + H2O = 1,2-diacylglycerol + a choline phosphate.
Catalysis of the reaction: phosphatidylcholine + H2O = 1,2-diacylglycerol + a choline phosphate.
Catalysis of the reaction: phosphatidylcholine + H2O = 1,2-diacylglycerol + a choline phosphate.
Catalysis of the reaction: phosphatidylcholine + H2O = 1,2-diacylglycerol + a choline phosphate.
Catalysis of the reaction: phosphatidylcholine + H2O = 1,2-diacylglycerol + a choline phosphate.
Catalysis of the reaction: phosphatidylcholine + H2O = 1,2-diacylglycerol + a choline phosphate.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin sulfate.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 2'-O-sulfate. Results in sulfation of glucuronic acid and iduronic acid residues.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 2'-O-sulfate. Results in sulfation of glucuronic acid and iduronic acid residues.
Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + heparan sulfate = adenosine 3',5'-bisphosphate + sulfated heparan sulfate.
The chemical reactions and pathways resulting in the breakdown of raffinose, the trisaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the breakdown of raffinose, the trisaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
The chemical reactions and pathways resulting in the breakdown of raffinose, the trisaccharide beta-D-fructofuranosyl alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranoside.
Catalysis of the reaction: phosphatidylinositol-3,4,5-trisphosphate + H2O = phosphatidylinositol-3,4-bisphosphate + phosphate.
The process in which a solute is transported from one side of the vacuolar membrane to the other.
The process in which an amino acid is transported from one side of the vacuolar membrane to the other.
The directed movement of basic amino acids out of the vacuole, across the vacuolar membrane.
The directed movement of neutral amino acids out of the vacuole, across the vacuolar membrane.
The directed movement of basic amino acids into the vacuole across the vacuolar membrane.
The directed movement of neutral amino acids into the vacuole across the vacuolar membrane.
The volume enclosed by the hydrogenosome membrane.
The volume enclosed by the melanosome membrane.
The volume enclosed by the microneme membrane.
The volume enclosed by the protein storage vacuole membrane.
The controlled breakdown of the membranes of multivesicular bodies.
Any process in which a protein is transported to, or maintained at, the phagophore assembly site (PAS).
Any process in which a protein is transported to, or maintained at, the phagophore assembly site (PAS).
Any process in which a protein is transported to, or maintained at, the phagophore assembly site (PAS).
The directed movement of substances from early endosomes to the Golgi.
The directed movement of substances from early endosomes to the Golgi.
The directed movement of substances from late endosomes to the Golgi.
The directed movement of substances from late endosomes to the Golgi.
Any process in which a protein is transported to, or maintained at, the kinetochore.
Any process in which a protein is transported to, or maintained at, the kinetochore.
Any process in which a protein is transported to, or maintained at, a specific location on a chromosome.
Any process in which a protein is transported to, or maintained at, a specific location on a chromosome.
Any process in which a protein is transported to, or maintained at, the rDNA repeats on a chromosome in the nucleolus.
Any process in which a protein is transported to, or maintained at, the rDNA repeats on a chromosome in the nucleolus.
A process in which a protein transports or maintains the localization of another protein to the nucleus.
A process in which a protein transports or maintains the localization of another protein to the nucleus.
A process in which a protein transports or maintains the localization of another protein to the nucleus.
A process in which a protein transports or maintains the localization of another protein to the nucleus.
A process in which a protein transports or maintains the localization of another protein to the nucleus.
The process in which calcium salts are deposited into calcareous tooth structures such as dental enamel, dentin and cementum.
The innermost portion of the centromeric region of a chromosome, encompassing the core region of a chromosome centromere and the proteins that bind to it.
The innermost portion of the centromeric region of a chromosome, encompassing the core region of a chromosome centromere and the proteins that bind to it.
The portion of the centromeric region of a chromosome that flanks the core region, encompassing repeated regions of a chromosome centromere and the proteins that bind to it.
The aggregation, arrangement and bonding together of proteins and centromeric DNA molecules to form a centromeric protein-DNA complex. Includes the formation of the chromatin structures which form a platform for the kinetochore, and assembly of the kinetochore onto this specialized chromatin. In fission yeast and higher eukaryotes this process also includes the formation of heterochromatin at the outer repeat (pericentric) regions of the centromere.
The aggregation, arrangement and bonding together of proteins and centromeric DNA molecules to form a centromeric protein-DNA complex. Includes the formation of the chromatin structures which form a platform for the kinetochore, and assembly of the kinetochore onto this specialized chromatin. In fission yeast and higher eukaryotes this process also includes the formation of heterochromatin at the outer repeat (pericentric) regions of the centromere.
The aggregation, arrangement and bonding together of proteins and centromeric DNA molecules to form a centromeric protein-DNA complex. Includes the formation of the chromatin structures which form a platform for the kinetochore, and assembly of the kinetochore onto this specialized chromatin. In fission yeast and higher eukaryotes this process also includes the formation of heterochromatin at the outer repeat (pericentric) regions of the centromere.
The cell cycle process in which centromeres are physically detached from each other during chromosome separation.
Interacting selectively and non-covalently with U3 small nucleolar RNA.
Interacting selectively and non-covalently with box C/D small nucleolar RNA.
Interacting selectively and non-covalently with box H/ACA small nucleolar RNA.
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the mitochondrial matrix; results in transcriptional upregulation of nuclear genes encoding mitochondrial stress proteins.
A multisubunit proteasome complex that localizes in the cytoplasm as dot-like structures when cells are in a quiescent state.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin B6 stimulus. Vitamin B6 encompasses pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate.
The process in which cells degrade mature ribosomes under conditions of starvation.
Any protein complex that binds to a specialized RNA cap structure at any time in the lifetime of the RNA.
A protein complex found in the cytoplasm that binds the 5' cap structure of an mRNA, and typically consists of the cap-binding protein eIF4E, the adaptor protein eIF4G, and a multi-factor complex comprising eIF1, eIF2, eIF3 and eIF5. This complex mediates recruitment of the 40S subunit to mRNA.
Catalysis of the reaction: 2-naphthaldehyde + NAD+ + H2O = 2-naphthoate + NADH + H+.
Catalysis of the reaction: 1-naphthoic acid + NADH + O2 + H+ = cis-1,2-dihydroxy-1,2-dihydro-8-carboxynaphthalene + NAD+.
Catalysis of the reaction: cis-1,2-dihydroxy-1,2-dihydro-8-carboxynaphthalene = 1,2-dihydroxy-8-carboxynaphthalene + 2 H+ + 2 e-.
Catalysis of the reaction: 3-formylsalicylic acid + O2 + H2O = 2-hydroxyisophthalic acid + hydrogen peroxide.
Catalysis of the reaction: 2-hydroxyisophthalic acid = salicylate + CO2.
Catalysis of the reaction: 1-naphthaldehyde + NAD+ + H2O = 1-naphthoic acid + NADH + H+.
Catalysis of the reaction: 2-methylnaphthalene + NADH + O2 + H+ = 2-hydroxymethylnaphthalene + NAD+ + H2O.
Catalysis of the reaction: 1,2-dihydroxy-8-carboxynaphthalene + O2 = 2-carboxy-2-hydroxy-8-carboxychromene.
Catalysis of the reaction: 2-carboxy-2-hydroxy-8-carboxychromene = 2-hydroxy-3-carboxybenzalpyruvate.
Catalysis of the reaction: 2-hydroxy-3-carboxybenzalpyruvate + H2O = 3-formylsalicylic acid + pyruvate.
Catalysis of the reaction: 4-hydroxymethylsalicylaldehyde + NAD+ + H2O = 4-hydroxymethylsalicylate + NADH + 2 H+.
Catalysis of the reaction: 2-hydroxy-4-hydroxymethylbenzalpyruvate + H2O = pyruvate + 4-hydroxymethylsalicylaldehyde.
Catalysis of the reaction: 2-hydroxy-7-hydroxymethylchromene-2-carboxylate = 2-hydroxy-4-hydroxymethylbenzalpyruvate.
Catalysis of the reaction: 1,2-dihydroxy-7-hydroxymethylnaphthalene + O2 = 2-hydroxy-7-hydroxymethylchromene-2-carboxylate.
Catalysis of the reaction: 1-methylnaphthalene + NADH + H+ + O2 = 1-hydroxymethylnaphthalene + NAD+ + H2O.
Catalysis of the reaction: 1,2-dihydroxy-8-methylnaphthalene + O2 = 2-hydroxy-8-methylchromene-2-carboxylate + H+.
Catalysis of the reaction: 2-hydroxy-8-methylchromene-2-carboxylate = 2-hydroxy-3-methylbenzalpyruvate.
Catalysis of the reaction: 2-hydroxy-3-methylbenzalpyruvate + H2O = pyruvate + 3-methylsalicylaldehyde.
Catalysis of the reaction: 3-methylsalicylaldehyde + NAD+ = 3-methylsalicylate + NADH + H+.
Catalysis of the reaction: 3,3',5,5'-tetrabromobisphenol A + 2 H+ + 2 e- = 3,3',5-tribromobisphenol A + HBr.
Catalysis of the reaction: 3-monobromobisphenol A + 2 H+ + 2 e- = bisphenol A + HBr.
Catalysis of the reaction: dimethylarsenous acid + R2S-CH3 = trimethylarsine oxide + R2SH.
Catalysis of the reaction: trimethylarsine oxide + 2 H+ + 2 e- = trimethylarsine + H2O.
Catalysis of the reaction: 5-aminosalicylate + O2 = cis-4-amino-6-carboxy-2-oxo-hexa-3,5-dienoate.
Catalysis of the reaction: trans-4-amino-6-carboxy-2-oxo-hexa-3,5-dienoate + H2O = fumarylpyruvate + NH3.
Catalysis of the reaction: fumarylpyruvate + H2O = fumarate + pyruvate + H+.
Catalysis of the reaction: 2,4-dichloroaniline + 2 H+ + 2 e- = 4-chloroaniline + HCl.
Catalysis of the reaction: cyromazine + H2O = N-cyclopropylammeline + NH3.
Catalysis of the reaction: N-cyclopropylammeline + H2O = N-cyclopropylammelide + NH3.
Catalysis of the reaction: N-cyclopropylammelide + H2O = cyclopropylamine + cyanuric acid.
Catalysis of the reaction: dimethylarsinate + 3 H+ + 2 e- = dimethylarsinous acid + H2O.
The aggregation, arrangement and bonding together of a set of components to form the cytochrome bc(1) complex (also known as ubiquinol-cytochrome c reductase), in the mitochondrial inner membrane.
The aggregation, arrangement and bonding together of a set of components to form respiratory chain complex II.
The aggregation, arrangement and bonding together of a set of components to form respiratory chain complex II, in the mitochondrial inner membrane.
Catalysis of the reaction: 3,3',5-tribromobisphenol A + 2 H+ + 2 e- = 3,3'-dibromobisphenol A + HBr.
Catalysis of the reaction: 3,3'-dibromobisphenol A + 2 H+ + 2 e- = 3-monobromobisphenol A + HBr.
Catalysis of the reaction: o-nitrobenzoate + NADPH + H+ = o-hydroxylaminobenzoate + NADP+.
Catalysis of the reaction: 2-hydroxylaminobenzoate + NAD(P)H = anthranilate + NAD(P)+ + H2O.
Catalysis of the reaction: pertechnetate ion + 3/2 H2 = technetium (IV) oxide + H2O + OH-.
Catalysis of the reaction: bisphenol A + NADH + H+ + O2 = 1,2-bis(4-hydroxyphenyl)-2-propanol + NAD+ + H2O.
Catalysis of the reaction: bisphenol A + NADH + H+ + O2 = 2,2-bis(4-hydroxyphenyl)-1-propanol + NAD+ + H2O.
Catalysis of the reaction: 1,2-bis(4-hydroxyphenyl)-2-propanol = 4,4'-dihydroxy-alpha-methylstilbene + H2O.
Catalysis of the reaction: 2,2-bis(4-hydroxyphenyl)-1-propanol + NADH + H+ + O2 = 2,3-bis(4-hydroxyphenyl)-1,2-propanediol + NAD+ + H2O.
Catalysis of the reaction: 2,3-bis(4-hydroxyphenyl)-1,2-propanediol + O2 = 4-hydroxyphenacyl alcohol + 4-hydroxybenzoate + 2 H+ + 2 e-.
Catalysis of the reaction: 4,4'-dihydroxy-alpha-methylstilbene + O2 = 4-hydroxybenzaldehyde + 4-hydroxyacetophenone + 2 H+ + 2 e-.
Catalysis of the reaction: 1-nitro-1,2-dihydro-1,3,5-triazine + 2 H2O = 1-nitro-1,3,5-triazinane-2,4-diol.
Catalysis of the reaction: chromate = chromium (III).
Catalysis of the reaction: isoproturon + H2O = formaldehyde + monodemethylisoproturon + 2 H+ + 2 e-.
Catalysis of the reaction: monodemethylisoproturon + H2O = hydroxymonodemethylisoproturon + 2 H+ + 2 e-.
Catalysis of the reaction: hydroxymonodemethylisoproturon + H2O = formaldehyde + 4'-(2-hydroxyisopropyl)phenylurea + 2 H+ + 2 e-.
Catalysis of the reaction: 4'-(2-hydroxyisopropyl)phenylurea + H2O = 4'-(2-hydroxyisopropyl)phenylaniline + carbamic acid.
Catalysis of the reaction: monodemethylisoproturon + H2O = didemethylisoproturon + formaldehyde + 2 H+ + 2 e-.
Catalysis of the reaction: didemethylisoproturon + H2O = carbamic acid + 4-isopropylaniline.
Catalysis of the reaction: didemethylisoproturon + H2O = 4'-(2-hydroxyisopropyl)phenylurea + 2 H+ + 2 e-.
Catalysis of the reaction: 4-isopropylaniline + H2O = 4'-(2-hydroxyisopropyl)phenylaniline + 2 H+ + 2 e-.
Catalysis of the reaction: N-isopropylacetanilide + OH- = N-isopropylaniline + acetate.
Catalysis of the reaction: N-isopropylacetanilide + 1/2 O2 = acetanilide + acetone.
Catalysis of the reaction: limonene + H2O = alpha-terpineol.
Catalysis of the reaction: fumarate + n-hexane = (1-methylpentyl)succinate.
Catalysis of the reaction: 4-methyloctanoyl-CoA = 4-methyloct-2-enoyl-CoA + 2 H+ + 2 e-.
Catalysis of the reaction: 4-methyloct-2-enoyl-CoA + H2O = 3-hydroxy-4-methyloctanoyl-CoA.
Catalysis of the reaction: 3-hydroxy-4-methyloctanoyl-CoA = 4-methyl-3-oxooctanoyl-CoA + 2 H+ + 2 e-.
Interacting selectively and non-covalently with a 21U-RNA, a 21-nucleotide RNA characterized by a uridine 5'-monophosphate and a modified 3' end resistant to periodate degradation. 21U-RNAs are derived from distinct, autonomously expressed loci within the genome.
Interacting selectively and non-covalently with a piRNA, a Piwi-associated RNA, a 24- to 30-nucleotide RNA derived from repeat or complex DNA sequence elements and processed by a Dicer-independent mechanism.
The chemical reactions and pathways involving 21U-RNAs, a class of single-stranded RNA molecules of about 21 nucleotides in length characterized by a uridine 5'-monophosphate and a modified 3' end resistant to periodate degradation. 21U-RNAs are derived from distinct, autonomously expressed loci within the genome.
The chemical reactions and pathways resulting in the breakdown of 21U-RNAs, a class of single-stranded RNA molecules of about 21 nucleotides in length characterized by a uridine 5'-monophosphate and a modified 3' end resistant to periodate degradation. 21U-RNAs are derived from distinct, autonomously expressed loci within the genome.
The chemical reactions and pathways resulting in the breakdown of 21U-RNAs, a class of single-stranded RNA molecules of about 21 nucleotides in length characterized by a uridine 5'-monophosphate and a modified 3' end resistant to periodate degradation. 21U-RNAs are derived from distinct, autonomously expressed loci within the genome.
The chemical reactions and pathways resulting in the breakdown of 21U-RNAs, a class of single-stranded RNA molecules of about 21 nucleotides in length characterized by a uridine 5'-monophosphate and a modified 3' end resistant to periodate degradation. 21U-RNAs are derived from distinct, autonomously expressed loci within the genome.
The chemical reactions and pathways involving piRNAs, Piwi-associated RNAs, a class of 24- to 30-nucleotide RNA derived from repeat or complex DNA sequence elements and processed by a Dicer-independent mechanism.
The chemical reactions and pathways involving piRNAs, Piwi-associated RNAs, a class of 24- to 30-nucleotide RNA derived from repeat or complex DNA sequence elements and processed by a Dicer-independent mechanism.
The chemical reactions and pathways resulting in the breakdown of piRNAs, Piwi-associated RNAs, a class of 24- to 30-nucleotide RNA derived from repeat or complex DNA sequence elements and processed by a Dicer-independent mechanism.
The chemical reactions and pathways resulting in the breakdown of piRNAs, Piwi-associated RNAs, a class of 24- to 30-nucleotide RNA derived from repeat or complex DNA sequence elements and processed by a Dicer-independent mechanism.
The chemical reactions and pathways resulting in the breakdown of piRNAs, Piwi-associated RNAs, a class of 24- to 30-nucleotide RNA derived from repeat or complex DNA sequence elements and processed by a Dicer-independent mechanism.
The chemical reactions and pathways resulting in the breakdown of piRNAs, Piwi-associated RNAs, a class of 24- to 30-nucleotide RNA derived from repeat or complex DNA sequence elements and processed by a Dicer-independent mechanism.
The directed movement of hydroxyproline into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The directed movement of hydroxyproline into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Enables the transfer of L-hydroxyproline from one side of a membrane to the other.
The volume enclosed by the rhoptry membrane.
The volume enclosed by the synaptic vesicle membrane.
Catalysis of the removal of the 5-phosphate group of a phosphatidylinositol phosphate.
Catalysis of the removal of the 5-phosphate group of a phosphatidylinositol phosphate.
Catalysis of the removal of the 4-phosphate group of a phosphatidylinositol phosphate.
Catalysis of the removal of the 4-phosphate group of a phosphatidylinositol phosphate.
Catalysis of the removal of the 4-phosphate group of a phosphatidylinositol phosphate.
Catalysis of the removal of the 4-phosphate group of a phosphatidylinositol phosphate.
Catalysis of the removal of the 4-phosphate group of a phosphatidylinositol phosphate.
Catalysis of the reaction: 1-phosphatidyl-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate.
Catalysis of the reaction: 1-phosphatidyl-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate.
Catalysis of the reaction: 1-phosphatidyl-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate.
Catalysis of the removal of the phosphate group from phosphothreonine by cleavage of the C-OP bond with the concomitant abstraction of the alpha proton, generating a double bond-containing product.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
Catalysis of the reaction: 2-oxoglutarate + CoA + NAD(P)+ = succinyl-CoA + CO2 + NAD(P)H.
Catalysis of the reaction: 2-oxoglutarate + CoA + NAD+ = succinyl-CoA + CO2 + NADH.
Catalysis of the reaction: pyruvate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H.
Catalysis of the reaction: pyruvate + CoA + NAD+ = acetyl-CoA + CO2 + NADH.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
The response by the male to a hermaphrodite after initial contact following mate finding. The male stops forward locomotion, presses the ventral side of his tail against his partner's body, and begins moving backward along the hermaphrodite. Male response behavior is initiated when sensory neurons located in the rays of his tail contact a potential mate.
The sharp ventral turn performed by the male as he approaches either the hermaphrodite head or tail, whilst trying to locate his partner's vulva. Turning occurs via a sharp ventral coil of the male's tail.
Location, by the male, of his partner's vulva when backing along the ventral side of the hermaphrodite during mating. The male stops at the vulva, coordinates his movements to the hermaphrodite's, and positions his tail precisely over the vulva so that he may insert his spicules and ejaculate.
Insertion of the male copulatory spicules into the hermaphrodite. Spicule insertion behavior initiates when the male cloaca contacts the vulva. During most mating encounters, the spicule tips will prod the vulva continuously until they partially penetrate, which then causes the protractors to contract completely so that the spicules extend through the vulva.
Catalysis of the exonucleolytic cleavage of oligodeoxyribonucleotides to yield deoxyribonucleoside 5'-phosphates.
Catalysis of the exonucleolytic cleavage of oligoribonucleotides to yield ribonucleoside 5'-phosphates.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tumor necrosis factor stimulus.
Any process in which a protein is transported to, and/or maintained in, a specific location at the level of a cell. Localization at the cellular level encompasses movement within the cell, from within the cell to the cell surface, or from one location to another at the surface of a cell.
Any process in which a protein is transported to, and/or maintained in, a specific location at the level of a cell. Localization at the cellular level encompasses movement within the cell, from within the cell to the cell surface, or from one location to another at the surface of a cell.
Any process in which a protein is transported to, and/or maintained in, a specific location at the level of a cell. Localization at the cellular level encompasses movement within the cell, from within the cell to the cell surface, or from one location to another at the surface of a cell.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
A protein complex that possesses GTP cyclohydrolase I activity. In E. coli and human, the complex is a homodecamer, and monomers are catalytically inactive.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a laminar fluid shear stress stimulus. Laminar fluid flow is the force acting on an object in a system where the fluid is moving across a solid surface in parallel layers. As an example, laminar shear stress can be seen where blood flows against the luminal side of blood vessel walls.
Interacting selectively and non-covalently with a tetrahydrobiopterin, 5,6,7,8-tetrahydrobiopterin or a derivative thereof; tetrahydrobiopterins are enzyme cofactors that carry electrons in redox reactions.
Interacting selectively and non-covalently with a tetrahydrobiopterin, 5,6,7,8-tetrahydrobiopterin or a derivative thereof; tetrahydrobiopterins are enzyme cofactors that carry electrons in redox reactions.
Interacting selectively and non-covalently with a tetrahydrobiopterin, 5,6,7,8-tetrahydrobiopterin or a derivative thereof; tetrahydrobiopterins are enzyme cofactors that carry electrons in redox reactions.
Interacting selectively and non-covalently with 2-amino-5-(carbamimidamido)pentanoic acid.
Interacting selectively and non-covalently with 2-amino-5-(carbamimidamido)pentanoic acid.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.
The aggregation, arrangement and bonding together of a set of components to form a protein complex, occurring at the level of an individual cell.
The aggregation, arrangement and bonding together of a set of components to form a protein complex, occurring at the level of an individual cell.
The aggregation, arrangement and bonding together of a set of components to form a protein complex, occurring at the level of an individual cell.
The aggregation, arrangement and bonding together of strand exchange proteins (recombinases) into higher order oligomers on single-stranded DNA, involved in the conversion of the mating-type locus from one allele to another.
Elongation of a fatty acid chain into which one C-C double bond has been introduced.
Elongation of a fatty acid chain into which two or more C-C double bonds have been introduced.
The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD), beginning with the synthesis of tryptophan or aspartate from simpler precursors; biosynthesis may be of either the oxidized form, NAD, or the reduced form, NADH.
The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD), beginning with the synthesis of aspartate from simpler precursors; biosynthesis may be of either the oxidized form, NAD, or the reduced form, NADH.
A protein complex localization process that takes place at the cellular level; as a result, a protein complex is transported to, or maintained in, a specific location within a cell.
A protein complex localization process that takes place at the cellular level; as a result, a protein complex is transported to, or maintained in, a specific location within a cell.
A protein complex localization process that takes place at the cellular level; as a result, a protein complex is transported to, or maintained in, a specific location within a cell.
Any process in which a RITS complex is transported to, or maintained in, a specific location.
Any process in which a RITS complex is transported to, or maintained in, a specific location.
Any process in which a microtubule is maintained in a specific location in a cell by attachment to a spindle pole body. Microtubules attach to spindle pole bodies at the minus end.
Any process in which a microtubule is maintained in a specific location in a cell by attachment to a spindle pole body. Microtubules attach to spindle pole bodies at the minus end.
Any process in which a microtubule is maintained in a specific location in a cell by attachment to a spindle pole body. Microtubules attach to spindle pole bodies at the minus end.
Enables the transfer of retinol from one side of a membrane to the other. Retinol is vitamin A1, 2,6,6-trimethyl-1-(9'-hydroxy-3',7'-dimethylnona-1',3',5',7'-tetraenyl)cyclohex-1-ene, one of the three components that makes up vitamin A.
Enables the transfer of retinol from one side of a membrane to the other. Retinol is vitamin A1, 2,6,6-trimethyl-1-(9'-hydroxy-3',7'-dimethylnona-1',3',5',7'-tetraenyl)cyclohex-1-ene, one of the three components that makes up vitamin A.
The directed movement of retinol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Retinol is vitamin A1, 2,6,6-trimethyl-1-(9'-hydroxy-3',7'-dimethylnona-1',3',5',7'-tetraenyl)cyclohex-1-ene, one of the three components that makes up vitamin A.
Enables the transfer of glutathione, the tripeptide glutamylcysteinylglycine, from one side of a membrane to the other.
The directed movement of glutathione, the tripeptide glutamylcysteinylglycine, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The process in which the nucleoprotein complex (composed of the broken single-strand DNA and the recombinase) searches and identifies a region of homology in intact duplex DNA at the mating-type locus. The broken single-strand DNA displaces the like strand and forms Watson-Crick base pairs with its complement, forming a duplex in which each strand is from one of the two recombining DNA molecules. This process occurs as part of gene conversion at the mating-type locus.
The chemical reactions and pathways resulting in the formation of carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y, carried out by individual cells.
The chemical reactions and pathways resulting in the breakdown of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline.
The chemical reactions and pathways resulting in the breakdown of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline.
The chemical reactions and pathways resulting in the breakdown of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline.
Enables the transfer of an L-amino acid from the inside of the cell to the outside of the cell across a membrane.
Enables the transfer of an L-amino acid from the inside of the cell to the outside of the cell across a membrane.
The directed movement of a mitochondrion by attachment to a microtubule, followed by elongation of the microtubule by tubulin polymerization.
The directed movement of a mitochondrion by attachment to a microtubule, followed by elongation of the microtubule by tubulin polymerization.
The directed movement of a mitochondrion by attachment to a microtubule, followed by elongation of the microtubule by tubulin polymerization.
The directed movement of a mitochondrion by attachment to a microtubule, followed by elongation of the microtubule by tubulin polymerization.
The chemical reactions and pathways involving various organic and inorganic nitrogenous compounds, as carried out by individual cells.
The directed movement of a mitochondrion along a microfilament, mediated by motor proteins.
The directed movement of a mitochondrion along a microfilament, mediated by motor proteins.
The directed movement of a mitochondrion along a microfilament, mediated by motor proteins.
The directed movement of a mitochondrion along a microfilament, mediated by motor proteins.
The directed movement of a mitochondrion along a microfilament, mediated by motor proteins.
The directed movement of the mitochondrion to a specific location, by a process involving microtubules.
The directed movement of the mitochondrion to a specific location, by a process involving microtubules.
The directed movement of the mitochondrion to a specific location, by a process involving microtubules.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
The chemical reactions and pathways resulting in the formation of a macromolecule, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass, carried out by individual cells.
The chemical reactions and pathways resulting in the formation of a macromolecule, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass, carried out by individual cells.
The chemical reactions and pathways resulting in the formation of a macromolecule, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass, carried out by individual cells.
The chemical reactions and pathways resulting in the formation of a macromolecule, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass, carried out by individual cells.
The chemical reactions and pathways resulting in the formation of a macromolecule, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass, carried out by individual cells.
The chemical reactions and pathways resulting in the formation of a macromolecule, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass, carried out by individual cells.
A lipid monolayer that surrounds and encloses an organelle.
Catalysis of the removal of a methyl group from trimethylated lysine at position 4 of the histone H3 protein.
Catalysis of the removal of a methyl group from dimethylated lysine at position 4 of the histone H3 protein.
Catalysis of the reaction: histone H3 N6-methyl-L-lysine (position 4) + O2 + FAD + H2O = histone H3 L-lysine (position 4) + H2O2 + formaldehyde + FADH2. This reaction is the removal of a methyl group from monomethylated lysine at position 4 of the histone H3 protein.
The chemical reactions and pathways involving cortisol, the steroid hormone 11-beta-17,21-trihydroxypregn-4-ene-3,20-dione. Cortisol is synthesized from cholesterol in the adrenal gland and controls carbohydrate, fat and protein metabolism and has anti-inflammatory properties.
The chemical reactions and pathways resulting in the formation of cortisol, the steroid hormone 11-beta-17,21-trihydroxypregn-4-ene-3,20-dione. Cortisol is synthesized from cholesterol in the adrenal gland and controls carbohydrate, fat and protein metabolism and has anti-inflammatory properties.
The chemical reactions and pathways resulting in the formation of cortisol, the steroid hormone 11-beta-17,21-trihydroxypregn-4-ene-3,20-dione. Cortisol is synthesized from cholesterol in the adrenal gland and controls carbohydrate, fat and protein metabolism and has anti-inflammatory properties.
The chemical reactions and pathways resulting in the formation of cortisol, the steroid hormone 11-beta-17,21-trihydroxypregn-4-ene-3,20-dione. Cortisol is synthesized from cholesterol in the adrenal gland and controls carbohydrate, fat and protein metabolism and has anti-inflammatory properties.
The chemical reactions and pathways resulting in the formation of cortisol, the steroid hormone 11-beta-17,21-trihydroxypregn-4-ene-3,20-dione. Cortisol is synthesized from cholesterol in the adrenal gland and controls carbohydrate, fat and protein metabolism and has anti-inflammatory properties.
A process in which extrachromosomal circular DNA molecules are transported to, or maintained in, a specific location in cells contributing to their aging.
A process in which extrachromosomal circular DNA molecules are transported to, or maintained in, a specific location in cells contributing to their aging.
A process in which extrachromosomal circular DNA molecules are transported to, or maintained in, a specific location in cells contributing to their aging.
The chemical reactions and pathways resulting in the breakdown of retinoic acid, one of the three components that makes up vitamin A.
The chemical reactions and pathways resulting in the breakdown of retinoic acid, one of the three components that makes up vitamin A.
The chemical reactions and pathways resulting in the breakdown of retinoic acid, one of the three components that makes up vitamin A.
The chemical reactions and pathways resulting in the breakdown of retinoic acid, one of the three components that makes up vitamin A.
The chemical reactions and pathways resulting in the formation of nucleobases, nucleosides, nucleotides and nucleic acids.
The chemical reactions and pathways resulting in the formation of nucleobases, nucleosides, nucleotides and nucleic acids.
The chemical reactions and pathways resulting in the formation of nucleobases, nucleosides, nucleotides and nucleic acids.
The chemical reactions and pathways resulting in the formation of nucleobases, nucleosides, nucleotides and nucleic acids.
The chemical reactions and pathways resulting in the breakdown of nucleobases, nucleosides, nucleotides and nucleic acids.
The chemical reactions and pathways resulting in the breakdown of nucleobases, nucleosides, nucleotides and nucleic acids.
The chemical reactions and pathways resulting in the breakdown of nucleobases, nucleosides, nucleotides and nucleic acids.
The chemical reactions and pathways resulting in the breakdown of nucleobases, nucleosides, nucleotides and nucleic acids.
The chemical reactions and pathways resulting in the breakdown of a nucleobase-containing small molecule: a nucleobase, a nucleoside, or a nucleotide.
The chemical reactions and pathways resulting in the breakdown of a nucleobase-containing small molecule: a nucleobase, a nucleoside, or a nucleotide.
The chemical reactions and pathways resulting in the breakdown of a nucleobase-containing small molecule: a nucleobase, a nucleoside, or a nucleotide.
A protein complex with ubiquitin ligase activity that is involved in proteasomal degradation of fructose-1,6-bisphosphatase (FBPase) and phosphoenolpyruvate carboxykinase during the transition from gluconeogenic to glycolytic growth conditions. In S. cerevisiae, the GID (Glucose Induced degradation Deficient) complex consists of Vid30p, Rmd5p, Vid24p, Vid28p, Gid7p, Gid8p, and Fyv10p.
Enables the transfer of isopropylmalate from one side of a membrane to the other.
The directed movement of isopropylmalate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The chemical reactions and pathways involving non-coding RNA transcripts (ncRNAs).
The chemical reactions and pathways resulting in the breakdown of non-coding RNA transcripts (ncRNAs). Includes the breakdown of cryptic unstable transcripts (CUTs).
The chemical reactions and pathways resulting in the breakdown of non-coding RNA transcripts (ncRNAs). Includes the breakdown of cryptic unstable transcripts (CUTs).
The chemical reactions and pathways resulting in the breakdown of non-coding RNA transcripts (ncRNAs). Includes the breakdown of cryptic unstable transcripts (CUTs).
A protein complex that contains ezrin, Na+/H+ exchanger regulatory factor (NHERF, also called EBP50), and two copies of the cystic fibrosis transmembrane conductance regulator (CFTR). The CFTR molecules interact with NHERF via their cytoplasmic tail domains; the complex is thought to link the CFTR channel to the actin cytoskeleton and contribute to the regulation of channel activity.
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
A protein complex that is located in the endoplasmic reticulum (ER) and is formed by the association of an immunoglobulin heavy chain with the proteins of the ER chaperone complex; the latter include BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
A protein complex that is located in the endoplasmic reticulum (ER) and is formed by the association of an immunoglobulin heavy chain with the proteins of the ER chaperone complex; the latter include BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1.
An integrin complex that comprises one alpha1 subunit and one beta1 subunit.
An integrin complex that comprises one alpha1 subunit and one beta1 subunit.
An integrin complex that comprises one alpha1 subunit and one beta1 subunit.
An integrin complex that comprises one alpha2 subunit and one beta1 subunit.
An integrin complex that comprises one alpha2 subunit and one beta1 subunit.
An integrin complex that comprises one alpha3 subunit and one beta1 subunit.
An integrin complex that comprises one alpha3 subunit and one beta1 subunit.
An integrin complex that comprises one alpha3 subunit and one beta1 subunit.
An integrin complex that comprises one alpha4 subunit and one beta1 subunit.
An integrin complex that comprises one alpha4 subunit and one beta1 subunit.
An integrin complex that comprises one alpha4 subunit and one beta1 subunit.
An integrin complex that comprises one alpha4 subunit and one beta7 subunit.
An integrin complex that comprises one alpha4 subunit and one beta7 subunit.
The directed movement of a motile cell or organism in response to the presence of arachidonic acid.
The series of molecular signals generated as a consequence of a retinoic acid receptor binding to one of its physiological ligands that results in the spatial identity of regions along the anterior-posterior axis of the pronephros.
The series of molecular signals generated as a consequence of a retinoic acid receptor binding to one of its physiological ligands that results in the spatial identity of regions along the anterior-posterior axis of the pronephros.
The developmental process that results in the creation of defined areas or spaces within the pronephros along the anterior/posterior axis to which cells respond and eventually are instructed to differentiate.
A protein complex that consists of inhibin, type III transforming growth factor beta receptor (also known as betaglycan), and the type II activin receptor ActRII. The complex is thought to negatively regulate the activity of activin B.
An integrin complex that comprises one alpha5 subunit and one beta1 subunit.
An integrin complex that comprises one alpha5 subunit and one beta1 subunit.
An integrin complex that comprises one alpha5 subunit and one beta1 subunit.
An integrin complex that comprises one alpha6 subunit and one beta1 subunit.
An integrin complex that comprises one alpha6 subunit and one beta1 subunit.
An integrin complex that comprises one alpha6 subunit and one beta1 subunit.
An integrin complex that comprises one alpha6 subunit and one beta4 subunit.
An integrin complex that comprises one alpha6 subunit and one beta4 subunit.
An integrin complex that comprises one alpha7 subunit and one beta1 subunit.
An integrin complex that comprises one alpha7 subunit and one beta1 subunit.
An integrin complex that comprises one alpha8 subunit and one beta1 subunit.
An integrin complex that comprises one alpha8 subunit and one beta1 subunit.
An integrin complex that comprises one alpha9 subunit and one beta1 subunit.
An integrin complex that comprises one alpha9 subunit and one beta1 subunit.
An integrin complex that comprises one alpha10 subunit and one beta1 subunit.
An integrin complex that comprises one alpha10 subunit and one beta1 subunit.
An integrin complex that comprises one alpha11 subunit and one beta1 subunit.
An integrin complex that comprises one alpha11 subunit and one beta1 subunit.
An integrin complex that comprises one alphav subunit and one beta1 subunit.
An integrin complex that comprises one alphav subunit and one beta1 subunit.
An integrin complex that comprises one alphav subunit and one beta3 subunit.
An integrin complex that comprises one alphav subunit and one beta3 subunit.
An integrin complex that comprises one alphav subunit and one beta5 subunit.
An integrin complex that comprises one alphav subunit and one beta5 subunit.
An integrin complex that comprises one alphav subunit and one beta6 subunit.
An integrin complex that comprises one alphav subunit and one beta6 subunit.
An integrin complex that comprises one alphav subunit and one beta8 subunit.
An integrin complex that comprises one alphav subunit and one beta8 subunit.
An integrin complex that comprises one alphaL subunit and one beta2 subunit.
An integrin complex that comprises one alphaL subunit and one beta2 subunit.
An integrin complex that comprises one alphaM subunit and one beta2 subunit.
An integrin complex that comprises one alphaM subunit and one beta2 subunit.
An integrin complex that comprises one alphaX subunit and one beta2 subunit.
An integrin complex that comprises one alphaX subunit and one beta2 subunit.
An integrin complex that comprises one alphaD subunit and one beta2 subunit.
An integrin complex that comprises one alphaD subunit and one beta2 subunit.
An integrin complex that comprises one alphaE subunit and one beta7 subunit.
A protein complex that comprises three core spliceosomal proteins, designated E, F, and G. Formation of the E.F.G complex is essential but not sufficient for the formation of a stable U1 snRNP complex.
A ribonucleoprotein complex formed by the association of the U11 and U12 small nuclear ribonucleoproteins.
A ribonucleoprotein complex formed by the association of the U11 and U12 small nuclear ribonucleoproteins.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a prostagladin stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a prostagladin E stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a prostagladin F stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a prostagladin I stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gonadotropin stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a luteinizing hormone stimulus.
Catalysis of the reaction: D-allulose 6-phosphate = D-fructose 6-phosphate.
Catalysis of the hydrolysis of a tripeptide.
A protein complex that spans a membrane and forms a water-filled channel across the phospholipid bilayer allowing selective ion transport down its electrochemical gradient.
An ion channel complex through which cations pass.
An ion channel complex through which calcium ions pass.
An ion channel complex through which potassium ions pass.
An ion channel complex through which sodium ions pass.
An ion channel complex through which chloride ions pass.
A protein complex that possesses methyltransferase activity.
A large (20 S) protein complex that possesses protein arginine methyltransferase activity and modifies specific arginines to dimethylarginines in the arginine- and glycine-rich domains of several spliceosomal Sm proteins, thereby targeting these proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein (snRNP) core particles. Proteins found in the methylosome include the methyltransferase JBP1 (PRMT5), pICln (CLNS1A), MEP50 (WDR77), and unmethylated forms of SM proteins that have RG domains.
A large (20 S) protein complex that possesses protein arginine methyltransferase activity and modifies specific arginines to dimethylarginines in the arginine- and glycine-rich domains of several spliceosomal Sm proteins, thereby targeting these proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein (snRNP) core particles. Proteins found in the methylosome include the methyltransferase JBP1 (PRMT5), pICln (CLNS1A), MEP50 (WDR77), and unmethylated forms of SM proteins that have RG domains.
Interacting selectively and non-covalently with an inhibin complex, a dimer of one inhibin-alpha subunit and one inhibin-beta subunit.
Interacting selectively and non-covalently with an inhibin monomer, any of the polypeptides that combine to form activin and inhibin dimers.
Interacting selectively and non-covalently with an inhibin monomer, any of the polypeptides that combine to form activin and inhibin dimers.
Interacting selectively and non-covalently with an inhibin monomer, any of the polypeptides that combine to form activin and inhibin dimers.
Interacting selectively and non-covalently with an inhibin monomer, any of the polypeptides that combine to form activin and inhibin dimers.
Interacting selectively and non-covalently with an inhibin monomer, any of the polypeptides that combine to form activin and inhibin dimers.
Interacting selectively and non-covalently with an inhibin monomer, any of the polypeptides that combine to form activin and inhibin dimers.
Interacting selectively and non-covalently with an inhibin monomer, any of the polypeptides that combine to form activin and inhibin dimers.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type III transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type III transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type III transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type III transforming growth factor beta receptor.
Interacting selectively and non-covalently with a type III transforming growth factor beta receptor.
A protein complex that contains pICln (CLNS1A) and several Sm proteins, including SmD1, SmD2, SmE, SmF, and SmG.
A protein complex that contains Gemin3 (DDX20), Gemin4, and Gemin5, and can bind to snRNAs; may be an intermediate in SMN complex assembly.
A protein complex that contains Gemin6, Gemin7, and unrip (STRAP), and can bind to snRNAs; may play a role in snRNP assembly.
A protein complex that contains the survival motor neuron (SMN) protein and Gemin2; may form the stable core of the larger SMN complex.
A protein complex formed by the association of several methylated Sm proteins with the SMN complex; the latter contains the survival motor neuron (SMN) protein and at least eight additional integral components, including the Gemin2-8 and unrip proteins; additional proteins, including galectin-1 and galectin-3, are also found in the SMN-SM complex. The SMN-Sm complex is involved in spliceosomal snRNP assembly in the cytoplasm.
The modification of histone H3 by the removal of a methyl group from lysine at position 4 of the histone.
The modification of histone H3 by the removal of a methyl group from a trimetylated lysine at position 4 of the histone.
The modification of histone H3 by the removal of a methyl group from a trimetylated lysine at position 4 of the histone.
Catalysis of the cleavage of a gamma-linked glutamate bond.
The formation or destruction of chromatin structures on newly replicated DNA, coupled to strand elongation.
The formation or destruction of chromatin structures, occurring outside the context of DNA replication.
The controlled breakdown of nucleosomes on newly replicated DNA, coupled to strand elongation.
The controlled breakdown of nucleosomes outside the context of DNA replication.
Degradation of a cell nucleus by lysosomal microautophagy.
The modification of histone H3 by addition of a methyl group to lysine at position 79 of the histone.
The modification of histone H3 by addition of a methyl group to lysine at position 79 of the histone.
The modification of histone H3 by addition of a methyl group to lysine at position 79 of the histone.
An SMN-Sm protein complex formed by the association of the methylated Sm proteins B/B', D1, D2, D3, E, F, and G with the SMN complex.
An SMN-Sm protein complex formed by the association of the methylated Sm proteins B/B', D3, E, F, and G, and Lsm10 and Lsm11, with the SMN complex. This complex forms Sm cores on U7 snRNA.
A transcription factor TFIIIB-beta complex that contains the TATA-binding protein (TBP), B'' and a specialized homolog of the conserved subunit BRF referred to as BRFU or TFIIIB50, which found in human but not conserved in yeast; the complex is involved in the regulation of transcription from type 3 (upstream) RNA polymerase III promoters.
A transcription factor TFIIIB-beta complex that contains the TATA-binding protein (TBP), B'' and BRF, and is involved in the regulation of transcription from type 2 RNA polymerase III promoters.
A transcription factor complex that forms part of the TFIIIC complex, observed in human. The complex is poorly characterized, but contains the 250-kDa form of HsBdp1, and is thought to include nuclear factor 1 (NF1). It stimulates binding by human TFIIIC2 and is required for transcription activity.
A transcription factor complex that forms part of the TFIIIC complex, observed in human; composed of five subunits (GTF3C1/hTFIIIC220/TFIIICalpha, GTF3C2/hTFIIIC110/TFIIICbeta, GTF3C3/hTFIIIC102/TFIIICgamma, GTF3C4/hTFIIIC90/TFIIICdelta and GTF3C5/hTFIIIC63/TFIIICepsilon in human) that together recognize the type 2 RNA polymerase III promoter.
Catalysis of the reaction: acyl-CoA + cholesterol = a cholesterol ester + CoA.
Catalysis of the reaction: acyl-CoA + cholesterol = a cholesterol ester + CoA.
Catalysis of the reaction: acyl-CoA + cholesterol = a cholesterol ester + CoA.
Catalysis of the reaction: acyl-CoA + cholesterol = a cholesterol ester + CoA.
Catalysis of the reaction: acyl-CoA + cholesterol = a cholesterol ester + CoA.
Catalysis of the reaction: acyl-CoA + cholesterol = a cholesterol ester + CoA.
Catalysis of the reaction: acyl-CoA + cholesterol = a cholesterol ester + CoA.
Catalysis of the reaction: acyl-CoA + cholesterol = a cholesterol ester + CoA.
Catalysis of the reaction: acyl-CoA + ergosterol = CoA + ergosterol ester.
Catalysis of the reaction: acyl-CoA + lanosterol = CoA + lanosterol ester.
Catalysis of the reaction: histone H4 N6-acetyl-L-lysine (position 16) + H2O = histone H4 L-lysine (position 16) + acetate. This reaction represents the removal of an acetyl group from lysine at position 16 of the histone H4 protein.
A protein complex that contains TFIIIC, topoisomerase 1, and Sub1/PC4. Characterized in human, the complex is involved in regulating transcription from RNA polymerase III (Pol III) promoters. Topoisomerase 1 and Sub1 enhance the accuracy of transcription termination, and promote reinitiation by Pol III.
A protein complex that contains the tumor suppressor protein adenomatous polyposis coli (APC), alpha-tubulin, gamma-tubulin, and the Rac1 and Cdc42 effector IQGAP1; may play a role in cytoskeleton organization.
A protein complex that contains the tumor suppressor protein adenomatous polyposis coli (APC) and the Rac1 and Cdc42 effector IQGAP1; may play a role in cytoskeleton organization and cell migration.
A protein complex that contains the tumor suppressor protein adenomatous polyposis coli (APC), the small GTPase Cdc42, and the Rac1 and Cdc42 effector IQGAP1; may play a role in cytoskeleton organization and cell migration.
A protein complex that contains the tumor suppressor protein adenomatous polyposis coli (APC), the small GTPase Rac1, and the Rac1 and Cdc42 effector IQGAP1; may play a role in cytoskeleton organization and cell migration.
A protein complex that contains the tumor suppressor protein adenomatous polyposis coli (APC), the small GTPase Cdc42, and CLIP-170; may play a role in cytoskeleton organization and cell migration.
A protein complex that contains Par3, the tumor suppressor protein adenomatous polyposis coli (APC), and the kinesin-related protein KIF3A; involved in establishing neuronal cell polarity.
A protein complex that contains the Scribble protein (a cell polarity determinant) and the tumor suppressor protein adenomatous polyposis coli (APC); may be involved in the control of cell proliferation.
A protein complex that contains the Scribble protein (a cell polarity determinant), the tumor suppressor protein adenomatous polyposis coli (APC), and beta-catenin; may be involved in the control of cell proliferation.
A protein complex that acts as an aryl hydrocarbon (Ah) receptor. Cytosolic and nuclear Ah receptor complexes have different subunit composition, but both contain the ligand-binding subunit AhR.
A protein complex that acts as an aryl hydrocarbon (Ah) receptor. Cytosolic and nuclear Ah receptor complexes have different subunit composition, but both contain the ligand-binding subunit AhR.
An aryl hydrocarbon receptor complex found in the cytosol, in which the ligand-binding subunit AhR is not bound to ligand; consists of AhR, two molecules of HSP90, the protein kinase c-Src, and the immunophilin XAP2/AIP.
An aryl hydrocarbon receptor complex found in the cytosol, in which the ligand-binding subunit AhR is not bound to ligand; consists of AhR, two molecules of HSP90, the protein kinase c-Src, and the immunophilin XAP2/AIP.
An aryl hydrocarbon receptor complex found in the cytosol, in which the ligand-binding subunit AhR is not bound to ligand; consists of AhR, two molecules of HSP90, the protein kinase c-Src, and the immunophilin XAP2/AIP.
An aryl hydrocarbon receptor (AhR) complex found in the nucleus; ; consists of ligand-bound AhR and the aryl hydrocarbon receptor nuclear translocator (ARNT).
An aryl hydrocarbon receptor (AhR) complex found in the nucleus; ; consists of ligand-bound AhR and the aryl hydrocarbon receptor nuclear translocator (ARNT).
An aryl hydrocarbon receptor (AhR) complex found in the nucleus; ; consists of ligand-bound AhR and the aryl hydrocarbon receptor nuclear translocator (ARNT).
The chemical reactions and pathways involving any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone, as carried out by individual cells.
A process in which an iron ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
A process in which an iron ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
A process in which an iron ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
A process in which an iron ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
A process in which an iron ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
A process in which an iron ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
A process in which an iron ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
A process in which an iron ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
A process in which an iron ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
A process in which an iron ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of iron ions (Fe) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of iron ions (Fe) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of iron ions (Fe) from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of iron ions (Fe) from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of iron ions (Fe) from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of iron ions (Fe) from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
Any process that modulates the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other.
Any process that modulates the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that modulates the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Any process that activates or increases the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
Catalysis of the reaction: geranyl diphosphate = (E)-beta-ocimene + diphosphate.
The controlled breakdown of the basement membrane in the context of a normal process such as imaginal disc eversion.
The controlled breakdown of the basement membrane in the context of a normal process such as imaginal disc eversion.
The modification of histone H4 by addition of one or more methyl groups to lysine at position 20 of the histone.
The modification of histone H4 by addition of one or more methyl groups to lysine at position 20 of the histone.
The modification of histone H4 by addition of one or more methyl groups to lysine at position 20 of the histone.
The modification of histone H4 by addition of one methyl group to lysine at position 20 of the histone.
The modification of histone H4 by addition of one methyl group to lysine at position 20 of the histone.
The modification of histone H4 by addition of two methyl groups to lysine at position 20 of the histone.
The modification of histone H4 by addition of two methyl groups to lysine at position 20 of the histone.
The modification of histone H4 by addition of three methyl groups to lysine at position 20 of the histone.
The modification of histone H4 by addition of three methyl groups to lysine at position 20 of the histone.
The volume enclosed by the membrane of a secretory granule.
A process in which glutathione is transported across a membrane.
A process in which glutathione is transported across a membrane.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a histamine stimulus. Histamine, the biogenic amine 2-(1H-imidazol-4-yl)ethanamine, is involved in local immune responses as well as regulating physiological function in the gut and acting as a neurotransmitter.
The volume enclosed by the membranes of a recycling endosome.
Catalysis of the reaction: 2-hydroxy-4-isopropenylcyclohexane-1-carboxyl-CoA = 4-isopropenyl-2-ketocyclohexane-1-carboxyl-CoA + 2 H+ + 2 e-.
Catalysis of the reaction: 4-isopropenyl-2-ketocyclohexane-1-carboxyl-CoA + H2O = 3-isopropenylpimelyl-CoA.
Catalysis of the reaction: glyphosate + OH- = glyoxylate + aminomethylphosphonic acid + H+ + 2 e-.
Catalysis of the reaction: N-cyclohexylformamide + OH- = cyclohexylamine + formate.
Catalysis of the reaction: dimethylmalonate + H+ = isobutyrate + CO2.
Catalysis of the reaction: pivalate + H+ + HSCoA + ATP = pivalyl-CoA + PPi + AMP.
Catalysis of the reaction: pivalyl-CoA = 3-methylbutyryl-CoA.
Catalysis of the reaction: salicylate + O2 + NAD(P)H + H+ = gentisate + H2O + NAD(P)+.
Catalysis of the reaction: 9-fluorenone + O2 + 2 H+ + 2 e- = 1-hydro-1,1a-dihydroxy-9-fluorenone.
Catalysis of the reaction: 1-hydro-1,1a-dihydroxy-9-fluorenone + H2O = 2,3-dihydroxy-2'-carboxybiphenyl + 3 H+ + 2 e-.
Catalysis of the reaction: 2,3-dihydroxy-2'-carboxybiphenyl + O2 = 2-hydroxy-6-oxo-6-(2-carboxyphenyl)-hexa-2,4-dienoate + H+.
Catalysis of the reaction: 2-hydroxy-6-oxo-6-(2-carboxyphenyl)-hexa-2,4-dienoate + H2O = cis-2-hydroxypenta-2,4-dienoate + phthalate + H+.
Catalysis of the reaction: (+)-(3S,4R)-cis-3,4-dihydroxy-3,4-dihydrofluorene = 3,4-dihydroxyfluorene + 2 H+ + 2 e-.
Catalysis of the reaction: isobutylamine + NADPH + O2 = isobutylhydroxylamine + NADP+ + H2O.
Catalysis of the reaction: hypophosphite + 2-oxoglutarate + O2 = succinate + phosphite + CO2.
Catalysis of the reaction: cyclopropanecarboxylate + CoASH = cyclopropanecarboxyl-CoA + OH-.
Catalysis of the reaction: cyclopropanecarboxyl-CoA = crotonoyl-CoA.
Catalysis of the reaction: cyclohexane + O2 + NAD(P)H + H+ = cyclohexanol + NAD(P)+ + H2O.
Catalysis of the reaction: cyclohexane + O2 + NAD(P)H + H+ = cyclohexanol + NAD(P)+ + H2O.
Catalysis of the reaction: adipate + CoASH = adipyl-CoA + OH-.
Catalysis of the reaction: hydrogen (2R,3S)-3-methyloxiran-2-ylphosphonic acid + glutathione = hydrogen (1R,2R)-1-glutathio-2-hydroxypropylphosphonic acid.
Catalysis of the reaction: hydrogen (2R,3S)-3-methyloxiran-2-ylphosphonic acid + L-cysteine = hydrogen (1R,2R)-1-L-cysteine-2-hydroxypropylphosphonic acid.
Catalysis of the reaction: TNP dihydride Meisenheimer complex (aci form) = TNP dihydride Meisenheimer complex (nitro form).
Catalysis of the reaction: trinitrophenol dihydride Meisenheimer complex (aci form) = 2,4-dinitrophenol hydride Meisenheimer complex + NO2. Trinitrophenol is also known as TNP and dinitrophenol is also known as DNP.
Catalysis of the reaction: trinitrophenol dihydride Meisenheimer complex (aci form) = 2,4-dinitrophenol hydride Meisenheimer complex + NO2. Trinitrophenol is also known as TNP and dinitrophenol is also known as DNP.
Catalysis of the reaction: 2,4-dinitrocyclohexanone + OH- = 4,6-dinitrohexanoate.
Catalysis of the reaction: branched-chain dodecylbenzene sulfonate + 1/2 O2 + H+ = sulfurous acid + branched-chain dodecyl-4-hydroxy-benzene + sulfite.
Catalysis of the reaction: 3-hydroxy-2-naphthoate + O2 = (3E)-3-[(6Z)-6-(carboxymethylene)cyclohexa-2,4-dien-1-ylidene]-2-oxopropanate.
Catalysis of the reaction: benzo(a)pyrene + O2 = benzo(a)pyrene-11,12-epoxide.
Catalysis of the reaction: benzo(a)pyrene-trans-11,12-dihydrodiol = 11,12-dihydroxybenzo(a)pyrene + 2 H+ + 2 e-.
Catalysis of the reaction: benzo(a)pyrene + O2 = benzo(a)pyrene-cis-11,12-dihydrodiol.
Catalysis of the reaction: 4,5-dihydroxybenzo(a)pyrene + C1 unit = hydroxymethoxybenzo(a)pyrene.
Catalysis of the reaction: benzo(a)pyrene + O2 = benzo(a)pyrene-cis-4,5-dihydrodiol.
Catalysis of the reaction: benzo(a)pyrene-cis-4,5-dihydrodiol = 4,5-dihydroxybenzo(a)pyrene + H2.
Catalysis of the reaction: 4,5-dihydroxybenzo(a)pyrene + O2 = 4,5-chrysenedicarboxylate.
Catalysis of the reaction: benzo(a)pyrene + O2 = benzo(a)pyrene-cis-9,10-dihydrodiol.
Catalysis of the reaction: 9,10-dihydroxybenzo(a)pyrene + O2 = cis-4-(8-hydroxypyren-7-yl)-2-oxobut-3-enoate.
Catalysis of the reaction: benzo(a)pyrene + O2 = benzo(a)pyrene-cis-7,8-dihydrodiol.
Catalysis of the reaction: benzo(a)pyrene-cis-7,8-dihydrodiol + O2 = cis-4-(7-hydroxypyren-8-yl)-2-oxobut-3-enoate.
Catalysis of the reaction: cis-4-(8-hydroxypyren-7-yl)-2-oxobut-3-enoate = 10-oxabenzo(def)chrysen-9-one + formate + H+.
Catalysis of the reaction: anthracene + 2 H2O = cis-9,10-dihydroanthracene-9,10-diol.
Catalysis of the reaction: cis-9,10-dihydroanthracene-9,10-diol = 9,10-anthraquinone + 4 H+ + 4 e-.
Catalysis of the reaction: androsta-1,4-diene-3,17-dione + reduced ferredoxin + O2 = 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + H2O + oxidized ferredoxin.
Catalysis of the reaction: 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + NADPH + H+ + O2 = 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + NADP+ + H2O.
Catalysis of the reaction: (3E,1Z)-4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate + H2O = (2E,4E)-2-hydroxyhexa-2,4-dienoate + 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oate + H+.
Catalysis of the reaction: citronellol + NAD+ = citronellal + NADH + H+.
Catalysis of the reaction: citronellal + NAD+ + OH- = citronellate + NADH + H+.
Catalysis of the reaction: citronellate + CoASH + ATP = citronellyl-CoA + AMP + PPi.
Catalysis of the reaction: citronellyl-CoA + NAD+ = cis-geranyl-CoA + NADH + H+.
Catalysis of the reaction: tetralin + O2 + NADH + H+ = cis-1,2-dihydroxy-1,2,5,6,7,8-hexahydronaphthalene + NAD+.
Catalysis of the reaction: cis-1,2-dihydroxy-1,2,5,6,7,8-hexahydronaphthalene + NAD+ = 1,2-dihydroxy-5,6,7,8-tetrahydronaphthalene + NADH + H+.
Catalysis of the reaction: 1,2-dihydroxy-5,6,7,8-tetrahydronaphthalene + O2 = 4-(2-oxocyclohexyl)-2-hydroxy-buta-2,4-dienoate + H+.
Catalysis of the reaction: 4-(2-oxocyclohexyl)-2-hydroxy-buta-2,4-dienoate + H2O = 2-hydroxydec-2,4-diene-1,10-dioate + H+.
Catalysis of the reaction: 2-hydroxydec-2,4-diene-1,10-dioate + H2O = (2Z)-2,4-dihydroxydec-2-enedioate.
Catalysis of the reaction: (2Z)-2,4-dihydroxydec-2-enedioate = pyruvate + 7-oxoheptanoate.
Catalysis of the reaction: (R)-1,2,3,4-tetrahydronaphthol = 1,2,3,4-tetrahydronaphthalone + 2 H+ + 2 e-.
Catalysis of the reaction: geranial + NAD+ + OH- = geranylate + NADH + H+.
Catalysis of the reaction: geranylate + CoASH = trans-geranyl-CoA + OH-.
Catalysis of the reaction: 2-mercaptobenzothiazole + O2 + 2 H+ + 2 e- = 2-mercaptobenzothiazole-cis-6,7-dihydrodiol.
Catalysis of the reaction: 2-mercaptobenzothiazole + 1/2 O2 = 6-hydroxy-2-mercaptobenzothiazole.
Catalysis of the reaction: 6-hydroxy-2-mercaptobenzothiazole + 1/2 O2 = 6,7-dihydroxy-2-mercaptobenzothiazole.
Catalysis of the reaction: 2-mercaptobenzothiazole-cis-6,7-dihydrodiol = 6,7-dihydroxy-2-mercaptobenzothiazole + 2 H+ + 2 e-.
Catalysis of the reaction: (-)-(2S,5R)-menthone + NAD+ = (5R)-menth-2-enone + NADH + H+.
Catalysis of the reaction: (5R)-menth-2-enone + H2O = (5R)-3-hydroxymenthone.
Catalysis of the reaction: (5R)-3-hydroxymenthone + NAD+ = mentha-1,3-dione + NADH + H+.
Catalysis of the reaction: mentha-1,3-dione + CoASH = 3,7-dimethyl-5-oxo-octyl-CoA.
Catalysis of the reaction: thiophene-2-carboxylate + ATP + CoASH = thiophene-2-carboxyl-CoA + AMP + PPi.
Catalysis of the reaction: 2-oxoglutaryl-CoA + OH- = 2-oxoglutarate + CoASH.
Catalysis of the reaction: naphthyl-2-methyl-succinate + succinyl-CoA = naphthyl-2-methyl-succinyl-CoA + succinate.
Catalysis of the reaction: naphthyl-2-methyl-succinyl-CoA = naphthyl-2-methylene-succinyl-CoA + 2 H+ + 2 e-.
Catalysis of the reaction: naphthyl-2-methylene-succinyl-CoA + H2O = naphthyl-2-hydroxymethyl-succinyl-CoA.
Catalysis of the reaction: naphthyl-2-hydroxymethyl-succinyl-CoA = naphthyl-2-oxomethyl-succinyl-CoA + 2 H+ + 2 e-.
Catalysis of the reaction: naphthyl-2-oxomethyl-succinyl-CoA + CoASH = 2-naphthoyl-CoA + succinyl-CoA.
Catalysis of the reaction: 2-naphthoyl-CoA + OH- = 2-naphthoate + CoASH.
Catalysis of the reaction: isooctane + 1/2 O2 = 2,4,4-trimethyl-1-pentanol.
Catalysis of the reaction: 2,4,4-trimethyl-3-oxopentanoyl-CoA + CoASH = pivalyl-CoA + propanoyl-CoA.
Catalysis of the reaction: 4,4-dimethyl-3-oxopentanal + H2O = 4,4-dimethyl-3-oxopentanoate + 3 H+ + 2 e-.
Catalysis of the reaction: 2,4,4-trimethyl-3-oxopentanoate + H+ = 2,2-dimethyl-3-pentanone + CO2.
Catalysis of the reaction: 4,4-dimethyl-3-oxopentanoate + H+ = 3,3-dimethyl-2-butanone + CO2.
Catalysis of the reaction: androst-4-ene-3,17-dione + O2 + 2 H+ + 2 e- = 9alpha-hydroxy-4-androstene-3,17-dione + H2O.
Catalysis of the reaction: (2E,4E)-2-hydroxyhexa-2,4-dienoate + H2O = 4-hydroxy-2-oxohexanoate.
Catalysis of the reaction: 2-(methylthio)benzothiazole + 1/2 O2 = 2-(methylsulfinyl)benzothiazole.
Catalysis of the reaction: 2-hydroxybenzothiazole + 1/2 O2 = 2,6-dihydroxybenzothiazole.
Catalysis of the reaction: benzothiazole + 1/2 O2 = 2-hydroxybenzothiazole.
Catalysis of the reaction: 2-mercaptobenzothiazole + reduced acceptor = benzothiazole + hydrogen sulfide + oxidized acceptor.
Catalysis of the reaction: benzothiazole-2-sulfonate + H2O = 2-hydroxybenzothiazole + HSO3-.
Catalysis of the reaction: 2,6-dihydroxybenzothiazole + 1/2 O2 = 2,6,7-trihydroxybenzothiazole.
Catalysis of the reaction: 2,4,4-trimethyl-1-pentanol = 2,4,4-trimethylpentanal + 2 H+ + 2 e-.
Catalysis of the reaction: 2,4,4-trimethylpentanal + H2O = 2,4,4-trimethylpentanoate + 3 H+ + 2 e-.
Catalysis of the reaction: 2,4,4-trimethylpentanoate + CoASH = 2,4,4-trimethylpentanoyl-CoA + OH-.
Catalysis of the reaction: 2,4,4-trimethylpentanoyl-CoA = 2,4,4-trimethylpent-2-enoyl-CoA + 2 H+ + 2 e-.
Catalysis of the reaction: 2,4,4-trimethylpent-2-enoyl-CoA + H2O = 2,4,4-trimethyl-3-hydroxypentanoyl-CoA.
Catalysis of the reaction: 2,4,4-trimethyl-3-hydroxypentanoyl-CoA = 2,4,4-trimethyl-3-oxopentanoyl-CoA + 2 H+ + 2 e-.
Catalysis of the reaction: 2,4,4-trimethyl-3-oxopentanoyl-CoA + OH- = 2,4,4-trimethyl-3-oxopentanoate + CoASH.
Catalysis of the reaction: 2,2-dimethyl-3-pentanone + 1/2 O2 = 1-hydroxy-4,4-dimethylpentan-3-one.
Catalysis of the reaction: 1-hydroxy-4,4-dimethylpentan-3-one = 4,4-dimethyl-3-oxopentanal + 2 H+ + 2 e-.
Catalysis of the reaction: trans-geranyl-CoA = cis-geranyl-CoA.
Catalysis of the reaction: thioacetamide + O2 + 2 H+ + 2 e- = thioacetamide S-oxide + H2O.
Catalysis of the reaction: thioacetamide S-oxide + O2 + 2 H+ + 2 e- = thioacetamide S,S-dioxide + H2O.
Catalysis of the reaction: caffeine + O2 + 2 H+ + 2 e- = 1,3,7-trimethyluric acid + H2O.
Catalysis of the reaction: isoniazid + H2O = isonicotinate + hydrazine.
Catalysis of the reaction: isonicotinate + acceptor + H2O = 2-hydroxyisonicotinate + reduced acceptor.
Catalysis of the reaction: 2-hydroxyisonicotinate + acceptor + H2O = citrazinate + reduced acceptor.
Catalysis of the reaction: 2,3,6-trihydroxyisonicotinate = 2,3,6-trihydroxypyridine + CO2.
Catalysis of the reaction: citrazinate + H2O = 2,3,6-trihydroxyisonicotinate + 2 H+ + 2 e-.
Catalysis of the reaction: citrazinate + H2O = cis-aconitamide.
Catalysis of the reaction: cis-aconitamide + H2O = cis-aconitate + HN3.
Catalysis of the reaction: gamma-N-formylaminovinylacetate + H2O = gamma-aminovinylacetate + HCOOH.
Catalysis of the reaction: gamma-aminovinylacetate + H2O = succinic semialdehyde + NH3.
Catalysis of the reaction: endosulfan + O2 + 2 H+ + 2 e- = endosulfan sulfate + H2O.
Catalysis of the reaction: endosulfan hemisulfate + H2O = endosulfan monoalcohol + 2 H+ + sulfate.
Catalysis of the reaction: endosulfan diol = endosulfan ether + H2O.
Catalysis of the reaction: endosulfan diol = endosulfan hydroxyether + 2 H+ + 2 e-.
Catalysis of the reaction: endosulfan lactone + H2O = endosulfan hydroxycarboxylate + H+.
Catalysis of the reaction: N-nitrodimethylamine + O2 + 2 H+ + 2 e- = N-nitromethylamine + formaldehyde + H2O.
Catalysis of the reaction: 4-hydroxypyridine + O2 + H+ + NADPH = pyridine-3,4-diol + H2O + NADP+.
Catalysis of the reaction: pryidine-3,4-diol + O2 = 3-(N-formyl)-formiminopyruvate.
Catalysis of the reaction: 3-formiminopyruvate + H2O = 3-formylpyruvate + HN3.
Catalysis of the reaction: 4-(1-ethyl-1,4-dimethyl-pentyl)phenol + O2 + 2 H+ + 2 e- = hydroquinone + 3,6-dimethylheptan-3-ol.
Catalysis of the reaction: hexadecyltrimethylammonium chloride + NAD(P)H + H+ + O2 = trimethylamine + hexadecanal + NAD(P)+ + H2O.
Catalysis of the reaction: N,N,N-trimethylamine + NADPH + H+ + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O.
Catalysis of the reaction: 3-(N-formyl)-formiminopyruvate + H2O = 3-formiminopyruvate + formate.
Catalysis of the reaction: endosulfan hydroxyether = endosulfan lactone + 2 H+ + 2 e-.
Catalysis of the reaction: endosulfan sulfate + H2O = endosulfan diol + sulfite.
Catalysis of the reaction: endosulfan ether + O2 + 2 H+ + 2 e- = endosulfan hydroxyether + H2O.
Catalysis of the reaction: 5-chloro-2-oxopent-4-enoate + H2O = 5-chloro-4-hydroxy-2-oxopentanate.
Catalysis of the reaction: 5-chloro-4-hydroxy-2-oxopentanate = pyruvate + chloroacetaldehyde.
Catalysis of the reaction: N-isopropylaniline + O2 + 2 H+ + NADH = catechol + NAD+ + isopropylamine.
Catalysis of the reaction: acetanilide + O2 + 2 H+ + NADH = catechol + NAD+ + acetamide.
Catalysis of the reaction: 2-chloro-N-isopropylacetanilide + O2 + 2 H+ + NADH = 2-chloro-N-isopropylacetamide + catechol + NAD+.
Catalysis of the reaction: 6-hydroxypseudooxynicotine + H2O + OH- = 6-hydroxy-3-succinoylpyridine + 4 H+ + 4 e- + methylamine.
Catalysis of the reaction: 6-hydroxy-3-succinoylpyridine + H2O = succinic semialdehyde + 2,5-dihydroxypyridine.
Catalysis of the reaction: phthalate + O2 + NADH + H+ = phthalate 3,4-cis-dihydrodiol + NAD+.
Catalysis of the reaction: phthalate 3,4-cis-dihydrodiol + NAD+ = 3,4-dihydroxyphthalate + NADH + H+.
Catalysis of the reaction: trinitrophenol hydride Meisenheimer complex = 2,4-dinitrophenol + nitrite. Trinitrophenol is also known as TNP.
Catalysis of the reaction: trinitrophenol hydride Meisenheimer complex = 2,4-dinitrophenol + nitrite. Trinitrophenol is also known as TNP.
Catalysis of the reaction: 4-methyl-3-oxooctanoyl-CoA + CoA = acetyl-CoA + 2-methylhexanoyl-CoA.
Catalysis of the reaction: 2-methylhexanoyl-CoA = 2-methylhex-2-enoyl-CoA + 2 H+ + e-.
Catalysis of the reaction: 2-methylhex-2-enoyl-CoA + H2O = 3-hydroxy-2-methylhexanoyl-CoA.
Catalysis of the reaction: 3-hydroxy-2-methylhexanoyl-CoA = 2-methyl-3-oxohexanoyl-CoA + 2 H+ + 2 e-.
Catalysis of the reaction: 2-methyl-3-oxohexanoyl-CoA + CoA = propanoyl-CoA + butyryl-CoA.
Catalysis of the reaction: pyrene + 2 H+ + 2 e- + O2 = cis-4,5-dihydroxy-4,5-dihydropyrene.
Catalysis of the reaction: cis-4,5-dihydroxy-4,5-dihydropyrene = 4,5-dihydroxypyrene + 2 H+ + 2 e-.
Catalysis of the reaction: 4,5-dihydroxypyrene + O2 = phenanthrene-4,5-dicarboxylate + 2 H+.
Catalysis of the reaction: phenanthrene-4,5-dicarboxylate + H+ = phenanthrene-4-carboxylate + CO2.
Catalysis of the reaction: cis-3,4-phenanthrenedihydrodiol-4-carboxylate = 3,4-dihydroxyphenanthrene + H+ + 2 e- + CO2.
Catalysis of the reaction: pyrene + O2 + 2 H+ + 2 e- = pyrene-4,5-oxide + H2O.
Catalysis of the reaction: pyrene-4,5-oxide + H2O = trans-4,5-dihydroxy-4,5-dihydropyrene.
Catalysis of the reaction: pyrene + O2 + 2 H+ + 2 e- = pyrene-1,2-oxide + H2O.
Catalysis of the reaction: 1-hydroxypyrene + O2 + 2 H+ + 2 e- = 1-hydroxypyrene-6,7-oxide + H2O.
Catalysis of the reaction: 1-hydroxypyrene + O2 + 2 H+ + 2 e- = 1-hydroxypyrene-7,8-oxide + H2O.
Catalysis of the reaction: 1-hydroxypyrene + XSO3- = 1-pyrenylsulfate + HX.
Catalysis of the reaction: 1-hydroxypyrene + XCH3 = 1-methoxypyrene + HX.
Catalysis of the reaction: 1-methoxypyrene + O2 + 2 H+ + 2 e- = 1-methoxypyrene-6,7-oxide + H2O.
Catalysis of the reaction: 1-hydroxy-6-methoxypyrene + XCH3 = 1,6-dimethoxypyrene + HX.
Catalysis of the reaction: phenanthrene-4-carboxylate + 2 H+ + 2 e- + O2 = cis-3,4-phenanthrenedihydrodiol-4-carboxylate.
Catalysis of the reaction: 2,4-dichlorotoluene + NADH + H+ + O2 = 4,6-dichloro-3-methyl-cis-1,2-dihydroxycyclohexa-3,5-diene + NAD+.
Catalysis of the reaction: 4,6-dichloro-3-methylcatechol + O2 = 3,5-dichloro-3-methyl-cis,cis-muconate + 2 H+.
Catalysis of the reaction: perchlorate + 2 H+ + 2 e- = chlorate + H2O.
Catalysis of the reaction: pryrole-2-carboxylate + NADH + O2 + H+ = 5-hydroxypyrrole-2-carboxylate + NAD+ + H2O.
Catalysis of the reaction: 5-hydroxypyrrole-2-carboxylate = 5-oxo-4,5-dihydropyrrole-2-carboxylate.
Catalysis of the reaction: 5-oxo-4,5-dihydropyrrole-2-carboxylate + 2 H2O = 2-oxoglutarate + NH3.
Catalysis of the reaction: pryrole-2-carboxylate + H+ = pyrrole + CO2.
Catalysis of the reaction: cis-2-methyl-5-isopropylhexa-2,5-dienoic acid + ATP + CoASH = cis-2-methyl-5-isopropylhexa-2,5-dienoyl-CoA + AMP + PPi.
Catalysis of the reaction: trans-2-methyl-5-isopropylhexa-2,5-dienoic acid + ATP + CoASH = trans-2-methyl-5-isopropylhexa-2,5-dienoyl-CoA + AMP + PPi.
Catalysis of the reaction: 3-hydroxy-2,6-dimethyl-5-methylene-heptanoyl-CoA + NAD+ = 2,6-dimethyl-5-methylene-3-oxo-heptanoyl-CoA + NADH+ + H+.
Catalysis of the reaction: 2,6-dimethyl-5-methylene-3-oxo-heptanoyl-CoA + CoASH = 3-isopropylbut-3-enoyl-CoA + propanoyl-CoA.
Catalysis of the reaction: 3-isopropylbut-3-enoyl-CoA + H2O = 3-isopropylbut-3-enoic acid + CoASH.
Catalysis of the reaction: terephthalate + H2O = benzoate + HCO3-.
Catalysis of the reaction: 2,6-dihydroxypseudooxynicotine + H2O = 2,6-dihydroxypyridine + 4-methylaminobutyrate.
Catalysis of the reaction: 1,1-dichloroethane + 2 H+ + 2 e- = chloroethane + HCl.
Catalysis of the reaction: phenylboronic acid + O2 + 2 H+ + 2 e- = phenol + B(OH)3.
Catalysis of the reaction: o-hydroxylaminobenzoate = 3-hydroxyanthranilate.
Catalysis of the reaction: malonate semialdehyde + H+ = acetaldehyde + CO2.
Catalysis of the reaction: perillyl-CoA + H2O = 2-hydroxy-4-isopropenylcyclohexane-1-carboxyl-CoA.
Catalysis of the reaction: diphenyl ether + O2 = 2,3-dihydroxydiphenyl ether.
Catalysis of the reaction: 2,3-dihydroxydiphenyl ether + O2 + H2O = 2-hydroxymuconate + phenol.
Catalysis of the reaction: diphenyl ether + NADH + O2 + H+ = phenol + catechol + NAD+.
Catalysis of the reaction: 3-nitrophenol + 2 NADH + 2 H+ = 3-hydroxyaminophenol + 2 NAD+ + H2O.
Catalysis of the reaction: aminohydroquinone + 2 e- + 2 H+ + 1/2 O2 = 1,2,4-benzenetriol + NH3.
The process leading to the attainment of the full functional capacity of endothelin by conversion of Big-endothelin substrate into mature endothelin.
Any process involved in the conversion of a primary box C/D type small nucleolar RNA (snoRNA) transcript into a mature box C/D snoRNA.
Any process involved in the conversion of a primary box H/ACA type small nucleolar RNA (snoRNA) transcript into a mature box H/ACA snoRNA.
Any process involved in the conversion of a primary box C/D type small nucleolar RNA (snoRNA) transcript that resides within, and is processed from, the intron of a pre-mRNA into a mature box C/D snoRNA.
Any process involved in the conversion of a primary box H/ACA type small nucleolar RNA (snoRNA) transcript that resides within, and is processed from, the intron of a pre-mRNA into a mature box H/ACA snoRNA.
A histone deacetylase complex that is involved in transcriptional regulation. In S. cerevisiae, this complex consists of Set3p, Snt1p, Hos4p, Sif2p, Cpr1p, Hos2p, and Hst1p.
A histone deacetylase complex that is involved in transcriptional regulation. In S. cerevisiae, this complex consists of Set3p, Snt1p, Hos4p, Sif2p, Cpr1p, Hos2p, and Hst1p.
The modification of a histone by addition of one or more methyl groups to a lysine residue.
The modification of a histone by addition of a methyl group to an arginine residue.
The modification of histone H3 by addition of a methyl group to arginine at position 2 of the histone.
The modification of histone H3 by addition of a methyl group to arginine at position 2 of the histone.
The modification of histone H3 by addition of a methyl group to arginine at position 2 of the histone.
The modification of histone H3 by addition of a methyl group to arginine at position 17 of the histone.
The modification of histone H3 by addition of a methyl group to arginine at position 17 of the histone.
The modification of histone H3 by addition of a methyl group to arginine at position 17 of the histone.
The modification of histone H3 by addition of a methyl group to arginine at position 26 of the histone.
The modification of histone H3 by addition of a methyl group to arginine at position 26 of the histone.
The modification of histone H3 by addition of a methyl group to arginine at position 26 of the histone.
A protein complex that contains a protein kinase (Sid2 in S. pombe) and its regulatory subunit (Mob1). The Sid2p-Mob1p kinase complex is a component of the septation initiation network in fission yeast (called the mitotic exit network in S. cerevisiae) and is required for cytokinesis. The analogous complex in S. cerevisiae is called Dbf2p-Mob1p complex.
A protein complex that contains a protein kinase (Sid2 in S. pombe) and its regulatory subunit (Mob1). The Sid2p-Mob1p kinase complex is a component of the septation initiation network in fission yeast (called the mitotic exit network in S. cerevisiae) and is required for cytokinesis. The analogous complex in S. cerevisiae is called Dbf2p-Mob1p complex.
A protein complex that contains a protein kinase (Sid2 in S. pombe) and its regulatory subunit (Mob1). The Sid2p-Mob1p kinase complex is a component of the septation initiation network in fission yeast (called the mitotic exit network in S. cerevisiae) and is required for cytokinesis. The analogous complex in S. cerevisiae is called Dbf2p-Mob1p complex.
A protein complex involved that contains proteins known in Schizosaccharomyces as Swi5 monomers and Swi2, and is involved in mating type switching.
A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
A protein complex that contains the precursor form of NF-kappaB (p105), the NF-kappaB inhibitor ABIN-2, and the kinase TPL-2 (MAP3K8); the complex stabilizes TPL-2 and is involved in signaling in lipopolysaccharide (LPS)-stimulated macrophages.
A protein complex that contains the homeodomain proteins PDX1, PBX1b and MRG1 (MEIS2) and is involved in the transcriptional regulation of pancreatic acinar cell-specific genes.
Catalysis of the removal of one or more acetyl groups from a protein, requiring NAD.
A protein complex that contains CREB and FHL2, and is involved in transcriptional regulation.
A protein complex that contains CREB and FHL3, and is involved in transcriptional regulation.
The peptide cleavage of mitochondrial proteins, including cleavage contributing to their import.
The removal of an acetyl group from an acetylated lysine residue in a peptide or protein.
Any large protein complex that contains Ecsit and NDUFAF1, is located in the mitochondrion, and is involved in the assembly of complex I of the oxidative phosphorylation system. In mammalian cells, three complexes of approximately 500, 600, and 850 kDa containing the 45 kDa isoform of Ecsit and NDUFAF1 have been observed.
Directly binding to and delivering iron ions to a target protein.
Interacting selectively and non-covalently with one or more specific sites on an immunoglobulin receptor molecule.
Interacting selectively and non-covalently with one or more specific sites on the Fc-gamma receptor I complex. The complex functions primarily as an activating receptor for IgG.
A cohesin complex that mediates sister chromatid cohesion in the nucleus during mitosis; has a subunit composition distinct from that of the meiotic cohesin complex.
A cohesin complex that mediates sister chromatid cohesion in the nucleus during meiosis; has a subunit composition distinct from that of the mitotic cohesin complex.
A region of the nuclear envelope to which a microtubule organizing center (MTOC) attaches; protein complexes embedded in the nuclear envelope mediate direct or indirect linkages between the microtubule cytoskeleton and the nuclear envelope.
A region of the nuclear envelope to which a microtubule organizing center (MTOC) attaches; protein complexes embedded in the nuclear envelope mediate direct or indirect linkages between the microtubule cytoskeleton and the nuclear envelope.
A region of the nuclear envelope to which a microtubule organizing center (MTOC) attaches; protein complexes embedded in the nuclear envelope mediate direct or indirect linkages between the microtubule cytoskeleton and the nuclear envelope.
A nuclear membrane  protein complex  which connects the nuclear outer and inner membranes together, and links links the nuclear lumen to cytoplasmic microtubules during meiosis.
A nuclear membrane  protein complex  which connects the nuclear outer and inner membranes together, and links links the nuclear lumen to cytoplasmic microtubules during meiosis.
A nuclear membrane  protein complex  which connects the nuclear outer and inner membranes together, and links links the nuclear lumen to cytoplasmic microtubules during meiosis.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a microtubule organizing center attachment site. A microtubule organizing center attachment site is a region of the nuclear envelope to which a microtubule organizing center (MTOC) attaches.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a microtubule organizing center attachment site. A microtubule organizing center attachment site is a region of the nuclear envelope to which a microtubule organizing center (MTOC) attaches.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a microtubule organizing center attachment site. A microtubule organizing center attachment site is a region of the nuclear envelope to which a microtubule organizing center (MTOC) attaches.
A protein complex that consist of complement components C5b6 and C7 stably inserted in a cell membrane. Formation of the SC5b-7 complex is the first phase of membrane attack complex assembly.
A protein complex that consists of a GTPase activator protein (GAP) for Ras and three Src family protein tyrosine kinases, Fyn, Lyn and Yes. The complex is involved in signaling upon platelet activation.
A protein complex that comprises one integrin alphav subunit, one integrin beta5 subunit, and vitronectin.
An oligosaccharyltransferase (OST) complex that contains at least seven polypeptides and is the major OST complex in mammalian cells. Of the three forms of mammalian OST complex identified, the OSTI complex has the weakest affinity for ribosomes.
An oligosaccharyltransferase (OST) complex that contains the seven polypeptides found in OST complex I, plus heterotrimeric Sec61alpha-beta-gamma. Of the three forms of mammalian OST complexes identified, the OSTII complex has intermediate affinity for ribosomes.
An oligosaccharyltransferase (OST) complex that contains the seven polypeptides found in OST complex I, plus heterotrimeric Sec61alpha-beta-gamma and the tetrameric TRAP complex. Of the three forms of mammalian OST complexes identified, the OSTIII complex has the strongest affinity for ribosomes.
Growth of epithelial tubes that originate from pits in an open tracheal system and grow towards each other to meet and form a continuous open tube called the dorsal trunk. The dorsal trunk extends from the anterior spiracle to the posterior spiracle of the larva and forms the main airway of the insect tracheal system.
The clearance of liquid from the epithelial tubes of an open tracheal system, shortly before the emergence of the larva, to generate an air-filled tubule system.
The most apical region of the lateral plasma membrane of an invertebrate epithelial cell. The subapical complex lies above the zonula adherens and the septate junction, and is comparable to the position of the tight junction of vertebrate cells.
Catalysis of the reaction: ATP + a phosphatidylinositol = ADP + a phosphatidylinositol 3-phosphate. This reaction is the addition of a phosphate group to phosphatidylinositol or one of its phosphorylated derivatives at the 3' position of the inositol ring.
The blackening of the wounded area of the cuticle or the surface of invading pathogens, parasites or parasitoids, resulting from a proteolytic cascade leading to the de novo synthesis and deposition of melanin.
Any process that affects the rate, extent or location of the melanization defense response during injury or invasion.
Any process that increases the rate or extent of the melanization defense response during injury or invasion.
Any process that increases the rate or extent of the melanization defense response during injury or invasion.
Any process that increases the rate or extent of the melanization defense response during injury or invasion.
Any process that increases the rate or extent of the melanization defense response during injury or invasion.
Any process that increases the rate or extent of the melanization defense response during injury or invasion.
Any process that increases the rate or extent of the melanization defense response during injury or invasion.
Any process that reduces the rate or extent of the melanization defense response. This regulation is critical to limit melanization to the site of injury or infection.
Any process that reduces the rate or extent of the melanization defense response. This regulation is critical to limit melanization to the site of injury or infection.
Any process that reduces the rate or extent of the melanization defense response. This regulation is critical to limit melanization to the site of injury or infection.
Any process that reduces the rate or extent of the melanization defense response. This regulation is critical to limit melanization to the site of injury or infection.
Any process that reduces the rate or extent of the melanization defense response. This regulation is critical to limit melanization to the site of injury or infection.
Events resulting in the formation of a multilayered cellular sheath surrounding an invader and thus preventing its development. This defense mechanism is often seen in insects in response to nematodes or parasitoids, which are too large to be phagocytosed by individual hemocytes. In some organisms the capsule is blackened due to melanization.
Formation of a multilayered, melanized sheath of cells around a foreign invader.
The terminal region of a polytene chromosome.
Combining with the peptide myosuppressin to initiate a change in cell activity.
Modulates the activity of any of the phosphatidylinositol 3-kinases (PI3Ks). Regulatory subunits can link a PI3K catalytic subunit to upstream signaling events and help position the catalytic subunits close to their lipid substrates.
Modulates the activity of any of the phosphatidylinositol 3-kinases (PI3Ks). Regulatory subunits can link a PI3K catalytic subunit to upstream signaling events and help position the catalytic subunits close to their lipid substrates.
The increase in length of the aristal core. The arista is the terminal segment of the antenna and consists of a central core and a series of lateral extensions.
The increase in length of the aristal laterals. The arista is the terminal segment of the antenna and consists of a central core and a series of lateral extensions.
The regionalization process that gives rise to the patterns of cell differentiation in the cuticle.
The process that gives rise to the patterns of cell differentiation that will arise in the chitin-based adult cuticle. An example of this process is adult chitin-based cuticle pattern formation in Drosophila melanogaster.
Any process by which an organism retains a population of somatic stem cells, undifferentiated cells in the embryo or adult which can undergo unlimited division and give rise to cell types of the body other than those of the germ-line.
Any process that modulates the frequency, rate or extent of Rac protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Rac protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Rac protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Rac protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Rac protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Rac protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Rac protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Rac protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Rac protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Rac protein signal transduction.
Any process that modulates the frequency, rate or extent of Rho protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Rho protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Rho protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Rho protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Rho protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Rho protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Rho protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Rho protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Rho protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Rho protein signal transduction.
The process in which relatively unspecialized cells acquire specialized structural and/or functional features of leading edge cells, cells at the front of a migrating epithelial sheet.
The commitment of cells to leading edge cell fate and their capacity to differentiate into leading edge cells. Leading edge cells are found at the front of a migrating epithelial sheet.
The process in which a cell becomes capable of differentiating autonomously into a leading edge cell regardless of its environment; upon determination, the cell fate cannot be reversed.
The commitment of cells to leading edge cell fate during dorsal closure. Leading edge cells are the dorsal-most cells of the migrating epidermis.
A phosphatidylinositol 3-kinase complex that contains a catalytic class III phosphoinositide 3-kinase (PI3K) subunit bound to a regulatory (adaptor) subunit. Additional adaptor proteins may be present. Class III PI3Ks have a substrate specificity restricted to phosphatidylinositol (PI).
A phosphatidylinositol 3-kinase complex that contains a catalytic class III phosphoinositide 3-kinase (PI3K) subunit bound to a regulatory (adaptor) subunit. Additional adaptor proteins may be present. Class III PI3Ks have a substrate specificity restricted to phosphatidylinositol (PI).
Modulates the activity of histone deacetylase.
Modulates the activity of histone acetyltransferase.
Interacting selectively and non-covalently with the enzyme histone acetyltransferase.
The initial contact step made between the sperm plasma membrane and outer layer of the egg during fertilization.
An endocytosis process that results in penetration of the egg shell through the micropyle (a specialized anterior opening in the vitelline envelope) and entry of the entire sperm, including the surrounding plasma membrane and the sperm tail, into the egg cytoplasm. This step in fertilization is seen in Drosophila, where a plasma membrane fusion event between the sperm and the egg does not occur.
Assembly of the haploid nucleus of the unfertilized egg.
The conversion at fertilization of the inactive sperm nucleus into a male pronucleus with its chromosomes processed for the first zygotic division.
Removal of the sperm nuclear envelope, allowing entry of maternal factors into the sperm nucleus.
Unwinding of the condensed nuclear chromatin of an inactive sperm nucleus.
Replacement of sperm-specific chromosomal proteins with somatic histones, to allow the paternal genome to acquire a nucleosomal chromatin organization compatible with nuclear activity.
Replacement of sperm-specific chromosomal proteins with somatic histones, to allow the paternal genome to acquire a nucleosomal chromatin organization compatible with nuclear activity.
Assembly of a nuclear envelope containing nuclear pores and a lamina around the male pronucleus, the final step in sperm pronuclear formation.
Formation and organization of an aster composed of microtubule arrays originating from the sperm basal body and extending virtually to the egg periphery. The sperm aster ensures the appropriate positioning of the male and female pronuclei.
The gradual disintegration of the sperm plasma membrane following insemination. This process is seen in Drosophila after entry of the entire sperm, surrounded by its plasma membrane, into the egg.
The gradual disintegration of the sperm plasma membrane following insemination. This process is seen in Drosophila after entry of the entire sperm, surrounded by its plasma membrane, into the egg.
The gradual disintegration of the sperm plasma membrane following insemination. This process is seen in Drosophila after entry of the entire sperm, surrounded by its plasma membrane, into the egg.
The directed movement of the male and female pronuclei towards each other prior to their fusion.
The rotation of centrosomes and associated pronuclei in one-cell embryos such as those of Caenorhabditis elegans, occurring as a transition between pronuclear migration and pronuclear fusion.
Catalysis of the transfer of a methyl group to juvenile hormone acid.
The process whose specific outcome is the progression of the embryonic heart tube over time, from its formation to the mature structure. The heart tube forms as the heart rudiment from the heart field.
The process in which a relatively unspecialized cell acquires the specialized structural and/or functional features of a cell that will form part of the cardiac organ of an individual.
The process in which a relatively unspecialized cell acquires the specialized structural and/or functional features of a cell that will form part of the cardiac organ of an individual.
The commitment of dorsal vessel cardioblast cells to an aortic cell fate and their capacity to differentiate into aortic cells. An example of this process is found in Drosophila melanogaster.
The commitment of dorsal vessel cardioblast cells to a heart proper cell fate and their capacity to differentiate into heart cells. An example of this process is found in Drosophila melanogaster.
The establishment, maintenance and elaboration of cell differentiation that results in the anterior/posterior subdivision of the embryonic heart tube. In Drosophila this results in subdivision of the dorsal vessel into to the posterior heart proper and the anterior aorta.
A protein complex that facilitates the assembly of nucleosomes on to newly synthesized DNA. In Drosophila, the complex comprises ASF1 and histones H3 and H4.
A SWI/SNF-type complex that contains 8 to 14 proteins, including both conserved (core) and nonconserved components; contains the ATPase product of the Drosophila brm (brahma) or mammalian SMARCA2/BAF190B/BRM gene, or an ortholog thereof.
A class of nuclear body measuring 20-25 nm in diameter and distributed throughout the interchromatin space, linked together by thin fibrils. They are believed to be storage centers for various snRNAs, snRNPs, serine/arginine-rich proteins and RNA polymerase II. A typical mammalian cell contains 25-50 clusters of interchromatin granules. Interchromatin granule clusters do not contain the heterogeneous nuclear RNA-binding proteins (hnRNPs).
A nucleoplasmic speckle distributed in the interchromatin space of cells in close proximity to chromatin. Omega speckles are distinct from interchromatin granules and contain heterogeneous nuclear RNA-binding proteins (hnRNPs).
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of nuclear specks, a class of nuclear body in which splicing factors are localized.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of nuclear specks, a class of nuclear body in which splicing factors are localized.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of nuclear specks, a class of nuclear body in which splicing factors are localized.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of nuclear specks, a class of nuclear body in which splicing factors are localized.
Interacting selectively and non-covalently with a histone in which a residue has been modified by methylation. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes.
Any process that modulates the frequency, rate or extent of the addition of an acetyl group to a histone protein.
Any process that activates or increases the frequency, rate or extent of the addition of an acetyl group to a histone protein.
Any process that activates or increases the frequency, rate or extent of the addition of an acetyl group to a histone protein.
Any process that activates or increases the frequency, rate or extent of the addition of an acetyl group to a histone protein.
Any process that activates or increases the frequency, rate or extent of the addition of an acetyl group to a histone protein.
Any process that activates or increases the frequency, rate or extent of the addition of an acetyl group to a histone protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of an acetyl group to a histone protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of an acetyl group to a histone protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of an acetyl group to a histone protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of an acetyl group to a histone protein.
A complex containing both protein and micro-RNA (miRNA) molecules. miRNAs are approximately 22 nucleotide noncoding RNAs derived from endogenous genes; they are processed from the stem of a longer hairpin like structure termed a pre-miRNA.
The stage-specific break down of the larval midgut during Drosophila metamorphosis, to allow replacement of larval structures by tissues and structures that form the adult fly.
The stage-specific break down of the larval salivary glands during Drosophila metamorphosis, to allow replacement of larval structures by tissues and structures that form the adult fly.
The stage-specific programmed cell death of salivary gland cells during salivary gland histolysis.
The stage-specific programmed cell death of salivary gland cells during salivary gland histolysis.
The stage-specific programmed cell death of salivary gland cells during salivary gland histolysis.
The stage-specific programmed cell death of salivary gland cells during salivary gland histolysis.
Any process induced by ecdysone that directly activates salivary gland programmed cell death during salivary gland histolysis.
Any process induced by ecdysone that directly activates salivary gland programmed cell death during salivary gland histolysis.
Any process induced by ecdysone that directly activates salivary gland programmed cell death during salivary gland histolysis.
The onset of prepupal development when the larval stops crawling, everts its spiracles and the larval cuticle becomes the puparium or pupal case that surrounds the organism for the duration of metamorphosis.
The onset of prepupal development when the larval stops crawling, everts its spiracles and the larval cuticle becomes the puparium or pupal case that surrounds the organism for the duration of metamorphosis.
The act of becoming a pupa, a resting stage in the life cycle of organisms with complete metamorphosis. This event marks the end of the prepupal period and the beginning of the pupal period.
The act of becoming a pupa, a resting stage in the life cycle of organisms with complete metamorphosis. This event marks the end of the prepupal period and the beginning of the pupal period.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a ecdysone stimulus.
The series of molecular signals generated by ecdysone binding to the ecdysone receptor complex.
The decondensing (loosening) and swelling of the chromosomal sites of hormone-responsive genes on polytene chromosomes in response to increased production of the steroid hormone 20-hydroxyecdysone (ecdysone) in Drosophila larvae approaching pupation.
Any process induced by the steroid hormone 20-hydroxyecdysone (ecdysone) that directly activates any of the steps required for programmed cell death.
The decondensing (loosening) and swelling of the chromosomal sites of target genes on polytene chromosomes following response to a stimulus, to facilitate sudden bursts of transcriptional activity in response to transient environmental signals.
The decondensing (loosening) and swelling of the chromosomal sites of heat shock genes on polytene chromosomes in response to a heat shock stimulus.
Any process induced by hormones that directly activates any of the steps required for programmed cell death.
The assembly and organization of an axoneme, the bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements.
The assembly and organization of an axoneme, the bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements.
The assembly and organization of an axoneme, the bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements.
The assembly and organization of an axoneme, the bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements.
The assembly and organization of an axoneme, the bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements.
The assembly and organization of an axoneme, the bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements.
The assembly and organization of an axoneme, the bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements.
The assembly and organization of an axoneme, the bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements.
The transfer of small interfering RNA molecules (siRNAs) from the Dicer family of enzymes that cleave the double-stranded RNA, onto the nuclease-containing RNA-initiated silencing complex (RISC), in the context of RNA interference.
Any cellular process that results in the specification, formation or maintenance polarization of a cell's architecture along its apical/basal axis so that the apical and basal regions of the cell have different membrane, extracellular matrix and sub-membrane cellular components.
The specification and formation of the polarity of a cell along its apical/basal axis.
Retaining the established polarization of a cell along its apical/basal axis.
Interacting selectively and non-covalently with any inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
The progressive compaction of the spermatid chromatin so that it reaches a level of condensation that is not compatible with nuclear activities such as transcription or DNA replication.
The replacement of somatic histones within sperm chromatin with sperm-specific histones or protamines with unique DNA-binding properties, resulting in condensation of the sperm chromatin.
The replacement of somatic histones within sperm chromatin with sperm-specific histones or protamines with unique DNA-binding properties, resulting in condensation of the sperm chromatin.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nicotine stimulus.
Any process that results in a change in the behavior of an organism as a result of a nicotine stimulus.
The stage-specific programmed cell death of cells of the larval midgut, during histolysis of the larval organ.
The stage-specific programmed cell death of cells of the larval midgut, during histolysis of the larval organ.
A multimeric complex that is able to catalyze the addition of methyl groups to histone proteins.
A multimeric protein complex that can methylate lysine-27 and lysine-9 residues of histone H3. In Drosophila the core subunits of the complex include ESC, E(Z), CAF1 (NURF-55) and SU(Z)12. In mammals the core subunits of the complex include EED, EZH2, SUZ12 and RBBP4.
A multimeric protein complex that can methylate lysine-27 and lysine-9 residues of histone H3. In Drosophila the core subunits of the complex include ESC, E(Z), CAF1 (NURF-55) and SU(Z)12. In mammals the core subunits of the complex include EED, EZH2, SUZ12 and RBBP4.
The directed movement of a hemocyte within the embryo. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. In Drosophila, embryonic hemocytes originate from the head mesoderm as a cluster of cells. The cluster splits into two and one group of cells crosses the amnioserosa. Both populations then spread toward the middle of the embryo and then disperse evenly throughout the embryo.
The directed movement of a hemocyte within the embryo. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. In Drosophila, embryonic hemocytes originate from the head mesoderm as a cluster of cells. The cluster splits into two and one group of cells crosses the amnioserosa. Both populations then spread toward the middle of the embryo and then disperse evenly throughout the embryo.
Interacting selectively and non-covalently with 20-hydroxyecdysone (ecdysone). Ecdysone is an ecdysteroid produced by the prothoracic glands of immature insects and the ovaries of adult females, which stimulates growth and molting.
An abundant nuclear complex, which was originally identified in mammalian systems as a factor required for transcription elongation on chromatin templates. The FACT complex has been shown to destablilize the interaction between the H2A/H2B dimer and the H3/H4 tetramer of the nucleosome, thus reorganizing the structure of the nucleosome. In this way, the FACT complex may play a role in DNA replication and other processes that traverse the chromatin, as well as in transcription elongation. FACT is composed of two proteins that are evolutionarily conserved in all eukaryotes and homologous to mammalian Spt16 and SSRP1. In metazoans, the SSRP1 homolog contains an HMG domain; however in fungi and protists, it does not. For example, in S. cerevisiae the Pob3 protein is homologous to SSRP1, but lacks the HMG chromatin binding domain. Instead, the yFACT complex of Spt16p and Pob3p, binds to nucleosomes where multiple copies of the HMG-domain containing protein Nhp6p have already bound, but Nhp6p does not form a stable complex with the Spt16p/Pob3p heterodimer.
A multiprotein complex that mediates monoubiquitination of lysine residues of histone H2A (lysine-118 in Drosophila or lysine-119 in mammals). The complex is required for stable long-term maintenance of transcriptionally repressed states and is involved in chromatin remodeling.
The proteolytic release of a transcriptionally active sterol regulatory element binding protein (SREBP) from intracellular membranes, freeing it to move to the nucleus to upregulate transcription of target genes, in response to altered levels of one or more lipids.
The proteolytic release of a transcriptionally active sterol regulatory element binding protein (SREBP) from intracellular membranes, freeing it to move to the nucleus to upregulate transcription of target genes, in response to altered levels of one or more lipids.
The proteolytic release of a transcriptionally active sterol regulatory element binding protein (SREBP) from intracellular membranes, freeing it to move to the nucleus to upregulate transcription of target genes, in response to altered levels of one or more lipids.
The proteolytic release of a transcriptionally active sterol regulatory element binding protein (SREBP) from intracellular membranes, freeing it to move to the nucleus to upregulate transcription of target genes, in response to altered levels of one or more lipids.
Learning to anticipate future events on the basis of past experience with the consequences of one's own behavior.
The process in which the anatomical structures of appendages are generated and organized. An appendage is an organ or part that is attached to the trunk of an organism, such as a limb or a branch.
The process in which the anatomical structures of a limb are generated and organized. A limb is a paired appendage of a tetrapod used for locomotion or grasping.
The process in which the anatomical structures of appendages are generated and organized. An appendage is an organ or part that is attached to the trunk of an organism.
The process in which the anatomical structures of the hindlimb are generated and organized.
The process, occurring in the embryo, in which the anatomical structures of a skeletal limb joint are generated and organized. A skeletal limb joint is the connecting structure between the bones of a limb.
The process in which the anatomical structures of genitalia are generated and organized. The genitalia are the organs of reproduction or generation, external and internal.
The process, occurring in the embryo, by which the anatomical structures of the appendage are generated and organized. An appendage is an organ or part that is attached to the trunk of an organism, such as a limb or a branch.
The process, occurring in the embryo, by which the anatomical structures of the forelimb are generated and organized. The forelimbs are the front limbs of an animal, e.g. the arms of a human.
The process, occurring in the embryo, by which the anatomical structures of the forelimb are generated and organized. The forelimbs are the front limbs of an animal, e.g. the arms of a human.
The process, occurring in the embryo, by which the anatomical structures of the hindlimbs are generated and organized. The hindlimbs are the posterior limbs of an animal.
The process, occurring in the embryo, by which the anatomical structures of the pectoral fin are generated and organized. Pectoral fins are bilaterally paired fins mounted laterally and located behind the gill covers of fish. These fins are used for lateral mobility and propulsion.
The process, occurring in the embryo, by which the anatomical structures of the pelvic fin are generated and organized. The pelvic fins are bilaterally paired fins mounted in a ventral-lateral position on most fish. These fins are used primarily for lateral mobility and propulsion.
The process, occurring after embryonic development, by which the anatomical structures of an appendage are generated and organized. An appendage is an organ or part that is attached to the trunk of an organism, such as a limb or a branch.
The process in which a post-anal tail is generated and organized. A post-anal tail is a muscular region of the body that extends posterior to the anus. The post-anal tail may aid locomotion and balance.
The process in which the anatomical structures of analia are generated and organized. The analia is the posterior-most vertral appendage that develops from the genital disc. An example of this process is analia morphogenesis in Drosophila melanogaster.
The process, occurring in the embryo, by which the anatomical structures of the medial fin are generated and organized. Medial fins are unpaired fins of fish, usually located dorsomedially or ventromedially and primarily used for stability while swimming.
The process, occurring in the embryo, by which the anatomical structures of the dorsal fin are generated and organized. A dorsal fin is an unpaired medial fin on the dorsal aspect of a fish that provides lateral stability while swimming. Generally fish have one or two dorsal fins.
The process, occurring in the embryo, by which the anatomical structures of the caudal fin are generated and organized. The caudal fin is an unpaired medial fin mounted at the caudal end of the fish and is the main fin used for propulsion.
The process, occurring in the embryo, by which the anatomical structures of the embryonic anal fin are generated and organized. An anal fin is an unpaired medial fin on the ventral aspect near the caudal end of a fish, which provides lateral stability while swimming.
The process, occurring after embryonic development, by which the anatomical structures of the genitalia are generated and organized.
The process, occurring after embryonic development, by which the anatomical structures of the limb are generated and organized. A limb is an appendage of an animal used for locomotion or grasping.
The process, occurring after embryonic development, by which the anatomical structures of the forelimb are generated and organized. The forelimbs are the front limbs of an organism.
The process, occurring after embryonic development, by which the anatomical structures of the hindlimb are generated and organized.
The process, occurring after embryonic development, by which the anatomical structures of the pectoral fin are generated and organized. Pectoral fins are bilaterally paired fins mounted laterally and located behind the gill covers of fish. These fins are used for lateral mobility and propulsion.
The process, occurring after embryonic development, by which the anatomical structures of the pelvic fin are generated and organized. The pelvic fins are bilaterally paired fins mounted in a ventral-lateral position on most fish. These fins are used primarily for lateral mobility and propulsion.
The process, occurring after embryonic development, by which the anatomical structures of the medial fin are generated and organized. Medial fins are unpaired fins of fish, usually located dorsomedially or ventromedially and primarily used for stability while swimming.
The process, occurring after embryonic development, by which the anatomical structures of the caudal fin are generated and organized. The caudal fin is an unpaired medial fin mounted at the caudal end of the fish and is the main fin used for propulsion.
The process, occurring after embryonic development, by which the anatomical structures of the dorsal fin are generated and organized. A dorsal fin is an unpaired medial fin on the dorsal aspect of a fish that provides lateral stability while swimming. Generally fish have one or two dorsal fins.
The process, occurring after embryonic development, by which the anatomical structures of the anal fin are generated and organized. An anal fin is an unpaired medial fin on the ventral aspect near the caudal end of a fish, which provides lateral stability while swimming.
The process in which the anatomical structures of the forelimb are generated and organized. The forelimbs are the front limbs of an animal, e.g. the arms of a human.
The process in which the anatomical structures of the forelimb are generated and organized. The forelimbs are the front limbs of an animal, e.g. the arms of a human.
The process in which the anatomical structures of the pectoral fin are generated and organized. Pectoral fins are bilaterally paired fins mounted laterally and located behind the gill covers of fish. These fins are used for lateral mobility and propulsion.
The process in which the anatomical structures of the pelvic fin are generated and organized. Pelvic fins are bilaterally paired fins mounted in a ventral-lateral position on most fish. These fins are used primarily for lateral mobility and propulsion.
The process in which the anatomical structures of the medial fin are generated and organized. A medial fin is an unpaired fin of fish, usually located dorsomedially or ventromedially and primarily used for stability while swimming.
The process in which the anatomical structures of the dorsal fin are generated and organized. A dorsal fin is an unpaired medial fin on the dorsal aspect of fish that provides lateral stability while swimming. Generally fish have one or two dorsal fins.
The process in which the anatomical structures of the caudal fin are generated and organized. A caudal fin is an unpaired medial fin mounted at the caudal end of the fish, and is the main fin used for propulsion.
The process in which the anatomical structures of the anal fin are generated and organized. An anal fin is an unpaired medial fin on the ventral aspect near the caudal end of a fish, which provides lateral stability while swimming.
A multi-subunit complex deposited by the spliceosome upstream of messenger RNA exon-exon junctions. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay.
A multi-subunit complex deposited by the spliceosome upstream of messenger RNA exon-exon junctions. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay.
The joining of specific branches of a tubular system to form a continuous network.
Fusing of specific tracheal branches in an open tracheal system to branches from neighboring hemisegments to form a continuous tracheal network. Branch fusion is mediated by individual cells at the tip of each branch, which contact a similar cell and undergo a coordinated series of morphogenetic events that create a bicellular fusion joint.
Creation of the central hole of a tube in an anatomical structure through which gases and/or liquids flow.
Creation of the central hole of a tube in an anatomical structure through which gases and/or liquids flow.
Creation of the central hole of a tube in an open tracheal system through which gases flow.
Ensuring that a tube is of the correct length and diameter. Tube size must be maintained not only during tube formation, but also throughout development and in some physiological processes.
Ensuring that an epithelial tube in an open tracheal system is of the correct length and diameter. Tracheal tubes undergo highly regulated tube-size increases during development, expanding up to 40 times their initial size by the end of larval life. Tube size appears to be controlled by regulation of apical membrane expansion and secretion, rather than by changes in cell number, size or shape.
Ensuring that tracheal cells form and maintain tubular structures with the correct size and shape for their position in the network. This is essential for efficient flow of gases through the tracheal network.
Allocation of epithelial cells within each migrating branch in an open tracheal system to distinct tracheal cell fates. During the migration phase each branch forms a well-defined number of cell types (including fusion cells, terminal cells and branch cells) at precise positions.
Allocation of epithelial cells within each migrating branch in an open tracheal system to distinct tracheal cell fates. During the migration phase each branch forms a well-defined number of cell types (including fusion cells, terminal cells and branch cells) at precise positions.
The process in which a cell in an open tracheal system becomes capable of differentiating autonomously into a terminal cell in an environment that is neutral with respect to the developmental pathway; upon specification, the cell fate can be reversed. Terminal cells send long and bifurcated hollow branches toward target tissues to allow oxygen exchange.
Any process that restricts, stops or prevents a cell from adopting a terminal cell fate in an open tracheal system. Once the terminal and fusion fates have been correctly induced, inhibitory feedback loops prevent the remaining branch cells from assuming similar fates.
Any process that restricts, stops or prevents a cell from adopting a terminal cell fate in an open tracheal system. Once the terminal and fusion fates have been correctly induced, inhibitory feedback loops prevent the remaining branch cells from assuming similar fates.
Any process that restricts, stops or prevents a cell from adopting a terminal cell fate in an open tracheal system. Once the terminal and fusion fates have been correctly induced, inhibitory feedback loops prevent the remaining branch cells from assuming similar fates.
Any process that restricts, stops or prevents a cell from adopting a terminal cell fate in an open tracheal system. Once the terminal and fusion fates have been correctly induced, inhibitory feedback loops prevent the remaining branch cells from assuming similar fates.
Any process that restricts, stops or prevents a cell from adopting a terminal cell fate in an open tracheal system. Once the terminal and fusion fates have been correctly induced, inhibitory feedback loops prevent the remaining branch cells from assuming similar fates.
The process in which a cell becomes capable of differentiating autonomously into a fusion cell in an environment that is neutral with respect to the developmental pathway; upon specification, the cell fate can be reversed. Fusion cells allow the interconnection of adjacent tracheal metameres during tracheal tube fusion.
Any process that restricts, stops or prevents a cell from adopting a fusion cell fate. Once the terminal and fusion fates have been correctly induced, inhibitory feedback loops prevent the remaining branch cells from assuming similar fates.
Any process that restricts, stops or prevents a cell from adopting a fusion cell fate. Once the terminal and fusion fates have been correctly induced, inhibitory feedback loops prevent the remaining branch cells from assuming similar fates.
Any process that restricts, stops or prevents a cell from adopting a fusion cell fate. Once the terminal and fusion fates have been correctly induced, inhibitory feedback loops prevent the remaining branch cells from assuming similar fates.
Any process that restricts, stops or prevents a cell from adopting a fusion cell fate. Once the terminal and fusion fates have been correctly induced, inhibitory feedback loops prevent the remaining branch cells from assuming similar fates.
Ensuring that a tube in an open tracheal system is of the correct diameter. When primary branches form their lumens are small (less than 2 micrometers) in caliber and must undergo regulated expansion during larval life to reach their mature size.
Ensuring that a tube in an open tracheal system is of the correct diameter. When primary branches form their lumens are small (less than 2 micrometers) in caliber and must undergo regulated expansion during larval life to reach their mature size.
Ensuring that a tube in an open tracheal system is of the correct diameter. When primary branches form their lumens are small (less than 2 micrometers) in caliber and must undergo regulated expansion during larval life to reach their mature size.
Ensuring that a tube in an open tracheal system is of the correct length.
Ensuring that a tube in an open tracheal system is of the correct length.
Ensuring that tracheal tubes in an open tracheal system maintain their epithelial structure during the cell shape changes and movements that occur during the branching process.
Formation and/or maintenance of a lineage boundary between compartments in an imaginal disc that cells cannot cross, thus separating the populations of cells in each compartment.
The stages of blood cell formation that take place within the embryo.
The stages of blood cell formation that take place within the embryo.
The stages of blood cell formation that take place within the embryo.
The process in which a relatively unspecialized cell derived from the embryonic head mesoderm acquires the specialized features of a mature hemocyte. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen.
The process in which a relatively unspecialized cell derived from the embryonic head mesoderm acquires the specialized features of a mature hemocyte. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen.
The process in which an embryonic mesoderm-derived hemocyte precursor cell acquires the specialized features of the phagocytic blood-cell type, the plasmatocyte.
The process in which an embryonic mesoderm-derived hemocyte precursor cell acquires the specialized features of a crystal cell. Crystal cells are a class of cells that contain crystalline inclusions and are involved in the melanization of pathogenic material in the hemolymph.
The stages of blood cell formation that take place after completion of embryonic development.
The production of blood cells from the larval lymph gland. The lymph gland consists of three to six bilaterally paired lobes that are attached to the cardioblasts during larval stages, and it degenerates during pupal stages.
The production of blood cells from the larval lymph gland. The lymph gland consists of three to six bilaterally paired lobes that are attached to the cardioblasts during larval stages, and it degenerates during pupal stages.
The production of blood cells from the larval lymph gland. The lymph gland consists of three to six bilaterally paired lobes that are attached to the cardioblasts during larval stages, and it degenerates during pupal stages.
The process in which a relatively unspecialized cell derived from the larval lymph gland acquires the specialized features of a mature hemocyte. The lymph gland consists of three to six bilaterally paired lobes that are attached to the cardioblasts during larval stages, and it degenerates during pupal stages. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this process is found in Drosophila melanogaster.
The process in which a relatively unspecialized larval lymph gland-derived hemocyte precursor cell acquires the specialized features of the phagocytic blood-cell type, the plasmatocyte.
The process in which a relatively unspecialized larval lymph gland-derived hemocyte precursor cell acquires the specialized features of a crystal cell. Crystal cells are a class of cells that contain crystalline inclusions and are involved in the melanization of pathogenic material in the hemolymph.
The process in which a relatively unspecialized hemocyte precursor cell acquires the specialized features of a lamellocyte. Lamellocytes are a hemocyte lineage that exists only in larvae, but are seldom observed in healthy animals. Lamellocytes differentiate massively in the lymph glands after parasitization and are large flat cells devoted to encapsulation of invaders too large to be phagocytosed by plasmatocytes.
The multiplication or reproduction of hemocytes, resulting in the expansion of the cell population. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen.
Catalysis of the transfer of a phosphate group to a histone. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes.
Catalysis of the transfer of a phosphate group to a serine residue of a histone. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic  chromosomes.
Catalysis of the transfer of a phosphate group to the serine-10 residue of the N-terminal tail of histone H3.
Catalysis of the transfer of a phosphate group to the serine-10 residue of the N-terminal tail of histone H3.
Catalysis of the transfer of a phosphate group to the serine-10 residue of the N-terminal tail of histone H3.
Catalysis of the transfer of a phosphate group to the serine-10 residue of the N-terminal tail of histone H3.
Behavior directed towards society, or taking place between members of the same species. Occurs predominantly, or only, in individuals that are part of a group.
Behavior directed towards society, or taking place between members of the same species. Occurs predominantly, or only, in individuals that are part of a group.
The movement of a larva through a feeding substrate whilst feeding on food.
Fine-tuning the spatial position of an organism in response to variability in their environment. For example, reorientation of an organism in the direction of a food source.
Fine-tuning the spatial position of a larva in response to variability in their environment. For example, reorientation of a larva in the direction of a food source.
The movement of a third instar larva through a substrate in search of a pupation site. This movement occurs without feeding and is characterized by short bursts of forward movement, separated by stops and repeated side-to-side head probes, followed normally by a change in direction.
Digging into the substrate by non-feeding larvae in search for food-free sites suitable for pupation.
An electron opaque backbone of the insect ovarian ring canal that is a part of or adjacent to the plasma membrane. The outer rim is established as the cleavage furrow is arrested, and contains F-actin, anillin, glycoproteins and at least one a protein with a high content of phosphorylated tyrosine residues.
An electron opaque backbone of the insect ovarian ring canal that is a part of or adjacent to the plasma membrane. The outer rim is established as the cleavage furrow is arrested, and contains F-actin, anillin, glycoproteins and at least one a protein with a high content of phosphorylated tyrosine residues.
An electron opaque backbone of the insect ovarian ring canal that is a part of or adjacent to the plasma membrane. The outer rim is established as the cleavage furrow is arrested, and contains F-actin, anillin, glycoproteins and at least one a protein with a high content of phosphorylated tyrosine residues.
A proteinaceous actin-rich layer of the insect ovarian ring canal that forms subcortically to the outer rim. The electron dense inner rim accumulates after the final mitotic division of each germline syncytia, and contains actin, a phosphotyrosine protein, and a number of cytoskeletal proteins.
A proteinaceous actin-rich layer of the insect ovarian ring canal that forms subcortically to the outer rim. The electron dense inner rim accumulates after the final mitotic division of each germline syncytia, and contains actin, a phosphotyrosine protein, and a number of cytoskeletal proteins.
A proteinaceous actin-rich layer of the insect ovarian ring canal that forms subcortically to the outer rim. The electron dense inner rim accumulates after the final mitotic division of each germline syncytia, and contains actin, a phosphotyrosine protein, and a number of cytoskeletal proteins.
Catalysis of the transfer of a phosphate group to a threonine residue of a histone. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic  chromosomes.
The first nine mitotic division cycles of the insect embryo, during which the dividing nuclei lie deep in the interior of the egg and divide nearly synchronously. This is the first phase of the syncytial period where nuclei divide in a common cytoplasm without cytokinesis.
Mitotic division cycles 10 to 13 of the insect embryo. This is the second phase of the syncytial period where nuclei divide in a common cytoplasm without cytokinesis. The majority of migrating nuclei reach the embryo surface during cycle 10, after which they divide less synchronously than before, and the syncytial blastoderm cycles lengthen progressively.
The specific behavior of an organism during the emergence from an egg shell. In Drosophila for example, the larva swings its head reiteratively through a semicircular arc, using its mouth hooks to tear apart the chorion in front of it and thus free itself from within the egg shell.
The emergence of an immature organism from a protective structure.
A multiprotein complex containing a heterodimeric E2F transcription factor and a Retinoblastoma (Rb) family member. This complex is capable of repressing transcription of E2F-regulated genes in order to regulate cell cycle progression.
The directed movement of nuclei within the syncytial embryo of insects. These precise temporal and spatial patterns of nuclear movement are coordinated with mitotic divisons and are required during blastoderm formation to reposition dividing nuclei from the interior of the syncytial embryo to the cortex.
The stepwise asymmetric spreading out of nuclei internally along the anterior-posterior axis of the developing insect embryo during mitotic cycles 4 to 6. This movement leads to the distribution of nuclei in a hollow ellipsoid underlying the cortex.
The stepwise asymmetric spreading out of nuclei internally along the anterior-posterior axis of the developing insect embryo during mitotic cycles 4 to 6. This movement leads to the distribution of nuclei in a hollow ellipsoid underlying the cortex.
The symmetric outward movement of the syncytial nuclei from their positions in the ellipsoid toward the periphery of the embryo, during mitotic cycles 8 and 9. This movement results in the placement of nuclei in a uniform monolayer at the cortex of the developing embryo.
Reorganization of the pre-existing, functional larval central nervous system into one that can serve the novel behavioral needs of the adult. An example of this process is found in Drosophila melanogaster.
Reorganization of the pre-existing, functional larval central nervous system into one that can serve the novel behavioral needs of the adult. An example of this process is found in Drosophila melanogaster.
Any process of posttranscriptional gene inactivation (silencing) mediated by small RNA molecules that may trigger mRNA degradation or negatively regulate translation.
Any process of posttranscriptional gene inactivation (silencing) mediated by small RNA molecules that may trigger mRNA degradation or negatively regulate translation.
Downregulation of gene expression through the action of microRNAs (miRNAs), endogenous 21-24 nucleotide small RNAs processed from stem-loop RNA precursors (pre-miRNAs). Once incorporated into a RNA-induced silencing complex (RISC), miRNAs can downregulate gene expression by either of two posttranscriptional mechanisms: endolytic cleavage of mRNA cleavage or translational repression, usually accompanied by poly-A tail shortening and subsequent degradation of the mRNA.
Downregulation of gene expression through the action of microRNAs (miRNAs), endogenous 21-24 nucleotide small RNAs processed from stem-loop RNA precursors (pre-miRNAs). Once incorporated into a RNA-induced silencing complex (RISC), miRNAs can downregulate gene expression by either of two posttranscriptional mechanisms: endolytic cleavage of mRNA cleavage or translational repression, usually accompanied by poly-A tail shortening and subsequent degradation of the mRNA.
Downregulation of gene expression through the action of microRNAs (miRNAs), endogenous 21-24 nucleotide small RNAs processed from stem-loop RNA precursors (pre-miRNAs). Once incorporated into a RNA-induced silencing complex (RISC), miRNAs can downregulate gene expression by either of two posttranscriptional mechanisms: endolytic cleavage of mRNA cleavage or translational repression, usually accompanied by poly-A tail shortening and subsequent degradation of the mRNA.
Interacting selectively and non-covalently with a small interfering RNA, a 21-23 nucleotide RNA that is processed from double stranded RNA (dsRNA) by an RNAse enzyme.
Interacting selectively and non-covalently with a microRNA, a 21-23 nucleotide RNA that is processed from a stem-loop RNA precursor (pre-miRNA) that is encoded within plant and animal genomes.
The specific avoidance actions or reactions of an organism in response to the perception of salt.
The establishment, maintenance and elaboration of the anterior/posterior axis of the leg imaginal disc.
Formation and/or maintenance of a lineage boundary between anterior and posterior compartments of the leg disc that cells cannot cross, thus separating the populations of cells in each compartment.
Formation of the tracheal pits, the first tube-like structures to form in the open tracheal system. Once cells are determined to their tracheal cell fate, the tracheal pits arise by invagination of each ectodermal cluster of tracheal placode cells, between 5 and 7 hours after egg laying. An example of this is found in Drosophila melanogaster.
Formation of the tracheal pits, the first tube-like structures to form in the open tracheal system. Once cells are determined to their tracheal cell fate, the tracheal pits arise by invagination of each ectodermal cluster of tracheal placode cells, between 5 and 7 hours after egg laying. An example of this is found in Drosophila melanogaster.
Any process that modulates the frequency, rate or extent of lamellocyte differentiation. Lamellocytes differentiate massively in the lymph glands after parasitization and are large flat cells devoted to encapsulation of invaders too large to be phagocytosed by plasmatocytes.
Any process that stops, prevents, or reduces the frequency, rate or extent of lamellocyte differentiation. Lamellocytes differentiate massively in the lymph glands after parasitization and are large flat cells devoted to encapsulation of invaders too large to be phagocytosed by plasmatocytes.
Any process that stops, prevents, or reduces the frequency, rate or extent of lamellocyte differentiation. Lamellocytes differentiate massively in the lymph glands after parasitization and are large flat cells devoted to encapsulation of invaders too large to be phagocytosed by plasmatocytes.
Any process that stops, prevents, or reduces the frequency, rate or extent of lamellocyte differentiation. Lamellocytes differentiate massively in the lymph glands after parasitization and are large flat cells devoted to encapsulation of invaders too large to be phagocytosed by plasmatocytes.
Any process that stops, prevents, or reduces the frequency, rate or extent of lamellocyte differentiation. Lamellocytes differentiate massively in the lymph glands after parasitization and are large flat cells devoted to encapsulation of invaders too large to be phagocytosed by plasmatocytes.
Any process that activates or increases the frequency, rate or extent of lamellocyte differentiation. Lamellocytes differentiate massively in the lymph glands after parasitization and are large flat cells devoted to encapsulation of invaders too large to be phagocytosed by plasmatocytes.
Any process that activates or increases the frequency, rate or extent of lamellocyte differentiation. Lamellocytes differentiate massively in the lymph glands after parasitization and are large flat cells devoted to encapsulation of invaders too large to be phagocytosed by plasmatocytes.
Any process that activates or increases the frequency, rate or extent of lamellocyte differentiation. Lamellocytes differentiate massively in the lymph glands after parasitization and are large flat cells devoted to encapsulation of invaders too large to be phagocytosed by plasmatocytes.
Any process that activates or increases the frequency, rate or extent of lamellocyte differentiation. Lamellocytes differentiate massively in the lymph glands after parasitization and are large flat cells devoted to encapsulation of invaders too large to be phagocytosed by plasmatocytes.
Any process that activates or increases the frequency, rate or extent of lamellocyte differentiation. Lamellocytes differentiate massively in the lymph glands after parasitization and are large flat cells devoted to encapsulation of invaders too large to be phagocytosed by plasmatocytes.
Any process that modulates the frequency, rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this is found in Drosophila melanogaster.
Any process that stops, prevents or reduces the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this is found in Drosophila melanogaster.
Any process that stops, prevents or reduces the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this is found in Drosophila melanogaster.
Any process that stops, prevents or reduces the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this is found in Drosophila melanogaster.
Any process that stops, prevents or reduces the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this is found in Drosophila melanogaster.
Any process that stops, prevents or reduces the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) which are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this is found in Drosophila melanogaster.
Any process that activates or increases the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) that are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this process is found in Drosophila melanogaster.
Any process that activates or increases the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) that are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this process is found in Drosophila melanogaster.
Any process that activates or increases the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) that are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this process is found in Drosophila melanogaster.
Any process that activates or increases the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) that are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this process is found in Drosophila melanogaster.
Any process that activates or increases the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) that are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this process is found in Drosophila melanogaster.
Any process that activates or increases the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) that are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this process is found in Drosophila melanogaster.
The process whose specific outcome is the progression of the pupa over time, from its formation to the mature structure. The pupa is a dormant life stage interposed between the larval and the adult stages in insects that undergo a complete metamorphosis.
The process whose specific outcome is the progression of the prepupa over time, from its formation to the mature structure. The prepupal stage is a life stage interposed between the larval and the pupal stages in insects that undergo a complete metamorphosis. The start of the pre-pupal stage is marked by pupariation, and the end is marked by pupation.
The process in which the anatomical structures of a spermathecum, a sperm storage organ, are generated and organized. Paired spermathecae lie at the anterior end of the insect uterus on the dorsal side. Each spermatheca consists of an oval shaped capsule, connected to the uterus by a spermathecal stalk.
Competitive interactions within multicellular organisms between cell populations that differ in growth rates, leading to the elimination of the slowest-growing cells.
The process whose specific outcome is the progression of the clypeo-labral disc over time, from its formation to the metamorphosis to form adult structures. The clypeo-labral disc develops into the labrum, anterior cibarial plate, fish trap bristles, epistomal sclerite.
Progression of the eye-antennal imaginal disc over time, from its initial formation through to its metamorphosis to form adult structures including the eye, antenna, head capsule and maxillary palps.
Progression of the genital imaginal disc over time, from its initial formation through to its metamorphosis to form the adult terminalia, comprising the entire set of internal and external genitalia and analia. Both sexes of Drosophila have a single genital disc formed from the female and male genital primordia, and the anal primordium. The anal primordium develops in both sexes, forming either male or female analia. However, only one of the genital primordia develops in each sex, forming either the male or the female genitalia.
Progression of the haltere imaginal disc over time, from its initial formation through to its metamorphosis to form the adult capitellum, pedicel, haltere sclerite, metathoracic spiracle and metanotum.
Progression of the labial imaginal disc over time, from its initial formation through to its metamorphosis to form adult structures including parts of the proboscis.
Progression of the leg imaginal disc over time, from its initial formation through to its metamorphosis to form adult structures including the leg, coxa and ventral thoracic pleura.
Progression of the prothoracic disc over time, from its initial formation through to its metamorphosis to form the adult humerous and anterior spiracle.
Progression of the wing disc over time, from its initial formation through to its metamorphosis to form adult structures including the wing hinge, wing blade and pleura.
The process that gives rise to the patterns of cell differentiation that will arise in the genital imaginal disc.
The process giving rise to the pattern of cell differentiation in the wing imaginal disc.
The process that gives rise to the patterns of cell differentiation in the leg imaginal disc.
The establishment, maintenance and elaboration of the anterior/posterior axis of the genital disc. An anterior and posterior compartment form in each of the three genital disc primoridia (the female genital disc primordium, the male genital disc primordium and the anal primordium).
Allocation of embryonic cells to the genital imaginal disc founder populations. Early in development at the blastoderm stage, the anlage of the genital disc of both sexes consists of three primordia: the female genital primoridum lcoated anteriorly, the anal primoridum located posteriorly, and the male gential primordium between the two.
Interacting selectively and non-covalently with the catalytic subunit of glutamate-cysteine ligase.
Any process that modulates the activity of glutamate-cysteine ligase.
Any process that stops or reduces the activity of the enzyme glutamate-cysteine ligase.
Any process that stops or reduces the activity of the enzyme glutamate-cysteine ligase.
Any process that stops or reduces the activity of the enzyme glutamate-cysteine ligase.
Any process that stops or reduces the activity of the enzyme glutamate-cysteine ligase.
Any process that activates or increases the activity of glutamate-cysteine ligase, typically by lowering its sensitivity to inhibition by glutathione and by increasing its affinity for glutamate.
Any process that activates or increases the activity of glutamate-cysteine ligase, typically by lowering its sensitivity to inhibition by glutathione and by increasing its affinity for glutamate.
Any process that activates or increases the activity of glutamate-cysteine ligase, typically by lowering its sensitivity to inhibition by glutathione and by increasing its affinity for glutamate.
Any process that activates or increases the activity of glutamate-cysteine ligase, typically by lowering its sensitivity to inhibition by glutathione and by increasing its affinity for glutamate.
Any process that activates or increases the activity of glutamate-cysteine ligase, typically by lowering its sensitivity to inhibition by glutathione and by increasing its affinity for glutamate.
A long, thin, polarized cell projection that contains actin and can extend for distances many times the diameter of the cell. Cytonemes represent extensions of cell cytoplasm and typically have a diameter of approximately 0.2um.
Formation of a cytoneme, a long, thin and polarized actin-based cytoplasmic extension that projects from a cell.
The directed movement of a germ cell from their site of production to the gonad, through the attraction of cells towards their target.
The directed movement of a germ cell from their site of production to the gonad, through the repulsion of cells away from a tissue.
Programmed cell death of an errant germ line cell that is outside the normal migratory path or ectopic to the gonad. This is an important mechanism of regulating germ cell survival within the embryo.
Programmed cell death of an errant germ line cell that is outside the normal migratory path or ectopic to the gonad. This is an important mechanism of regulating germ cell survival within the embryo.
A series of molecular signals initiated by glutamate binding to a glutamate receptor on the surface of the target cell, followed by the movement of ions through a channel in the receptor complex. Ends with regulation of a downstream cellular process, e.g. transcription.
Combining with the neuropeptide proctolin, to initiate a change in cell activity.
Combining with the neuropeptide corazonin to initiate a change in cell activity.
The chemical reactions and pathways resulting in the formation of any of the vitamin A compounds, retinol, retinal (retinaldehyde) and retinoic acid. Animals cannot synthesize vitamin A de novo, but form it through oxidative cleavage of carotenoids.
The chemical reactions and pathways resulting in the formation of any of the vitamin A compounds, retinol, retinal (retinaldehyde) and retinoic acid. Animals cannot synthesize vitamin A de novo, but form it through oxidative cleavage of carotenoids.
The chemical reactions and pathways resulting in the formation of any of the vitamin A compounds, retinol, retinal (retinaldehyde) and retinoic acid. Animals cannot synthesize vitamin A de novo, but form it through oxidative cleavage of carotenoids.
The chemical reactions and pathways resulting in the formation of any of the vitamin A compounds, retinol, retinal (retinaldehyde) and retinoic acid. Animals cannot synthesize vitamin A de novo, but form it through oxidative cleavage of carotenoids.
The process in which the anatomical structures of a tube are generated and organized. Epithelial and endothelial tubes transport gases, liquids and cells from one site to another and form the basic structure of many organs and tissues, with tube shape and organization varying from the single-celled excretory organ in Caenorhabditis elegans to the branching trees of the mammalian kidney and insect tracheal system.
Interacting selectively and non-covalently with dopamine, a catecholamine neurotransmitter formed by aromatic-L-amino-acid decarboxylase from 3,4-dihydroxy-L-phenylalanine.
Catalysis of the addition of a methyl group to either of the unmethylated terminal nitrogen atoms (also called omega nitrogen) in peptidyl-arginine to form an omega-N-G-monomethylated arginine residue.  The reaction is S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine.
Catalysis of the addition of a methyl group to either of the unmethylated terminal nitrogen atoms (also called omega nitrogen) in peptidyl-arginine to form an omega-N-G-monomethylated arginine residue.  The reaction is S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine.
Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the same terminal nitrogen (omega nitrogen) residue that was previously methylated, resulting in asymmetrical peptidyl-N(omega),N(omega)-dimethylated arginine residues.
Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the same terminal nitrogen (omega nitrogen) residue that was previously methylated, resulting in asymmetrical peptidyl-N(omega),N(omega)-dimethylated arginine residues.
Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the same terminal nitrogen (omega nitrogen) residue that was previously methylated, resulting in asymmetrical peptidyl-N(omega),N(omega)-dimethylated arginine residues.
Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the terminal nitrogen (omega nitrogen) residue that is not already methylated, resulting in symmetrical peptidyl-N(omega),N'(omega)-dimethyled arginine residues.
Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the terminal nitrogen (omega nitrogen) residue that is not already methylated, resulting in symmetrical peptidyl-N(omega),N'(omega)-dimethyled arginine residues.
Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the terminal nitrogen (omega nitrogen) residue that is not already methylated, resulting in symmetrical peptidyl-N(omega),N'(omega)-dimethyled arginine residues.
Catalysis of the transfer of a methyl group to the carbon atom of an arginine residue in a protein.
The addition of a methyl group onto a carbon atom of an arginine residue in a protein.
The addition of a methyl group onto a nitrogen atom of an arginine residue in a protein.
The addition of a methyl group onto a terminal nitrogen (omega nitrogen) atom of an arginine residue in a protein.
Catalysis of the transfer of an N-acetylgalactosaminyl residue from UDP-N-acetyl-galactosamine to an acceptor molecule, forming an alpha-1,4 linkage.
The vesicular release of glutamate from a presynapse, across a chemical synapse, the subsequent activation of glutamate receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
Catalysis of the transfer of a galactose group from UDP-galactose to an acceptor molecule.
Catalysis of the transfer of a glucosyl group from UDP-glucose to an acceptor molecule.
Catalysis of the transfer of a xylosyl group from UDP-xylose to an acceptor molecule.
A cytoskeleton-like structure, originating from the basal body at the proximal end of a cilium, and extending proximally toward the cell nucleus. Rootlets are typically 80-100 nm in diameter and contain cross striae distributed at regular intervals of approximately 55-70 nm.
A cytoskeleton-like structure, originating from the basal body at the proximal end of a cilium, and extending proximally toward the cell nucleus. Rootlets are typically 80-100 nm in diameter and contain cross striae distributed at regular intervals of approximately 55-70 nm.
Interacting selectively and non-covalently with a glutamate receptor.
Interacting selectively and non-covalently with an ionotropic glutamate receptor. Ionotropic glutamate receptors bind glutamate and exert an effect through the regulation of ion channels.
Interacting selectively and non-covalently with a G protein-coupled glutamate receptor (a metabotropic glutamate receptor).
Interacting selectively and non-covalently with a G protein-coupled glutamate receptor (a metabotropic glutamate receptor).
Interacting selectively and non-covalently with a nuclear hormone receptor, a ligand-dependent receptor found in the nucleus of the cell.
Interacting selectively and non-covalently with a steroid hormone receptor.
Interacting selectively and non-covalently with a glucocorticoid receptor.
The process in which the anatomical structures of the internal genitalia are generated and organized. The internal genitalia are the internal sex organs such as the uterine tube, the uterus and the vagina in female mammals, and the testis, seminal vesicle, ejaculatory duct and prostate in male mammals.
The process in which the anatomical structures of the external genitalia are generated and organized. The external genitalia are the outer sex organs, such as the penis or vulva in mammals.
The process in which the anatomical structures of the gonads are generated and organized. A gonad is an animal organ producing gametes, e.g. the testes or the ovary in mammals.
The sex-specific patterns of primoridia growth and differentiation in the genital imaginal disc. The anal primordium of the genital disc develops in both sexes, but depending on the genetic sex gives rise to either male or female analia. Depending on the genetic sex, only one of the two genital primordia develop. In females the female genital primordium develops and gives rise to the female genitalia whereas the male primordium is repressed. Conversely, in males the male genital primordium develops and gives rise to the male genitalia whereas the female genital primordium is repressed.
The increase in size or mass of an entire multicellular organism, as opposed to cell growth.
The increase in size or mass of an organ. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that function together as to perform a specific function.
The increase in size or mass of a meristem, a region of tissue in a plant that is composed of one or more undifferentiated cells capable of undergoing mitosis and differentiation.
A complex having histone acetylase activity on chromatin, as well as ATPase, DNA helicase and structural DNA binding activities. The complex is thought to be involved in double-strand DNA break repair. Subunits of the human complex include HTATIP/TIP60, TRRAP, RUVBL1, BUVBL2, beta-actin and BAF53/ACTL6A. In yeast, the complex has 13 subunits, including the catalytic subunit Esa1 (homologous to human Tip60).
A complex having histone acetylase activity on chromatin, as well as ATPase, DNA helicase and structural DNA binding activities. The complex is thought to be involved in double-strand DNA break repair. Subunits of the human complex include HTATIP/TIP60, TRRAP, RUVBL1, BUVBL2, beta-actin and BAF53/ACTL6A. In yeast, the complex has 13 subunits, including the catalytic subunit Esa1 (homologous to human Tip60).
The addition of a mannose residue to a protein acceptor molecule.
The transfer of mannose from dolichyl activated mannose to the hydroxyl group of a seryl or threonyl residue of a protein acceptor molecule, to form an O-linked protein-sugar linkage.
Progression of the endocrine system over time, from its formation to a mature structure. The endocrine system is a system of hormones and ductless glands, where the glands release hormones directly into the blood, lymph or other intercellular fluid, and the hormones circulate within the body to affect distant organs. The major glands that make up the human endocrine system are the hypothalamus, pituitary, thyroid, parathryoids, adrenals, pineal body, and the reproductive glands which include the ovaries and testes.
Progression of the ring gland over time, from its formation to a mature structure. The ring gland is a neuroendocrine organ found in higher Dipterans, which is composed of the prothoracic gland, the corpus allatum, and the corpora cardiacum. The ring gland is the site of production and release of ecdysteroids and juvenile hormones.
Progression of the exocrine system over time, from its formation to a mature structure. The exocrine system is a system of hormones and glands, where the glands secrete straight to a target site via ducts or tubes. The human exocrine system includes the salivary glands, sweat glands and many glands of the digestive system.
Interacting selectively and non-covalently with a phthalate, any ester or salt of phthalic acid.
Interacting selectively and non-covalently with diphenyl phthalate, C(20)H(14)O(4).
Interacting selectively and non-covalently with dibutyl phthalate, C(16)H(22)O(4).
Interacting selectively and non-covalently with dibutyl phthalate, C(16)H(22)O(4).
Interacting selectively and non-covalently with ethanol, CH(3)-CH(2)-OH.
The process in which the anatomical structures of a spiracle are generated and organized. Spiracles are the openings in the insect open tracheal system; externally they connect to the epidermis and internally they connect to the tracheal trunk.
The process in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs
The process in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs
The process in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs
The process in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs
The process in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs
The process in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs
The process in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs
The process in which microRNAs (miRNAs) direct the cleavage of target mRNAs. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA base pairing with near-perfect complementarity to the target mRNA will typically direct targeted endonucleolytic cleavage of the mRNA. Many plant miRNAs downregulate gene expression through this mechanism.
The process in which microRNAs (miRNAs) direct the cleavage of target mRNAs. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA base pairing with near-perfect complementarity to the target mRNA will typically direct targeted endonucleolytic cleavage of the mRNA. Many plant miRNAs downregulate gene expression through this mechanism.
The process in which microRNAs (miRNAs) direct the cleavage of target mRNAs. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA base pairing with near-perfect complementarity to the target mRNA will typically direct targeted endonucleolytic cleavage of the mRNA. Many plant miRNAs downregulate gene expression through this mechanism.
The transfer of a microRNA (miRNA) strand from a miRNA:miRNA duplex onto the RNA-initiated silencing complex (RISC).
The transfer of a microRNA (miRNA) strand from a miRNA:miRNA duplex onto the RNA-initiated silencing complex (RISC).
The transfer of a microRNA (miRNA) strand from a miRNA:miRNA duplex onto the RNA-initiated silencing complex (RISC).
The transfer of a microRNA (miRNA) strand from a miRNA:miRNA duplex onto the RNA-initiated silencing complex (RISC).
Transport of pre-microRNAs (pre-miRNAs) from the nucleus to the cytoplasm. Pre-miRNAs are a ~60-70 nucleotide stem loop intermediate in miRNA production, produced by the nuclear cleavage of a primary miRNA (pri-mRNA) transcript. Pre-miRNAs are transported from the nucleus to the cytoplasm where further cleavage occurs to produce a mature miRNA product.
Transport of pre-microRNAs (pre-miRNAs) from the nucleus to the cytoplasm. Pre-miRNAs are a ~60-70 nucleotide stem loop intermediate in miRNA production, produced by the nuclear cleavage of a primary miRNA (pri-mRNA) transcript. Pre-miRNAs are transported from the nucleus to the cytoplasm where further cleavage occurs to produce a mature miRNA product.
Transport of pre-microRNAs (pre-miRNAs) from the nucleus to the cytoplasm. Pre-miRNAs are a ~60-70 nucleotide stem loop intermediate in miRNA production, produced by the nuclear cleavage of a primary miRNA (pri-mRNA) transcript. Pre-miRNAs are transported from the nucleus to the cytoplasm where further cleavage occurs to produce a mature miRNA product.
Transport of pre-microRNAs (pre-miRNAs) from the nucleus to the cytoplasm. Pre-miRNAs are a ~60-70 nucleotide stem loop intermediate in miRNA production, produced by the nuclear cleavage of a primary miRNA (pri-mRNA) transcript. Pre-miRNAs are transported from the nucleus to the cytoplasm where further cleavage occurs to produce a mature miRNA product.
Transport of pre-microRNAs (pre-miRNAs) from the nucleus to the cytoplasm. Pre-miRNAs are a ~60-70 nucleotide stem loop intermediate in miRNA production, produced by the nuclear cleavage of a primary miRNA (pri-mRNA) transcript. Pre-miRNAs are transported from the nucleus to the cytoplasm where further cleavage occurs to produce a mature miRNA product.
The regionalization process that divides an organism or part of an organism into a series of semi-repetitive parts, or segments, often arranged along a longitudinal axis.
Division of the central nervous system into a series of semi-repetitive parts or segments.
Division of the brain into a series of semi-repetitive parts or segments.
Division of an appendage, an organ or part that is attached to the main body of an organism, into a series of semi-repetitive parts or segments. Most arthropod appendages, such as the legs and antennae, are visibly segmented.
Division of an imaginal disc-derived leg into a series of semi-repetitive parts or segments. The Drosophila leg, for example, has nine segments, each separated from the next by a flexible joint.
Partitioning the insect head anlage into a fixed number of segmental units. The number of segments composing the insect head has long been a subject of debate, but it is generally agreed that there are 6 or 7 segments. From anterior to posterior the head segments are the procephalic segments (labral, (ocular), antennal and intercalary) and the gnathal segments (mandibular, maxillary and labial).
Partitioning the insect head anlage into procephalic (labral, (ocular), antennal and intercalary) segments. The procephalic segments lie anterior to the gnathal (posterior head) segments, and are pattered by different segmentation gene cascades to the abdominal, thoracic and posterior head (gnathal) segments.
Partitioning the posterior region of the insect head anlage into gnathal (mandibular, maxillary and labial) segments. Unlike the anterior head (procephalic) segments, formation of the posterior head (gnathal) segments occurs by a similar mechanism to trunk segmentation, where a cascade of gap genes, pair-rule genes and segment-polarity genes subdivide the embryo into progressively smaller domains.
Partitioning of the blastoderm embryo into trunk segmental units. In Drosophila, the trunk segments include thoracic segments and abdominal segments A1 to A8.
The specification of the characteristic structures of the intercalary segment of the anterior head, following establishment of segment boundaries. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
The specification of the characteristic structures of trunk segments, following establishment of segment boundaries. In Drosophila, the trunk segments include thoracic segments and abdominal segments A1 to A8. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
The process that gives rise to the patterns of cell differentiation in the chitin-based larval cuticle. An example of this is found in Drosophila melanogaster.
Allocation of embryonic cells to the wing disc founder populations, groups of cells that are committed to contribute to the formation of a wing imaginal disc.
The process whose specific outcome is the progression of a tube over time, from its initial formation to a mature structure. Epithelial and endothelial tubes transport gases, liquids and cells from one site to another and form the basic structure of many organs and tissues including lung and trachea, kidney, the mammary gland, the vascular system and the gastrointestinal and urinary-genital tracts.
Any process that modulates the diameter of a tube.
Ensuring that the Malpighian tubule is the correct width. Malpighian tubules have a uniform circumference along their length; the circumference of the tubes is eight cells during the time the cells are dividing, after which the cells rearrange producting tubes with a cirumference of two cells.
Ensuring that a Malpighian tubule is the correct length and diameter.
Catalysis of the reaction: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,6-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
Catalysis of the reaction: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + 2 H(+).
A multiprotein complex that binds microtubules in a Hedgehog-dependent manner, and is required for signal transduction by members of the Hedgehog family of proteins. The core components of the complex are the serine/threonine protein kinase Fused, the kinesin motor protein Costal2 (Cos2), and a zinc finger transcription factor (Gli family members in humans, and Cubitus interruptus (Ci) in Drosophila).
A multiprotein complex that binds microtubules in a Hedgehog-dependent manner, and is required for signal transduction by members of the Hedgehog family of proteins. The core components of the complex are the serine/threonine protein kinase Fused, the kinesin motor protein Costal2 (Cos2), and a zinc finger transcription factor (Gli family members in humans, and Cubitus interruptus (Ci) in Drosophila).
Catalysis of the hydroxylation of an ecdysteroid at carbon position 25. Ecdysteroids are a group of polyhydroxylated ketosteroids which initiate post-embryonic development, particularly metamorphosis, in insects and other arthropods.
Any process that modulates the frequency, rate or extent of removal of phosphate groups from a molecule.
Any process that modulates the frequency, rate or extent of removal of phosphate groups from a protein.
Any process the stops, prevents, or reduces the frequency, rate or extent of removal of phosphate groups from a molecule.
Any process the stops, prevents, or reduces the frequency, rate or extent of removal of phosphate groups from a molecule.
Any process the stops, prevents, or reduces the frequency, rate or extent of removal of phosphate groups from a molecule.
Any process the stops, prevents, or reduces the frequency, rate or extent of removal of phosphate groups from a molecule.
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a molecule.
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a molecule.
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a molecule.
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a molecule.
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a molecule.
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a protein.
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a protein.
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a protein.
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a protein.
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a protein.
Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a protein.
Any process the stops, prevents, or reduces the frequency, rate or extent of removal of phosphate groups from a protein.
Any process the stops, prevents, or reduces the frequency, rate or extent of removal of phosphate groups from a protein.
Any process the stops, prevents, or reduces the frequency, rate or extent of removal of phosphate groups from a protein.
Any process the stops, prevents, or reduces the frequency, rate or extent of removal of phosphate groups from a protein.
Any process the stops, prevents, or reduces the frequency, rate or extent of removal of phosphate groups from a protein.
The regionalization process that subdivides the wing imaginal disc into the wing and notum (body wall) subfields, thus determining whether cells ultimately differentiate wing or notum-specific structures.
The process in which a cell in the larval wing imaginal disc becomes capable of differentiating autonomously into a notum cell, if left in its normal environment.
The process in which a cell in the larval wing imaginal disc becomes capable of differentiating autonomously into a wing cell, if left in its normal environment.
Catalysis of the sequential cleavage of mononucleotides from a free 5' terminus of a DNA molecule.
The migration of an epidermal cell along or through a wound gap that contributes to the reestablishment of a continuous epidermis.
Formation of hardened covering (a scab) at a wound site. The scab has multiple functions including limiting blood loss, providing structural stability to the wound and guarding against infection.
The process in which a relatively unspecialized cell acquires specialized features of a hair cell.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of non-sensory hairs. These hairs are polarized cellular extensions that cover much of the insect epidermis.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of non-sensory hairs. These hairs are polarized cellular extensions that cover much of the insect epidermis.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of non-sensory hairs. These hairs are polarized cellular extensions that cover much of the insect epidermis.
A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of an imaginal disc-derived wing hair. A wing hair is an actin-rich, polarized, non-sensory apical projection that protrudes from each of the approximately 30,000 wing epithelial cells. An example of this is found in Drosophila melanogaster.
A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of an imaginal disc-derived wing hair. A wing hair is an actin-rich, polarized, non-sensory apical projection that protrudes from each of the approximately 30,000 wing epithelial cells. An example of this is found in Drosophila melanogaster.
A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of an imaginal disc-derived wing hair. A wing hair is an actin-rich, polarized, non-sensory apical projection that protrudes from each of the approximately 30,000 wing epithelial cells. An example of this is found in Drosophila melanogaster.
A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of an imaginal disc-derived wing hair. A wing hair is an actin-rich, polarized, non-sensory apical projection that protrudes from each of the approximately 30,000 wing epithelial cells. An example of this is found in Drosophila melanogaster.
Extrusion of a cellular projection from the apical membrane of an epithelial cell in an imaginal disc-derived wing. Outgrowth initiates approximately 35 hours after puparium formation from the distal side of the cell, and at this stage the cellular extension is termed a prehair.
Extrusion of a cellular projection from the apical membrane of an epithelial cell in an imaginal disc-derived wing. Outgrowth initiates approximately 35 hours after puparium formation from the distal side of the cell, and at this stage the cellular extension is termed a prehair.
Growth of a prehair in the approximately 10 hour period following its emergence from an epidermal cell in an imaginal disc-derived wing. Prehair elongation is guided and/or driven by the polymerization of actin filaments and the orderly crosslinking of filaments into bundles.
Growth of a prehair in the approximately 10 hour period following its emergence from an epidermal cell in an imaginal disc-derived wing. Prehair elongation is guided and/or driven by the polymerization of actin filaments and the orderly crosslinking of filaments into bundles.
Determination of the site in the cell of an imaginal disc-derived wing at which a prehair initiates outgrowth. Restriction of prehair initiation to the distalmost part of a cell is essential to ensure that each wing epithelial cell produces one adult hair that points distally.
Determination of the site in the cell of an imaginal disc-derived wing at which a prehair initiates outgrowth. Restriction of prehair initiation to the distalmost part of a cell is essential to ensure that each wing epithelial cell produces one adult hair that points distally.
Ensuring that hairs in the imaginal disc-derived wing continue to point distally during development, following the initial establishment of wing hair polarity.