The orderly movement of a mesenchymal cell from one site to another that will contribute to the formation of a limb bud.
An intercellular bridge that connects the germline cells of a male cyst.
An intercellular bridge that connects the germline cells of a male cyst.
An intercellular bridge that connects the germline cells of a female cyst.
An intercellular bridge that connects the germline cells of a female cyst.
Interacting selectively and non-covalently with a Toll-like protein, a pattern recognition receptor that binds pattern motifs from a variety of microbial sources to initiate an innate immune response.
Interacting selectively and non-covalently with an enhancer, a transcription regulatory region that is somewhat distal from the core promoter and which enhances transcription from that promoter.
The ordered and organized complex of DNA and protein that forms regions of the chromosome that are being actively transcribed.
The ordered and organized complex of DNA and protein that forms regions of the chromosome that are not being actively transcribed.
The series of molecular signals mediated by the serine/threonine kinase Hippo or one of its orthologs. In Drosophila, Hippo in complex with the scaffold protein Salvador (Sav), phosphorylates and activates Warts (Wts), which in turn phosphorylates and inactivates the Yorkie (Yki) transcriptional activator. The core fly components hippo, sav, wts and mats are conserved in mammals as STK4/3 (MST1/2), SAV1/WW45, LATS1/2 and MOB1.
The series of molecular signals mediated by the serine/threonine kinase Hippo or one of its orthologs. In Drosophila, Hippo in complex with the scaffold protein Salvador (Sav), phosphorylates and activates Warts (Wts), which in turn phosphorylates and inactivates the Yorkie (Yki) transcriptional activator. The core fly components hippo, sav, wts and mats are conserved in mammals as STK4/3 (MST1/2), SAV1/WW45, LATS1/2 and MOB1.
The series of molecular signals mediated by the serine/threonine kinase Hippo or one of its orthologs. In Drosophila, Hippo in complex with the scaffold protein Salvador (Sav), phosphorylates and activates Warts (Wts), which in turn phosphorylates and inactivates the Yorkie (Yki) transcriptional activator. The core fly components hippo, sav, wts and mats are conserved in mammals as STK4/3 (MST1/2), SAV1/WW45, LATS1/2 and MOB1.
The series of molecular signals mediated by the serine/threonine kinase Hippo or one of its orthologs. In Drosophila, Hippo in complex with the scaffold protein Salvador (Sav), phosphorylates and activates Warts (Wts), which in turn phosphorylates and inactivates the Yorkie (Yki) transcriptional activator. The core fly components hippo, sav, wts and mats are conserved in mammals as STK4/3 (MST1/2), SAV1/WW45, LATS1/2 and MOB1.
The series of molecular signals mediated by the serine/threonine kinase Hippo or one of its orthologs. In Drosophila, Hippo in complex with the scaffold protein Salvador (Sav), phosphorylates and activates Warts (Wts), which in turn phosphorylates and inactivates the Yorkie (Yki) transcriptional activator. The core fly components hippo, sav, wts and mats are conserved in mammals as STK4/3 (MST1/2), SAV1/WW45, LATS1/2 and MOB1.
The series of molecular signals mediated by the serine/threonine kinase Hippo or one of its orthologs. In Drosophila, Hippo in complex with the scaffold protein Salvador (Sav), phosphorylates and activates Warts (Wts), which in turn phosphorylates and inactivates the Yorkie (Yki) transcriptional activator. The core fly components hippo, sav, wts and mats are conserved in mammals as STK4/3 (MST1/2), SAV1/WW45, LATS1/2 and MOB1.
Any process that modulates the frequency, rate or extent of hippo signaling.
Any process that modulates the frequency, rate or extent of hippo signaling.
Any process that modulates the frequency, rate or extent of hippo signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of hippo signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of hippo signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of hippo signaling.
Any process that activates or increases the frequency, rate or extent of hippo signaling.
Any process that activates or increases the frequency, rate or extent of hippo signaling.
Any process that activates or increases the frequency, rate or extent of hippo signaling.
The proteolytic cleavages to the Notch protein that occur as a result of ligand binding. Ligand binding at the cell surface exposes an otherwise inaccessible cleavage site in the extracellular portion of Notch, which when cleaved releases a membrane-tethered form of the Notch intracellular domain. Subsequent cleavage within the transmembrane domain then leads to the release of the soluble Notch intracellular domain (NICD).
The proteolytic cleavages to the Notch protein that occur as a result of ligand binding. Ligand binding at the cell surface exposes an otherwise inaccessible cleavage site in the extracellular portion of Notch, which when cleaved releases a membrane-tethered form of the Notch intracellular domain. Subsequent cleavage within the transmembrane domain then leads to the release of the soluble Notch intracellular domain (NICD).
The proteolytic cleavages to the Notch protein that occur prior to ligand binding. A primary cleavage event within the extracellular domain whilst the Notch protein in still in the secretory pathway, leads to the transportation of a processed heterodimer to the cell surface.
The removal of phosphoric residues from peptidyl-O-phospho-tyrosine to form peptidyl-tyrosine.
The chemical reactions and pathways involving long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more.
The chemical reactions and pathways involving long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more.
The chemical reactions and pathways involving a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty-acyl group.
The chemical reactions and pathways involving a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty-acyl group.
The chemical reactions and pathways resulting in the formation of a long-chain fatty-acyl-CoA any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more.
The chemical reactions and pathways resulting in the formation of a long-chain fatty-acyl-CoA any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more.
The chemical reactions and pathways resulting in the formation of a long-chain fatty-acyl-CoA any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more.
The chemical reactions and pathways resulting in the formation of a long-chain fatty-acyl-CoA any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more.
The chemical reactions and pathways resulting in the formation of a long-chain fatty-acyl-CoA any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more.
A multiprotein complex at least composed of serine palmitoyltransferases and ORM proteins (known as ORMDL proteins in mammals and other higher vertebrates) that plays a key role in sphingolipid homeostasis.
The directed movement of the purine ribonucleoside inosine, also known as hypoxanthine riboside, 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 inosine 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 inosine 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 inosine 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 hypoxanthine, 6-hydroxypurine, 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 hypoxanthine, 6-hydroxypurine, 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 hypoxanthine 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 hypoxanthine 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 hypoxanthine 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 acetyl-CoA is transported across a membrane. Acetyl-CoA is a derivative of coenzyme A in which the sulfhydryl group is acetylated; it is a metabolite derived from several pathways (e.g. glycolysis, fatty acid oxidation, amino-acid catabolism) and is further metabolized by the tricarboxylic acid cycle. It is a key intermediate in lipid and terpenoid biosynthesis.
The process in which coenzyme A is transported across a membrane. Coenzyme A, 3'-phosphoadenosine-(5')diphospho(4')pantatheine, is an acyl carrier in many acylation and acyl-transfer reactions in which the intermediate is a thiol ester.
The process in which flavin-adenine dinucleotide (FAD) is transported across a membrane. FAD forms the coenzyme of the prosthetic group of various flavoprotein oxidoreductase enzymes, in which it functions as an electron acceptor by being reversibly converted to its reduced form.
The process in which heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
The process in which a nicotinamide adenine dinucleotide is transported across a membrane; transport may be of either the oxidized form, NAD, or the reduced form, NADH.
The process in which nicotinamide mononucleotide is transported across a membrane. Nicotinamide mononucleotide is a ribonucleotide in which the nitrogenous base, nicotinamide, is in beta-n-glycosidic linkage with the c-1 position of d-ribose. It is a constituent of NAD and NADP.
A heterodimeric protein complex containing Toll-like receptor 1 (TLR1) and Toll-like receptor 2 (TLR2).
A heterodimeric protein complex containing Toll-like receptor 1 (TLR1) and Toll-like receptor 2 (TLR2).
A heterodimeric protein complex containing Toll-like receptor 1 (TLR1) and Toll-like receptor 2 (TLR2).
A heterodimeric protein complex containing Toll-like receptor 1 (TLR1) and Toll-like receptor 2 (TLR2).
A heterodimeric protein complex containing Toll-like receptor 1 (TLR1) and Toll-like receptor 2 (TLR2).
A heterodimeric protein complex containing Toll-like receptor 2 (TLR2) and Toll-like receptor 6 (TLR6).
A heterodimeric protein complex containing Toll-like receptor 2 (TLR2) and Toll-like receptor 6 (TLR6).
A heterodimeric protein complex containing Toll-like receptor 2 (TLR2) and Toll-like receptor 6 (TLR6).
A heterodimeric protein complex containing Toll-like receptor 2 (TLR2) and Toll-like receptor 6 (TLR6).
A heterodimeric protein complex containing Toll-like receptor 2 (TLR2) and Toll-like receptor 6 (TLR6).
Any process involved in the maintenance of an internal steady state of triglyceride within a cell or between a cell and its external environment.
The series of molecular signals initiated by binding of a ligand to any of the peroxisome proliferator activated receptors (alpha, beta or gamma) in the nuclear membrane, and ending with the initiation or termination of the transcription of target genes.
The series of molecular signals initiated by binding of a ligand to any of the peroxisome proliferator activated receptors (alpha, beta or gamma) in the nuclear membrane, and ending with the initiation or termination of the transcription of target genes.
The series of molecular signals initiated by binding of a ligand to any of the peroxisome proliferator activated receptors (alpha, beta or gamma) in the nuclear membrane, and ending with the initiation or termination of the transcription of target genes.
Any process that modulates the frequency, rate or extent of the peroxisome proliferator activated receptor signaling pathway.
Any process that modulates the frequency, rate or extent of the peroxisome proliferator activated receptor signaling pathway.
Any process that modulates the frequency, rate or extent of the peroxisome proliferator activated receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the peroxisome proliferator activated receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the peroxisome proliferator activated receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the peroxisome proliferator activated receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the peroxisome proliferator activated receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the peroxisome proliferator activated receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of the peroxisome proliferator activated receptor signaling pathway.
A ubiquitin ligase complex in which a cullin from the Cul8 subfamily and a RING domain protein form the catalytic core. In S. cerevisiae, Mms1p acts as the adaptor protein and substrate specificity is conferred by any of a number of different proteins.
The aggregation, arrangement and bonding together of proteins and DNA molecules to form a protein-DNA complex, in which the complex is formed through interaction of the protein(s) with a interferon-stimulated response element (ISRE) in the DNA.
A nuclear body associated with the histone gene locus that is thought to contain all of the factors necessary for histone mRNA transcription and pre-mRNA processing. In Drosophila, U7 snRNP is located in the histone locus body rather than the distinct Cajal body.
The directed movement of thymine, 5-methyluracil, 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 thymine, 5-methyluracil, 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 thymine, 5-methyluracil, 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 thymine, 5-methyluracil, 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 thymine, 5-methyluracil, 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 the selenocysteine insertion sequence (SECIS), a regulatory sequence within mRNA which directs incorporation of a selenocysteine at a stop codon (UGA) during translation.
An immunoglobulin-like complex that is present in at least the plasma membrane of pre-B cells, and that is composed of two identical immunoglobulin heavy chains and two surrogate light chains, each composed of the lambda-5 and VpreB proteins, and a signaling subunit, a heterodimer of the Ig-alpha and Ig-beta proteins.
A heterodimeric ubiquitin conjugating enzyme complex that catalyzes assembly of K63-linked polyubiquitin chains and is involved in NF-kappaB activation. In humans at least, the complex comprises the ubiquitin-conjugating enzyme UBC13 and ubiquitin-conjugating enzyme variant 1A (UEV1A).
The growing (plus) end of a microtubule. In vitro, microtubules polymerize more quickly at the plus end than at the minus end. In vivo, microtubule growth occurs only at the plus end, and the plus end switches between periods of growth and shortening, a behavior known as dynamic instability.
The growing (plus) end of a microtubule. In vitro, microtubules polymerize more quickly at the plus end than at the minus end. In vivo, microtubule growth occurs only at the plus end, and the plus end switches between periods of growth and shortening, a behavior known as dynamic instability.
A process in which a protein is transported to, or maintained at, a microtubule.
Interacting selectively and non-covalently with a chondroitin sulfate proteoglycan, any proteoglycan containing chondroitin sulfate as the glycosaminoglycan carbohydrate unit.
Interacting selectively and non-covalently with chondroitin sulfate, a glycosaminoglycan made up of two alternating monosaccharides: D-glucuronic acid (GlcA) and N-acetyl-D-galactosamine (GalNAc).
Interacting selectively and non-covalently with a zymogen, an enzymatically inactive precursor of an enzyme that is often convertible to an active enzyme by proteolysis.
The directed movement of a sterol into a cell or organelle. Sterols are steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule.
The directed movement of a sterol into a cell or organelle. Sterols are steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule.
The directed movement of water (H2O) from one side of an epithelium to the other.
The process in which carbon dioxide (CO2) is transported across a membrane.
Enables the transfer of carbon dioxide (CO2) from one side of a membrane to the other.
Catalysis of the reaction: (S)-3-hydroxyacyl-CoA + NAD(P)+ = 3-oxoacyl-CoA + NAD(P)H + H+, where the acyl group is a very long-chain fatty acid residue. A very long-chain fatty acid is a fatty acid which has a chain length greater than C22.
Enables the transmembrane transfer of an ion by a channel that opens when ATP has been bound by the channel complex or one of its constituent parts.
The process in which a sterol is transported across a membrane. Sterols are steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule.
The chemical reactions and pathways involving a thioester, a compound of general formula RC(=O)SR' in which the linking oxygen in an ester is replaced by a sulfur atom. They are the product of esterification between a carboxylic acid and a thiol.
The chemical reactions and pathways resulting in the formation of a thioester, a compound of general formula RC(=O)SR' in which the linking oxygen in an ester is replaced by a sulfur atom. They are the product of esterification between a carboxylic acid and a thiol.
The chemical reactions and pathways resulting in the formation of a thioester, a compound of general formula RC(=O)SR' in which the linking oxygen in an ester is replaced by a sulfur atom. They are the product of esterification between a carboxylic acid and a thiol.
The chemical reactions and pathways resulting in the formation of a thioester, a compound of general formula RC(=O)SR' in which the linking oxygen in an ester is replaced by a sulfur atom. They are the product of esterification between a carboxylic acid and a thiol.
The chemical reactions and pathways resulting in the formation of a thioester, a compound of general formula RC(=O)SR' in which the linking oxygen in an ester is replaced by a sulfur atom. They are the product of esterification between a carboxylic acid and a thiol.
A series of molecular signals initiated by the binding of a SLIT protein to a Roundabout (ROBO) family receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a SLIT protein to a Roundabout (ROBO) family receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a SLIT protein to a Roundabout (ROBO) family 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 Roundabout signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Roundabout signaling pathway.
Any process that activates or increases the frequency, rate or extent of the Roundabout signaling pathway.
The initial formation of a transcriptionally silent chromatin structure such as heterochromatin at silent mating-type loci.
The initial formation of a transcriptionally silent chromatin structure such as heterochromatin at the telomere.
The maintenance of chromatin in a transcriptionally silent state such as heterochromatin at silent mating-type loci.
The maintenance of chromatin in a transcriptionally silent state such as heterochromatin at the telomere.
The appearance of chemokine (C-X-C motif) ligand 9 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-X-C motif) ligand 9 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-X-C motif) ligand 9 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 chemokine (C-X-C motif) ligand 9.
Any process that modulates the frequency, rate, or extent of production of chemokine (C-X-C motif) ligand 9.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of chemokine (C-X-C motif) ligand 9.
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of chemokine (C-X-C motif) ligand 9.
Any process that activates or increases the frequency, rate, or extent of production of chemokine (C-X-C motif) ligand 9.
Any process that activates or increases the frequency, rate, or extent of production of chemokine (C-X-C motif) ligand 9.
Positive regulation of an adaptive immune response mediated via cytokine production by helper T cell.
Positive regulation of a T cell mediated immune response mediated via cytokine production by a helper T cell.
Positive regulation of a T cell mediated immune response mediated via cytokine production by a helper T cell.
Positive regulation of a B cell mediated immune response mediated via cytokine production by a helper T cell.
Positive regulation of a B cell mediated immune response mediated via cytokine production by a helper T cell.
Catalysis of the transfer of a phosphate group to a tyrosine 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 tyrosine-41 residue of histone H3.
Catalysis of the transfer of a phosphate group to the tyrosine-41 residue of histone H3.
Catalysis of the transfer of a phosphate group to the threonine-11 residue of the N-terminal tail of histone H3.
Catalysis of the transfer of a phosphate group to the threonine-11 residue of the N-terminal tail of histone H3.
Catalysis of the transfer of a phosphate group to the threonine-6 residue of the N-terminal tail of histone H3.
Catalysis of the transfer of a phosphate group to the threonine-6 residue of the N-terminal tail of histone H3.
The modification of histones by addition of a phosphate group to a serine residue.
The modification of histones by addition of a phosphate group to a threonine residue.
The modification of histones by addition of a phosphate group to a tyrosine residue.
The modification of histone H3 by the addition of an phosphate group to a threonine residue at position 11 of the histone.
The modification of histone H3 by the addition of an phosphate group to a threonine residue at position 6 of the histone.
The modification of histone H3 by the addition of a phosphate group to a tyrosine residue at position 41 of the histone.
Catalysis of the reaction: 5alpha-dihydrotestosterone + NAD+ = 5alpha-androstane-3,17-dione + NADH.
Any process in which a protein is transported to, and/or maintained at the synapse, the junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell.
Any process that initiates the activity of the inactive enzyme MAP kinase in the context of an innate immune response, a defense response mediated by germline encoded components that directly recognize components of potential pathogens.
A MAPK cascade that contributes to an innate immune response, a defense response mediated by germline encoded components that directly recognize components of potential pathogens.
Any process that initiates the activity of the inactive enzyme MAP kinase kinase in the context of an innate immune response, a defense response mediated by germline encoded components that directly recognize components of potential pathogens.
Any process that initiates the activity of the inactive enzyme MAP kinase kinase kinase in the context of an innate immune response, a defense response mediated by germline encoded components that directly recognize components of potential pathogens.
Any process that terminates the activity of the active enzyme MAP kinase in the context of an innate immune response, a defense response mediated by germline encoded components that directly recognize components of potential pathogens.
Signaling between cells of the same type. The signal produced by the signaling cell binds to a receptor on, and affects a cell of the same type.
Any process that mediates the transfer of information between the extracellular matrix and a cell.
Any process that mediates the transfer of information between the extracellular matrix and a cell.
The process in which gluconate is transported across a membrane. Gluconate is the aldonic acid derived from glucose.
The process in which gluconate is transported across a membrane. Gluconate is the aldonic acid derived from glucose.
The process in which gluconate is transported across a membrane. Gluconate is the aldonic acid derived from glucose.
Any process that modulates the frequency, rate or extent of the directed movement of a gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane 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 gluconate across a membrane by means of some agent such as a transporter or pore.
The process in which acetate is transported across a membrane. Acetate is the 2-carbon carboxylic acid ethanoic acid.
The directed movement of copper cation across a membrane.
The directed movement of copper cation across a membrane.
The directed movement of copper cation across a membrane.
The process in which a phosphate is transported across a membrane.
The process in which triose phosphate (glyceraldehyde 3-phosphate) is transported across a membrane. Glyceraldehyde 3-phosphate is any organic three carbon compound phosphate ester.
The process in which triose phosphate (glyceraldehyde 3-phosphate) is transported across a membrane. Glyceraldehyde 3-phosphate is any organic three carbon compound phosphate ester.
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum.
Interacting selectively and non-covalently with cyclic-di-GMP, cyclic dimeric guanosine monophosphate.
Interacting selectively and non-covalently with cyclic-di-GMP, cyclic dimeric guanosine monophosphate.
Interacting selectively and non-covalently with cyclic-di-GMP, cyclic dimeric guanosine monophosphate.
Catalysis of the reaction: geranylgeranyl diphosphate = halima-5(6),13-dien-15-yl diphosphate.
Catalysis of the reaction: geranylgeranyl diphosphate = halima-5(6),13-dien-15-yl diphosphate.
The chemical reactions and pathways resulting in the formation of tuberculosinol (halima-5,6,dien-15-ol), a secondary metabolite in Mycobacteria.
The chemical reactions and pathways resulting in the formation of tuberculosinol (halima-5,6,dien-15-ol), a secondary metabolite in Mycobacteria.
The chemical reactions and pathways resulting in the formation of tuberculosinol (halima-5,6,dien-15-ol), a secondary metabolite in Mycobacteria.
The orderly movement of a cell from one site to another that will contribute to the differentiation of an endothelial cell that will form de novo blood vessels and tubes.
The directed movement of a dipeptide across a membrane by means of some agent such as a transporter or pore. A dipeptide is a combination of two amino acids linked together by a peptide (-CO-NH-) bond.
The directed movement of a tripeptide across a membrane by means of some agent such as a transporter or pore. A tripeptide is a compound containing three amino acids linked together by peptide bonds.
The directed movement of nickel (Ni) cations across a membrane by means of some agent such as a transporter or pore.
The process in which borate is transported across a membrane. Borate is the anion (BO3)3-; boron is a group 13 element, with properties which are borderline between metals and non-metals.
The process in which borate is transported across a membrane. Borate is the anion (BO3)3-; boron is a group 13 element, with properties which are borderline between metals and non-metals.
Catalysis of the reaction: 1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + L-cysteine + ATP = 1-D-myo-inosityl-2-L-cysteinylamido-2-deoxy-alpha-D-glucopyranoside + AMP + diphosphate + 2 H+. 1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol is also known as glucosaminyl-inositol or GlcN-Ins, and 1-D-myo-inosityl-2-L-cysteinylamido-2-deoxy-alpha-D-glucopyranoside as desacetylmycothiol or Cys-GlcN-Ins.
Catalysis of the reaction: 1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + L-cysteine + ATP = 1-D-myo-inosityl-2-L-cysteinylamido-2-deoxy-alpha-D-glucopyranoside + AMP + diphosphate + 2 H+. 1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol is also known as glucosaminyl-inositol or GlcN-Ins, and 1-D-myo-inosityl-2-L-cysteinylamido-2-deoxy-alpha-D-glucopyranoside as desacetylmycothiol or Cys-GlcN-Ins.
Catalysis of the reaction: 1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol + L-cysteine + ATP = 1-D-myo-inosityl-2-L-cysteinylamido-2-deoxy-alpha-D-glucopyranoside + AMP + diphosphate + 2 H+. 1-(2-amino-2-deoxy-alpha-D-glucopyranoside)-1D-myo-inositol is also known as glucosaminyl-inositol or GlcN-Ins, and 1-D-myo-inosityl-2-L-cysteinylamido-2-deoxy-alpha-D-glucopyranoside as desacetylmycothiol or Cys-GlcN-Ins.
Catalysis of the reaction: 1-D-myo-inosityl-2-L-cysteinylamido-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = mycothiol + coenzyme A + H+. Mycothiol is also known as AcCys-GlcN-Ins and 1-D-myo-inosityl-2-L-cysteinylamido-2-deoxy-alpha-D-glucopyranoside as Cys-GlcN-Ins or desacetylmycothiol.
The component of a thylakoid 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 a thylakoid 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 a plastid thylakoid 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 a plastid thylakoid 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 a plastid thylakoid membrane consisting of gene products and protein complexes that are loosely bound to its lumenal surface, but not integrated into the hydrophobic region.
The component of a plastid thylakoid membrane consisting of gene products and protein complexes that are loosely bound to its lumenal surface, but not integrated into the hydrophobic region.
The component of a plastid thylakoid membrane consisting of gene products and protein complexes that are loosely bound to its lumenal surface, but not integrated into the hydrophobic region.
The component of a plastid thylakoid membrane consisting of gene products and protein complexes that are loosely bound to its stromal surface, but not integrated into the hydrophobic region.
The component of a plastid thylakoid membrane consisting of gene products and protein complexes that are loosely bound to its stromal surface, but not integrated into the hydrophobic region.
The component of a plastid thylakoid membrane consisting of gene products and protein complexes that are loosely bound to its stromal surface, but not integrated into the hydrophobic region.
The component of a plastid 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 a plastid 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 a plastid inner 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 a plastid inner 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 a plastid inner membrane consisting of gene products and protein complexes that are loosely bound to its stromal surface, but not integrated into the hydrophobic region.
The component of a plastid inner membrane consisting of gene products and protein complexes that are loosely bound to its stromal surface, but not integrated into the hydrophobic region.
The component of a plastid inner membrane consisting of gene products and protein complexes that are loosely bound to its stromal surface, but not integrated into the hydrophobic region.
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-alpha stimulus. Interferon-alpha is a type I 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-alpha stimulus. Interferon-alpha is a type I 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-alpha stimulus. Interferon-alpha is a type I 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-alpha stimulus. Interferon-alpha is a type I 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-alpha stimulus. Interferon-alpha is a type I 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-beta stimulus. Interferon-beta is a type I 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-beta stimulus. Interferon-beta is a type I 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-beta stimulus. Interferon-beta is a type I 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-beta stimulus. Interferon-beta is a type I interferon.
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 interferon-alpha stimulus. Interferon-alpha is a type I interferon.
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 interferon-alpha stimulus. Interferon-alpha is a type I interferon.
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 interferon-alpha stimulus. Interferon-alpha is a type I interferon.
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 interferon-alpha stimulus. Interferon-alpha is a type I interferon.
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 interferon-alpha stimulus. Interferon-alpha is a type I interferon.
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 interferon-beta stimulus. Interferon-beta is a type I interferon.
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 interferon-beta stimulus. Interferon-beta is a type I interferon.
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 interferon-beta stimulus. Interferon-beta is a type I interferon.
The formation of a macromolecular complex between the coat proteins and proteins and/or lipoproteins that are going to be transported by a vesicle.
Catalysis of the reaction: L-ascorbate 6-phosphate + H2O = 3-keto-L-gulonate 6-phosphate.
The process in which a vitamin is transported across a membrane. A vitamin is one of a number of unrelated organic substances that occur in many foods in small amounts and that are necessary in trace amounts for the normal metabolic functioning of the body.
The establishment of the diencephalon with respect to the left and right halves.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, which contributes to determination of organismal asymmetry with respect to the left and right halves.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, which contributes to determination of organismal asymmetry with respect to the left and right halves.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, which contributes to determination of organismal asymmetry with respect to the left and right halves.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, which contributes to determination of organismal asymmetry with respect to the left and right halves.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, which contributes to determination of organismal asymmetry with respect to the left and right halves.
Any process that modulates the frequency, rate or extent of activity of any TGF-beta receptor signaling pathway that is involved in the determination of organismal asymmetry with regard to its left and right halves.
Any process that modulates the frequency, rate or extent of activity of any TGF-beta receptor signaling pathway that is involved in the determination of organismal asymmetry with regard to its left and right halves.
Any process that modulates the frequency, rate or extent of activity of any TGF-beta receptor signaling pathway that is involved in the determination of organismal asymmetry with regard to its left and right halves.
Any process that modulates the frequency, rate or extent of activity of any TGF-beta receptor signaling pathway that is involved in the determination of organismal asymmetry with regard to its left and right halves.
Any process that modulates the frequency, rate or extent of activity of any TGF-beta receptor signaling pathway that is involved in the determination of organismal asymmetry with regard to its left and right halves.
Determination of the asymmetric location of the pancreas with respect to the left and right halves of the organism.
Any process that increases the rate, frequency, or extent of blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels and contribute to the series of events that restore integrity to damaged vasculature.
The series of molecular signals initiated by luteinizing hormone binding to a receptor, where the activated receptor signals via downstream effectors that contribute to progression of the ovarian follicle over time, from its formation to the mature structure.
Combining with the choriogonadotropin hormone to initiate a change in cell activity.
Combining with the choriogonadotropin hormone to initiate a change in cell activity.
Combining with the choriogonadotropin hormone to initiate a change in cell activity.
Interacting selectively and non-covalently with any lipase.
The segregation of angioblasts into discrete arterial and venous vessels from one common precursor vessel.
The directional migration of angioblast cells as part of selective angioblast sprouting, which results in angioblast segregation into arterial and venous populations.
The orderly movement of angioblasts, cells involved in blood vessel morphogenesis.
Any process that modulates the frequency, rate or extent of angioblast cell migration involved in selective angioblast sprouting.
Interacting selectively and non-covalently with a chylomicron, a large lipoprotein particle (diameter 75-1200 nm) composed of a central core of triglycerides and cholesterol surrounded by a protein-phospholipid coating. The proteins include one molecule of apolipoprotein B-48 and may include a variety of apolipoproteins, including APOAs, APOCs and APOE.
The directed movement of angioblasts from the lateral mesoderm to the midline which occurs as part of the formation of the early midline vasculature.
Any process that modulates the frequency, rate or extent of the series of molecular signals initiated by binding of an extracellular ligand to a Notch receptor on the surface of the target cell that contributes to heart induction.
Any process that activates or increases the frequency, rate or extent of the series of molecular signals initiated by binding of an extracellular ligand to a Notch receptor on the surface of the target cell that contributes to heart induction.
The spontaneous peristaltic movements of the stomach that aid in digestion, moving food through the stomach and out through the pyloric sphincter into the duodenum.
The process in which the liquid and liquid-suspended solid contents of the stomach exit through the pylorus into the duodenum.
Interacting selectively and non-covalently with double-stranded DNA containing an A/A mispair.
Interacting selectively and non-covalently with double-stranded DNA containing an A/G mispair.
Interacting selectively and non-covalently with double-stranded DNA containing an A/G mispair.
Interacting selectively and non-covalently with double-stranded DNA containing an A/G mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a C/C mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a T/T mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a C/T mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a C/T mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a C/T mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a G/G mispair.
Any process that modulates the rate, frequency or extent of the synthesis or release of any leukotriene following a stimulus as part of an inflammatory response.
Any process that increases the rate, frequency or extent of the synthesis or release of any leukotriene following a stimulus as part of an inflammatory response.
Any process that decreases the rate, frequency or extent of the synthesis or release of any leukotriene following a stimulus as part of an inflammatory response.
The aggregation, arrangement and bonding together of a set of components to form a SNARE complex, a protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers.
The disaggregation of the SNARE protein complex into its constituent components. The SNARE complex is a protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers.
Any process that modulates the frequency, rate or extent of disassembly of the SNARE complex. The SNARE complex is a protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers.
Catalysis of the reaction: UDP-galactose + lipopolysaccharide = UDP + 1,5 alpha-D-galactosyl-lipopolysaccharide.
Catalysis of the reaction: UDP-galactose + lipopolysaccharide = UDP + 1,5 alpha-D-galactosyl-lipopolysaccharide.
Interacting selectively and non-covalently with the cyclic AMP response element (CRE), a short palindrome-containing sequence found in the promoters of genes whose expression is regulated in response to cyclic AMP.
Interacting selectively and non-covalently with the cyclic AMP response element (CRE), a short palindrome-containing sequence found in the promoters of genes whose expression is regulated in response to cyclic AMP.
Interacting selectively and non-covalently with the cyclic AMP response element (CRE), a short palindrome-containing sequence found in the promoters of genes whose expression is regulated in response to cyclic AMP.
Interacting selectively and non-covalently with the cyclic AMP response element (CRE), a short palindrome-containing sequence found in the promoters of genes whose expression is regulated in response to cyclic AMP.
Interacting selectively and non-covalently with the cyclic AMP response element (CRE), a short palindrome-containing sequence found in the promoters of genes whose expression is regulated in response to cyclic AMP.
The chemical reactions and pathways involving the dipeptide beta-alanyl-L-histidine (carnosine).
The chemical reactions and pathways resulting in the formation of the dipeptide beta-alanyl-L-histidine (carnosine).
The chemical reactions and pathways resulting in the formation of the dipeptide beta-alanyl-L-histidine (carnosine).
The chemical reactions and pathways resulting in the formation of the dipeptide beta-alanyl-L-histidine (carnosine).
The chemical reactions and pathways resulting in the formation of the dipeptide beta-alanyl-L-histidine (carnosine).
Interacting selectively and non-covalently with the MH2 (MAD homology 2) domain of a protein. The MH2 domain is found at the carboxy terminus of MAD related proteins such as Smads. The MH2 domain mediates interaction with a wide variety of proteins and provides specificity and selectivity to Smad function and also is critical for mediating interactions in Smad oligomers.
Interacting selectively and non-covalently with the MH1 (MAD homology 1) domain of a protein. The MH1 domain is found at the amino terminus of MAD related proteins such as Smads and can mediate DNA binding in some proteins. Smads also use the MH1 domain to interact with some transcription factors.
The development of the portion of the ureteric bud tube that contributes to the morphogenesis of the metanephros.
The development of the portion of the ureteric bud that contributes to the morphogenesis of the ureter. The ureter ureteric bud is the initial structure that forms the ureter.
Any process that modulates the frequency, rate or extent of myosin light chain kinase activity.
Any process that activates or increases the frequency, rate or extent of myosin light chain kinase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of myosin light chain kinase activity.
Any process that modulates the frequency, rate or extent of myosin-light-chain-phosphatase activity.
Any process that activates or increases the frequency, rate or extent of myosin-light-chain-phosphatase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of myosin-light-chain-phosphatase activity.
The removal of an alkyl group from one or more nucleotides within an DNA molecule.
Removal of the methyl group from one or more nucleotides within a DNA molecule involving the oxidation (i.e. electron loss) of one or more atoms.
The hydrolytic removal of the methyl group from one or more nucleotides within a DNA molecule.
The removal of the methyl group from one or more nucleotides within an RNA molecule involving oxidation (i.e. electron loss) of one or more atoms.
Catalysis of the removal of a methyl group from one or more nucleosides within a DNA molecule.
Catalysis of the removal of a methyl group from one or more nucleosides within a RNA molecule involving the oxidation (i.e. electron loss) of one or more atoms.
Catalysis of the removal of the methyl group from one or more nucleotides within a DNA molecule involving the oxidation (i.e. electron loss) of one or more atoms.
A multimeric protein complex that removes monoubiquitin from histone H2A. In Drosophila and mammals, the core of the complex is composed of Calypso/BAP1 and Asx/ASXL1, respectively.
The modification of histone H2A by addition of a single ubiquitin group.
A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 29 of the ubiquitin monomers, is added to a protein. K29-linked ubiquitination targets the substrate protein for degradation.
The removal of the ubiquitin group from a monoubiquitinated protein.
The removal of the ubiquitin group from a monoubiquitinated protein.
The removal of the ubiquitin group from a monoubiquitinated histone protein.
The removal of the ubiquitin group from a monoubiquitinated histone protein.
The removal of the ubiquitin group from a monoubiquitinated histone H2A protein.
The removal of the ubiquitin group from a monoubiquitinated histone H2A protein.
A protein deubiquitination process in which a K29-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 29 of the ubiquitin monomers, is removed from a protein.
A protein deubiquitination process in which a K29-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 29 of the ubiquitin monomers, is removed from a protein.
The directed movement of proline, pyrrolidine-2-carboxylic acid, across a membrane by means of some agent such as a transporter or pore.
A heterodimer of NF-kappa B p50 and p65 subunits.
A heterodimer of NF-kappa B p50 and p65 subunits.
A heterodimer of NF-kappa B p50 and p65 subunits.
A heterodimer of NF-kappa B p50 and p65 subunits.
A heterodimer of NF-kappa B p50 and p65 subunits.
The directed movement of substances from the plasma membrane back to the trans-Golgi network, mediated by vesicles.
Catalysis of the reaction: 3-hydroxypropanoate + NADP+ = 3-oxopropanoate + H+ + NADPH.
Catalysis of the reaction: 3-hydroxypropanoate + NADP+ = 3-oxopropanoate + H+ + NADPH.
Catalysis of the reaction: 3-hydroxypropanoate + NADP+ = 3-oxopropanoate + H+ + NADPH.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine in glycosidic linkage with uridine diphosphate, that contribute to the biosynthesis of chitin.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine in glycosidic linkage with uridine diphosphate, that contribute to the biosynthesis of chitin.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine in glycosidic linkage with uridine diphosphate, that contribute to the biosynthesis of chitin.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine in glycosidic linkage with uridine diphosphate, that contribute to the biosynthesis of chitin.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine in glycosidic linkage with uridine diphosphate, that contribute to the biosynthesis of chitin.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine in glycosidic linkage with uridine diphosphate, that contribute to the biosynthesis of chitin.
The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine in glycosidic linkage with uridine diphosphate, that contribute to the biosynthesis of chitin.
Catalysis of the reaction: NADH + H2O = AMP + NMNH + 2 H+.
Catalysis of the reaction: NADH + H2O = AMP + NMNH + 2 H+.
The appearance of chemokine (C-C motif) ligand 6 (CCL6) 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 chemokine (C-C motif) ligand 6 (CCL6).
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of chemokine (C-C motif) ligand 6 (CCL6).
Any process that activates or increases the frequency, rate, or extent of production of chemokine (C-C motif) ligand 6 (CCL6).
The regulated release of chemokine (C-C motif) ligand 6 (CCL6) from a cell.
Any process that modulates the rate, frequency or extent of the regulated release of chemokine (C-C motif) ligand 6 (CCL6) from a cell.
Any process that stops, prevents, or reduces the frequency, rate, or extent of the regulated release of chemokine (C-C motif) ligand 6 (CCL6) from a cell.
Any process that activates or increases the frequency, rate, or extent of the regulated release of chemokine (C-C motif) ligand 6 (CCL6) from a cell.
Interacting selectively and non-covalently with the carbohydrate response element (ChoRE) found in the promoters of genes whose expression is regulated in response to carbohydrates, such as the triglyceride synthesis genes.
Catalysis of the reaction: 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate + H2O = 8-oxo-7,8-dihydrodeoxyguanosine phosphate + diphosphate. 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate, or 8-oxo-dGTP, is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for DNA synthesis causing transversion mutations. 8-oxo-dGTPase hydrolyses 8-oxo-dGTP to its monophosphate form to prevent the misincorporation of 8-oxo-dGTP into cellular DNA.
Catalysis of the reaction: 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate + H2O = 8-oxo-7,8-dihydrodeoxyguanosine phosphate + diphosphate. 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate, or 8-oxo-dGTP, is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for DNA synthesis causing transversion mutations. 8-oxo-dGTPase hydrolyses 8-oxo-dGTP to its monophosphate form to prevent the misincorporation of 8-oxo-dGTP into cellular DNA.
Catalysis of the reaction: 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate + H2O = 8-oxo-7,8-dihydrodeoxyguanosine phosphate + diphosphate. 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate, or 8-oxo-dGTP, is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for DNA synthesis causing transversion mutations. 8-oxo-dGTPase hydrolyses 8-oxo-dGTP to its monophosphate form to prevent the misincorporation of 8-oxo-dGTP into cellular DNA.
Catalysis of the reaction: 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate + H2O = 8-oxo-7,8-dihydrodeoxyguanosine phosphate + diphosphate. 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate, or 8-oxo-dGTP, is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for DNA synthesis causing transversion mutations. 8-oxo-dGTPase hydrolyses 8-oxo-dGTP to its monophosphate form to prevent the misincorporation of 8-oxo-dGTP into cellular DNA.
Catalysis of the reaction: 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate + H2O = 8-oxo-7,8-dihydrodeoxyguanosine phosphate + diphosphate. 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate, or 8-oxo-dGTP, is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for DNA synthesis causing transversion mutations. 8-oxo-dGTPase hydrolyses 8-oxo-dGTP to its monophosphate form to prevent the misincorporation of 8-oxo-dGTP into cellular DNA.
Any process that increases the frequency, rate or extent of disassembly of the SNARE complex. The SNARE complex is a protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers.
Any process that decreases the frequency, rate or extent of disassembly of the SNARE complex. The SNARE complex is a protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers.
Any process that modulates the frequency, rate or extent of assembly of the SNARE complex. The SNARE complex is a protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers.
Any process that increases the frequency, rate or extent of assembly of the SNARE complex. The SNARE complex is a protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers.
Any process that decreases the frequency, rate or extent of assembly of the SNARE complex. The SNARE complex is a protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers.
The establishment of the nervous system with respect to the left and right halves.
The regulated release of interferon-beta from a cell.
The regulated release of interferon-beta from a cell.
Any process that modulates the frequency, rate, or extent of interferon-beta secretion.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta secretion.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta secretion.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta secretion.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta secretion.
Any process that stops, prevents, or reduces the frequency, rate, or extent of interferon-beta secretion.
Any process that activates or increases the frequency, rate, or extent of interferon-beta secretion.
Any process that activates or increases the frequency, rate, or extent of interferon-beta secretion.
Any process that activates or increases the frequency, rate, or extent of interferon-beta secretion.
Any process that activates or increases the frequency, rate, or extent of interferon-beta secretion.
Any process that activates or increases the frequency, rate, or extent of interferon-beta secretion.
Any process that activates or increases the frequency, rate, or extent of interferon-beta secretion.
A multiprotein nickel-containing complex that possesses urease activity (catalysis of the hydrolysis of urea to ammonia and carbon dioxide).
Removal of the initiating methionine or formylmethionine residue from a protein that contributes to protein maturation, the attainment of the full functional capacity of a protein.
Removal of the methyl group from one or more nucleotides within a single-stranded DNA molecule involving the oxidation (i.e. electron loss) of one or more atoms.
Removal of the methyl group from one or more nucleotides within a single-stranded RNA molecule involving the oxidation (i.e. electron loss) of one or more atoms.
The signaling process in which signaling from the receptor ROBO is brought to an end, rather than being reversibly modulated.
Interacting selectively and non-covalently with the Roundabout (ROBO) receptor, a transmembrane receptor.
The series of molecular signals generated as a consequence of the insulin receptor binding to its physiological ligand, where the signal is passed on via the phosphatidylinositol 3-kinase cascade.
The series of molecular signals generated as a consequence of the insulin receptor binding to its physiological ligand, where the signal is passed on via the phosphatidylinositol 3-kinase cascade.
The series of molecular signals generated as a consequence of the insulin receptor binding to its physiological ligand, where the signal is passed on via the phosphatidylinositol 3-kinase cascade.
The series of molecular signals generated as a consequence of the insulin receptor binding to its physiological ligand, where the signal is passed on via the phosphatidylinositol 3-kinase cascade.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to one of its physiological ligands, where the signal is passed on via the MAPKKK cascade.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to one of its physiological ligands, where the signal is passed on via the MAPKKK cascade.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to one of its physiological ligands, where the signal is passed on via the MAPKKK cascade.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to one of its physiological ligands, where the signal is passed on via the MAPKKK cascade.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to one of its physiological ligands, where the signal is passed on via the MAPKKK cascade.
Catalysis of the reaction: pheophorbide a + H2O = pyropheophorbide a + methanol + CO2. The reaction occurs in two steps; pheophoridase catalyzes the conversion of pheophorbide a to a precursor of pyropheophorbide a, C-13(2)-carboxylpyropheophorbide a, by demethylation, and then the precursor is decarboxylated non-enzymatically to yield pyropheophorbide a.
Catalysis of the reaction: pheophorbide a + H2O = pyropheophorbide a + methanol + CO2. The reaction occurs in two steps; pheophoridase catalyzes the conversion of pheophorbide a to a precursor of pyropheophorbide a, C-13(2)-carboxylpyropheophorbide a, by demethylation, and then the precursor is decarboxylated non-enzymatically to yield pyropheophorbide a.
Any process that modulates the frequency, rate or extent of chromatin binding. Chromatin binding is the selective interaction with chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
Any process that stops or reduces the frequency, rate or extent of chromatin binding. Chromatin binding is the selective interaction with chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
Any process that increases the frequency, rate or extent of chromatin binding. Chromatin binding is the selective interaction with chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
Any process that modulates the size of a kidney.
Any process that modulates the size of a pronephric kidney.
Any process that modulates the size of a metanephric kidney.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via effectors other than beta-catenin.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via effectors other than beta-catenin.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via effectors other than beta-catenin.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via effectors other than beta-catenin.
The methylation of the N-terminal proline of proteins.
The methylation of the N-terminal serine of proteins.
The monomethylation of the N-terminal serine of proteins to form the derivative N-methylserine.
The dimethylation of the N-terminal serine of proteins to form the derivative N,N-dimethylserine.
The trimethylation of the N-terminal serine of proteins to form the derivative N,N,N-trimethylserine.
The modification of histone H4 by the removal of a methyl group from lysine at position 20 of the histone.
Catalysis of the reaction: histone H4 N6-methyl-L-lysine (position 20) + 2-oxoglutarate + O2 = histone H4 L-lysine (position 20) + succinate + formaldehyde + CO2. This reaction is the removal of a methyl group from lysine at position 20 of the histone H4 protein.
The series of molecular signals generated as a consequence of a retinoic acid receptor binding to one of its physiological ligands that results in regions of the embryo being delineated into the area in which the pronephric kidney will develop.
The lipid bilayer surrounding an azurophil granule, a primary lysosomal granule found in neutrophil granulocytes that contains a wide range of hydrolytic enzymes and is released into the extracellular fluid.
The volume enclosed by the membrane of an azurophil granule, a primary lysosomal granule found in neutrophil granulocytes that contains a wide range of hydrolytic enzymes and is released into the extracellular fluid.
The lipid bilayer surrounding a specific granule, a granule with a membranous, tubular internal structure, found primarily in mature neutrophil cells. Most are released into the extracellular fluid. Specific granules contain lactoferrin, lysozyme, vitamin B12 binding protein and elastase.
The volume enclosed by the membrane of a specific granule, a granule with a membranous, tubular internal structure, found primarily in mature neutrophil cells. Most are released into the extracellular fluid. Specific granules contain lactoferrin, lysozyme, vitamin B12 binding protein and elastase.
The process of binding or confining an extracellular signaling ligand, such that the ligand is unable to bind to its cell surface receptor.
The process of binding or confining an extracellular signaling ligand, such that the ligand is unable to bind to its cell surface receptor.
Confining a bone morphogenetic protein (BMP) to the extracellular matrix (ECM), such that it is separated from other components of the signaling pathway, including its cell surface receptor. Bone morphogenetic proteins (BMPs) are secreted as homodimers, non-covalently associated with N-terminal pro-peptides, and are targeted to the extracellular matrix through interaction with matrix proteins.
Confining a bone morphogenetic protein (BMP) to the extracellular matrix (ECM), such that it is separated from other components of the signaling pathway, including its cell surface receptor. Bone morphogenetic proteins (BMPs) are secreted as homodimers, non-covalently associated with N-terminal pro-peptides, and are targeted to the extracellular matrix through interaction with matrix proteins.
Confining a bone morphogenetic protein (BMP) to the extracellular matrix (ECM), such that it is separated from other components of the signaling pathway, including its cell surface receptor. Bone morphogenetic proteins (BMPs) are secreted as homodimers, non-covalently associated with N-terminal pro-peptides, and are targeted to the extracellular matrix through interaction with matrix proteins.
Confining a bone morphogenetic protein (BMP) to the extracellular matrix (ECM), such that it is separated from other components of the signaling pathway, including its cell surface receptor. Bone morphogenetic proteins (BMPs) are secreted as homodimers, non-covalently associated with N-terminal pro-peptides, and are targeted to the extracellular matrix through interaction with matrix proteins.
Confining TGFbeta to the extracellular matrix (ECM) such that it is separated from other components of the signaling pathway, including its cell surface receptor. TGFbeta is secreted as part of a latent complex that is targeted to the extracellular matrix through latent-TGFbeta-binding protein (LTBP)-mediated association with matrix proteins.
Confining TGFbeta to the extracellular matrix (ECM) such that it is separated from other components of the signaling pathway, including its cell surface receptor. TGFbeta is secreted as part of a latent complex that is targeted to the extracellular matrix through latent-TGFbeta-binding protein (LTBP)-mediated association with matrix proteins.
Confining TGFbeta to the extracellular matrix (ECM) such that it is separated from other components of the signaling pathway, including its cell surface receptor. TGFbeta is secreted as part of a latent complex that is targeted to the extracellular matrix through latent-TGFbeta-binding protein (LTBP)-mediated association with matrix proteins.
Confining TGFbeta to the extracellular matrix (ECM) such that it is separated from other components of the signaling pathway, including its cell surface receptor. TGFbeta is secreted as part of a latent complex that is targeted to the extracellular matrix through latent-TGFbeta-binding protein (LTBP)-mediated association with matrix proteins.
A series of molecular signals in which a cell uses calcium ions released from an intracellular store to convert a signal into a response.
A series of molecular signals in which a cell uses calcium ions released from an intracellular store to convert a signal into a response.
A series of molecular signals in which a cell uses calcium ions released from an intracellular store to convert a signal into a response.
A series of molecular signals in which a cell uses calcium ions imported from an extracellular source to convert a signal into a response.
A series of molecular signals in which a cell uses calcium ions imported from an extracellular source to convert a signal into a response.
A series of molecular signals in which a cell uses calcium ions imported from an extracellular source to convert a signal into a response.
A series of molecular signals in which a cell uses calcium ions imported from an extracellular source to convert a signal into a response.
Combining with a purine or purine derivative (purine nucleoside or purine nucleotide) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. A nucleotide is a compound that consists of a nucleoside esterified with a phosphate molecule.
Combining with a purine or purine derivative (purine nucleoside or purine nucleotide) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. A nucleotide is a compound that consists of a nucleoside esterified with a phosphate molecule.
The series of molecular signals generated as a consequence of a receptor binding to an extracellular purine or purine derivative to initiate a change in cell activity.
The series of molecular signals generated as a consequence of a receptor binding to an extracellular purine or purine derivative to initiate a change in cell activity.
The series of molecular signals generated as a consequence of a receptor binding to an extracellular purine or purine derivative and transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity.
The series of molecular signals generated as a consequence of a receptor binding to an extracellular purine or purine derivative and transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity.
The series of molecular signals generated as a consequence of a receptor binding to an extracellular purine nucleotide and transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity.
The series of molecular signals generated as a consequence of a receptor binding to an extracellular purine nucleotide and transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity.
The series of molecular signals generated as a consequence of a receptor binding to an extracellular purine nucleotide and transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity.
The series of molecular signals generated as a consequence of a receptor binding to an extracellular purine nucleotide to initiate a change in cell activity.
The series of molecular signals generated as a consequence of a receptor binding to an extracellular purine nucleotide to initiate a change in cell activity.
The binding activity of a molecule that brings together two or more molecules in a signaling pathway, permitting those molecules to function in a coordinated way. Adaptor molecules themselves do not have catalytic activity.
The directed movement of a protein to a specific location within the extracellular region.
The directed movement of a protein to a specific location within the extracellular region.
Any process that activates or increases the frequency, rate or extent of the Wnt signaling pathway by the directed movement of a Wnt protein within the extracellular region.
Any process that activates or increases the frequency, rate or extent of the Wnt signaling pathway by the directed movement of a Wnt protein within the extracellular region.
Any process that activates or increases the frequency, rate or extent of the Wnt signaling pathway by the directed movement of a Wnt protein within the extracellular region.
Any process that activates or increases the frequency, rate or extent of the Wnt signaling pathway by the directed movement of a Wnt protein within the extracellular region.
Any process that activates or increases the frequency, rate or extent of the Wnt signaling pathway by the directed movement of a Wnt protein within the extracellular region.
Any process that activates or increases the frequency, rate or extent of the Wnt signaling pathway by the directed movement of a Wnt protein within the extracellular region.
Any process that activates or increases the frequency, rate or extent of the Wnt signaling pathway by the directed movement of a Wnt protein within the extracellular region.
Interacting selectively and non-covalently with a ganglioside, a ceramide oligosaccharide carrying in addition to other sugar residues, one or more sialic acid residues.
Catalysis of the reaction: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate. This reaction is the hydrolysis of an acetyl group from N-acetylglucosaminylinositol.
Catalysis of the reaction: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate. This reaction is the hydrolysis of an acetyl group from N-acetylglucosaminylinositol.
Catalysis of the reaction: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate. This reaction is the hydrolysis of an acetyl group from N-acetylglucosaminylinositol.
Catalysis of the reaction: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + acetate. This reaction is the hydrolysis of an acetyl group from N-acetylglucosaminylinositol.
Catalysis of the addition of a methylthioether group (-SCH3) to a nucleic acid or protein acceptor.
Catalysis of the methylthiolation (-SCH3 addition) at the C2 of the adenosine ring of N6-isopentenyladenosine (i6A) in tRNA, to form 2-methylthio-N6-isopentenyladenosine (ms2i6A).
Catalysis of the methylthiolation (-SCH3 addition) at the C2 of the adenosine ring of N6-threonylcarbomyladenosine (t6A) in tRNA, to form 2-methylthio-N6-threonylcarbamoyladenosine (ms2t6A).
Catalysis of the methylthiolation (-SCH3 addition) of the beta-carbon of peptidyl-aspartic acid to form peptidyl-L-beta-methylthioaspartic acid.
The addition of a methylthioether group (-SCH3) to a nucleotide in a tRNA molecule.
The removal of an acyl group, any group or radical of the form RCO- where R is an organic group, from a protein amino acid.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands, which stops, prevents, or reduces the frequency, rate or extent of the occurrence or rate of cell death by apoptotic process in the bone marrow.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands, which stops, prevents, or reduces the frequency, rate or extent of the occurrence or rate of cell death by apoptotic process in the bone marrow.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands, which stops, prevents, or reduces the frequency, rate or extent of the occurrence or rate of cell death by apoptotic process in the bone marrow.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands, which stops, prevents, or reduces the frequency, rate or extent of the occurrence or rate of cell death by apoptotic process in the bone marrow.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands, which contributes to hemopoiesis.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands, which contributes to hemopoiesis.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands, which contributes to hemopoiesis.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands, which contributes to hemopoiesis.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands, which activates or increases the frequency, rate or extent of cell proliferation in the bone marrow.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands, which activates or increases the frequency, rate or extent of cell proliferation in the bone marrow.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands, which activates or increases the frequency, rate or extent of cell proliferation in the bone marrow.
Catalysis of the transfer of a nitric oxide (NO) group to a sulphur atom within a cysteine residue of a protein.
Catalysis of the transfer of a nitric oxide (NO) group to a sulphur atom within a cysteine residue of a protein.
Transfer of a nitric oxide (NO) group from one cysteine residue to another.
Transfer of a nitric oxide (NO) group from one cysteine residue to another.
Transfer of a nitric oxide (NO) group from one cysteine residue to another.
Transfer of a nitric oxide (NO) group from one cysteine residue to another.
The series of molecular signals generated as a consequence of a fibroblast growth factor-type receptor binding to one of its physiological ligands, which contributes to the progression of the orbitofrontal cortex over time from its initial formation until its mature state.
The series of molecular signals generated as a consequence of a fibroblast growth factor-type receptor binding to one of its physiological ligands, which contributes to the progression of the orbitofrontal cortex over time from its initial formation until its mature state.
The series of molecular signals generated as a consequence of a fibroblast growth factor-type receptor binding to one of its physiological ligands, which contributes to the progression of the orbitofrontal cortex over time from its initial formation until its mature state.
The removal of a glutamate residue from a protein. Glutamate residues in proteins can be gene-encoded, or added as side chains during the protein modification process of polyglutamylation.
The removal of a C-terminal, gene-encoded glutamate residue from a protein.
The removal of a glutamate residue from the side chain of a protein. Glutamate side chains are added to glutamic acid residues within the primary protein sequence during polyglutamylation.
The removal of a glutamate residue from the side chain of a protein. Glutamate side chains are added to glutamic acid residues within the primary protein sequence during polyglutamylation.
The removal of a branching point glutamate residue. A branching point glutamate connects a glutamate side chain to a gene-encoded glutamate residue.
Interacting selectively and non-covalently with the AP-2 adaptor complex. The AP-2 adaptor complex is a heterotetrameric AP-type membrane coat adaptor complex that consists of alpha, beta2, mu2 and sigma2 subunits and links clathrin to the membrane surface of a vesicle. In at least humans, the AP-2 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different alpha genes (alphaA and alphaC).
Interacting selectively and non-covalently with a stem-loop in an RNA molecule. An RNA stem-loop is a secondary RNA structure consisting of a double-stranded RNA (dsRNA) stem and a terminal loop.
Interacting selectively and non-covalently with a stem-loop in an RNA molecule. An RNA stem-loop is a secondary RNA structure consisting of a double-stranded RNA (dsRNA) stem and a terminal loop.
Interacting selectively and non-covalently with a stem-loop in a small nuclear RNA (snRNA). An RNA stem-loop is a secondary RNA structure consisting of a double-stranded RNA (dsRNA) stem and a terminal loop.
Interacting selectively and non-covalently with a stem-loop in a small nuclear RNA (snRNA). An RNA stem-loop is a secondary RNA structure consisting of a double-stranded RNA (dsRNA) stem and a terminal loop.
Interacting selectively and non-covalently with a stem-loop in a small nuclear RNA (snRNA). An RNA stem-loop is a secondary RNA structure consisting of a double-stranded RNA (dsRNA) stem and a terminal loop.
The binding activity of a molecule that brings together clathrin and one or more other molecules, permitting them to function in a coordinated way.
A histone deubiquitination process in which a ubiquitin monomer is removed from a conserved lysine residue in the C-terminus of histone H2B. The conserved lysine residue is K119 in fission yeast, K123 in budding yeast, or K120 in mammals.
A histone deubiquitination process in which a ubiquitin monomer is removed from a conserved lysine residue in the C-terminus of histone H2B. The conserved lysine residue is K119 in fission yeast, K123 in budding yeast, or K120 in mammals.
A histone deubiquitination process in which a ubiquitin monomer is removed from a conserved lysine residue in the C-terminus of histone H2B. The conserved lysine residue is K119 in fission yeast, K123 in budding yeast, or K120 in mammals.
The disaggregation of a stress granule into its constituent protein and RNA parts.
A long, thin projection from a root epidermal cell that contains F-actin and tubulin, and a cell wall.
The tip portion of an outgrowth of a root epidermal cell.
Enables the directed movement of ceramides into, out of or within a cell, or between cells. Ceramides are a class of lipid composed of sphingosine linked to a fatty acid.
The directed movement of a ceramide from the endoplasmic reticulum (ER) to the Golgi. Ceramides are a class of lipid composed of sphingosine linked to a fatty acid.
The directed movement of a ceramide from the endoplasmic reticulum (ER) to the Golgi. Ceramides are a class of lipid composed of sphingosine linked to a fatty acid.
The directed movement of a ceramide from the endoplasmic reticulum (ER) to the Golgi. Ceramides are a class of lipid composed of sphingosine linked to a fatty acid.
The progression of the intrahepatic bile ducts over time, from their formation to the mature structure. Intrahepatic bile ducts (bile ducts within the liver) collect bile from bile canaliculi in the liver, and connect to the extrahepatic bile ducts (bile ducts outside the liver).
The progression of the intrahepatic bile ducts over time, from their formation to the mature structure. Intrahepatic bile ducts (bile ducts within the liver) collect bile from bile canaliculi in the liver, and connect to the extrahepatic bile ducts (bile ducts outside the liver).
A renal system process in which glucose is taken up from the collecting ducts and proximal and distal loops of the nephron. In non-mammalian species, absorption may occur in related structures.
A renal system process in which glucose is taken up from the collecting ducts and proximal and distal loops of the nephron. In non-mammalian species, absorption may occur in related structures.
The process in which a receptor is activated by another receptor. Receptor transactivation can occur through different mechanisms and includes cross-talk between signaling pathways where one receptor activates a receptor for a different ligand, and also activation of subunits within a receptor oligomer.
A series of molecular signals initiated by the binding of juvenile hormone to a receptor, and ending with regulation of cell state or activity.
A series of molecular signals initiated by the binding of juvenile hormone to a receptor, and ending with regulation of cell state or activity.
The directed movement of ceramides into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Ceramides are a class of lipid composed of sphingosine linked to a fatty acid.
The progression of the cystic duct over time, from its formation to the mature structure. The cystic duct runs from the gall bladder to the common bile duct.
The deposition of hydroxyapatite, involved in the progression of the skeleton from its formation to its mature state.
A protein complex that contains at least CD40 (a cell surface receptor of the tumour necrosis factor receptor (TNFR) superfamily), and other signaling molecules.
A complex composed of two proteins, prohibitin 1 and prohibitin 2 (PHB1/PHB-1 and PHB2/PHB-2) that is highly conserved amongst eukaryotes and associated with the inner mitochondrial membrane. The mitochondrial prohibitin complex is a macromolecular supercomplex composed of repeating heterodimeric subunits of PHB1 and PHB2. The mitochondrial prohibitin complex plays a role in a number of biological processes, including mitochondrial biogenesis and function, development, replicative senescence, and cell death.
Preserving the permeability barrier between the blood and the brain in a stable functional or structural state. The cells in the brain are packed tightly together preventing the passage of most molecules from the blood into the brain. Only lipid soluble molecules or those that are actively transported can pass through the blood-brain barrier.
Preserving the permeability barrier between the blood and the brain in a stable functional or structural state. The cells in the brain are packed tightly together preventing the passage of most molecules from the blood into the brain. Only lipid soluble molecules or those that are actively transported can pass through the blood-brain barrier.
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 exposure to a stilbenoid. Stilbenoids are secondary products of heartwood formation in trees that can act as phytoalexins. Stilbenoids are hydroxylated derivatives of stilbene. They belong to the family of phenylpropanoids and share most of their biosynthesis pathway with chalcones.
The process in which a bacterium enters a host cell. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The process in which a bacterium enters a host cell. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The transfer of information occurring at the level of a multicellular organism.
Any process leading to the attainment of the full functional capacity of a signal. A signal is a physical entity or change in state that is used to transfer information to trigger a response, and is functional when it can activate a receptor.
Interacting selectively and non-covalently with a purine ribonucleoside triphosphate, a compound consisting of a purine base linked to a ribose sugar esterified with triphosphate on the sugar.
The specific behavior of an organism in response to a novel environment or stimulus.
The specific behavior of an organism in response to a novel environment or stimulus.
The specific behavior of an organism in response to a novel environment or stimulus.
The specific behavior of an organism in response to a novel environment or stimulus.
The specific movement from place to place of an organism in response to a novel environment.
Catalysis of the reaction: S-adenosyl-L-methionine + (histone H3)-arginine (position 17) = S-adenosyl-L-homocysteine + (histone H3)-N-methyl-arginine (position 17). This reaction is the addition of a methyl group to arginine at position 17 of histone H3.
Catalysis of the reaction: S-adenosyl-L-methionine + (histone H3)-arginine (position 17) = S-adenosyl-L-homocysteine + (histone H3)-N-methyl-arginine (position 17). This reaction is the addition of a methyl group to arginine at position 17 of histone H3.
Combining with L-DOPA to initiate a change in cell activity. L-DOPA is the modified amino acid (2S)-2-amino-3-(3,4-dihydroxyphenyl) propanoic acid, and is the precursor to dopamine, norepinephrine (noradrenaline) and epinephrine.
Combining with L-DOPA to initiate a change in cell activity. L-DOPA is the modified amino acid (2S)-2-amino-3-(3,4-dihydroxyphenyl) propanoic acid, and is the precursor to dopamine, norepinephrine (noradrenaline) and epinephrine.
The process of removing one or more phosphate groups from a phosphorylated anandamide.
The process in which a relatively unspecialized cell acquires specialized features of a smooth muscle cell of the intestine.
The directed movement of substances from endosomes to the melanosome, a specialised lysosome-related organelle.
Catalysis of the reaction: a 3-oxo-delta-4,5-steroid + NADPH + H(+) = a 5-beta-3-oxo-steroid + NADP(+).
The fluctuation in mating behavior that occurs over an approximately 24 hour cycle.
The fluctuation in mating behavior that occurs over an approximately 24 hour cycle.
A complex that functions in transcription termination of RNA polymerase II transcribed non-coding RNAs. This complex interacts with the carboxy-terminal domain (CTD) of PolII and the terminator sequences in the nascent RNA transcript. In yeast this complex consists of Nrd1p, Nab3p, and Sen1p.
Interacting selectively and non-covalently with the AP-1 adaptor complex. The AP-1 adaptor complex is a heterotetrameric AP-type membrane coat adaptor complex that consists of beta1, gamma, mu1 and sigma1 subunits and links clathrin to the membrane surface of a vesicle. In at least humans, the AP-1 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different genes (gamma1 and gamma2, mu1A and mu1B, and sigma1A, sigma1B and sigma1C).
Interacting selectively and non-covalently with the AP-3 adaptor complex. The AP-3 adaptor complex is a heterotetrameric AP-type membrane coat adaptor complex that consists of beta3, delta, mu3 and sigma3 subunits and is found associated with endosomal membranes. In at least humans, the AP-3 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different genes (beta3A and beta3B, mu3A and mu3B, and sigma3A and sigma3B).
Formation of a macromolecular complex between the cytoplasmic coat proteins on clathrin-coated vesicles and proteins and/or lipoproteins that are going to be transported by a vesicle.
Formation of a macromolecular complex between proteins of the AP-1 adaptor complex and proteins and/or lipoproteins that are going to be transported by a clathrin-coated vesicle. The AP-1 adaptor protein complex is a component of the cytoplasmic coat found on clathrin-coated vesicles, and binds to sorting signals of cargo to facilitate their trafficking.
Formation of a macromolecular complex between proteins of the AP-3 adaptor complex and proteins and/or lipoproteins that are going to be transported by a clathrin-coated vesicle. In some cases, the AP-3 complex is a heterotetrameric AP-type membrane coat adaptor complex that, in some organisms, links clathrin to the membrane surface of a vesicle.
A series of molecular signals initiated by the binding of interleukin-18 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
The activity of linking kinesins, cytoplasmic proteins responsible for moving vesicles and organelles towards the distal end of microtubules, to melanosomes.
A protein complex required for the methylation of a glutamine (Gln) residue in the protein release factor eRF1. In S. cerevisiae, this complex consists of at least Trm112p and Mtq2p.
A protein complex that functions as a guanine nucleotide exchange factor (GEF) and converts Rab-GDP to Rab-GTP. In S. cerevisiae, this complex consists of at least Mon1 and Ccz1, and serves as a GEF for the Rab Ypt7p.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of a cell in the epidermis that contributes to the migration of an epidermal cell along or through a wound gap to reestablish a continuous epidermis.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of a cell in the epidermis that contributes to the migration of an epidermal cell along or through a wound gap to reestablish a continuous epidermis.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of a cell in the epidermis that contributes to the migration of an epidermal cell along or through a wound gap to reestablish a continuous epidermis.
Any series of molecular signals generated as a consequence of binding to a toll-like 4 receptor, where the MyD88 adaptor molecule mediates transduction of the signal. Toll-like 4 receptors bind bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like 4 receptor, where the MyD88 adaptor molecule mediates transduction of the signal. Toll-like 4 receptors bind bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like 2 receptor where the MyD88 adaptor molecule mediates transduction of the signal. Toll-like 2 receptors are pattern recognition receptors that bind microbial pattern motifs to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like 2 receptor where the MyD88 adaptor molecule mediates transduction of the signal. Toll-like 2 receptors are pattern recognition receptors that bind microbial pattern motifs to initiate an innate immune response.
Interacting selectively and non-covalently with a Toll-like 4 protein, a pattern recognition receptor that binds bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
Interacting selectively and non-covalently with a Toll-like 2 protein, a pattern recognition receptor that binds microbial pattern motifs to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the TIRAP/MAL adaptor mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the TIRAP/MAL adaptor mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the TIRAP/MAL adaptor mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the TIRAP/MAL adaptor mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor 4 where the TIRAP/MAL adaptor mediates transduction of the signal. Toll-like 4 receptors are pattern recognition receptors that bind bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor 4 where the TIRAP/MAL adaptor mediates transduction of the signal. Toll-like 4 receptors are pattern recognition receptors that bind bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor 4 where the TIRAP/MAL adaptor mediates transduction of the signal. Toll-like 4 receptors are pattern recognition receptors that bind bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor 4 where the TIRAP/MAL adaptor mediates transduction of the signal. Toll-like 4 receptors are pattern recognition receptors that bind bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the TRIF adaptor mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the TRIF adaptor mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the TRIF adaptor mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like 4 receptor where the TRIF adaptor mediates transduction of the signal. Toll-like 4 receptors are pattern recognition receptors that bind bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like 4 receptor where the TRIF adaptor mediates transduction of the signal. Toll-like 4 receptors are pattern recognition receptors that bind bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like 4 receptor where the TRIF adaptor mediates transduction of the signal. Toll-like 4 receptors are pattern recognition receptors that bind bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the TRAM adaptor mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor where the TRAM adaptor mediates transduction of the signal. Toll-like receptors directly bind pattern motifs from a variety of microbial sources to initiate innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor 4 where the TRAM adaptor mediates transduction of the signal. Toll-like 4 receptors are pattern recognition receptors that bind bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
Any series of molecular signals generated as a consequence of binding to a toll-like receptor 4 where the TRAM adaptor mediates transduction of the signal. Toll-like 4 receptors are pattern recognition receptors that bind bacterial lipopolysaccharide (LPS) to initiate an innate immune response.
The process whose specific outcome is the progression of an ovary that produces an ovule over time, from its formation to the mature structure. The ovary is the enlarged basal portion of a carpel and matures into a fruit. An ovule is the multicellular structure that gives rise to and contains the female reproductive cells, and develops into a seed.
Catalysis of the reaction: an enone + NADPH + H+ = a ketone + NADP+.
The process in which an oligopeptide is transported across a membrane. Oligopeptides are molecules that contain a small number (2 to 20) of amino-acid residues connected by peptide linkages.
Enables the transfer of oligopeptides from one side of a membrane to the other. Oligopeptides are molecules that contain a small number (2 to 20) of amino-acid residues connected by peptide linkages.
Enables the transfer of oligopeptides from one side of a membrane to the other. Oligopeptides are molecules that contain a small number (2 to 20) of amino-acid residues connected by peptide linkages.
The process in which a tricarboxylic acid is transported across a membrane.
The process whose specific outcome is the progression of a neuromast hair cell over time, from its formation to the mature structure. A neuromast hair cell is a hair cell that acts as a sensory receptor of the neuromast; it is morphologically polarized as a result of the relative position of the single kinocilium and the clusters of stereocilia on its apical surface. Cell development does not include the steps involved in committing a cell to a specific fate.
The process whose specific outcome is the progression of an anterior lateral line neuromast hair cell over time, from its formation to the mature structure. A neuromast hair cell is a hair cell that acts as a sensory receptor of the neuromast; it is morphologically polarized as a result of the relative position of the single kinocilium and the clusters of stereocilia on its apical surface. Cell development does not include the steps involved in committing a cell to a specific fate.
The process whose specific outcome is the progression of a posterior lateral line neuromast hair cell over time, from its formation to the mature structure. A neuromast hair cell is a hair cell that acts as a sensory receptor of the neuromast; it is morphologically polarized as a result of the relative position of the single kinocilium and the clusters of stereocilia on its apical surface. Cell development does not include the steps involved in committing a cell to a specific fate.
The change in form (cell shape and size) that occurs when a neuromast hair cell progresses from its initial formation to its mature state. A neuromast hair cell is a hair cell that acts as a sensory receptor of the neuromast; it is morphologically polarized as a result of the relative position of the single kinocilium and the clusters of stereocilia on its apical surface.
The change in form (cell shape and size) that occurs when an anterior lateral line neuromast hair cell progresses from its initial formation to its mature state. A neuromast hair cell is a hair cell that acts as a sensory receptor of the neuromast; it is morphologically polarized as a result of the relative position of the single kinocilium and the clusters of stereocilia on its apical surface.
The change in form (cell shape and size) that occurs when a posterior lateral line neuromast hair cell progresses from its initial formation to its mature state. A neuromast hair cell is a hair cell that acts as a sensory receptor of the neuromast; it is morphologically polarized as a result of the relative position of the single kinocilium and the clusters of stereocilia on its apical surface.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 15.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 15.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 21.
Any series of molecular signals generated as a consequence of binding to toll-like receptor 21.
The migration of a memory T cell from the blood vessels into the surrounding tissue. A memory T cell is a distinctly differentiated long-lived T cell that has the phenotype CD45RO-positive and CD127-positive.
The migration of a helper T cell from the blood vessels into the surrounding tissue. A helper T-cell is an effector T cell that provides help in the form of secreted cytokines to other immune cells.
The migration of a helper T cell from the blood vessels into the surrounding tissue. A helper T-cell is an effector T cell that provides help in the form of secreted cytokines to other immune cells.
The passage of a helper T cell between the tight junctions of endothelial cells lining blood vessels, typically the fourth and final step of cellular extravasation.
The passage of a helper T cell between the tight junctions of endothelial cells lining blood vessels, typically the fourth and final step of cellular extravasation.
A cytoskeletal structure surrounding the axoneme and outer dense fibers of the sperm flagellum. Consists of two longitudinal columns connected by closely arrayed semicircular ribs that assemble from distal to proximal throughout spermiogenesis. The fibrous sheath probably influences the degree of flexibility, plane of flagellar motion, and the shape of the flagellar beat.
A cytoskeletal structure surrounding the axoneme and outer dense fibers of the sperm flagellum. Consists of two longitudinal columns connected by closely arrayed semicircular ribs that assemble from distal to proximal throughout spermiogenesis. The fibrous sheath probably influences the degree of flexibility, plane of flagellar motion, and the shape of the flagellar beat.
The migration of a T-helper 1 cell from the blood vessels into the surrounding tissue. A T-helper 1 cell is a CD4-positive, alpha-beta T cell that has the phenotype T-bet-positive and produces interferon-gamma.
The passage of a T-helper 1 cell between the tight junctions of endothelial cells lining blood vessels, typically the fourth and final step of cellular extravasation. A T-helper 1 cell is a CD4-positive, alpha-beta T cell that has the phenotype T-bet-positive and produces interferon-gamma.
A series of molecular signals initiated by the binding of the chemokine CCL5 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 the chemokine CCL5 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 the chemokine CCL5 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
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 drug stimulus. A drug is a substance used in the diagnosis, treatment or prevention of a disease.
A series of molecular signals initiated by the binding of macrophage migration inhibitory 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 macrophage migration inhibitory factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A protein complex that binds macrophage migration inhibitory factor. Comprises CD74 and CD44 cell surface proteins.
A protein complex comprising nitric oxide synthase 2 and CD74. This stable complex formation is thought to prevent CD74 degradation by caspases.
The chemical reactions and pathways resulting in the breakdown of a mitochondrial protein. This process is necessary to maintain the healthy state of mitochondria and is thought to occur via the induction of an intramitochondrial lysosome-like organelle that acts to eliminate the damaged oxidised mitochondrial proteins without destroying the mitochondrial structure.
The chemical reactions and pathways resulting in the breakdown of a mitochondrial protein. This process is necessary to maintain the healthy state of mitochondria and is thought to occur via the induction of an intramitochondrial lysosome-like organelle that acts to eliminate the damaged oxidised mitochondrial proteins without destroying the mitochondrial structure.
The process in which cells degrade mitochondria by inducing a vacuole-like structure which directly engulfs and degrades the unhealthy mitochondria by accumulating lysosomes.
The migration of a monocyte from the blood vessels into the surrounding tissue.
The migration of a CD8-positive, alpha-beta T cell from the blood vessels into the surrounding tissue.
The migration of a CD8-positive, alpha-beta cytotoxic T cell from the blood vessels into the surrounding tissue.
The migration of a T-helper 17 cell from the blood vessels into the surrounding tissue.
The directed movement of an astrocyte guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
The orderly movement of a hematopoietic stem cell from one site to another. A hematopoietic stem cell is a cell from which all cells of the lymphoid and myeloid lineages develop, including blood cells and cells of the immune system.
The process of regulating the proliferation and elimination of monocytes such that the total number of monocytes within a whole or part of an organism is stable over time in the absence of an outside stimulus.
The movement of a monocyte from the bone marrow to the blood stream.
The directed movement of a helper T cell in response to an external stimulus.
The directed movement of a T-helper 17 cell in response to an external stimulus.
The directed movement of a T-helper 1 cell in response to an external stimulus.
The directed movement of a T-helper 2 cell in response to an external stimulus.
The switching of activated B cells from IgM biosynthesis to IgE biosynthesis, accomplished through a recombination process involving an intrachromosomal deletion between switch regions that reside 5' of the IgM and IgE constant region gene segments in the immunoglobulin heavy chain locus, that is dependent on the activity of interleukin 4 (IL-4).
The change in morphology and behavior of a memory T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
The change in morphology and behavior of a CD4-positive, alpha-beta T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
The change in morphology and behavior of a T-helper 1 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
The change in morphology and behavior of a T helper 2 cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
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 nitrogen dioxide (NO2) stimulus.
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 nitrogen dioxide (NO2) stimulus.
Interacting selectively and non-covalently with chemokine (C-C motif) ligand 2.
Interacting selectively and non-covalently with chemokine (C-C motif) ligand 12.
Interacting selectively and non-covalently with chemokine (C-C motif) ligand 7.
Interacting selectively and non-covalently with the cytokine, macrophage migration inhibitory factor.
The directed movement of tRNA from the cytoplasm to the nucleus.
The directed movement of tRNA from the cytoplasm to the nucleus.
The directed movement of large protein complexes along microtubules from the cell body toward the tip of a cilium (also called flagellum), mediated by motor proteins.
The directed movement of large protein complexes along microtubules from the tip of a cilium (also called flagellum) toward the cell body, mediated by motor proteins.
A series of molecular signals initiated by the binding of interleukin-12 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 interleukin-12 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 interleukin-15 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 interleukin-15 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
The chemical reactions and pathways resulting in the formation of CD24, a CD marker and cell adhesion molecule that occurs on many B-lineage cells and mature granulocytes, and is involved in B cell activation and differentiation as well as T cell co-stimulation.
The chemical reactions and pathways resulting in the formation of CD24, a CD marker and cell adhesion molecule that occurs on many B-lineage cells and mature granulocytes, and is involved in B cell activation and differentiation as well as T cell co-stimulation.
The chemical reactions and pathways resulting in the formation of CD24, a CD marker and cell adhesion molecule that occurs on many B-lineage cells and mature granulocytes, and is involved in B cell activation and differentiation as well as T cell co-stimulation.
The chemical reactions and pathways resulting in the formation of CD24, a CD marker and cell adhesion molecule that occurs on many B-lineage cells and mature granulocytes, and is involved in B cell activation and differentiation as well as T cell co-stimulation.
A process in which a sodium ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
The multiplication or reproduction of common myeloid progenitor cells, resulting in the expansion of a cell population. A common myeloid progenitor cell is a progenitor cell committed to the myeloid lineage.
Interacting selectively and non-covalently with lysophosphatidic acid (LPA), a phospholipid derivative that acts as a potent mitogen due to its activation of high-affinity G protein-coupled receptors.
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 hepatocyte growth factor 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 hepatocyte growth factor stimulus.
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 hepatocyte growth factor stimulus.
Interacting selectively and non-covalently with S-nitrosoglutathione, a nitrosothiol considered to be a natural nitric oxide (NO) donor involved in S-nitrosylation, and in the storage and transport of nitric oxide in biological systems.
Interacting selectively and non-covalently with a dinitrosyl-iron complex. Nitric oxide (NO) is stored as dinitrosyl-iron complexes, which form spontaneously from Glutathione (GSH), S-nitrosoglutathione, and trace amounts of ferrous ions, or by reaction of iron-sulfur centers with NO.
Interacting selectively and non-covalently with a dinitrosyl-iron complex. Nitric oxide (NO) is stored as dinitrosyl-iron complexes, which form spontaneously from Glutathione (GSH), S-nitrosoglutathione, and trace amounts of ferrous ions, or by reaction of iron-sulfur centers with NO.
Interacting selectively and non-covalently with a dinitrosyl-iron complex. Nitric oxide (NO) is stored as dinitrosyl-iron complexes, which form spontaneously from Glutathione (GSH), S-nitrosoglutathione, and trace amounts of ferrous ions, or by reaction of iron-sulfur centers with NO.
The accumulation and maintenance in cells or tissues of nitric oxide (NO). Nitric oxide is stored in the form of dinitrosyl-iron complexes, which are stabilized, and possibly sequestered, by binding to glutathione S-transferase proteins.
A change in the morphology or behavior of a hepatic stellate cell resulting from exposure to a cytokine, chemokine, hormone, cellular ligand or soluble factor.
The bidirectional movement of large protein complexes along microtubules within a cilium that contributes to cilium assembly.
The bidirectional movement of large protein complexes along microtubules within a cilium that contributes to cilium assembly.
The bidirectional movement of large protein complexes along microtubules within a cilium that contributes to cilium assembly.
The multiplication or reproduction of cells, resulting in the expansion of a cell population that contributes to compound eye morphogenesis.
The process of forcing a substance into another organism, either by penetrating the skin of the other organism or by applying the substance externally to a sensitive tissue such as those that surround the eyes.
The process which begins with venom being forced into an organism by the bite or sting of another organism, and ends with the manifestation of some change or damage to the bitten organism.
The expansion of a CD4-positive, alpha-beta T cell population by cell division.
The expansion of a CD8-positive, alpha-beta T cell population by cell division.
The expansion of an activated CD4-positive, alpha-beta T cell population by cell division.
The expansion of an activated CD8-positive, alpha-beta T cell population by cell division.
Any process that contributes to cytokine production by a CD4-positive, alpha-beta T cell.
Any process that contributes to cytokine production by a T-helper 1 cell.
Any process that contributes to cytokine production by a T-helper 2 cell.
The appearance of granzyme A due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The directed movement of a natural killer cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
The region of the myelin sheath furthest from the axon.
The region of the myelin sheath nearest to the axon.
Any process in which a protein is transported to, and/or maintained in, the abaxonal region of the myelin sheath. The abaxonal region is the region of the myelin sheath furthest from the axon.
Any process that modulates the pH of the lysosomal lumen, measured by the concentration of the hydrogen ion.
Any process that increases the pH of the lysosomal lumen, measured by the concentration of the hydrogen ion.
Any process involved in sustaining the fidelity and copy number of DNA trinucleotide repeats. DNA trinucleotide repeats are naturally occurring runs of three base-pairs.
The directed movement of a B cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
Catalysis of the hydrolysis of cardiolipin (1,3-bis(3-phosphatidyl)glycerol) to form phosphatidic acid (PA).
The directional movement of an organism from one side of an epithelium to the other within its host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The directional movement of an organism from one side of an epithelium to the other within its host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Interacting selectively and non-covalently with chemokine (C-C motif) ligand 19.
Interacting selectively and non-covalently with chemokine (C-C motif) ligand 21.
The binding of a mesangial cell to the extracellular matrix via adhesion molecules. A mesangial cell is a cell that encapsulates the capillaries and venules in the kidney.
The chemical reactions and pathways occurring in the cytoplasm and resulting in the breakdown of a ribosomal RNA (rRNA) molecule, initiated by the enzymatic addition of a sequence of adenylyl residues (polyadenylation) at the 3' end the target rRNA truncated degradation intermediate.
A developmental process, independent of morphogenetic (shape) change, that is required for the dorsal motor nucleus of the vagus nerve to attain its fully functional state.
The process in which the dorsal motor nucleus of the vagus nerve is generated and organized. Morphogenesis pertains to the creation of form.
The process that contributes to the act of creating the structural organization of the dorsal motor nucleus of the vagus nerve. This process pertains to the physical shaping of a rudimentary structure.
The process that gives rise to the dorsal motor nucleus of the vagus nerve. This process pertains to the initial formation of a structure from unspecified parts.
The orderly movement of a motor neuron precursor cell that contributes to formation of the dorsal motor nucleus of the vagus nerve.
The directed movement of a motile cell in response to the presence of fibroblast growth factor (FGF).
The directed movement of an endothelial cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
The directed movement of an endothelial cell in response to the presence of fibroblast growth factor (FGF).
The movement of a B cell to cross a high endothelial venule in response to an external stimulus.
A non-membranous macromolecular complex containing proteins and translationally silenced mRNAs. RNA granules contain proteins that control the localization, stability, and translation of their RNA cargo. Different types of RNA granules (RGs) exist, depending on the cell type and cellular conditions.
A non-membranous macromolecular complex containing proteins and translationally silenced mRNAs. RNA granules contain proteins that control the localization, stability, and translation of their RNA cargo. Different types of RNA granules (RGs) exist, depending on the cell type and cellular conditions.
A non-membranous macromolecular complex containing proteins and translationally silenced mRNAs. RNA granules contain proteins that control the localization, stability, and translation of their RNA cargo. Different types of RNA granules (RGs) exist, depending on the cell type and cellular conditions.
A series of molecular signals initiated by the binding of interleukin-4 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 interleukin-4 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 interleukin-13 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 interleukin-13 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
The regulated release of proinsulin from secretory granules (B granules) in the B cells of the pancreas; accompanied by cleavage of proinsulin to form mature insulin, in response to a glucose stimulus.
Any process that increases the frequency, rate or extent of the regulated release of insulin that contributes to the response of a cell to glucose.
The process in which the anatomical structures of the pronephric glomerulus are generated and organized. The pronephric glomerulus is part of the pronephric nephron and is restricted to one body segment.
The progression of the pronephric proximal tubule over time, from its formation to the mature structure. A pronephric nephron tubule is an epithelial tube that is part of the pronephros.
The process whose specific outcome is the progression of the pronephric distal tubule over time, from its formation to the mature structure. A pronephric nephron tubule is an epithelial tube that is part of the pronephros.
The process in which relatively unspecialized cells acquire specialized structural and/or functional features that characterize the cells of the pronephric nephron tubule as it progresses from its formation to the mature state.
The process in which a relatively unspecialized cell acquires the specialized structural and/or functional features of an angioblast cell. Angioblasts are one of the two products formed from hemangioblast cells (the other being pluripotent hemopoietic stem cells).
The chemical reactions and pathways resulting in the formation of CD80, a CD marker that occurs on antigen presenting cells such as activated B cells and monocytes that provides a co-stimulatory signal necessary for T cell activation and survival.
The chemical reactions and pathways resulting in the formation of CD80, a CD marker that occurs on antigen presenting cells such as activated B cells and monocytes that provides a co-stimulatory signal necessary for T cell activation and survival.
The chemical reactions and pathways resulting in the formation of CD80, a CD marker that occurs on antigen presenting cells such as activated B cells and monocytes that provides a co-stimulatory signal necessary for T cell activation and survival.
The chemical reactions and pathways resulting in the formation of CD80, a CD marker that occurs on antigen presenting cells such as activated B cells and monocytes that provides a co-stimulatory signal necessary for T cell activation and survival.
The chemical reactions and pathways resulting in the formation of CD86, a CD marker that occurs on antigen presenting cells that provides co-stimulatory signals necessary for T cell activation and survival.
The chemical reactions and pathways resulting in the formation of CD86, a CD marker that occurs on antigen presenting cells that provides co-stimulatory signals necessary for T cell activation and survival.
The chemical reactions and pathways resulting in the formation of CD86, a CD marker that occurs on antigen presenting cells that provides co-stimulatory signals necessary for T cell activation and survival.
The chemical reactions and pathways resulting in the formation of CD86, a CD marker that occurs on antigen presenting cells that provides co-stimulatory signals necessary for T cell activation and survival.
The directed movement of a mature natural killer cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). A mature natural killer cell is a natural killer cell that is developmentally mature and expresses a variety of inhibitory and activating receptors that recognize MHC class and other stress related molecules.
The process of providing, via surface-bound receptor-ligand pairs, a second, antigen-independent, signal in addition to that provided by the T cell receptor to augment CD4-positive, alpha-beta T cell activation.
Any process involved in the maintenance of an internal steady state of nickel cations within an organism or cell.
Any process involved in the maintenance of an internal steady state of nickel ions at the level of a cell.
The orderly movement of a cell from one site to another that will contribute to the progression of the kidney over time, from its formation to the mature organ.
The orderly movement of a cell from one site to another that will contribute to the progression of the metanephric kidney over time, from its formation to the mature organ.
The orderly movement of undifferentiated metanephric mesenchymal cells (precursors to metanephric mesangial cells) from the mesenchyme into the cleft of the developing glomerulus, during development of the metanephros.
A series of molecular signals initiated by the binding of a ligand to an alpha-type platelet-derived growth factor receptor (PDGFalpha) on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a ligand to an alpha-type platelet-derived growth factor receptor (PDGFalpha) on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a ligand to an alpha-type platelet-derived growth factor receptor (PDGFalpha) on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a ligand to an alpha-type platelet-derived growth factor receptor (PDGFalpha) on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a ligand to a beta-type platelet-derived growth factor receptor (PDGFbeta) on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a ligand to a beta-type platelet-derived growth factor receptor (PDGFbeta) on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a ligand to a beta-type platelet-derived growth factor receptor (PDGFbeta) on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a ligand to a beta-type platelet-derived growth factor receptor (PDGFbeta) on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A postsynaptic membrane that is part of another organism, i.e. a secondary organism with which the first organism is interacting. A postsynaptic membrane is a specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft). Neurotransmitters transmit the signal across the synaptic cleft to the postsynaptic membrane.
Any process that increases the frequency, rate or extent of metanephric mesenchymal cell migration as a result of the series of molecular signals generated as a consequence of a platelet-derived growth factor receptor-beta binding to one of its physiological ligands.
Any process that increases the frequency, rate or extent of metanephric mesenchymal cell migration as a result of the series of molecular signals generated as a consequence of a platelet-derived growth factor receptor-beta binding to one of its physiological ligands.
Any process that increases the frequency, rate or extent of metanephric mesenchymal cell migration as a result of the series of molecular signals generated as a consequence of a platelet-derived growth factor receptor-beta binding to one of its physiological ligands.
Any process that increases the frequency, rate or extent of metanephric mesenchymal cell migration as a result of the series of molecular signals generated as a consequence of a platelet-derived growth factor receptor-beta binding to one of its physiological ligands.
Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane.
Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane.
Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane.
Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane.
Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane.
Any process that decreases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane.
Any process that decreases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane.
Any process that decreases the frequency, rate or extent of the passage or uptake of molecules by the mitochondrial membrane.
A complex for the transport of metabolites into the cell, consisting of 4 subunits: a transmembrane substrate-binding protein (known as the S component), and an energy-coupling module that comprises two ATP-binding proteins (known as the A and A' components) and a transmembrane protein (known as the T component). Transport of the substrate across the membrane is driven by the hydrolysis of ATP.
A complex for the transport of metabolites into the cell, consisting of 4 subunits: a transmembrane substrate-binding protein (known as the S component), and an energy-coupling module that comprises two ATP-binding proteins (known as the A and A' components) and a transmembrane protein (known as the T component). Transport of the substrate across the membrane is driven by the hydrolysis of ATP.
A complex for the transport of metabolites into the cell, consisting of 4 subunits: a transmembrane substrate-binding protein (known as the S component), and an energy-coupling module that comprises two ATP-binding proteins (known as the A and A' components) and a transmembrane protein (known as the T component). Transport of the substrate across the membrane is driven by the hydrolysis of ATP.
Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to tellurite [TeO3(2-)]. Methylated derivatives of tellurite include Te(CH3)2 (dimethyltelluride) and Te2(CH3)2 (dimethylditelluride).
Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to tellurite [TeO3(2-)]. Methylated derivatives of tellurite include Te(CH3)2 (dimethyltelluride) and Te2(CH3)2 (dimethylditelluride).
Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to tellurite [TeO3(2-)]. Methylated derivatives of tellurite include Te(CH3)2 (dimethyltelluride) and Te2(CH3)2 (dimethylditelluride).
Catalysis of the reaction: n-alkanal + NADP+ = alk-2-enal + NADPH + H+.
A developmental process, independent of morphogenetic (shape) change, that is required for the ureter to attain its fully functional state. The ureter is a muscular tube that transports urine from the kidney to the urinary bladder or from the Malpighian tubule to the hindgut.
Increases the activity of deubiquitinase, an enzyme that catalyzes the hydrolysis of various forms of polymeric ubiquitin sequences.
The process whose specific outcome is the progression of the adrenal cortex over time, from its formation to the mature structure. The adrenal cortex is located at the periphery of the adrenal gland and controls glucose and electrolyte metabolism, response to stress and sexual development through the production of different classes of steroid hormones (glucocorticoids, mineralocorticoids and androgens).
The process that gives rise to the adrenal cortex. This process pertains to the initial formation of a structure from unspecified parts. The adrenogonadal primordium from which the adrenal cortex is formed derives from a condensation of coelomic epithelial cells (the urogenital ridge; the same structure from which gonads and kidney also originate).
Construction of an egg coat, a specialized extracellular matrix that surrounds the ovum of animals. The egg coat provides structural support and can play an essential role in oogenesis, fertilization and early development.
Construction of an egg coat, a specialized extracellular matrix that surrounds the ovum of animals. The egg coat provides structural support and can play an essential role in oogenesis, fertilization and early development.
Construction of an egg coat, a specialized extracellular matrix that surrounds the ovum of animals. The egg coat provides structural support and can play an essential role in oogenesis, fertilization and early development.
Construction of an egg coat, a specialized extracellular matrix that surrounds the ovum of animals. The egg coat provides structural support and can play an essential role in oogenesis, fertilization and early development.
The action of a molecule that contributes to the structural integrity of an egg coat. An egg coat is a specialized extracellular matrix that surrounds the ovum of animals. The egg coat provides structural support and can play an essential role in oogenesis, fertilization and early development.
The action of a molecule that contributes to the structural integrity of an egg coat. An egg coat is a specialized extracellular matrix that surrounds the ovum of animals. The egg coat provides structural support and can play an essential role in oogenesis, fertilization and early development.
A specialized extracellular matrix that surrounds the plasma membrane of the ovum of animals. The egg coat provides structural support and can play an essential role in oogenesis, fertilization and early development.
A specialized extracellular matrix that surrounds the plasma membrane of the ovum of animals. The egg coat provides structural support and can play an essential role in oogenesis, fertilization and early development.
Any process in which an organism modulates the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
Any process in which an organism modulates the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
Any process in which an organism modulates the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
Any process in which an organism modulates the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
Any process in which an organism modulates the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
Any process in which an organism activates, maintains or increases the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
Any process in which an organism activates, maintains or increases the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
Any process in which an organism activates, maintains or increases the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
A protein complex that initiates the formation of double-strand breaks (DSBs) required for meiotic recombination. Consists of a protein that catalyses formation of the double-strand breaks (Spo11 in S. cerevisiae and Rec12 in S. pombe), and a number of accessory proteins.
The elimination by an organism of sodium in the urine.
Any process where water is taken up from the collecting ducts and proximal and distal loops of the nephron, which acts to decrease the amount of urine that is excreted from the body per unit time.
Any process where sodium ions are taken up from the collecting ducts and proximal and distal loops of the nephron, which contributes to decreasing the amount of sodium that is excreted in urine per unit time.
The process in which angiotensin decreases the amount of sodium that is excreted in urine over a unit of time.
The process in which an organism effects a change in the structure or processes of a second organism.
The process in which an organism effects a change in the structure or processes of a second organism.
The process in which an organism effects a change in the structure or processes of a second organism.
The process in which an organism effects a change in the structure or processes of a second organism.
A DNA recombination process that results in the unidirectional transfer of genetic material from a donor sequence to a highly homologous acceptor.
A gene conversion process in which a segment of about 50-200 base pairs is transferred from the donor to the acceptor.
A gene conversion process in which a segment of more than 1000 base pairs is transferred from the donor to the acceptor.
A DNA recombination process that results in the equal exchange of genetic material between the recombining DNA molecules.
A DNA recombination process that results in the equal exchange of genetic material between the recombining DNA molecules.
A DNA recombination process that results in the equal exchange of genetic material between the recombining DNA molecules.
A DNA recombination process that results in the equal exchange of genetic material between the recombining DNA molecules.
The chemical reactions and pathways involving palmatine, a berberine alkaloid found in many plants.
The chemical reactions and pathways resulting in the formation of palmatine, a berberine alkaloid found in many plants.
The chemical reactions and pathways resulting in the formation of palmatine, a berberine alkaloid found in many plants.
The chemical reactions and pathways resulting in the formation of palmatine, a berberine alkaloid found in many plants.
The chemical reactions and pathways resulting in the formation of palmatine, a berberine alkaloid found in many plants.
The chemical reactions and pathways involving berbamunine, an isoquinoline alkaloid.
The chemical reactions and pathways resulting in the formation of berbamunine, an isoquinoline alkaloid.
The chemical reactions and pathways resulting in the formation of berbamunine, an isoquinoline alkaloid.
The chemical reactions and pathways resulting in the formation of berbamunine, an isoquinoline alkaloid.
The chemical reactions and pathways resulting in the formation of berbamunine, an isoquinoline alkaloid.
The chemical reactions and pathways involving an indole alkaloid, an alkaloid containing an indole skeleton.
The chemical reactions and pathways resulting in the formation of an indole alkaloid, an alkaloid containing an indole skeleton.
The chemical reactions and pathways resulting in the formation of an indole alkaloid, an alkaloid containing an indole skeleton.
The chemical reactions and pathways resulting in the formation of an indole alkaloid, an alkaloid containing an indole skeleton.
The chemical reactions and pathways resulting in the formation of an indole alkaloid, an alkaloid containing an indole skeleton.
The chemical reactions and pathways involving an ergot alkaloid, an indole alkaloid.
The chemical reactions and pathways resulting in the formation of an ergot alkaloid.
The chemical reactions and pathways resulting in the formation of an ergot alkaloid.
The chemical reactions and pathways resulting in the formation of an ergot alkaloid.
The chemical reactions and pathways resulting in the formation of an ergot alkaloid.
The region at either end of the longest axis of a cylindrical or elongated cell, where polarized growth occurs.
A cell tip at which no growth takes place. For example, in fission yeast the cell end newly formed by cell division does not grow immediately upon its formation, and lacks actin cytoskeletal structures.
A cell tip at which no growth takes place. For example, in fission yeast the cell end newly formed by cell division does not grow immediately upon its formation, and lacks actin cytoskeletal structures.
A cell tip which has existed for at least one complete cell cycle, and at which polarized growth occurs. For example, in fission yeast the cell end that existed prior to cell division grows immediately after division, and contains a distinctive complement of proteins including actin cytoskeletal structures.
A cell tip that was newly formed at the last cell division, and that has started to grow after the cell has activated bipolar cell growth (i.e. in which new end take-off, NETO, has taken place). New end take-off is when monopolar cells initiate bipolar growth.
A cell tip that was newly formed at the last cell division, and that has started to grow after the cell has activated bipolar cell growth (i.e. in which new end take-off, NETO, has taken place). New end take-off is when monopolar cells initiate bipolar growth.
A cell tip that was newly formed at the last cell division, and that has started to grow after the cell has activated bipolar cell growth (i.e. in which new end take-off, NETO, has taken place). New end take-off is when monopolar cells initiate bipolar growth.
A cell tip that was newly formed at the last cell division, and that has started to grow after the cell has activated bipolar cell growth (i.e. in which new end take-off, NETO, has taken place). New end take-off is when monopolar cells initiate bipolar growth.
A cell tip which has existed for at least one complete cell cycle, and at which polarized growth occurs, which is part of a cell that has activated bipolar cell growth (i.e. in which new end take-off, NETO, has taken place). For example, in fission yeast the cell end that existed prior to cell division grows immediately after division, and contains a distinctive complement of proteins including actin cytoskeletal structures.
A cell tip which has existed for at least one complete cell cycle, and at which polarized growth occurs, which is part of a cell that has activated bipolar cell growth (i.e. in which new end take-off, NETO, has taken place). For example, in fission yeast the cell end that existed prior to cell division grows immediately after division, and contains a distinctive complement of proteins including actin cytoskeletal structures.
A cell tip which has existed for at least one complete cell cycle, and at which polarized growth occurs, which is part of a cell that has activated bipolar cell growth (i.e. in which new end take-off, NETO, has taken place). For example, in fission yeast the cell end that existed prior to cell division grows immediately after division, and contains a distinctive complement of proteins including actin cytoskeletal structures.
A membrane-bound structure present in the nucleus of a spermatozoon. There is variation in the number of endonuclear canals between sperm of different organisms, and some species lack these structures altogether. The endonuclear canal may provide a supporting role for the sperm nucleus, and originates during spermiogenesis from an invagination of the nuclear envelope.
The process whose specific outcome is the progression of the cloaca over time, from it's formation to the mature structure. The cloaca is the common chamber into which intestinal, genital and urinary canals open in vertebrates.
A process that is carried out at the cellular level and results in the assembly, arrangement of constituent parts, or disassembly of the outer segment of a photoreceptor cell, a sensory cell that reacts to the presence of light. The outer segment of the photoreceptor cell contains the light-absorbing materials.
A process that is carried out at the cellular level and results in the assembly, arrangement of constituent parts, or disassembly of the outer segment of a photoreceptor cell, a sensory cell that reacts to the presence of light. The outer segment of the photoreceptor cell contains the light-absorbing materials.
The progression of the oviduct epithelium over time from its initial formation to the mature structure. An oviduct is a tube through which an ova passes from the ovary to the uterus, or from the ovary to the outside of the organism. The oviduct epithelium is the specialized epithelium that lines the oviduct.
The progression of an epithelium of the uterus over time from its initial formation to the mature structure. An epithelium is a tissue that covers the internal or external surfaces of an anatomical structure.
The process in which anatomical structures of the oviduct are generated and organized. An oviduct is a tube through which an ova passes from the ovary to the uterus, or from the ovary to the outside of the organism.
The process in which the nephric duct grows along its axis. A nephric duct is a tube that drains a primitive kidney.
The process in which relatively unspecialized cells acquire specialized structural and/or functional features of an epithelial cell that characterize the cells of the kidney as it progresses from its formation to the mature state.
Interacting selectively and non-covalently with a Krueppel-associated box (KRAB) domain of a protein. The approximately 75 amino acid KRAB domain is enriched in charged amino acids, and is found in the N-terminal regions of many zinc finger-containing transcription factors.
Interacting selectively and non-covalently with a Krueppel-associated box (KRAB) domain of a protein. The approximately 75 amino acid KRAB domain is enriched in charged amino acids, and is found in the N-terminal regions of many zinc finger-containing transcription factors.
Any process in which a horizontal cell is transported to, and/or maintained in, a specific location within the inner nuclear layer (INL) of the retina. A horizontal cell is a neuron that laterally connects other neurons in the inner nuclear layer (INL) of the retina. Targeting of retinal neurons to the appropriate lamina is vital to establish the architecture of the retina.
Any process in which a horizontal cell is transported to, and/or maintained in, a specific location within the inner nuclear layer (INL) of the retina. A horizontal cell is a neuron that laterally connects other neurons in the inner nuclear layer (INL) of the retina. Targeting of retinal neurons to the appropriate lamina is vital to establish the architecture of the retina.
Any process in which a horizontal cell is transported to, and/or maintained in, a specific location within the inner nuclear layer (INL) of the retina. A horizontal cell is a neuron that laterally connects other neurons in the inner nuclear layer (INL) of the retina. Targeting of retinal neurons to the appropriate lamina is vital to establish the architecture of the retina.
Any process in which a horizontal cell is transported to, and/or maintained in, a specific location within the inner nuclear layer (INL) of the retina. A horizontal cell is a neuron that laterally connects other neurons in the inner nuclear layer (INL) of the retina. Targeting of retinal neurons to the appropriate lamina is vital to establish the architecture of the retina.
A cellular protein complex localization that acts on a chromosome passenger complex; as a result, the complex is transported to, or maintained in, a specific location at the spindle midzone. A chromosome passenger complex is a protein complex that contains the BIR-domain-containing protein Survivin, Aurora B kinase, INCENP and Borealin, and coordinates various events based on its location to different structures during the course of mitosis. The spindle midzone is the area in the center of the spindle where the spindle microtubules from opposite poles overlap.
A cellular protein complex localization that acts on a chromosome passenger complex; as a result, the complex is transported to, or maintained in, a specific location at the spindle midzone. A chromosome passenger complex is a protein complex that contains the BIR-domain-containing protein Survivin, Aurora B kinase, INCENP and Borealin, and coordinates various events based on its location to different structures during the course of mitosis. The spindle midzone is the area in the center of the spindle where the spindle microtubules from opposite poles overlap.
A cellular protein complex localization that acts on a chromosome passenger complex; as a result, the complex is transported to, or maintained in, a specific location at the spindle midzone. A chromosome passenger complex is a protein complex that contains the BIR-domain-containing protein Survivin, Aurora B kinase, INCENP and Borealin, and coordinates various events based on its location to different structures during the course of mitosis. The spindle midzone is the area in the center of the spindle where the spindle microtubules from opposite poles overlap.
A cellular protein complex localization that acts on a chromosome passenger complex; as a result, the complex is transported to, or maintained in, a specific location at the spindle midzone. A chromosome passenger complex is a protein complex that contains the BIR-domain-containing protein Survivin, Aurora B kinase, INCENP and Borealin, and coordinates various events based on its location to different structures during the course of mitosis. The spindle midzone is the area in the center of the spindle where the spindle microtubules from opposite poles overlap.
A cellular protein complex localization that acts on a chromosome passenger complex; as a result, the complex is transported to, or maintained in, a specific location at the spindle midzone. A chromosome passenger complex is a protein complex that contains the BIR-domain-containing protein Survivin, Aurora B kinase, INCENP and Borealin, and coordinates various events based on its location to different structures during the course of mitosis. The spindle midzone is the area in the center of the spindle where the spindle microtubules from opposite poles overlap.
A cellular protein complex localization that acts on a chromosome passenger complex; as a result, the complex is transported to, or maintained in, a specific location at the spindle midzone. A chromosome passenger complex is a protein complex that contains the BIR-domain-containing protein Survivin, Aurora B kinase, INCENP and Borealin, and coordinates various events based on its location to different structures during the course of mitosis. The spindle midzone is the area in the center of the spindle where the spindle microtubules from opposite poles overlap.
The process in which the developmental fate of a cell becomes restricted such that it will develop into a eosinophil cell. A eosinophil is any of the immature or mature forms of a granular leukocyte with a nucleus that usually has two lobes connected by one or more slender threads of chromatin, and cytoplasm containing coarse, round granules that are uniform in size and which can be stained by the dye eosin.
The process whose specific outcome is the progression of a megakaryocyte cell over time, from its formation to the mature structure. Megakaryocyte development does not include the steps involved in committing a cell to a megakaryocyte fate. A megakaryocyte is a giant cell 50 to 100 micron in diameter, with a greatly lobulated nucleus, found in the bone marrow.
The process involved in the specification of identity of an eosinophil cell. Once specification has taken place, a cell will be committed to differentiate down a specific pathway if left in its normal environment.
The cell fate determination process in which a cell becomes capable of differentiating autonomously into an eosinophil cell regardless of its environment; upon determination, the cell fate cannot be reversed.
A protein complex that associates dynamically with the vacuolar membrane, and is proposed to have a role in membrane-associated trafficking or regulatory processes. In S. cerevisiae the complex contains Seh1p, Sec13p, Npr2p, Npr3p, Iml1p, Mtc5p, Rtc1p, and Sea4p.
A protein complex that associates dynamically with the vacuolar membrane, and is proposed to have a role in membrane-associated trafficking or regulatory processes. In S. cerevisiae the complex contains Seh1p, Sec13p, Npr2p, Npr3p, Iml1p, Mtc5p, Rtc1p, and Sea4p.
The series of molecular signals generated as a consequence of a glial cell-derived neurotrophic factor receptor binding to one of its physiological ligands.
The series of molecular signals generated as a consequence of a glial cell-derived neurotrophic factor receptor binding to one of its physiological ligands.
The series of molecular signals generated as a consequence of a glial cell-derived neurotrophic factor receptor binding to one of its physiological ligands.
The series of molecular signals generated as a consequence of a glial cell-derived neurotrophic factor receptor binding to one of its physiological ligands.
A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
The chemical reactions and pathways involving dITP (deoxyinosine triphosphate (2'-deoxyinosine 5'-triphosphate). dITP is a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
The chemical reactions and pathways involving dITP (deoxyinosine triphosphate (2'-deoxyinosine 5'-triphosphate). dITP is a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
The chemical reactions and pathways involving dITP (deoxyinosine triphosphate (2'-deoxyinosine 5'-triphosphate). dITP is a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
The chemical reactions and pathways involving dITP (deoxyinosine triphosphate (2'-deoxyinosine 5'-triphosphate). dITP is a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
The chemical reactions and pathways involving dITP (deoxyinosine triphosphate (2'-deoxyinosine 5'-triphosphate). dITP is a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
The chemical reactions and pathways resulting in the breakdown of dITP, a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
The chemical reactions and pathways resulting in the breakdown of dITP, a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
The chemical reactions and pathways resulting in the breakdown of dITP, a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
The chemical reactions and pathways resulting in the breakdown of dITP, a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
The chemical reactions and pathways resulting in the breakdown of dITP, a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
The chemical reactions and pathways resulting in the breakdown of dITP, a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
The chemical reactions and pathways resulting in the breakdown of dITP, a deoxyinosine phosphate compound having a triphosphate group at the 5'-position.
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 potassium ion 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 potassium ion stimulus.
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 potassium ion stimulus.
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 potassium ion stimulus.
A protein complex that consists of an alphav-beta3 integrin complex bound to protein kinase C alpha.
A protein complex that consists of an alphav-beta3 integrin complex bound to protein kinase C alpha.
A protein complex that consists of an alphav-beta3 integrin complex bound to insulin-like growth factor-1 (IGF-1) and type I insulin-like growth factor receptor (IGF1R). IGF1R is a heterotetramer that consists of two alpha-subunits and two beta-subunits.
A protein complex that consists of an alphav-beta3 integrin complex bound to high mobility group box 1 protein.
A protein complex that consists of an alphav-beta3 integrin complex bound to high mobility group box 1 protein.
A region of the cilium between the basal body and proximal segment that is characterized by Y-shaped assemblages that connect axonemal microtubules to the ciliary membrane. The ciliary transition zone appears to function as a gate that controls ciliary membrane composition and separates the cytosol from the ciliary plasm.
A region of the cilium between the basal body and proximal segment that is characterized by Y-shaped assemblages that connect axonemal microtubules to the ciliary membrane. The ciliary transition zone appears to function as a gate that controls ciliary membrane composition and separates the cytosol from the ciliary plasm.
A region of the cilium between the basal body and proximal segment that is characterized by Y-shaped assemblages that connect axonemal microtubules to the ciliary membrane. The ciliary transition zone appears to function as a gate that controls ciliary membrane composition and separates the cytosol from the ciliary plasm.
Catalysis of the reaction: dITP + H2O = dIMP + diphosphate.
Catalysis of the reaction: dITP + H2O = dIMP + diphosphate.
Catalysis of the reaction: dITP + H2O = dIMP + diphosphate.
A protein deubiquitination process in which a K11-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 11 of the ubiquitin monomers, is removed from a protein.
A protein deubiquitination process in which a K11-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 11 of the ubiquitin monomers, is removed from a protein.
A series of molecular signals generated as a consequence of a nucleotide-binding domain, leucine rich repeat containing receptor (NLR) binding to one of its physiological ligands. NLRs are cytoplasmic receptors defined by their tripartite domain architecture that contains: a variable C-terminus, a middle nucleotide-binding domain, and a LRR domain that is variable in the repeats composition and number. The NLR signaling pathway begins with binding of a ligand to a NLR receptor and ends with regulation of a downstream cellular process.
A series of molecular signals generated as a consequence of a nucleotide-binding domain, leucine rich repeat containing receptor (NLR) binding to one of its physiological ligands. NLRs are cytoplasmic receptors defined by their tripartite domain architecture that contains: a variable C-terminus, a middle nucleotide-binding domain, and a LRR domain that is variable in the repeats composition and number. The NLR signaling pathway begins with binding of a ligand to a NLR receptor and ends with regulation of a downstream cellular process.
A series of molecular signals generated as a consequence of a nucleotide-binding domain, leucine rich repeat containing receptor (NLR) binding to one of its physiological ligands. NLRs are cytoplasmic receptors defined by their tripartite domain architecture that contains: a variable C-terminus, a middle nucleotide-binding domain, and a LRR domain that is variable in the repeats composition and number. The NLR signaling pathway begins with binding of a ligand to a NLR receptor and ends with regulation of a downstream cellular process.
A series of molecular signals generated as a consequence of a nucleotide-binding domain, leucine rich repeat containing receptor (NLR) binding to one of its physiological ligands. NLRs are cytoplasmic receptors defined by their tripartite domain architecture that contains: a variable C-terminus, a middle nucleotide-binding domain, and a LRR domain that is variable in the repeats composition and number. The NLR signaling pathway begins with binding of a ligand to a NLR receptor and ends with regulation of a downstream cellular process.
A series of molecular signals generated as a consequence of a nucleotide-binding domain, leucine rich repeat containing receptor (NLR) binding to one of its physiological ligands. NLRs are cytoplasmic receptors defined by their tripartite domain architecture that contains: a variable C-terminus, a middle nucleotide-binding domain, and a LRR domain that is variable in the repeats composition and number. The NLR signaling pathway begins with binding of a ligand to a NLR receptor and ends with regulation of a downstream cellular process.
A series of molecular signals generated as a consequence of a nucleotide-binding domain, leucine rich repeat containing receptor (NLR) binding to one of its physiological ligands. NLRs are cytoplasmic receptors defined by their tripartite domain architecture that contains: a variable C-terminus, a middle nucleotide-binding domain, and a LRR domain that is variable in the repeats composition and number. The NLR signaling pathway begins with binding of a ligand to a NLR receptor and ends with regulation of a downstream cellular process.
The process in which lactate is transported across a membrane. Lactate is 2-hydroxypropanoate, CH3-CHOH-COOH; L(+)-lactate is formed by anaerobic glycolysis in animal tissues, and DL-lactate is found in sour milk, molasses and certain fruit juices.
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 copper ions.
The process in which the association between sister chromatids of a replicated chromosome along the length of the centromeric region is maintained as chromosomes condense, attach to the spindle in a bipolar orientation, and congress to the metaphase plate during a meiotic cell cycle.
The process in which the association between sister chromatids of a replicated chromosome along the length of the centromeric region is maintained as chromosomes condense, attach to the spindle in a bipolar orientation, and congress to the metaphase plate during a meiotic cell cycle.
The process in which the association between sister chromatids of a replicated chromosome along the length of the centromeric region is maintained as chromosomes condense, attach to the spindle in a bipolar orientation, and congress to the metaphase plate during a meiotic cell cycle.
The process in which the association between sister chromatids of a replicated chromosome along the length of the chromosome arms, is maintained as chromosomes condense, attach to the spindle in a bipolar orientation, and congress to the metaphase plate during a meiotic cell cycle.
The process in which the association between sister chromatids of a replicated chromosome along the length of the chromosome arms, is maintained as chromosomes condense, attach to the spindle in a bipolar orientation, and congress to the metaphase plate during a meiotic cell cycle.
Interacting selectively and non-covalently with a DED domain (death effector domain) of a protein, a homotypic protein interaction module composed of a bundle of six alpha-helices that is related in structure to the death domain (DD).
The process whose specific outcome is the progression of a nail over time, from its formation to the mature structure. A nail is a horn-like envelope covering the outer end of a finger or toe, and consists of the nail plate, the nail matrix and the nail bed below it, and the grooves surrounding it.
The directed movement of lactate across a plasma membrane.
The process, occurring in the embryo, by which the anatomical structures of a nail plate are generated and organized. The nail plate is the hard and translucent portion of the nail, composed of keratin, and serves to protect the tips of digits.
The process in which a relatively unspecialized cell acquires specialized features of an amacrine cell, an interneuron generated in the inner nuclear layer (INL) of the vertebrate retina. Amacrine cells integrate, modulate, and interpose a temporal domain in the visual message presented to the retinal ganglion cells, with which they synapse in the inner plexiform layer. Amacrine cells lack large axons.
The rhythmic process of defecation that consists of an intestinal oscillator which regulates calcium waves. These waves in turn control a stereotypical, three-part pattern of muscle contractions. In some organisms, defecation can recur with a regularity more frequent than every 24 hours. For example, in a well-fed Caenorhabditis elegans, the defecation motor program occurs approximately every 45 seconds, and is temperature- and touch-compensated.
The rhythmic process of defecation that consists of an intestinal oscillator which regulates calcium waves. These waves in turn control a stereotypical, three-part pattern of muscle contractions. In some organisms, defecation can recur with a regularity more frequent than every 24 hours. For example, in a well-fed Caenorhabditis elegans, the defecation motor program occurs approximately every 45 seconds, and is temperature- and touch-compensated.
The rhythmic process of defecation that consists of an intestinal oscillator which regulates calcium waves. These waves in turn control a stereotypical, three-part pattern of muscle contractions. In some organisms, defecation can recur with a regularity more frequent than every 24 hours. For example, in a well-fed Caenorhabditis elegans, the defecation motor program occurs approximately every 45 seconds, and is temperature- and touch-compensated.
The rhythmic process of defecation that consists of an intestinal oscillator which regulates calcium waves. These waves in turn control a stereotypical, three-part pattern of muscle contractions. In some organisms, defecation can recur with a regularity more frequent than every 24 hours. For example, in a well-fed Caenorhabditis elegans, the defecation motor program occurs approximately every 45 seconds, and is temperature- and touch-compensated.
The process in which a relatively unspecialized cell acquires specialized structural and/or functional features of an enteroendocrine cell. Enteroendocrine cells are hormonally active epithelial cells in the gut that constitute the diffuse neuroendocrine system.
The chemical reactions and pathways resulting in the formation of arabinan, a polysaccharide composed of arabinose residues.
Catalysis of the hydrolysis of terminal 1,4-beta-linkages of N-acetyl-D-glucosamine (GlcNAc) polymers of chitin and chitodextrins. Typically, exochitinases progressively cleave off two subunits from the reducing or non-reducing ends of the chitin chain.
The process in which a relatively unspecialized cell acquires specialized features of a vascular smooth muscle cell.
The process in which a relatively unspecialized cell acquires specialized features of a vascular smooth muscle cell.
The process in which a relatively unspecialized cell acquires specialized features of a smooth muscle cell surrounding the aorta.
Catalysis of the reaction: isoguanine + H2O = xanthine + NH3.
Catalysis of the reaction: isoguanine + H2O = xanthine + NH3.
The attachment of a developing otolith to the kinocilia of tether cells in the inner ear.
The directed movement of an organism out of the body, tissues or cells of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The directed movement of an organism out of a cell of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The directed movement of an organism out of a cell 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 modulates the frequency, rate or extent of platelet aggregation in another organism. Platelet aggregation is the adhesion of one platelet to one or more other platelets via adhesion molecules.
Any process in which an organism modulates the frequency, rate or extent of platelet aggregation in another organism. Platelet aggregation is the adhesion of one platelet to one or more other platelets via adhesion molecules.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of platelet aggregation in a second organism.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of platelet aggregation in a second organism.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of platelet aggregation in a second organism.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of platelet aggregation in a second organism.
Any process in which an organism activates, maintains or increases the frequency, rate or extent of platelet aggregation in another organism.
Any process in which an organism activates, maintains or increases the frequency, rate or extent of platelet aggregation in another organism.
Any process in which an organism modulates the frequency, rate or extent of blood mast cell degranulation in another organism. Mast cell degranulation is the regulated exocytosis of secretory granules containing preformed mediators such as histamine, serotonin, and neutral proteases by a mast cell.
Any process in which an organism increases the frequency, rate or extent of blood mast cell degranulation in another organism.
Any process in which an organism increases the frequency, rate or extent of blood mast cell degranulation in another organism.
The chemical reactions and pathways performed by an organism resulting in the hydrolysis of proteins in another organism by cleavage of their peptide bonds.
The regulated release of parathyroid hormone into the circulatory system.
The regulated release of parathyroid hormone into the circulatory system.
The regulated release of parathyroid hormone into the circulatory system.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of blood coagulation in another organism. Blood coagulation is the sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot.
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 lack of contact with other members of the same species.
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 lack of contact with other members of the same species.
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 being rendered immobile.
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 being rendered immobile.
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 being rendered immobile.
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 being rendered immobile.
The progression of the aorta over time, from its initial formation to the mature structure. An aorta is an artery that carries blood from the heart to other parts of the body.
The progression of the ascending aorta over time, from its initial formation to the mature structure. The ascending aorta is the portion of the aorta in a two-pass circulatory system that lies between the heart and the arch of aorta. In a two-pass circulatory system blood passes twice through the heart to supply the body once.
The progression of the descending aorta over time, from its initial formation to the mature structure. The descending aorta is the portion of the aorta in a two-pass circulatory system from the arch of aorta to the point where it divides into the common iliac arteries. In a two-pass circulatory system blood passes twice through the heart to supply the body once.
The progression of the dorsal aorta over time, from its initial formation to the mature structure. The dorsal aorta is a blood vessel in a single-pass circulatory system that carries oxygenated blood from the gills to the rest of the body. In a single-pass circulatory system blood passes once through the heart to supply the body once.
The progression of the ventral aorta over time, from its initial formation to the mature structure. The ventral aorta is a blood vessel in a single-pass circulatory system that carries de-oxygenated blood from the heart to the gills. In a single-pass circulatory system blood passes once through the heart to supply the body once.
The process in which the anatomical structures of an aorta are generated and organized. An aorta is an artery that carries blood from the heart to other parts of the body.
The process in which the anatomical structures of the ascending aorta are generated and organized. The ascending aorta is the portion of the aorta in a two-pass circulatory system that lies between the heart and the arch of aorta. In a two-pass circulatory system blood passes twice through the heart to supply the body once.
The process in which the anatomical structures of the descending aorta are generated and organized. The descending aorta is the portion of the aorta in a two-pass circulatory system from the arch of aorta to the point where it divides into the common iliac arteries. In a two-pass circulatory system blood passes twice through the heart to supply the body once.
The process in which the anatomical structures of the dorsal aorta are generated and organized. The dorsal aorta is a blood vessel in a single-pass circulatory system that carries oxygenated blood from the gills to the rest of the body. In a single-pass circulatory system blood passes once through the heart to supply the body once.
The process in which the anatomical structures of the ventral aorta are generated and organized. The ventral aorta is a blood vessel in a single-pass circulatory system that carries de-oxygenated blood from the heart to the gills. In a single-pass circulatory system blood passes once through the heart to supply the body once.
The process in which a relatively unspecialized cell acquires specialized features of a skeletal muscle cell, a somatic cell located in skeletal muscle.
Any process in which an organism effects a change in the frequency, rate or extent of the activity of a calcium channel in another organism.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a calcium channel in another organism.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a calcium channel in another organism.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a calcium channel in another organism.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a voltage-gated calcium channel in another organism. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a voltage-gated calcium channel in another organism. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a voltage-gated calcium channel in another organism. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a voltage-gated calcium channel in another organism. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a voltage-gated calcium channel in another organism. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a voltage-gated calcium channel in another organism. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a low voltage-gated calcium channel in another organism. A low voltage-gated channel is a channel whose open state is dependent on low voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a low voltage-gated calcium channel in another organism. A low voltage-gated channel is a channel whose open state is dependent on low voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a low voltage-gated calcium channel in another organism. A low voltage-gated channel is a channel whose open state is dependent on low voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a low voltage-gated calcium channel in another organism. A low voltage-gated channel is a channel whose open state is dependent on low voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a low voltage-gated calcium channel in another organism. A low voltage-gated channel is a channel whose open state is dependent on low voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a high voltage-gated calcium channel in another organism. A high voltage-gated channel is a channel whose open state is dependent on high voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a high voltage-gated calcium channel in another organism. A high voltage-gated channel is a channel whose open state is dependent on high voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a high voltage-gated calcium channel in another organism. A high voltage-gated channel is a channel whose open state is dependent on high voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a high voltage-gated calcium channel in another organism. A high voltage-gated channel is a channel whose open state is dependent on high voltage across the membrane in which it is embedded.
Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a high voltage-gated calcium channel in another organism. A high voltage-gated channel is a channel whose open state is dependent on high voltage across the membrane in which it is embedded.
The controlled breakdown of a desmosome. A desmosome is a patch-like intercellular junction found in vertebrate tissues, consisting of parallel zones of two cell membranes, separated by an space of 25-35 nm, and having dense fibrillar plaques in the subjacent cytoplasm.
The morphogenetic process in which the foramen ovale closes after birth, to prevent blood flow between the right and left atria. In the fetal heart, the foramen ovale allows blood to enter the left atrium from the right atrium. Closure of the foramen ovale after birth stops this blood flow.
Interacting selectively and non-covalently with flurbiprofen.
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 vascular endothelial growth factor stimulus.
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 vascular endothelial growth factor stimulus.
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 vascular endothelial growth factor stimulus.
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 vascular endothelial growth factor stimulus.
Interacting selectively and non-covalently with a region containing frequent adenine and uridine bases within the 3' untranslated region of a mRNA molecule.
The regulated release of chemokine (C-C motif) ligand 2 (CCL2) from a cell.
The process in which a rRNA, ribosomal ribonucleic acid, is transported from the cytosol, into the mitochondrial matrix.
The process in which a rRNA, ribosomal ribonucleic acid, is transported from the cytosol, into the mitochondrial matrix.
The process in which a rRNA, ribosomal ribonucleic acid, transported from the cytosol, into the mitochondrial matrix.
The process in which a rRNA, ribosomal ribonucleic acid, transported from the cytosol, into the mitochondrial matrix.
The regulated release of any steroid that acts as a hormone into the circulatory system.
The regulated release of any corticosteroid hormone into the circulatory system.
The regulated release of any mineralocorticoid into the circulatory system. Mineralocorticoids are a class of steroid hormones that regulate water and electrolyte metabolism.
The regulated release of aldosterone into the circulatory system. Aldosterone is a pregnane-based steroid hormone produced by the outer-section (zona glomerulosa) of the adrenal cortex in the adrenal gland, and acts on the distal tubules and collecting ducts of the kidney to cause the conservation of sodium, secretion of potassium, increased water retention, and increased blood pressure. The overall effect of aldosterone is to increase reabsorption of ions and water in the kidney.
The regulated release of any glucocorticoid hormone into the circulatory system. Glucocorticoids are a class of steroid hormones that regulate a variety of physiological processes, in particular control of the concentration of glucose in blood.
The regulated release of corticosterone into the circulatory system. Corticosterone is a 21-carbon steroid hormone of the corticosteroid type produced in the cortex of the adrenal glands.
The regulated release of an androgen into the circulatory system. Androgens are steroid hormones that stimulate or control the development and maintenance of masculine characteristics in vertebrates.
The regulated release of testosterone into the circulatory system. Testosterone is an androgen having 17beta-hydroxy and 3-oxo groups, together with unsaturation at C-4-C-5.
The regulated release of estrogen into the circulatory system. Estrogen is a steroid hormone that stimulates or controls the development and maintenance of female sex characteristics in mammals.
The regulated release of estradiol into the circulatory system.
Interacting selectively and non-covalently with a microsatellite, a repeat_region in DNA containing repeat units (2 to 4 base pairs) that is repeated multiple times in tandem.
Interacting selectively and non-covalently with a microsatellite, a repeat_region in DNA containing repeat units (2 to 4 base pairs) that is repeated multiple times in tandem.
Interacting selectively and non-covalently with a microsatellite, a repeat_region in DNA containing repeat units (2 to 4 base pairs) that is repeated multiple times in tandem.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of peptidase activity, the catalysis of the hydrolysis of peptide bonds in a protein, in a second organism.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of peptidase activity, the catalysis of the hydrolysis of peptide bonds in a protein, in a second organism.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of peptidase activity, the catalysis of the hydrolysis of peptide bonds in a protein, in a second organism.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of peptidase activity, the catalysis of the hydrolysis of peptide bonds in a protein, in a second organism.
Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of peptidase activity, the catalysis of the hydrolysis of peptide bonds in a protein, in a second organism.
The regulated release of androstenedione (androst-4-ene-3,17-dione) into the circulatory system.
The regulated release of dehydroepiandrosterone (3beta-hydroxyandrost-5-en-17-one) into the circulatory system.
The regulated release of dehydroepiandrosterone (3beta-hydroxyandrost-5-en-17-one) into the circulatory system.
The regulated release of dehydroepiandrosterone (3beta-hydroxyandrost-5-en-17-one) into the circulatory system.
The regulated release of estrone into the circulatory system.
The regulated release of estrone into the circulatory system.
The appearance of a perforin protein due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The set of processes involved in identifying and degrading defective or aberrant non-coding RNA transcripts (ncRNAs) within the mitochondrion.
The set of processes involved in identifying and degrading defective or aberrant non-coding RNA transcripts (ncRNAs) within the mitochondrion.
The set of processes involved in identifying and degrading defective or aberrant non-coding RNA transcripts (ncRNAs) within the mitochondrion.
The set of processes involved in identifying and degrading messenger RNA (mRNA) within the mitochondrion.
The set of processes involved in identifying and degrading messenger RNA (mRNA) within the mitochondrion.
The set of processes involved in identifying and degrading messenger RNA (mRNA) within the mitochondrion.
Any process that modulates the frequency, rate or extent of gluconeogenesis, by regulation of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of gluconeogenesis, by regulation of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of gluconeogenesis, by regulation of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of gluconeogenesis, by regulation of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of gluconeogenesis, by regulation of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of gluconeogenesis by stopping, preventing, or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of oligopeptide transport, by regulation of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of oligopeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of oligopeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of oligopeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of oligopeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of oligopeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of oligopeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that stops, prevents or reduces the frequency, rate or extent of oligopeptide transport by stopping, preventing or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that stops, prevents or reduces the frequency, rate or extent of oligopeptide transport by stopping, preventing or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that stops, prevents or reduces the frequency, rate or extent of oligopeptide transport by stopping, preventing or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that stops, prevents or reduces the frequency, rate or extent of oligopeptide transport by stopping, preventing or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that stops, prevents or reduces the frequency, rate or extent of oligopeptide transport by stopping, preventing or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of dipeptide transport, by regulation of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of dipeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of dipeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of dipeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of dipeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of dipeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of dipeptide transport by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that stops, prevents or reduces the frequency, rate or extent of dipeptide transport by stopping, preventing or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that stops, prevents or reduces the frequency, rate or extent of dipeptide transport by stopping, preventing or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that stops, prevents or reduces the frequency, rate or extent of dipeptide transport by stopping, preventing or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that stops, prevents or reduces the frequency, rate or extent of dipeptide transport by stopping, preventing or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that stops, prevents or reduces the frequency, rate or extent of dipeptide transport by stopping, preventing or reducing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of the breakdown of starch, by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of the breakdown of starch, by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of the breakdown of starch, by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of the breakdown of starch, by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of the breakdown of starch, by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of the breakdown of starch, by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of the breakdown of starch, by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the breakdown of starch, by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the breakdown of starch, by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the breakdown of starch, by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the breakdown of starch, by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the breakdown of starch, by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the breakdown of starch, by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the breakdown of starch, by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of the glyoxylate cycle by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of the glyoxylate cycle by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of the glyoxylate cycle by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the glyoxylate cycle by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the glyoxylate cycle by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the glyoxylate cycle by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the glyoxylate cycle by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the glyoxylate cycle by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the glyoxylate cycle by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the glyoxylate cycle by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the glyoxylate cycle by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the glyoxylate cycle by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the glyoxylate cycle by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of the glyoxylate cycle by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of ergosterol biosynthetic process by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of ergosterol biosynthetic process by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of ergosterol biosynthetic process by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of ergosterol biosynthetic process by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of ergosterol biosynthetic process by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of ergosterol biosynthetic process by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of ergosterol biosynthetic process by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of ergosterol biosynthetic process by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of ergosterol biosynthetic process by modulating the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of ergosterol biosynthesis by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
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 interleukin-13 stimulus.
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 interleukin-13 stimulus.
The evagination of a Golgi membrane, resulting in formation of a COPI-coated vesicle.
Remodeling the acyl chains of premature (de novo synthesized) cardiolipin (1,3-bis(3-phosphatidyl)glycerol), through sequential deacylation and re-acylation reactions, to generate mature cardiolipin containing high-levels of unsaturated fatty acids.
Remodeling the acyl chains of premature (de novo synthesized) cardiolipin (1,3-bis(3-phosphatidyl)glycerol), through sequential deacylation and re-acylation reactions, to generate mature cardiolipin containing high-levels of unsaturated fatty acids.
Remodeling the acyl chains of premature (de novo synthesized) cardiolipin (1,3-bis(3-phosphatidyl)glycerol), through sequential deacylation and re-acylation reactions, to generate mature cardiolipin containing high-levels of unsaturated fatty acids.
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 protein that is not folded in its correct three-dimensional structure.
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 protein that is not folded in its correct three-dimensional structure.
Any process that modulates the frequency, rate or extent of sterol import, by regulation of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of sterol import, by regulation of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of sterol import, by regulation of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of sterol import, by regulation of transcription from an RNA polymerase II promoter.
Any process that modulates the frequency, rate or extent of sterol import, by regulation of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that activates or increases the frequency, rate or extent of sterol import by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
The removal of phosphoric residues from peptidyl-O-phospho-L-threonine to form peptidyl-threonine.
The removal of phosphoric residues from peptidyl-O-phospho-L-histidine to form peptidyl-histidine.
Selective degradation of protein aggregates by macroautophagy.
The microtubule organizing center that forms as part of the meiotic cell cycle; functionally homologous to the animal cell centrosome.
The chemical reactions and pathways resulting in the breakdown of carbamoyl phosphate, an intermediate in the urea cycle and other nitrogen compound metabolic pathways.
The chemical reactions and pathways resulting in the breakdown of carbamoyl phosphate, an intermediate in the urea cycle and other nitrogen compound metabolic pathways.
The chemical reactions and pathways resulting in the breakdown of carbamoyl phosphate, an intermediate in the urea cycle and other nitrogen compound metabolic pathways.
A heterodimeric transcription factor complex composed of proteins from the c-Fos, c-Jun, activating transcription factor (ATF) or JDP families. The subunits contain a basic leucine zipper (bZIP) domain that is essential for dimerization and DNA binding. Jun-Fos heterodimers bind preferentially to a heptamer consensus sequence (TPA responsive element (TRE)), whereas Jun-ATF dimers bind the cyclic AMP responsive element (CRE) to regulate transcription of target genes.
A heterodimeric transcription factor complex composed of proteins from the c-Fos, c-Jun, activating transcription factor (ATF) or JDP families. The subunits contain a basic leucine zipper (bZIP) domain that is essential for dimerization and DNA binding. Jun-Fos heterodimers bind preferentially to a heptamer consensus sequence (TPA responsive element (TRE)), whereas Jun-ATF dimers bind the cyclic AMP responsive element (CRE) to regulate transcription of target genes.
A heterodimeric transcription factor complex composed of proteins from the c-Fos, c-Jun, activating transcription factor (ATF) or JDP families. The subunits contain a basic leucine zipper (bZIP) domain that is essential for dimerization and DNA binding. Jun-Fos heterodimers bind preferentially to a heptamer consensus sequence (TPA responsive element (TRE)), whereas Jun-ATF dimers bind the cyclic AMP responsive element (CRE) to regulate transcription of target genes.
A heterodimeric transcription factor complex composed of proteins from the c-Fos, c-Jun, activating transcription factor (ATF) or JDP families. The subunits contain a basic leucine zipper (bZIP) domain that is essential for dimerization and DNA binding. Jun-Fos heterodimers bind preferentially to a heptamer consensus sequence (TPA responsive element (TRE)), whereas Jun-ATF dimers bind the cyclic AMP responsive element (CRE) to regulate transcription of target genes.
The removal of sugar residues from a glycosylated protein that contributes to the breakdown of a glycoprotein.
The modification of histone H2A by the addition of an phosphate group to a serine residue at position 139 of the histone.
Catalysis of the transfer of a phosphate group to the serine-139 residue of the C-terminal tail of histone H2A.
The process in which a relatively unspecialized cell acquires specialized features of a tongue muscle cell.
Any process that modulates the processes that arise as an organism progresses toward the end of its lifespan that results in a decline in behavioral activities such as locomotory behavior, and learning or memory.
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 trichostatin A stimulus.
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 trichostatin A stimulus.
A transcriptionally-silent heterochromatin structure present in senescent cells. Contains the condensed chromatin of one chromosome and is enriched for histone modifications. Thought to repress expression of proliferation-promoting genes.
A transcriptionally-silent heterochromatin structure present in senescent cells. Contains the condensed chromatin of one chromosome and is enriched for histone modifications. Thought to repress expression of proliferation-promoting genes.
The assembly of chromatin into senescence-associated heterochromatin foci (SAHF), transcriptionally-silent heterochromatin structures present in senescent cells, containing the condensed chromatin of one chromosome, and enriched for histone modifications. Formation of these chromatin structures is thought to repress expression of proliferation-promoting genes.
The assembly of chromatin into senescence-associated heterochromatin foci (SAHF), transcriptionally-silent heterochromatin structures present in senescent cells, containing the condensed chromatin of one chromosome, and enriched for histone modifications. Formation of these chromatin structures is thought to repress expression of proliferation-promoting genes.
The assembly of chromatin into senescence-associated heterochromatin foci (SAHF), transcriptionally-silent heterochromatin structures present in senescent cells, containing the condensed chromatin of one chromosome, and enriched for histone modifications. Formation of these chromatin structures is thought to repress expression of proliferation-promoting genes.
The process in which a relatively unspecialized cell acquires the specialized features of an endoderm cell, a cell of the inner of the three germ layers of the embryo.
The multiplication or reproduction of chondrocytes by cell division, resulting in the expansion of their population. A chondrocyte is a polymorphic cell that forms cartilage.
The multiplication or reproduction of chondrocytes by cell division, resulting in the expansion of their population. A chondrocyte is a polymorphic cell that forms cartilage.
The process whose specific outcome is the progression of a tendon over time, from its formation to the mature structure. A tendon is a fibrous, strong, connective tissue that connects muscle to bone or integument and is capable of withstanding tension. Tendons and muscles work together to exert a pulling force.
The process in which a relatively unspecialized cell acquires the specialized features of a tendon cell. Tendon cell are elongated fibrocytes in which the cytoplasm is stretched between the collagen fibres of the tendon. Tendon cells have a central cell nucleus with a prominent nucleolus, a well-developed rough endoplasmic reticulum, and are responsible for synthesis and turnover of tendon fibres and ground substance.
The process in which a relatively unspecialized cell acquires the specialized features of a tendon cell. Tendon cell are elongated fibrocytes in which the cytoplasm is stretched between the collagen fibres of the tendon. Tendon cells have a central cell nucleus with a prominent nucleolus, a well-developed rough endoplasmic reticulum, and are responsible for synthesis and turnover of tendon fibres and ground substance.
Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of nitric oxide (NO).
The process that gives rise to a tendon. This process pertains to the initial formation of a tendon from unspecified parts.
The process whose specific outcome is the progression of the deltoid tuberosity over time, from its formation to the mature structure. The deltoid tuberosity is the region on the shaft of the humerus to which the deltoid muscle attaches. The deltoid tuberosity develops through endochondral ossification in a two-phase process; an initiating tendon-dependent phase, and a muscle-dependent growth phase.
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 myofibril being extended beyond its slack length.
The series of events by which a muscle stretch stimulus is received by a cell and converted into a molecular signal.
Thin cylindrical membrane-covered projection on the surface of a rhabdomere.
The portion of the plasma membrane surrounding a microvillus of a rhabdomere.
The chemical reactions and pathways resulting in the formation of 7,8-dihydroneopterin 3'-triphosphate.
The chemical reactions and pathways resulting in the formation of 7,8-dihydroneopterin 3'-triphosphate.
The chemical reactions and pathways resulting in the formation of 7,8-dihydroneopterin 3'-triphosphate.
The chemical reactions and pathways resulting in the formation of 7,8-dihydroneopterin 3'-triphosphate.
The chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesise other tetrahydrofolate molecules.
A small subcellular vesicle, surrounded by a membrane, in the pellicle of ciliate protozoans that discharges a mucus-like secretion.
The chemical reactions and pathways resulting in the formation of pyridoxal 5'-phosphate, the active form of vitamin B6, from simpler components.
The chemical reactions and pathways resulting in the formation of pyridoxal 5'-phosphate, the active form of vitamin B6, from simpler components.
The chemical reactions and pathways resulting in the formation of pyridoxal 5'-phosphate, the active form of vitamin B6, from simpler components.
The chemical reactions and pathways resulting in the formation of pyridoxal 5'-phosphate, the active form of vitamin B6, from simpler components.
The chemical reactions and pathways resulting in the formation of pyridoxal 5'-phosphate, the active form of vitamin B6, from simpler components.
The chemical reactions and pathways resulting in the formation of pyridoxal 5'-phosphate, the active form of vitamin B6, from simpler components.
Interacting selectively and non-covalently with pre-messenger RNA (pre-mRNA), an intermediate molecule between DNA and protein that may contain introns and, at least in part, encodes one or more proteins. Introns are removed from pre-mRNA to form a mRNA molecule.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter 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).
Interacting selectively and non-covalently with the GAF domain of a protein.
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 macrophage colony-stimulating factor 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 macrophage colony-stimulating factor 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 macrophage colony-stimulating factor stimulus.
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 macrophage colony-stimulating factor stimulus.
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 macrophage colony-stimulating factor stimulus.
A body present in the cytoplasm of some dinoflagellates, which is the source of bioluminescence; emits light on acidification in the presence of oxygen.
Catalysis of the reaction: S-adenosyl-L-methionine + protein L-glutamine = S-adenosyl-L-homocysteine + protein N-methyl-L-glutamine.
A process in which a protein is transported to, or maintained in, a location within an endosome.
A process in which a protein is transported to, or maintained in, a location within an endosome.
The inner, i.e. lumen-facing, lipid bilayer of the cyanelle envelope; also faces the cyanelle stroma.
The outer, i.e. cytoplasm-facing, lipid bilayer of the cyanelle envelope.
The region between the inner and outer lipid bilayers of the cyanelle envelope; includes the peptidoglycan layer.
The region between the inner and outer lipid bilayers of the cyanelle envelope; includes the peptidoglycan layer.
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 interleukin-3 stimulus.
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 interleukin-3 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 erythropoietin stimulus. Erythropoietin is a glycoprotein hormone that controls erythropoiesis.
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 erythropoietin stimulus.
An transient hybrid organelle formed by fusion of a late endosome with a lysosome, and in which active degradation takes place.
The lipid bilayer surrounding an endolysosome. An endolysosome is a transient hybrid organelle formed by fusion of a late endosome with a lysosome.
The volume enclosed by the membrane of an endolysosome. An endolysosome is a transient hybrid organelle formed by fusion of a late endosome with a lysosome.
The process in which the anatomical structures of a limb joint are generated and organized. A limb joint is a flexible region that separates the rigid sections of a limb to allow movement in a controlled manner.
The process in which the anatomical structures of a limb joint are generated and organized. A limb joint is a flexible region that separates the rigid sections of a limb to allow movement in a controlled manner.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 7 (TMPRSS7); formation of the complex inhibits the serine protease activity of transmembrane protease serine 7.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 7 (TMPRSS7); formation of the complex inhibits the serine protease activity of transmembrane protease serine 7.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 7 (TMPRSS7); formation of the complex inhibits the serine protease activity of transmembrane protease serine 7.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 7 (TMPRSS7); formation of the complex inhibits the serine protease activity of transmembrane protease serine 7.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 7 (TMPRSS7); formation of the complex inhibits the serine protease activity of transmembrane protease serine 7.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 7 (TMPRSS7); formation of the complex inhibits the serine protease activity of transmembrane protease serine 7.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 11E (TMPRSS11E); formation of the complex inhibits the serine protease activity of transmembrane protease serine 11E.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 11E (TMPRSS11E); formation of the complex inhibits the serine protease activity of transmembrane protease serine 11E.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 11E (TMPRSS11E); formation of the complex inhibits the serine protease activity of transmembrane protease serine 11E.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 11E (TMPRSS11E); formation of the complex inhibits the serine protease activity of transmembrane protease serine 11E.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 11E (TMPRSS11E); formation of the complex inhibits the serine protease activity of transmembrane protease serine 11E.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and tissue-type plasminogen activator (PLAT); formation of the complex inhibits the serine protease activity of tissue-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and tissue-type plasminogen activator (PLAT); formation of the complex inhibits the serine protease activity of tissue-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and tissue-type plasminogen activator (PLAT); formation of the complex inhibits the serine protease activity of tissue-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and tissue-type plasminogen activator (PLAT); formation of the complex inhibits the serine protease activity of tissue-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and tissue-type plasminogen activator (PLAT); formation of the complex inhibits the serine protease activity of tissue-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and tissue-type plasminogen activator (PLAT); formation of the complex inhibits the serine protease activity of tissue-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and urokinase-type plasminogen activator (PLAU); formation of the complex inhibits the serine protease activity of urokinase-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and urokinase-type plasminogen activator (PLAU); formation of the complex inhibits the serine protease activity of urokinase-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and urokinase-type plasminogen activator (PLAU); formation of the complex inhibits the serine protease activity of urokinase-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and urokinase-type plasminogen activator (PLAU); formation of the complex inhibits the serine protease activity of urokinase-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and urokinase-type plasminogen activator (PLAU); formation of the complex inhibits the serine protease activity of urokinase-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and urokinase-type plasminogen activator (PLAU); formation of the complex inhibits the serine protease activity of urokinase-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and urokinase-type plasminogen activator (PLAU); formation of the complex inhibits the serine protease activity of urokinase-type plasminogen activator.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and thrombin (F2); formation of the complex inhibits the serine protease activity of thrombin.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and thrombin (F2); formation of the complex inhibits the serine protease activity of thrombin.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and thrombin (F2); formation of the complex inhibits the serine protease activity of thrombin.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and thrombin (F2); formation of the complex inhibits the serine protease activity of thrombin.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and thrombin (F2); formation of the complex inhibits the serine protease activity of thrombin.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and thrombin (F2); formation of the complex inhibits the serine protease activity of thrombin.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and prostate-specific antigen (KLK3); formation of the complex inhibits the serine protease activity of prostate-specific antigen.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and prostate-specific antigen (KLK3); formation of the complex inhibits the serine protease activity of prostate-specific antigen.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and prostate-specific antigen (KLK3); formation of the complex inhibits the serine protease activity of prostate-specific antigen.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and prostate-specific antigen (KLK3); formation of the complex inhibits the serine protease activity of prostate-specific antigen.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and prostate-specific antigen (KLK3); formation of the complex inhibits the serine protease activity of prostate-specific antigen.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and prostate-specific antigen (KLK3); formation of the complex inhibits the serine protease activity of prostate-specific antigen.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and plasma kallikrein (KLK1B); formation of the complex inhibits the serine protease activity of plasma kallikrein.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and plasma kallikrein (KLK1B); formation of the complex inhibits the serine protease activity of plasma kallikrein.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and plasma kallikrein (KLK1B); formation of the complex inhibits the serine protease activity of plasma kallikrein.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and plasma kallikrein (KLK1B); formation of the complex inhibits the serine protease activity of plasma kallikrein.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and plasma kallikrein (KLK1B); formation of the complex inhibits the serine protease activity of plasma kallikrein.
The process in which the guanylyltransferase enzyme responsible for adding a 7-methylguanosine cap on pre-mRNA becomes associated with the RNA polymerase II holoenzyme complex and the 5' end of a transcript.
The process in which the guanylyltransferase enzyme responsible for adding a 7-methylguanosine cap on pre-mRNA becomes associated with the RNA polymerase II holoenzyme complex and the 5' end of a transcript.
The negative regulation of cell adhesion process in which a neural crest cell physically separates from the rest of the neural tube.
The negative regulation of cell adhesion process in which a neural crest cell physically separates from the rest of the neural tube.
The negative regulation of cell adhesion process in which a neural crest cell physically separates from the rest of the neural tube.
Interacting selectively and non-covalently with a mediator complex. The mediator complex is a protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins.
The aggregation, arrangement and bonding together of a set of components to form a mediator complex. The mediator complex is a protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins.
The process whose specific outcome is the progression of a osteoclast from its formation to the mature structure. Cell development does not include the steps involved in committing a cell to a specific fate. An osteoclast is a specialized phagocytic cell associated with the absorption and removal of the mineralized matrix of bone tissue.
The negative regulation of cell adhesion process in which a cardiac neural crest cell physically separates from the rest of the neural tube.
The change in morphology and behavior of a CD8-positive, alpha-beta T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
A protein complex that is located at the ciliary transition zone and consists of several proteins some of which are membrane bound. Acts as an organiser of transition zone inner structure, specifically the Y-shaped links, in conjunction with the NPHP complex. The MKS complex also acts as part of the selective barrier that prevents diffusion of proteins between the ciliary cytoplasm and cellular cytoplasm as well as between the ciliary membrane and plasma membrane.
A protein complex that is located at the ciliary transition zone and consists of several proteins some of which are membrane bound. Acts as an organiser of transition zone inner structure, specifically the Y-shaped links, in conjunction with the NPHP complex. The MKS complex also acts as part of the selective barrier that prevents diffusion of proteins between the ciliary cytoplasm and cellular cytoplasm as well as between the ciliary membrane and plasma membrane.
A protein complex that is located at the ciliary transition zone and consists of several proteins some of which are membrane bound. Acts as an organiser of transition zone inner structure, specifically the Y-shaped links, in conjunction with the NPHP complex. The MKS complex also acts as part of the selective barrier that prevents diffusion of proteins between the ciliary cytoplasm and cellular cytoplasm as well as between the ciliary membrane and plasma membrane.
A protein complex that is located at the ciliary transition zone and consists of several proteins some of which are membrane bound. Acts as an organiser of transition zone inner structure, specifically the Y-shaped links, in conjunction with the NPHP complex. The MKS complex also acts as part of the selective barrier that prevents diffusion of proteins between the ciliary cytoplasm and cellular cytoplasm as well as between the ciliary membrane and plasma membrane.
A protein complex that is located at the ciliary transition zone and consists of several proteins some of which are membrane bound. Acts as an organiser of transition zone inner structure, specifically the Y-shaped links, in conjunction with the NPHP complex. The MKS complex also acts as part of the selective barrier that prevents diffusion of proteins between the ciliary cytoplasm and cellular cytoplasm as well as between the ciliary membrane and plasma membrane.
The chemical reactions and pathways involving the polyphenol, curcumin.
The chemical reactions and pathways involving the polyphenol, curcumin.
The chemical reactions and pathways involving the polyphenol, curcumin.
The chemical reactions and pathways involving the polyphenol, curcumin.
The chemical reactions and pathways involving the polyphenol, curcumin.
The chemical reactions and pathways involving the polyphenol, curcumin.
The chemical reactions and pathways involving the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin.
Interacting selectively and non-covalently with a long-chain fatty acid. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22.
Interacting selectively and non-covalently with a long-chain fatty acyl-CoA. A long-chain fatty acyl-CoA is any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more.
A dynamic, actin-rich projection extending from the surface of a migrating animal cell.
The modification of a protein amino acid by the addition of a malonyl (CO-CH2-CO) group.
The addition of a malonyl group (CO-CH2-CO) to peptidyl-lysine to form N6-malonyl-L-lysine.
The removal of a malonyl group (CO-CH2-CO), from an amino acid residue within a protein or peptide.
The process of removing a malonyl group (CO-CH2-CO) from an malonylated lysine residue in a peptide or protein.
The removal of a succinyl group (CO-CH2-CH2-CO) from a residue in a peptide or protein.
The removal of a succinyl group (CO-CH2-CH2-CO) from a succinylated lysine residue in a peptide or protein.
The modification of a peptidyl-lysine residue by the addition of a succinyl group (CO-CH2-CH2-CO) to form N6-succinyl-L-lysine.
A process in which a protein is transported to, or maintained at, the trailing edge. The trailing edge is the area of a motile cell opposite to the direction of movement.
A process in which a protein is transported to, or maintained in, a uropod. A uropod is a membrane projection with related cytoskeletal components at the trailing edge of a migrating cell.
A large plasma membrane-lined circular pore that perforates the flattened glomerular endothelium and, unlike those of other fenestrated capillaries, is not spanned by diaphragms; the density and size of glomerular fenestrae account, at least in part, for the high permeability of the glomerular capillary wall to water and small solutes.
A large plasma membrane-lined circular pore that perforates the flattened glomerular endothelium and, unlike those of other fenestrated capillaries, is not spanned by diaphragms; the density and size of glomerular fenestrae account, at least in part, for the high permeability of the glomerular capillary wall to water and small solutes.
Catalysis of the reaction: protein-malonyllysine + H2O => protein-lysine + malonate. This reaction is the removal of a malonyl group (CO-CH2-CO) from a malonylated lysine residue of a protein or peptide.
Catalysis of the reaction: protein-malonyllysine + H2O => protein-lysine + malonate. This reaction is the removal of a malonyl group (CO-CH2-CO) from a malonylated lysine residue of a protein or peptide.
Catalysis of the reaction: protein-malonyllysine + H2O => protein-lysine + malonate. This reaction is the removal of a malonyl group (CO-CH2-CO) from a malonylated lysine residue of a protein or peptide.
Catalysis of the reaction: protein-succinyllysine + H2O => protein-lysine + succinate. This reaction is the removal of a succinyl group (CO-CH2-CH2-CO) from a succinylated lysine residue of a protein or peptide.
Catalysis of the reaction: protein-succinyllysine + H2O => protein-lysine + succinate. This reaction is the removal of a succinyl group (CO-CH2-CH2-CO) from a succinylated lysine residue of a protein or peptide.
Catalysis of the reaction: protein-succinyllysine + H2O => protein-lysine + succinate. This reaction is the removal of a succinyl group (CO-CH2-CH2-CO) from a succinylated lysine residue of a protein or peptide.
A specialized cell-cell junction found between the cells of the excretory system, which provides a barrier for filtration of blood or hemolymph.
A specialized cell-cell junction found between the interdigitating foot processes of the glomerular epithelium (the podocytes) in the vertebrate kidney, which is adapted for facilitating glomerular filtration.
The aggregation, arrangement and bonding together of a set of components to form a filtration diaphragm, a specialized cell-cell junction found between the cells of the excretory system, which provides a barrier for filtration of blood or hemolymph.
The aggregation, arrangement and bonding together of a set of components to form a nephrocyte diaphragm, a specialized cell-cell junction found between nephrocytes of the insect kidney.
The aggregation, arrangement and bonding together of a set of components to form a slit diaphragm, specialized cell-cell junction found between the interdigitating foot processes of the glomerular epithelium (the podocytes) in the vertebrate kidney, which is adapted for facilitating glomerular filtration.
The directed movement of a muscle cell towards a tendon cell in response to an external stimulus. Tendon cells, for example, produce positive guidance cues that attract muscle cells.
The directed movement of a muscle cell towards a tendon cell in response to an external stimulus. Tendon cells, for example, produce positive guidance cues that attract muscle cells.
A region that surrounds the active zone of the presynaptic plasma membrane, and is specialized for the control of synaptic development.
A region that surrounds the active zone of the presynaptic plasma membrane, and is specialized for the control of synaptic development.
A cone-shaped structure in the head of a spermatozoon, which is formed by the coalescence of Golgi fragments following the completion of meiosis. The acroblast is situated adjacent to the acrosomal vesicle.
A membrane-tethered, short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum) that is similar in structure to a centriole and derives from it. The cilium basal body is the site of assembly and remodelling of the cilium and serves as a nucleation site for axoneme growth. As well as anchoring the cilium, it is thought to provide a selective gateway regulating the entry of ciliary proteins and vesicles by intraflagellar transport.
A membrane-tethered, short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum) that is similar in structure to a centriole and derives from it. The cilium basal body is the site of assembly and remodelling of the cilium and serves as a nucleation site for axoneme growth. As well as anchoring the cilium, it is thought to provide a selective gateway regulating the entry of ciliary proteins and vesicles by intraflagellar transport.
A membrane-tethered, short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum) that is similar in structure to a centriole and derives from it. The cilium basal body is the site of assembly and remodelling of the cilium and serves as a nucleation site for axoneme growth. As well as anchoring the cilium, it is thought to provide a selective gateway regulating the entry of ciliary proteins and vesicles by intraflagellar transport.
A membrane-tethered, short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum) that is similar in structure to a centriole and derives from it. The cilium basal body is the site of assembly and remodelling of the cilium and serves as a nucleation site for axoneme growth. As well as anchoring the cilium, it is thought to provide a selective gateway regulating the entry of ciliary proteins and vesicles by intraflagellar transport.
A membrane-tethered, short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum) that is similar in structure to a centriole and derives from it. The cilium basal body is the site of assembly and remodelling of the cilium and serves as a nucleation site for axoneme growth. As well as anchoring the cilium, it is thought to provide a selective gateway regulating the entry of ciliary proteins and vesicles by intraflagellar transport.
The covalent attachment of a fucosyl group to an acceptor molecule.
The process of transferring a fucosyl group to a serine or threonine residues in a protein acceptor molecule, to form an O-linked protein-sugar linkage.
The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the presence of light.
The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the presence of light.
The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the presence of light.
The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the presence of light.
The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the presence of light.
The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the absence of light.
The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the absence of light.
The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the absence of light.
The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the absence of light.
The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the absence of light.
The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the presence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the presence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the presence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the presence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the presence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the absence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the absence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the absence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the absence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the absence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants.
The process of transferring a fucosyl group to an N-glycan. An N-glycan is the carbohydrate portion of an N-glycoprotein when attached to a nitrogen from asparagine or arginine side-chains.
The formation of bone or of a bony substance, or the conversion of fibrous tissue or of cartilage into bone or a bony substance, that does not require the replacement of preexisting tissues.
Intramembranous ossification from the surface of a cartilage element as the perichondrium becomes a periosteum, without replacement of cartilage.
Direct ossification in which bone formation occurs as result of the direct transformation of non-bone cells into bone cells without cell division.
Ossification that requires the replacement of a preexisting tissue prior to bone tissue formation.
Ossification wherein bone tissue forms within ligamentous tissue.
Ossification wherein bone tissue forms within tendonous tissue.
The removal of tubulin heterodimers from the minus end of a microtubule.
Enables the transfer of a purine nucleotide-sugar from one side of a membrane to the other. Purine nucleotide-sugars are purine nucleotides in glycosidic linkage with a monosaccharide or monosaccharide derivative.
Enables the transmembrane transfer of an ion by a channel that opens when extracellular ammonia (NH3) has been bound by the channel complex or one of its constituent parts.
Enables the transmembrane transfer of an ion by a channel that opens when extracellular phenylacetaldehyde has been bound by the channel complex or one of its constituent parts.
Any process that activates or increases the frequency, rate or extent of unsaturated fatty acid biosynthetic process by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
The directed movement of GDP-fucose into the endoplasmic reticulum lumen. GDP-fucose is a substance composed of fucose in glycosidic linkage with guanosine diphosphate.
The directed movement of GDP-fucose into the endoplasmic reticulum lumen. GDP-fucose is a substance composed of fucose in glycosidic linkage with guanosine diphosphate.
The directed movement of GDP-fucose into the endoplasmic reticulum lumen. GDP-fucose is a substance composed of fucose in glycosidic linkage with guanosine diphosphate.
The directed movement of GDP-fucose into the Golgi lumen. GDP-fucose is a substance composed of fucose in glycosidic linkage with guanosine diphosphate.
The directed movement of GDP-fucose into the Golgi lumen. GDP-fucose is a substance composed of fucose in glycosidic linkage with guanosine diphosphate.
The directed movement of GDP-fucose into the Golgi lumen. GDP-fucose is a substance composed of fucose in glycosidic linkage with guanosine diphosphate.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of deprivation of iron ions.
A protein complex composed of two or more polypeptide subunits, and which possesses glutathione synthase activity (catalysis of the reaction: L-gamma-glutamyl-L-cysteine + ATP + glycine = ADP + glutathione + 2 H(+) + phosphate). In eukaryotes, the complex is homodimeric, in E. coli glutathione synthase exists as a tetramer, and in S. pombe the complex exists as a homodimer or a heterotetramer.
The chemical reactions and pathways resulting in the breakdown of D-serine, the D-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
The chemical reactions and pathways resulting in the breakdown of D-serine, the D-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
The chemical reactions and pathways resulting in the breakdown of D-serine, the D-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
Generation of the cleavage furrow, a shallow groove in the cell surface near the old metaphase plate that marks the site of cytokinesis. This process includes the recruitment and localized activation of signals such as RhoA at the site of the future furrow to ensure that furrowing initiates at the correct site in the cell.
Advancement of the cleavage furrow from the outside of the cell inward towards the center of the cell. The cleavage furrow acts as a 'purse string' which draws tight to separate daughter cells during cytokinesis and partition the cytoplasm between the two daughter cells. The furrow ingresses until a cytoplasmic bridge is formed.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a stimulus indicating the organism is under 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 chemical reactions and pathways resulting in the formation of phosphatidylinositol-3-phosphate, a phosphatidylinositol monophosphate carrying the phosphate group at the 3-position.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol-3-phosphate, a phosphatidylinositol monophosphate carrying the phosphate group at the 3-position.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol-3-phosphate, a phosphatidylinositol monophosphate carrying the phosphate group at the 3-position.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol-3-phosphate, a phosphatidylinositol monophosphate carrying the phosphate group at the 3-position.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol-3-phosphate, a phosphatidylinositol monophosphate carrying the phosphate group at the 3-position.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol-3-phosphate, a phosphatidylinositol monophosphate carrying the phosphate group at the 3-position.
The multiplication or reproduction of germ cells, reproductive cells in multicellular organisms, resulting in the expansion of a cell population.
Interacting selectively and non-covalently with a small molecule, any low molecular weight, monomeric, non-encoded molecule.
Any process that activates or increases the frequency, rate or extent of invasive growth as a result of deprivation of glucose, by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
The process by which an organism or tissue maintains a population of male germ-line stem cells.
The process by which an organism or tissue maintains a population of female germ-line stem cells.
The chemical reactions and pathways resulting in the breakdown of a leukotriene, a pharmacologically active substance derived from a polyunsaturated fatty acid, such as arachidonic acid.
The chemical reactions and pathways resulting in the breakdown of a leukotriene, a pharmacologically active substance derived from a polyunsaturated fatty acid, such as arachidonic acid.
The chemical reactions and pathways resulting in the breakdown of a leukotriene, a pharmacologically active substance derived from a polyunsaturated fatty acid, such as arachidonic acid.
The chemical reactions and pathways resulting in the breakdown of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways resulting in the breakdown of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways resulting in the breakdown of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways resulting in the breakdown of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways involving leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways involving Kdo2-lipid A, a lipopolysaccharide (LPS) component.
The chemical reactions and pathways resulting in the formation of Kdo2-lipid A, a lipopolysaccharide (LPS) component.
The chemical reactions and pathways resulting in the formation of Kdo2-lipid A, a lipopolysaccharide (LPS) component.
The chemical reactions and pathways resulting in the formation of Kdo2-lipid A, a lipopolysaccharide (LPS) component.
The chemical reactions and pathways resulting in the formation of Kdo2-lipid A, a lipopolysaccharide (LPS) component.
The chemical reactions and pathways resulting in the formation of Kdo2-lipid A, a lipopolysaccharide (LPS) component.
The chemical reactions and pathways resulting in the formation of Kdo2-lipid A, a lipopolysaccharide (LPS) component.
Interacting selectively and non-covalently with a class I 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 in a PEX19-dependent manner.
Interacting selectively and non-covalently with a class I 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 in a PEX19-dependent manner.
Interacting selectively and non-covalently with a class II 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 in a PEX19-independent manner.
Interacting selectively and non-covalently with a class II 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 in a PEX19-independent manner.
The chemical reactions and pathways involving 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate, a precursor of 4-amino-4-deoxy-L-arabinose (L-Ara4N).
The chemical reactions and pathways involving 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate, a precursor of 4-amino-4-deoxy-L-arabinose (L-Ara4N).
The chemical reactions and pathways resulting in the formation of 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate, a precursor of 4-amino-4-deoxy-L-arabinose (L-Ara4N).
The chemical reactions and pathways resulting in the formation of 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate, a precursor of 4-amino-4-deoxy-L-arabinose (L-Ara4N).
The chemical reactions and pathways resulting in the formation of 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate, a precursor of 4-amino-4-deoxy-L-arabinose (L-Ara4N).
The chemical reactions and pathways resulting in the formation of 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate, a precursor of 4-amino-4-deoxy-L-arabinose (L-Ara4N).
The chemical reactions and pathways resulting in the formation of 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate, a precursor of 4-amino-4-deoxy-L-arabinose (L-Ara4N).
The chemical reactions and pathways involving alpha-linolenic acid, an unsaturated omega-6 fatty acid that has the molecular formula C18H32O2.
The chemical reactions and pathways involving alpha-linolenic acid, an unsaturated omega-6 fatty acid that has the molecular formula C18H32O2.
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 inositol.
The chemical reactions and pathways involving very long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A very long-chain fatty acid is a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways involving very long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A very long-chain fatty acid is a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways involving medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. A medium-chain fatty acid is a fatty acid with a chain length of between C6 and C12.
The chemical reactions and pathways involving medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. A medium-chain fatty acid is a fatty acid with a chain length of between C6 and C12.
The chemical reactions and pathways resulting in the breakdown of very long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A very long-chain fatty acid is a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways resulting in the breakdown of very long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A very long-chain fatty acid is a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways resulting in the breakdown of very long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A very long-chain fatty acid is a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways resulting in the breakdown of medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A medium-chain fatty acid is a fatty acid with a chain length of between C6 and C12.
The chemical reactions and pathways resulting in the breakdown of medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A medium-chain fatty acid is a fatty acid with a chain length of between C6 and C12.
The chemical reactions and pathways resulting in the breakdown of medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A medium-chain fatty acid is a fatty acid with a chain length of between C6 and C12.
The chemical reactions and pathways resulting in the breakdown of a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty-acyl group.
The chemical reactions and pathways resulting in the breakdown of a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty-acyl group.
The chemical reactions and pathways resulting in the breakdown of a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty-acyl group.
The chemical reactions and pathways resulting in the breakdown of long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22.
The chemical reactions and pathways resulting in the breakdown of long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22.
The chemical reactions and pathways resulting in the breakdown of long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22.
A cable structure, surrounding some cell types (e.g. proximal or bronchial tubular epithelial cells), and composed of hyaluranon (HA), a ubiquitous connective tissue glycosaminoglycan.
A process that results in the aggregation, arrangement and bonding together of a hyaluranon cable, a cable structure, surrounding some cell types (e.g. proximal or bronchial tubular epithelial cells), and composed of hyaluranon (HA), a ubiquitous connective tissue glycosaminoglycan.
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 platelet-derived growth factor 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 platelet-derived growth factor stimulus.
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 platelet-derived growth factor stimulus.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, in the presence of double-stranded DNA; drives the unwinding of a DNA helix.
Interacting selectively and non-covalently with a member of the bone morphogenetic protein (BMP) family.
The modification of histone H3 by addition of two methyl groups to lysine at position 9 of the histone.
The modification of histone H3 by addition of two methyl groups to lysine at position 9 of the histone.
The modification of histone H3 by addition of three methyl groups to lysine at position 9 of the histone.
A multienzyme complex possessing three kinds of enzymes that catalyze the chain reactions in the fatty acid beta-oxidation cycle, enoyl-CoA hydratase (ECH), 3-hydroxyacyl-CoA dehydrogenase (HACD), and acetyl-CoA C-acyltransferase (KACT).
A microtubule-based flagellum (or cilium) that is part of a sperm, a mature male germ cell that develops from a spermatid.
A microtubule-based flagellum (or cilium) that is part of a sperm, a mature male germ cell that develops from a spermatid.
Interacting selectively and non-covalently with 3-sulfino-L-alanine (cysteine sulfinate).
A sperm-specific voltage-gated calcium channel that controls the intracellular calcium ion concentration and, thereby, the swimming behavior of sperm. Consists of a heteromeric tetramer surrounding a calcium ion- selective pore. May also contain additional auxiliary subunits.
A sperm-specific voltage-gated calcium channel that controls the intracellular calcium ion concentration and, thereby, the swimming behavior of sperm. Consists of a heteromeric tetramer surrounding a calcium ion- selective pore. May also contain additional auxiliary subunits.
Any process that decreases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a hydrogen peroxide (H2O2) stimulus.
Catalysis of the reaction: prostaglandin H2 + NADPH + H+ -> prostaglandin F2alpha + NADP+. This reaction is the reduction of prostaglandin H2 ((5Z,13E)-(15S)-9alpha,11alpha-Epidioxy-15-hydroxyprosta-5,13-dienoate) to prostaglandin F2alpha ((5Z,13E)-(15S)-9alpha,11alpha,15-Trihydroxyprosta-5,13-dienoate).
Catalysis of the reaction: prostaglandin H2 + NADPH + H+ -> prostaglandin F2alpha + NADP+. This reaction is the reduction of prostaglandin H2 ((5Z,13E)-(15S)-9alpha,11alpha-Epidioxy-15-hydroxyprosta-5,13-dienoate) to prostaglandin F2alpha ((5Z,13E)-(15S)-9alpha,11alpha,15-Trihydroxyprosta-5,13-dienoate).
Catalysis of the reaction: prostaglandin D2 + H+ + NADPH -> 11-epi-prostaglandin F2alpha + NADP+.
Catalysis of the reaction: prostaglandin D2 + H+ + NADPH -> 11-epi-prostaglandin F2alpha + NADP+.
Catalysis of the reaction: 15-keto-prostaglandin + NAD(P)H + H+ -> 13,14-dihydro-15-keto-prostaglandin + NAD(P)+. This reaction is the reduction of 15-keto-prostaglandin.
Catalysis of the reaction: 15-keto-prostaglandin + NAD(P)H + H+ -> 13,14-dihydro-15-keto-prostaglandin + NAD(P)+. This reaction is the reduction of 15-keto-prostaglandin.
Catalysis of the reaction: 15-keto-prostaglandin + NAD(P)H + H+ -> 13,14-dihydro-15-keto-prostaglandin + NAD(P)+. This reaction is the reduction of 15-keto-prostaglandin.
Catalysis of the reaction: 15-keto-prostaglandin + NAD(P)H + H+ -> 13,14-dihydro-15-keto-prostaglandin + NAD(P)+. This reaction is the reduction of 15-keto-prostaglandin.
Catalysis of the reaction: 15-keto-prostaglandin + NAD(P)H + H+ -> 13,14-dihydro-15-keto-prostaglandin + NAD(P)+. This reaction is the reduction of 15-keto-prostaglandin.
Catalysis of the reaction: 15-keto-prostaglandin + NAD(P)H + H+ -> 13,14-dihydro-15-keto-prostaglandin + NAD(P)+. This reaction is the reduction of 15-keto-prostaglandin.
Catalysis of the reaction: thromboxane B2 + NAD+ = 11-dehydro-thromboxane B2 + NADH + H+.
Catalysis of the reaction: prostaglandin H2 = 12-hydroxyheptadecatrienoic acid (HHT) + malonaldehyde (MDA).
The orderly movement of a Schwann cell from one site to another. A Schwann cell is a glial cell that ensheathes axons of neuron in the peripheral nervous system and is necessary for their maintainance and function.
Catalysis of the reaction: L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-aspartate.
Catalysis of the transfer of an amino group from kynurenine to an acceptor, usually a 2-oxo acid.
Catalysis of the transfer of an amino group from kynurenine to an acceptor, usually a 2-oxo acid.
The hydroxylation of peptidyl-histidine to form peptidyl-hydroxyhistidine.
Catalysis of the reaction: peptidyl L-histidine + 2-oxoglutarate + O2 = peptidyl hydroxy-L-histidine + succinate + CO2.
Catalysis of the reaction: peptidyl L-asparagine + 2-oxoglutarate + O2 = peptidyl 3-hydroxy-L-asparagine + succinate + CO2.
Catalysis of the reaction L-phenylalanine + oxaloacetate = phenylpyruvate + aspartate.
Interacting selectively and non-covalently with a kringle domain. Kringle domains are protein domains that fold into large loops stabilized by 3 disulfide linkages, and are important in protein-protein interactions with blood coagulation factors.
The process of regulating the proliferation and elimination of dendritic cells such that the total number of dendritic cells within a whole or part of an organism is stable over time in the absence of an outside stimulus.
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 mycotoxin stimulus. A mycotoxin is a toxic chemical substance produced by fungi.
A digestive process in which food, usually grass or hay, is swallowed into a multi-compartmented stomach, regurgitated, chewed again, and swallowed again.
Remodeling the acyl chains of phosphatidylglycerol, through sequential deacylation and re-acylation reactions, to generate phosphatidylglycerol containing different types of fatty acid acyl chains.
Remodeling the acyl chains of phosphatidylinositol, through sequential deacylation and re-acylation reactions, to generate phosphatidylinositol containing different types of fatty acid acyl chains.
Remodeling the acyl chains of phosphatidylserine, through sequential deacylation and re-acylation reactions, to generate phosphatidylserine containing different types of fatty acid acyl chains.
Remodeling the acyl chains of phosphatidylcholine, through sequential deacylation and re-acylation reactions, to generate phosphatidylcholine containing different types of fatty acid acyl chains.
Remodeling the acyl chains of phosphatidylethanolamine, through sequential deacylation and re-acylation reactions, to generate phosphatidylethanolamine containing different types of fatty acid acyl chains.
Remodeling the acyl chains of triacylglycerol, through sequential deacylation and re-acylation reactions, to generate triacylglycerol containing different types of fatty acid acyl chains.
Remodeling the acyl chains of diacylglycerol, through sequential deacylation and re-acylation reactions, to generate diacylglycerol containing different types of fatty acid acyl chains.
Remodeling the acyl chains of an acylglycerol, through sequential deacylation and re-acylation reactions, to generate an acylglycerol containing different types of fatty acid acyl chains.
Inner arm structure present on the outer doublet microtubules of ciliary and flagellar axonemes. The structure of inner dynein arms is complex and may vary within the axoneme. Inner dynein arms are heteromeric, comprising 8 different heavy chains and various subunits. Inner and outer dynein arms have different functions in the generation of microtubule-based motility.
Outer arm structure present on the outer doublet microtubules of ciliary and flagellar axonemes. Outer dynein arms contain 2-3 heavy chains, two or more intermediate chains and a cluster of 4-8 light chains. Inner and outer dynein arms have different functions in the generation of microtubule-based motility.
The aggregation, arrangement and bonding together of a set of components to form an axonemal dynein outer arm, an outer arm structure present on the outer doublet microtubules of ciliary and flagellar axonemes.
The aggregation, arrangement and bonding together of a set of components to form an axonemal dynein inner arm, an inner arm structure present on the outer doublet microtubules of ciliary and flagellar axonemes.
The regulated release of a melanocyte-stimulating hormone, any of a group of peptide hormones that are produced by cells in the intermediate lobe of the pituitary gland, and stimulate the production of melanin to increase pigmentation.
The regulated release of calcitonin, a peptide hormone that participates in calcium and phosphorus metabolism, from a cell.
The regulated release of oxytocin, a cyclic nonapeptide hormone with amino acid sequence CYIQNCPLG that also acts as a neurotransmitter in the brain, from a cell. Oxytocin is the principal uterine-contracting and milk-ejecting hormone of the posterior pituitary, and together with the neuropeptide vasopressin, is believed to influence social cognition and behavior.
Catalysis of the reaction: 3-hexaprenyl-4-hydroxy-5-methoxybenzoic acid -> 2-hexaprenyl-6-methoxyphenol + CO2.
The attachment of a cell to an underlying abiotic (non-living) substrate via adhesion molecules.
The growth of colonies in filamentous chains of cells as a result of an increase in temperature.
The growth of colonies in filamentous chains of cells as a result of an increase in temperature.
The growth of colonies in filamentous chains of cells as a result of an increase in temperature.
A reversible switch of a cell from one cell type or form to another, at a frequency above the expected frequency for somatic mutations. Phenotypic switching involves changes in cell morphology and altered gene expression patterns. For example, Candida albicans switches from white cells to opaque cells for sexual mating. Phenotypic switching also occurs in multicellular organisms; smooth muscle cells (SMCs) exhibit phenotypic transitions to allow rapid adaption to fluctuating environmental cues.
A reversible switch of a cell from one phenotype to another that occurs upon infection of a host or host cell. For example, Candida albicans switches from a unicellular form to an invasive multicellular filamentous form upon infection of host tissue. Phenotypic switching begins with changes in cell morphology and altered gene expression patterns and ends when the morphology of a population of cells has reverted back to the default state, accompanied by altered expression patterns.
The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to an increase in temperature.
Catalysis of the reaction: 3-methoxy-4-hydroxy-5-decaprenylbenzoic acid -> 2-methoxy-6-decaprenylphenol + CO2.
The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to deprivation of nourishment.
The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to a chemical stimulus.
A process that generates thiamine (vitamin B1) from derivatives of it without de novo synthesis.
Interacting selectively and non-covalently with the inorganic anion thiosulfate, a sulfur oxide that has formula O3S2.
Catalysis of the reaction: butane + O2 + NAD(P)H + H+ = butanol + NAD(P)+ + H2O.
Catalysis of the reaction: butane + O2 + NAD(P)H + H+ = butanol + NAD(P)+ + H2O.
Catalysis of the reaction: 2'-deoxyribonucleoside diphosphate + glutaredoxin disulfide + H2O -> ribonucleoside diphosphate + glutaredoxin.
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 neutral pH (pH close to 7) stimulus. pH is a measure of the acidity or basicity of an aqueous solution.
The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to a pH stimulus. pH is a measure of the acidity or basicity of an aqueous solution.
The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to a neutral pH (pH close to 7) stimulus.
A developmental process, independent of morphogenetic (shape) change, that is required for an osteoclast cell to attain its fully functional state. An osteoclast is a specialized phagocytic cell associated with the absorption and removal of the mineralized matrix of bone tissue, and which typically differentiates from monocytes.
The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to a biotic (living) stimulus.
A cellular protein localization process in which a protein is transported to, or maintained at, a linear element. A linear element is a proteinaceous scaffold associated with S. pombe chromosomes during meiotic prophase.
The chemical reactions and pathways involving asperthecin, an anthraquinone pigment obtained from the mould Aspergillus nidulans.
The chemical reactions and pathways resulting in the breakdown of asperthecin, an anthraquinone pigment obtained from the mould Aspergillus nidulans.
The chemical reactions and pathways resulting in the breakdown of asperthecin, an anthraquinone pigment obtained from the mould Aspergillus nidulans.
The chemical reactions and pathways resulting in the breakdown of asperthecin, an anthraquinone pigment obtained from the mould Aspergillus nidulans.
The chemical reactions and pathways resulting in the formation of asperthecin, an anthraquinone pigment obtained from the mould Aspergillus nidulans.
The chemical reactions and pathways resulting in the formation of asperthecin, an anthraquinone pigment obtained from the mould Aspergillus nidulans.
The chemical reactions and pathways resulting in the formation of asperthecin, an anthraquinone pigment obtained from the mould Aspergillus nidulans.
Definition: Catalysis of the reaction: 15-oxolipoxin A4 + NAD(P)H + H+ = 13,14-dihydro-15-oxolipoxin A4 + NAD(P)+.
The lipid bilayer surrounding an early phagosome.
The process in which a cell switches from growing as a round budding cell to growing as a filament (elongated cells attached end-to-end). An example of this is the yeast-hyphal transition of Candida albicans.
Catalysis of the reaction: abieta-7,13-diene-18-al + H2O + NAD+ = abieta-7,13-diene-18-oate + NADH + H+.
Catalysis of the reaction: abieta-7,13-diene + NADPH + H+ + O2 = abieta-7,13-dien-18-ol + NADP+ + H2O.
Catalysis of the reaction: indole + NAD(P)H + H+ + O2 = indolin-2-one + NAD(P)+ + H2O.
Catalysis of the reaction: indolin-2-one + NAD(P)H + H+ + O2 = 3-hydroxyindolin-2-one + NAD(P)+ + H2O.
Catalysis of the reaction: 3-hydroxyindolin-2-one + NAD(P)H + H+ + O2 = 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one + NAD(P)+ + H2O.
Catalysis of the reaction: 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one + NAD(P)H + H+ + O2 = 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one + NAD(P)+ + H2O.
A prolongation or process extending from a muscle cell. A muscle cell is a mature contractile cell, commonly known as a myocyte. This cell has as part of its cytoplasm myofibrils organized in various patterns.
A prolongation or process extending from a muscle cell. A muscle cell is a mature contractile cell, commonly known as a myocyte. This cell has as part of its cytoplasm myofibrils organized in various patterns.
A prolongation or process extending from a muscle cell. A muscle cell is a mature contractile cell, commonly known as a myocyte. This cell has as part of its cytoplasm myofibrils organized in various patterns.
The portion of the plasma membrane surrounding a muscle cell projection.
The chemical reactions and pathways involving zymosterol, (5alpha-cholesta-8,24-dien-3beta-ol).
The chemical reactions and pathways resulting in the formation of zymosterol, (5alpha-cholesta-8,24-dien-3beta-ol).
The chemical reactions and pathways resulting in the formation of zymosterol, (5alpha-cholesta-8,24-dien-3beta-ol).
The chemical reactions and pathways resulting in the formation of zymosterol, (5alpha-cholesta-8,24-dien-3beta-ol).
The chemical reactions and pathways resulting in the formation of zymosterol, (5alpha-cholesta-8,24-dien-3beta-ol).
Any process which produces dTMP, deoxyribosylthymine monophosphate (2'-deoxyribosylthymine 5'-phosphate) without de novo synthesis.
Any process which produces dTMP, deoxyribosylthymine monophosphate (2'-deoxyribosylthymine 5'-phosphate) without de novo synthesis.
Catalysis of the reaction: cholest-4-en-3-one + NADH + H+ + O2 = 26-hydroxycholest-4-en-3-one + NAD+ + H2O. This reaction involves the hydroxylation of the C26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate.
Catalysis of the reaction: androsta-1,4-diene-3,17-dione + NADH + H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O.
Catalysis of the reaction: androsta-1,4-diene-3,17-dione + NADH + H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O.
Catalysis of the reaction: ent-isokaurene + O2 + NADPH + H+ = ent-2alpha-hydroxyisokaurene + H2O + NADP+.
Catalysis of the reaction: ent-cassa-12,15-diene + O2 + NADPH + H+ = ent-11beta-hydroxycassa-12,15-diene + NADP+ + H2O.
Catalysis of the reaction: 10beta-hydroxytaxa-4(20),11-dien-5alpha-yl acetate + O2 + NADPH + H+ = 10beta,14beta-dihydroxytaxa-4(20),11-dien-5alpha-yl acetate + NADP+ + H2O.
Catalysis of the reaction: abieta-7,13-dien-18-ol + NADPH + H+ + O2 = abieta-7,13-dien-18-al + NADP+ + 2 H2O. This is a two step reaction. The first step is: abieta-7,13-dien-18-ol + NADPH + H+ + O2 = abieta-7,13-dien-18,18-diol + + NADP+ + H2O. The second step is a spontaneous reaction: abieta-7,13-dien-18,18-diol = abieta-7,13-dien-18-al + H2O.
The chemical reactions and pathways resulting in the breakdown of a histone protein by individual cells.
Any process that modulates the frequency, rate or extent of expression of a histone-encoding gene. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein.
Any process that increases the frequency, rate or extent of expression of a histone-encoding gene. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein.
Any process that increases the frequency, rate or extent of expression of a histone-encoding gene. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein.
Any process that increases the frequency, rate or extent of expression of a histone-encoding gene. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein.
Any process that increases the frequency, rate or extent of expression of a histone-encoding gene. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein.
Any process that decreases the frequency, rate or extent of expression of a histone-encoding gene. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein.
Any process that decreases the frequency, rate or extent of expression of a histone-encoding gene. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein.
Any process that decreases the frequency, rate or extent of expression of a histone-encoding gene. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein.
Any process that decreases the frequency, rate or extent of expression of a histone-encoding gene. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein.
Catalysis of the reaction: 9beta-pimara-7,15-diene + 3 O2 + 3 NADPH + 3 H+ = 9beta-pimara-7,15-dien-19-oate + 3 NADP+ + 4 H2O. This is a three-step reaction: (a) 9beta-pimara-7,15-diene + O2 + NADPH + H+ = 9beta-pimara-7,15-dien-19-ol + NADP+ + H2O, (b) 9beta-pimara-7,15-dien-19-ol + O2 + NADPH + H+ = 9neta-pimara-7,15-dien-19-al + NADP+ + 2 H2O, (c) 9beta-pimara-7,15-dien-19-al + O2 + NADPH + H+ = 9beta-pimara-7,15-dien-19-oate + NADP+ + H2O.
The covalent alteration performed by one organism of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) in another organism. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
The process in which the contractile ring is maintained, typically in response to an internal or external cue.
The process of an actomyosin ring getting smaller in diameter.
The process in which a contractile ring is assembled and/or maintained in a specific location.
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 stem cell factor (SCF) 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 stem cell factor (SCF) 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 stem cell factor (SCF) 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 stem cell factor (SCF) stimulus.
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 stem cell factor (SCF) stimulus.
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 stem cell factor (SCF) stimulus.
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 stem cell factor (SCF) stimulus.
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 stem cell factor (SCF) stimulus.
Catalysis of the reaction: dGTP + H2O = dGMP + diphosphate.
Catalysis of the reaction: dTTP + H2O = dTMP + diphosphate.
Catalysis of the reaction: GTP + H2O = GMP + diphosphate.
Catalysis of the reaction: GTP + H2O = GMP + diphosphate.
Catalysis of the reaction: ITP + H2O = IMP + diphosphate.
Catalysis of the reaction: UTP + H2O = UMP + diphosphate.
Catalysis of the reaction: XTP + H2O = xanthosine 5'-phosphate + diphosphate.
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 adenine.
A special chromosome region located towards one end of a chromosome that contains dispersed copies of short, repetitive DNA sequences and functions as a cis-acting element essential for presynaptic homologous chromosome pairing and chromosome-nuclear envelope attachment.
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 vitamin B1 (also called thiamin and thiamine).
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 vitamin B1 (also called thiamin and thiamine).
The process in which the mitotic cell cycle is halted during G2 phase as a result of deprivation of glucose.
A process in which a protein is transported to, or maintained in, a location within the nuclear inner membrane.
A process in which a protein is transported to, or maintained in, a location within the nuclear inner membrane.
The change in morphology and behavior of a granulocyte resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor.
The removal of glucuronic acid from a conjugated substrate.
The removal of glucuronic acid from an acyl-glucuronide.
The modification of an substrate by the conjugation of glucuronic acid to form an acyl-glucuronide (also called an acyl-glucuronoside).
Catalysis of the reaction: an acyl-glucuronoside + H2O = an alcohol + D-glucuronate.
Catalysis of the reaction: gallate + O2 = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate.
Catalysis of the reaction: taxusin + O2 + NADPH + H+ = 7beta-hydroxytaxusin + NADP+ + H2O.
The region between the plasma membrane and the cell wall, as found in organisms such as filamentous fungi.
The chemical reactions and pathways resulting in the breakdown of glutamate into 4-hydroxybutyrate.
The chemical reactions and pathways resulting in the breakdown of glutamate into succinate, that includes the conversion of 4-aminobutyrate to succinate semialdehyde by the 2-oxoglutarate-dependent gamma aminobutyrate (GABA) transaminase.
Catalysis of the reaction: succinate semialdehyde + NADP+ + H2O = succinate + NADPH + 2 H+.
Catalysis of the reaction: succinate semialdehyde + NADP+ + H2O = succinate + NADPH + 2 H+.
Catalysis of the reaction: succinate semialdehyde + NADP+ + H2O = succinate + NADPH + 2 H+.
Catalysis of the reaction: succinate semialdehyde + NADP+ + H2O = succinate + NADPH + 2 H+.
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 neutral pH (pH close to 7) stimulus. pH is a measure of the acidity or basicity of an aqueous solution.
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 menadione stimulus. Menadione (also called vitamin K3) is a naphthoquinone having a methyl substituent at the 2-position.
The directed movement of phytochelatin 2 (PC2) into the vacuole. Phytochelatin 2 is a glutathione-related peptide composed of (gamma-Glu-Cys)n-Gly where n=2, and where the Glu and Cys residues are linked through a gamma-carboxylamide bond.
The directed movement of phytochelatin 3 (PC3) into the vacuole. Phytochelatin 3 is a glutathione-related peptide composed of (gamma-Glu-Cys)n-Gly where n=3, and where the Glu and Cys residues are linked through a gamma-carboxylamide bond.
The directed movement of phytochelatin 4 (PC4) into the vacuole. Phytochelatin 4 is a glutathione-related peptide composed of (gamma-Glu-Cys)n-Gly where n=4, and where the Glu and Cys residues are linked through a gamma-carboxylamide bond.
The directed movement of cadmium ions into the vacuole.
The directed movement of a peroxisome along a microtubule, mediated by motor proteins.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a stimulus indicating the organism is under salt stress. The stress is usually an increase or decrease in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a menadione stimulus. Menadione (also called vitamin K3) is a naphthoquinone having a methyl substituent at the 2-position.
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 amiloride stimulus.
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 amiloride 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 methylamine stimulus.
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 methylamine stimulus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a multivesicular body. A multivesicular body is a type of late endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm.
The aggregation, arrangement and bonding together of a set of components to form a multivesicular body, a type of late endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm.
The aggregation, arrangement and bonding together of a set of components to form a multivesicular body, a type of late endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm.
The aggregation, arrangement and bonding together of a set of components to form a multivesicular body, a type of late endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm.
The chemical reactions and pathways resulting in the breakdown of raffinose that occur in the presence of oxygen.
The chemical reactions and pathways resulting in the breakdown of raffinose that occur in the presence of oxygen.
The chemical reactions and pathways resulting in the breakdown of raffinose that occur in the presence of oxygen.
The sequence of enzymatic reactions by which a cap structure is added to the 5' end of a nascent RNA polymerase II transcript. All RNA polymerase II transcripts receive a 7-methyl-G cap. Then for (at least) small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs), the7-methyl-G cap is hypermethylated to become a 2,2,7-trimethylguanosine (TMG) cap.
The appearance of granulysin due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
Catalysis of the reaction: L-DOPA + O2 = ? + H2O. This reaction catalyzes the oxygenation of the dopamine precursor L-DOPA, to the corresponding o-quinone.
Catalysis of the reaction: dopamine + O2 = ? + H2O. This reaction catalyzes the oxygenation of dopamine to the corresponding o-quinone.
The addition of a methyl group to the N7 atom in the base portion of a guanine nucleotide residue in an RNA molecule.
A multiprotein ATPase complex involved in the release of polyubiquitinated proteins, including those damaged by oxidative stress, from the outer mitochondria membrane into the cytoplasm where they are presented to the proteasome for proteolysis, a process also referred to as mitochondria-associated degradation (MAD). In budding yeast, this complex includes Cdc48p, Npl4p and Vms1p.
A multiprotein ATPase complex involved in the release of polyubiquitinated proteins, including those damaged by oxidative stress, from the outer mitochondria membrane into the cytoplasm where they are presented to the proteasome for proteolysis, a process also referred to as mitochondria-associated degradation (MAD). In budding yeast, this complex includes Cdc48p, Npl4p and Vms1p.
A multiprotein ATPase complex involved in the release of polyubiquitinated proteins, including those damaged by oxidative stress, from the outer mitochondria membrane into the cytoplasm where they are presented to the proteasome for proteolysis, a process also referred to as mitochondria-associated degradation (MAD). In budding yeast, this complex includes Cdc48p, Npl4p and Vms1p.
The growth of colonies in filamentous chains of cells into a substrate.
Self-propelled movement of an organism from one location to another through water, often by means of active fin movement.
The response to external or internal stimuli that results in the locomotory process of swimming. Swimming is the self-propelled movement of an organism through the water.
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 diuretic stimulus. A diuretic is an agent that promotes the excretion of urine through its effects on kidney function.
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 methylphenidate 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 methylphenidate 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 methylphenidate 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 gemcitabine stimulus. Gemcitabine is a 2'-deoxycytidine having geminal fluoro substituents in the 2'-position, and is used as a drug in the treatment of various carcinomas.
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 gemcitabine stimulus. Gemcitabine is a 2'-deoxycytidine having geminal fluoro substituents in the 2'-position, and is used as a drug in the treatment of various carcinomas.
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 statin stimulus. Statins are organooxygen compounds whose structure is related to compactin (mevastatin) and which may be used as an anticholesteremic drug due its EC 1.1.1.34/EC 1.1.1.88 (hydroxymethylglutaryl-CoA reductase) inhibitory properties.
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 statin stimulus. Statins are organooxygen compounds whose structure is related to compactin (mevastatin) and which may be used as an anticholesteremic drug due its EC 1.1.1.34/EC 1.1.1.88 (hydroxymethylglutaryl-CoA reductase) inhibitory properties.
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 lapatinib 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 5-fluorouracil 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 5-fluorouracil 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 antidepressant stimulus, a mood-stimulating drug.
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 anticonvulsant stimulus, a drug used to prevent seizures or reduce their severity.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a deprivation of nitrogen.
Any process that activates or increases the frequency, rate or extent of directed movement of proteins from the nucleus into the cytoplasm in response to deprivation of glucose.
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 L-canavanine stimulus. L-canavanine is L-homoserine substituted at oxygen with a guanidino (carbamimidamido) group.
The non-sexual aggregation between single-celled organisms of different species.
The non-sexual aggregation between single-celled organisms of different species mediated by interaction of a protein in one species and a carbohydrate in the other species. For example, coflocculation between S. pombe and E. coli is mediated by mannose residues in the yeast cell wall interacting with lectin protein in E. coli cell projections.
Actin-based structures involved in establishing close contact between Sertoli-Sertoli cells or Sertoli-spermatids in the seminiferous tubules of the testes.
The aggregation, arrangement and bonding together of a set of components to form a SAGA complex, a SAGA-type histone acetyltransferase complex that contains Spt8 (in budding yeast) or a homolog thereof.
A filamentous cortical structure formed, in S. pombe, by the eisosome component Pil1.
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 iloperidone 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 ximelagatran stimulus.
The phosphorylation by a protein of one or more of its own serine amino acid residues, or a serine residue on an identical protein.
The phosphorylation by a protein of a residue on an identical protein. For example, phosphorylation by the other kinase within a homodimer.
The phosphorylation by a protein of one or more of its own amino acid residues.
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 reflecting a decline in the level of oxygen.
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 stimulus reflecting a decline in the level of oxygen.
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 stimulus reflecting an increase in the level of oxygen.
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 reflecting an increase in the level of oxygen.
Removal of a DNA interstrand crosslink (a covalent attachment of DNA bases on opposite strands of the DNA) and restoration of the DNA. DNA interstrand crosslinks occur when both strands of duplex DNA are covalently tethered together (e.g. by an exogenous or endogenous agent), thus preventing the strand unwinding necessary for essential DNA functions such as transcription and replication.
Removal of a DNA interstrand crosslink (a covalent attachment of DNA bases on opposite strands of the DNA) and restoration of the DNA by a mechanism that involves the exchange, reciprocal or nonreciprocal, of genetic material between the broken DNA molecule and a homologous region of DNA.
Removal of a DNA interstrand crosslink (a covalent attachment of DNA bases on opposite strands of the DNA) and restoration of the DNA by a mechanism that does not involve homologous DNA recombination.
Removal of a DNA interstrand crosslink (a covalent attachment of DNA bases on opposite strands of the DNA) and restoration of the DNA by a mechanism that does not involve homologous DNA recombination.
A receptor-mediated endocytosis process that results in the movement of a B cell receptor from the plasma membrane to the inside of the cell.
A receptor-mediated endocytosis process that results in the movement of a B cell receptor from the plasma membrane to the inside of the cell.
A receptor-mediated endocytosis process that results in the movement of a B cell receptor from the plasma membrane to the inside of the cell.
The appearance of macrophage colony-stimulating factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The progression of the atrioventricular canal over time, from its formation to the mature structure. The atrioventricular canal is the part of the heart connecting the atrium to the cardiac ventricle.
The process in which the anatomical structures of lymph vessels are generated and organized. The lymph vessel is the vasculature carrying lymph.
The process in which the anatomical structures of the umbilical cord are generated and organized. The umbilical cord is an organ or embryonic origin consisting of the 2 umbilical arteries and the one umbilical vein. The umbilical cord connects the cardiovascular system of the fetus to the mother via the placenta.
The process in which a relatively unspecialized cell acquires specialized features of an ameloblast, a cylindrical epithelial cell in the innermost layer of the enamel organ.
The developmental growth that results in the increase in length of the embryonic heart tube. The embryonic heart tube is an epithelial tube that will give rise to the mature heart.
Catalysis of the reaction: S-adenosyl-L-methionine + adenine(2030) in 23S rRNA = S-adenosyl-L-homocysteine + rRNA containing N(6)-methyladenine(2030) in 23S rRNA.
Catalysis of the reaction: S-adenosyl-L-methionine + guanosine(1516) in 16S rRNA = N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine.
Any process in which a protein is transported to, and/or maintained in, the M band. The M band is the midline of aligned thick filaments in a sarcomere.
Any process in which a protein is transported to, and/or maintained in, the M band. The M band is the midline of aligned thick filaments in a sarcomere.
Any process in which a protein is transported to, and/or maintained in, the M band. The M band is the midline of aligned thick filaments in a sarcomere.
Any process in which a protein is transported to, and/or maintained in, the M band. The M band is the midline of aligned thick filaments in a sarcomere.
Catalysis of the reaction: 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O = 2-(acetylamino)-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-beta-D-glucopyranose + acetate.
Catalysis of the reaction: 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O = 2-(acetylamino)-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-beta-D-glucopyranose + acetate.
Catalysis of the reaction: 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O = 2-(acetylamino)-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-beta-D-glucopyranose + acetate.
Interacting selectively and non-covalently with a regulatory subunit of phosphatidylinositol 3-kinase. The regulatory subunit associates with the catalytic subunit to regulate both its activity and subcellular location.
Interacting selectively and non-covalently with a regulatory subunit of phosphatidylinositol 3-kinase. The regulatory subunit associates with the catalytic subunit to regulate both its activity and subcellular location.
Interacting selectively and non-covalently with the catalytic subunit of a phosphatidylinositol 3-kinase. The catalytic subunit catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring.
Interacting selectively and non-covalently with the catalytic subunit of a phosphatidylinositol 3-kinase. The catalytic subunit catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring.
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 sterol stimulus.
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 sterol stimulus.
Any process in which the SREBP-SCAP complex is maintained in the endoplasmic reticulum and prevented from moving elsewhere. The SREBP-SCAP complex is formed by the association of sterol regulatory element binding protein (SREBP) and SREBP-cleavage-activating protein (SCAP). In the absence of sterols, the SREBP-SCAP complex is packaged into COPII vesicles and travels to the Golgi apparatus to be processed. In the presence of sterols, the complex binds ER-resident proteins such as INSIG, which retain the complex in the ER.
Catalysis of the hydrolysis of a 5' tyrosyl-RNA phosphodiester bond between a protein and RNA. In picornaviruses, this covalent bond connects VPg, a viral-encoded protein essential for RNA replication, to the 5' end of all nascent picornavirus genomes; it is cleaved from viral RNA prior to its engaging in protein synthesis.
Catalysis of the hydrolysis of a 5' tyrosyl-RNA phosphodiester bond between a protein and RNA. In picornaviruses, this covalent bond connects VPg, a viral-encoded protein essential for RNA replication, to the 5' end of all nascent picornavirus genomes; it is cleaved from viral RNA prior to its engaging in protein synthesis.
Catalysis of the hydrolysis of a 5' tyrosyl-RNA phosphodiester bond between a protein and RNA. In picornaviruses, this covalent bond connects VPg, a viral-encoded protein essential for RNA replication, to the 5' end of all nascent picornavirus genomes; it is cleaved from viral RNA prior to its engaging in protein synthesis.
Catalysis of the hydrolysis of a 5' tyrosyl-RNA phosphodiester bond between a protein and RNA. In picornaviruses, this covalent bond connects VPg, a viral-encoded protein essential for RNA replication, to the 5' end of all nascent picornavirus genomes; it is cleaved from viral RNA prior to its engaging in protein synthesis.
Combining with a peptide pheromone, and transmitting the signal across the membrane to initiate a change in cell activity.
Combining with the mating-type peptide pheromone M-factor and transmitting the signal across the membrane to initiate a change in cell activity. M-factor is a nine-membered oligopeptide that consists of tyrosyl, threonyl, prolyl, lysyl, valyl, prolyl, tyrosyl, methionyl and methyl S-farnesylcysteinate residues joined in sequence, and is a peptide pheromone released by Schizosaccharomyces pombe cells of the cellular mating type Minus.
Combining with the mating-type peptide pheromone M-factor and transmitting the signal across the membrane to initiate a change in cell activity. M-factor is a nine-membered oligopeptide that consists of tyrosyl, threonyl, prolyl, lysyl, valyl, prolyl, tyrosyl, methionyl and methyl S-farnesylcysteinate residues joined in sequence, and is a peptide pheromone released by Schizosaccharomyces pombe cells of the cellular mating type Minus.
Combining with the mating-type peptide pheromone P-factor and transmitting the signal across the membrane to initiate a change in cell activity. P-factor is a polypeptide of 23 residues, with the sequence Thr-Tyr-Ala-Asp-Phe-Leu-Arg-Ala-Tyr-Gln-Ser-Trp-Asn-Thr-Phe-Val-Asn-Pro-Asp-Arg-Pro-Asn-Leu, and is a peptide pheromone released by Schizosaccharomyces pombe cells of the cellular mating type Plus.
Combining with the mating-type peptide pheromone P-factor and transmitting the signal across the membrane to initiate a change in cell activity. P-factor is a polypeptide of 23 residues, with the sequence Thr-Tyr-Ala-Asp-Phe-Leu-Arg-Ala-Tyr-Gln-Ser-Trp-Asn-Thr-Phe-Val-Asn-Pro-Asp-Arg-Pro-Asn-Leu, and is a peptide pheromone released by Schizosaccharomyces pombe cells of the cellular mating type Plus.
The regulated release of ghrelin from a cell. Ghrelin is a 28 amino acid hunger-stimulating peptide hormone.
The regulated release of pancreatic polypeptide (PP) from a cell. Pancreatic polypeptide is a 36 amino acid polypeptide secreted by islets of Langerhans cells in the pancreas.
Any series of molecular signals initiated by the binding of an extracellular ligand to a vascular endothelial growth factor receptor-1 (VEGFR-1) located on the surface of the receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by the binding of an extracellular ligand to a vascular endothelial growth factor receptor-1 (VEGFR-1) located on the surface of the receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by the binding of an extracellular ligand to a vascular endothelial growth factor receptor-1 (VEGFR-1) located on the surface of the receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by the binding of an extracellular ligand to a vascular endothelial growth factor receptor-2 (VEGFR-2) located on the surface of the receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by the binding of an extracellular ligand to a vascular endothelial growth factor receptor-2 (VEGFR-2) located on the surface of the receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by the binding of an extracellular ligand to a vascular endothelial growth factor receptor-2 (VEGFR-2) located on the surface of the receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by the binding of an extracellular ligand to a vascular endothelial growth factor receptor-2 (VEGFR-2) located on the surface of the receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by the binding of an extracellular ligand to a vascular endothelial growth factor receptor-3 (VEGFR-3) located on the surface of the receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by the binding of an extracellular ligand to a vascular endothelial growth factor receptor-3 (VEGFR-3) located on the surface of the receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any series of molecular signals initiated by the binding of an extracellular ligand to a vascular endothelial growth factor receptor-3 (VEGFR-3) located on the surface of the receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Combining with vascular endothelial growth factor A (VEGF-A) and transmitting the signal across the plasma membrane to initiate a change in cell activity.
Combining with vascular endothelial growth factor B (VEGF-B) and transmitting the signal across the plasma membrane to initiate a change in cell activity.
Combining with vascular endothelial growth factor C (VEGF-C) and transmitting the signal across the plasma membrane to initiate a change in cell activity.
Combining with vascular endothelial growth factor C (VEGF-C) and transmitting the signal across the plasma membrane to initiate a change in cell activity.
Combining with vascular endothelial growth factor D (VEGF-D) and transmitting the signal across the plasma membrane to initiate a change in cell activity.
Combining with vascular endothelial growth factor D (VEGF-D) and transmitting the signal across the plasma membrane to initiate a change in cell activity.
Combining with vascular endothelial growth factor D (VEGF-D) and transmitting the signal across the plasma membrane to initiate a change in cell activity.
Combining with vascular endothelial growth factor E (VEGF-E) and transmitting the signal across the plasma membrane to initiate a change in cell activity.
The progression of an avascular cornea over time, from its formation to the mature structure. Corneal avascularity (the absence of blood vessels in the cornea) is required for optical clarity and optimal vision. Avascular corneas are present in most animals, except Manatees.
Combining with placental growth factor (PlGF) and transmitting the signal across the plasma membrane to initiate a change in cell activity.
Combining with placental growth factor (PlGF) and transmitting the signal across the plasma membrane to initiate a change in cell activity.
Combining with placental growth factor (PlGF) and transmitting the signal across the plasma membrane to initiate a change in cell activity.
Any biological process involved in the maintenance of the steady-state number of hepatocytes within a population of cells. Hepatocytes are specialized epithelial cells of the liver that are organized into interconnected plates called lobules.
Any biological process involved in the maintenance of the steady-state number of epidermal stem cells within a population of cells.
Any biological process involved in the maintenance of the steady-state number of intestinal stem cells within a population of cells.
The movement of a dendritic cell within or between different tissues and organs of the body.
A series of molecular signals initiated by the binding of a ligand to the receptor Fas on the surface of the cell, and ending with regulation of a downstream cellular process, e.g. transcription. Fas is a death domain-containing member of the tumor necrosis factor receptor (TNFR) superfamily.
A series of molecular signals initiated by the binding of a ligand to the receptor Fas on the surface of the cell, and ending with regulation of a downstream cellular process, e.g. transcription. Fas is a death domain-containing member of the tumor necrosis factor receptor (TNFR) superfamily.
A series of molecular signals initiated by the binding of a ligand to the receptor Fas on the surface of the cell, and ending with regulation of a downstream cellular process, e.g. transcription. Fas is a death domain-containing member of the tumor necrosis factor receptor (TNFR) superfamily.
A series of molecular signals initiated by the binding of a ligand to the receptor Fas on the surface of the cell, and ending with regulation of a downstream cellular process, e.g. transcription. Fas is a death domain-containing member of the tumor necrosis factor receptor (TNFR) superfamily.
A series of molecular signals initiated by the binding of a ligand to the receptor Fas on the surface of the cell, and ending with regulation of a downstream cellular process, e.g. transcription. Fas is a death domain-containing member of the tumor necrosis factor receptor (TNFR) superfamily.
A series of molecular signals initiated by the binding of a ligand to the receptor Fas on the surface of the cell, and ending with regulation of a downstream cellular process, e.g. transcription. Fas is a death domain-containing member of the tumor necrosis factor receptor (TNFR) superfamily.
A series of molecular signals initiated by the binding of a ligand to the receptor Fas on the surface of the cell, and ending with regulation of a downstream cellular process, e.g. transcription. Fas is a death domain-containing member of the tumor necrosis factor receptor (TNFR) superfamily.
The lipid bilayer of a virion, a complete fully infectious extracellular virus particle.
The attachment of a lymphocyte to an endothelial cell of a high endothelial venule (HEV) via adhesion molecules. A HEV cell is an endothelial cell that is cuboidal, expresses leukocyte-specific receptors, and allows for passage of lymphocytes into bloodstream.
The attachment of a lymphocyte to an endothelial cell of a high endothelial venule (HEV) via adhesion molecules. A HEV cell is an endothelial cell that is cuboidal, expresses leukocyte-specific receptors, and allows for passage of lymphocytes into bloodstream.
The process of hardening a chitin-based cuticle by mineral incorporation. For example, the cuticle of crustaceans is hardened by the incorporation of calcium carbonate.
The process of hardening of a chitin-based cuticle by protein cross-linking, and the incorporation of phenolic precursors. This mechanism of cuticle hardening occurs in insects and is usually accompanied by darkening of the cuticle.
The specific behavior of an organism that combines cognitive functions and physical movement. For example, driving a car, throwing a ball, or playing a musical instrument.
Generation and organization of a platelet, a non-nucleated disk-shaped cell formed by extrusion from megakaryocytes, found in the blood of all mammals, and mainly involved in blood coagulation.
A developmental process, independent of morphogenetic (shape) change, that is required for a platelet to attain its fully functional state. A platelet is a non-nucleated disk-shaped cell formed by extrusion from megakaryocytes, found in the blood of all mammals, and mainly involved in blood coagulation.
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 L-cysteine stimulus. L-cysteine is an optically active form of cysteine having L-configuration.
Catalysis of the reaction: D-5-monosubstituted hydantoin = L-5-monosubstituted hydantoin.
The non-sexual aggregation of single-celled organisms mediated by the binding of cell wall proteins on one cell to galactose residues on the other.
The non-sexual aggregation of single-celled organisms mediated by the binding of cell wall proteins on one cell to mannose residues on the other.
The modification of histone H2A by addition of ubiquitin group at lysine 13 (H2A-K13) in metazoans, and at the equivalent residue in other organisms. Monoubiquitin is first attached to H2A-K13 and K63-linked ubiquitin chains are then extended from this monoubiquitin.
The modification of histone H2A by addition of ubiquitin group at lysine 15 (H2A-K15) in metazoans, and at the equivalent residue in other organisms. Monoubiquitin is first attached to H2A-K15 and K63-linked ubiquitin chains are then extended from this monoubiquitin.
The modification of histone H2A by addition of a single ubiquitin group to lysine-119 (H2A- K119) in metazoans, and at the equivalent residue in other organisms.
Catalysis of the reaction: 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a = bacteriochlorophyllide a + 2 H+.
Catalysis of the reaction: L-tyrosine + S-adenosyl-L-methionine + reduced acceptor = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + acceptor + 2 H+.
Catalysis of the reaction: 2,3-diphosphoglycerate (DPG) + ATP = cyclic 2,3-diphosphoglycerate (cDPG) + ADP + phosphate.
Catalysis of the reaction: 2,3-diphosphoglycerate (DPG) + ATP = cyclic 2,3-diphosphoglycerate (cDPG) + ADP + phosphate.
Catalysis of the reaction: 2-phosphoglycerate + ATP = 2,3-diphosphoglycerate + ADP.
The formation of a D-alanyl ester of lipoteichoic acid by transfer of D-Ala onto a membrane-associated lipoteichoic acid (LTA).
The formation of a D-alanyl ester of lipoteichoic acid by transfer of D-Ala onto a membrane-associated lipoteichoic acid (LTA).
The formation of a D-alanyl ester of lipoteichoic acid by transfer of D-Ala onto a membrane-associated lipoteichoic acid (LTA).
The elimination by an organism of potassium in the urine.
The elimination by an organism of potassium in the urine.
The elimination by an organism of potassium in the urine.
The process in which the sorocarp stalk is generated and organized. The sorocarp stalk is a tubular structure that consists of cellulose-covered cells stacked on top of each other and surrounded by an acellular stalk tube composed of cellulose and glycoprotein. An example of this process is found in Dictyostelium discoideum.
Catalysis of the interconversion of the two enantiomers of a chiral amino acid or amino acid derivative.
A double layer of lipid molecules that surrounds an ascus, a capsule containing the sexual spores in some fungi.
The release of transforming growth factor beta (TGF-beta) from its latent state. TGF-beta is secreted as part of a large latent complex (LLC) that is targeted to the extracellular matrix. Release of TGFbeta from its latent state is required for TGFbeta to bind to its receptors, and can occur by a variety of mechanisms.
The release of transforming growth factor beta (TGF-beta) from its latent state. TGF-beta is secreted as part of a large latent complex (LLC) that is targeted to the extracellular matrix. Release of TGFbeta from its latent state is required for TGFbeta to bind to its receptors, and can occur by a variety of mechanisms.
The release of transforming growth factor beta (TGF-beta) from its latent state. TGF-beta is secreted as part of a large latent complex (LLC) that is targeted to the extracellular matrix. Release of TGFbeta from its latent state is required for TGFbeta to bind to its receptors, and can occur by a variety of mechanisms.
The release of transforming growth factor beta (TGF-beta) from its latent state. TGF-beta is secreted as part of a large latent complex (LLC) that is targeted to the extracellular matrix. Release of TGFbeta from its latent state is required for TGFbeta to bind to its receptors, and can occur by a variety of mechanisms.
The release of transforming growth factor beta (TGF-beta) from its latent state. TGF-beta is secreted as part of a large latent complex (LLC) that is targeted to the extracellular matrix. Release of TGFbeta from its latent state is required for TGFbeta to bind to its receptors, and can occur by a variety of mechanisms.
The release of transforming growth factor beta (TGF-beta) from its latent state. TGF-beta is secreted as part of a large latent complex (LLC) that is targeted to the extracellular matrix. Release of TGFbeta from its latent state is required for TGFbeta to bind to its receptors, and can occur by a variety of mechanisms.
The release of transforming growth factor beta1 (TGF-beta1) from its latent state.
The release of transforming growth factor beta1 (TGF-beta1) from its latent state.
The release of transforming growth factor beta1 (TGF-beta1) from its latent state.
The release of transforming growth factor beta1 (TGF-beta1) from its latent state.
The release of transforming growth factor beta1 (TGF-beta1) from its latent state.
The release of transforming growth factor beta1 (TGF-beta1) from its latent state.
The release of transforming growth factor beta 2 (TGF-beta2) from its latent state.
The release of transforming growth factor beta 2 (TGF-beta2) from its latent state.
The release of transforming growth factor beta 2 (TGF-beta2) from its latent state.
The release of transforming growth factor beta 3 (TGF-beta3) from its latent state.
The release of transforming growth factor beta 3 (TGF-beta3) from its latent state.
The release of transforming growth factor beta 3 (TGF-beta3) from its latent state.
The ability of a photoreceptor to adjust to varying levels of light.
The processes required for a cone photoreceptor to recover, following light activation, so that it can respond to a subsequent light stimulus. Cone recovery requires the shutoff of active participants in the phototransduction cascade, including the visual pigment and downstream signal transducers.
The processes required for a cone photoreceptor to recover, following light activation, so that it can respond to a subsequent light stimulus. Cone recovery requires the shutoff of active participants in the phototransduction cascade, including the visual pigment and downstream signal transducers.
The chemical reactions and pathways resulting in the breakdown of a sequence-specific DNA-binding transcription factor by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a sequence-specific DNA-binding transcription factor by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a sequence-specific DNA-binding transcription factor by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a sequence-specific DNA-binding transcription factor by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a sequence-specific DNA-binding transcription factor by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
Binding a D-alanine and presenting it for processing or offloading to a cognate enzyme. Covalently binds the D-alanine via a phosphopantetheine prosthetic group and mediates protein-protein interactions with the enzyme conferring specificity. The carrier protein provides an essential link between the D-alanine-D-alanyl carrier protein ligase and the incorporation of D-alanine into lipoteichoic acid by transferring activated D-alanine to cell membrane phosphatidylglycerol (PG).
A process in which a protein is transported to, or maintained in, the T-tubule. The 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 in which a protein is transported to, or maintained in, the T-tubule. The 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 in which a protein is transported to, or maintained in, the T-tubule. The T-tubule is an invagination of the plasma membrane of a muscle cell that extends inward from the cell surface around each myofibril.
The directed movement of an opsin (a G protein-coupled receptor of photoreceptor cells) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter or pore.
Catalysis of the reaction: alpha-L-fucose = beta-L-fucose.
Catalysis of the reaction: alpha-L-fucose = beta-L-fucose.
Catalysis of the reaction: alpha-L-fucose = beta-L-fucose.
An apical protein complex that contains the proteins Kibra, Expanded and Merlin (Mer), or orthologs thereof. In humans, the complex contains KIBRA, FDM6 and NF2.
An apical protein complex that contains the proteins Kibra, Expanded and Merlin (Mer), or orthologs thereof. In humans, the complex contains KIBRA, FDM6 and NF2.
The directed movement of sodium ions from inside of a cell, across the plasma membrane and into the extracellular region.
The directed movement of sodium ions from inside of a cell, across the plasma membrane and into the extracellular region.
The directed movement of sodium ions from inside of a cell, across the plasma membrane and into the extracellular region.
The directed movement of sodium ions from inside of a cell, across the plasma membrane and into the extracellular region.
The directed movement of sodium ions from inside of a cell, across the plasma membrane and into the extracellular region.
A form of mutualism between a fungus and the roots of a vascular plant, where hyphae of the fungus penetrate the plant cell wall and invaginate its cell membrane. Once inside, the fungus forms highly branched structures for nutrient exchange with the plant called arbuscules. Aids in the acquisition by the plant of nutrients such as phosphorus from the soil.
A form of mutualism between a fungus and the roots of a vascular plant, where hyphae of the fungus penetrate the plant cell wall and invaginate its cell membrane. Once inside, the fungus forms highly branched structures for nutrient exchange with the plant called arbuscules. Aids in the acquisition by the plant of nutrients such as phosphorus from the soil.
A form of mutualism between a fungus and the roots of a vascular plant, where hyphae of the fungus penetrate the plant cell wall and invaginate its cell membrane. Once inside, the fungus forms highly branched structures for nutrient exchange with the plant called arbuscules. Aids in the acquisition by the plant of nutrients such as phosphorus from the soil.
Conversion of vitamin D3 from its largely inactive form (calciol, also called cholecalciferol) into a hormonally active form (calcitriol). Conversion requires 25-hydroxylation of calciol in the liver to form calcidiol, and subsequent 1,alpha-hydroxylation of calcidiol in the kidney to form calcitriol.
Conversion of vitamin D3 from its largely inactive form (calciol, also called cholecalciferol) into a hormonally active form (calcitriol). Conversion requires 25-hydroxylation of calciol in the liver to form calcidiol, and subsequent 1,alpha-hydroxylation of calcidiol in the kidney to form calcitriol.
Conversion of vitamin D3 from its largely inactive form (calciol, also called cholecalciferol) into a hormonally active form (calcitriol). Conversion requires 25-hydroxylation of calciol in the liver to form calcidiol, and subsequent 1,alpha-hydroxylation of calcidiol in the kidney to form calcitriol.
Conversion of vitamin D3 from its largely inactive form (calciol, also called cholecalciferol) into a hormonally active form (calcitriol). Conversion requires 25-hydroxylation of calciol in the liver to form calcidiol, and subsequent 1,alpha-hydroxylation of calcidiol in the kidney to form calcitriol.
Conversion of vitamin D3 from its largely inactive form (calciol, also called cholecalciferol) into a hormonally active form (calcitriol). Conversion requires 25-hydroxylation of calciol in the liver to form calcidiol, and subsequent 1,alpha-hydroxylation of calcidiol in the kidney to form calcitriol.
Any of the smallest contractile units of a myofibril (striated muscle fiber).
Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol.
Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol.
Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol.
Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol.
Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyldiphospho-ditrans,octacis-undecaprenol.
Catalysis of the reaction: D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate. The reaction occurs in two steps: L-glutamine + H2O = L-glutamate + NH3, and subsequently D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + NH3 = pyridoxal 5'-phosphate + 4 H2O + phosphate.
Catalysis of the reaction: D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate. The reaction occurs in two steps: L-glutamine + H2O = L-glutamate + NH3, and subsequently D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + NH3 = pyridoxal 5'-phosphate + 4 H2O + phosphate.
Catalysis of the reaction: reduced flavin + NAD+ = flavin + NADH + H+.
Catalysis of the reaction: reduced flavin + NAD+ = flavin + NADH + H+.
Catalysis of the reaction: 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMNH2 + O2 = 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMN + H2O.
Catalysis of the reaction: CDP + H2O = CMP + phosphate.
Any process in which DNA and associated proteins are formed into a compact, orderly structure within a nucleoid.
Compaction of DNA in a bacterial nucleoid into a compact structure. Often achieved by DNA supercoiling.
Compaction of DNA in a bacterial nucleoid into a compact structure. Often achieved by DNA supercoiling.
Compaction of DNA in a bacterial nucleoid into a compact structure. Often achieved by DNA supercoiling.
A protein-DNA complex that forms at the origin of replication during the initial step of DNA replication and allows the origin to become competent, or 'licensed', for replication.
A protein-DNA complex that forms at the origin of replication during the initial step of DNA replication and allows the origin to become competent, or 'licensed', for replication.
The aggregation, arrangement and bonding together of a set of components to form the pre-replicative complex, a protein-DNA complex that forms at the origin of replication during the initial step of DNA replication and allows the origin to become competent, or 'licensed', for replication.
The aggregation, arrangement and bonding together of a set of components to form the pre-replicative complex, a protein-DNA complex that forms at the origin of replication during the initial step of DNA replication and allows the origin to become competent, or 'licensed', for replication.
A protein-DNA complex that forms at the bacterial oriC during the initial step of DNA replication and allows the origin to become competent, or 'licensed', for replication.
The aggregation, arrangement and bonding together of a set of components to form the bacterial pre-replicative complex, a protein-DNA complex that forms at the bacterial oriC during the initial step of DNA replication and allows the origin to become competent, or 'licensed', for replication.
The aggregation, arrangement and bonding together of a set of components to form the bacterial pre-replicative complex, a protein-DNA complex that forms at the bacterial oriC during the initial step of DNA replication and allows the origin to become competent, or 'licensed', for replication.
A ring-shaped structure that forms at the medial cortex of a symmetrically dividing cell at the onset of cytokinesis; composed of members of the conserved family of filament forming proteins called septins as well as septin-associated proteins.
The appearance of chemokine (C-C motif) ligand 20 (CCL20) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-C motif) ligand 20 (CCL20) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-C motif) ligand 20 (CCL20) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
Catalysis of the reaction: thiocyanate (SCN-) + hydrogen peroxide (H2O2) = hypothiocyanite (OSCN-) + 2 H2O. Catalyzes the hydrogen peroxide oxidation of thiocyanate.
The controlled release of amylase from a cell.
The controlled release of amylase from a cell of the pancreas.
A RNA methyltransferase complex that catalyzes the post-transcriptional methylation of adenosine to form N6-methyladenosine (m6A). In budding yeast, the MIS complex consists of Mum2p, Ime4p and Slz1p. In vertebrates, the complex consists of METTL3, METTL14 and associated components WTAP, ZC3H13, VIRMA, CBLL1/HAKAI and in some cases of RBM15 (RBM15 or RBM15B).
A RNA methyltransferase complex that catalyzes the post-transcriptional methylation of adenosine to form N6-methyladenosine (m6A). In budding yeast, the MIS complex consists of Mum2p, Ime4p and Slz1p. In vertebrates, the complex consists of METTL3, METTL14 and associated components WTAP, ZC3H13, VIRMA, CBLL1/HAKAI and in some cases of RBM15 (RBM15 or RBM15B).
A RNA methyltransferase complex that catalyzes the post-transcriptional methylation of adenosine to form N6-methyladenosine (m6A). In budding yeast, the MIS complex consists of Mum2p, Ime4p and Slz1p. In vertebrates, the complex consists of METTL3, METTL14 and associated components WTAP, ZC3H13, VIRMA, CBLL1/HAKAI and in some cases of RBM15 (RBM15 or RBM15B).
A RNA methyltransferase complex that catalyzes the post-transcriptional methylation of adenosine to form N6-methyladenosine (m6A). In budding yeast, the MIS complex consists of Mum2p, Ime4p and Slz1p. In vertebrates, the complex consists of METTL3, METTL14 and associated components WTAP, ZC3H13, VIRMA, CBLL1/HAKAI and in some cases of RBM15 (RBM15 or RBM15B).
A RNA methyltransferase complex that catalyzes the post-transcriptional methylation of adenosine to form N6-methyladenosine (m6A). In budding yeast, the MIS complex consists of Mum2p, Ime4p and Slz1p. In vertebrates, the complex consists of METTL3, METTL14 and associated components WTAP, ZC3H13, VIRMA, CBLL1/HAKAI and in some cases of RBM15 (RBM15 or RBM15B).
A RNA methyltransferase complex that catalyzes the post-transcriptional methylation of adenosine to form N6-methyladenosine (m6A). In budding yeast, the MIS complex consists of Mum2p, Ime4p and Slz1p. In vertebrates, the complex consists of METTL3, METTL14 and associated components WTAP, ZC3H13, VIRMA, CBLL1/HAKAI and in some cases of RBM15 (RBM15 or RBM15B).
Catalysis of the reaction: formate + a quinone = CO2 + a quinol.
Catalysis of the reaction: formate + a quinone = CO2 + a quinol.
Catalysis of the reaction: formate + a quinone = CO2 + a quinol.
A multi-protein complex containing at least the T-cell receptor complex and the LAT (linker for activation of T cells) scaffold protein. Also contains a variety of signaling proteins including co-receptors, kinases, phosphatases and adaptors such as CD8. Connects events on the plasma membrane to distal signaling cascades to ultimately modulate T cell biology.
A multi-protein complex containing at least the T-cell receptor complex and the LAT (linker for activation of T cells) scaffold protein. Also contains a variety of signaling proteins including co-receptors, kinases, phosphatases and adaptors such as CD8. Connects events on the plasma membrane to distal signaling cascades to ultimately modulate T cell biology.
The aggregation, arrangement and bonding together of a set of components to form a TCR signalosome.
The aggregation, arrangement and bonding together of a set of components to form a TCR signalosome.
Combining with a short neuropeptide F and transmitting the signal within the cell to initiate a change in cell activity. Short neuropeptide F is an arthropod peptide of less than 28 residues (as small as 8-10 residues in some species) with a C-terminal RFamide or LRFamide.
Combining with a pyrokinin and transmitting the signal within the cell to induce a change in cell activity. Pyrokinins are a group of insect neuropeptides that share the common C-terminal pentapeptide sequence Phe-X-Pro-Arg-Leu-NH2 (X = S, T, K, A, or G). They play a central role in diverse physiological processes including stimulation of gut motility, production and release of sex pheromones, diapause, and pupariation.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, which promotes unfolding of protein substrates, and channel opening of the core proteasome.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, which promotes unfolding of protein substrates, and channel opening of the core proteasome.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, which promotes unfolding of protein substrates, and channel opening of the core proteasome.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, which promotes unfolding of protein substrates, and channel opening of the core proteasome.
Catalysis of the reaction: arachidonate + O(2) = (5Z,8S,9E,11Z,14Z)-8-hydroperoxyicosa-5,9,11,14-tetraenoate.
Catalysis of the reaction: arachidonate + O(2) = (5Z,8S,9E,11Z,14Z)-8-hydroperoxyicosa-5,9,11,14-tetraenoate.
The process in which double-stranded small interfering RNA (ds siRNA) molecules are converted to single-stranded small interfering RNA (ss siRNA).
The component of the cell outer membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the cell outer membrane consisting of gene products and protein complexes that are tethered to the periplasmic side of membrane by only a covalently attached anchor, embedded in the periplasmic side of the membrane only.
The component of the cell outer membrane consisting of gene products and protein complexes that are tethered to the periplasmic side of membrane by only a covalently attached anchor, embedded in the periplasmic side of the membrane only.
A mycolic acid-rich cell outer membrane containing a lipid bilayer and long-chain mycolic acids (hydroxylated branched-chain fatty acids) that are covalently linked to the cell wall peptidoglycan via an arabinogalactan network. Found in mycobacteria and related genera (e.g. corynebacteria).
A mycolic acid-rich cell outer membrane containing a lipid bilayer and long-chain mycolic acids (hydroxylated branched-chain fatty acids) that are covalently linked to the cell wall peptidoglycan via an arabinogalactan network. Found in mycobacteria and related genera (e.g. corynebacteria).
A mycolic acid-rich cell outer membrane containing a lipid bilayer and long-chain mycolic acids (hydroxylated branched-chain fatty acids) that are covalently linked to the cell wall peptidoglycan via an arabinogalactan network. Found in mycobacteria and related genera (e.g. corynebacteria).
A mycolic acid-rich cell outer membrane containing a lipid bilayer and long-chain mycolic acids (hydroxylated branched-chain fatty acids) that are covalently linked to the cell wall peptidoglycan via an arabinogalactan network. Found in mycobacteria and related genera (e.g. corynebacteria).
Catalysis of the reaction: acetyl-CoA + histone H3 L-lysine (position 14) = CoA + histone H3 N6-acetyl-L-lysine (position 14).
A protein complex that can catalyze the acetylation of lysine at position 14 in histone H3.
A protein complex that can catalyze the acetylation of lysine at position 14 in histone H3.
A protein complex that can catalyze the acetylation of lysine at position 14 in histone H3.
A protein complex that can catalyze the acetylation of lysine at position 14 in histone H3.
A protein complex that can catalyze the acetylation of lysine at position 14 in histone H3, and contains Mst2 as the catalytic subunit. In fission yeast, contains at least Mst2, Nto1, Ptf2, Ptf1 and Eaf6.
A protein complex that can catalyze the acetylation of lysine at position 14 in histone H3, and contains Mst2 as the catalytic subunit. In fission yeast, contains at least Mst2, Nto1, Ptf2, Ptf1 and Eaf6.
A protein complex that can catalyze the acetylation of lysine at position 14 in histone H3, and contains Mst2 as the catalytic subunit. In fission yeast, contains at least Mst2, Nto1, Ptf2, Ptf1 and Eaf6.
A trimeric protein complex containing a H-NS homodimer and a Cnu monomer. In bacteria, this complex negatively regulates transcription of a range of genes.
Catalysis of the reaction: acetyl-CoA + oxalate = acetate + oxalyl-CoA.
The hydrolysis of peptidyl-arginine to form peptidyl-citrulline at position 26 in histone H3.
The hydrolysis of peptidyl-arginine to form peptidyl-citrulline on a histone protein.
Any process that modulates the propensity of transfer RNA (tRNA) molecules to degradation. Includes processes that both stabilize and destabilize tRNAs.
Prevention of degradation of tRNA molecules.
Any process that decreases the stability of a tRNA molecule, making it more vulnerable to degradative processes.
The component of the mycolate outer membrane consisting of the gene products and protein complexes having either part of their peptide sequence embedded in the hydrophobic region of the membrane or some other covalently attached group such as a GPI anchor that is similarly embedded in the membrane.
The component of the mycolate outer membrane consisting of the gene products and protein complexes having either part of their peptide sequence embedded in the hydrophobic region of the membrane or some other covalently attached group such as a GPI anchor that is similarly embedded in the membrane.
The component of the mycolate outer membrane consisting of the gene products and protein complexes having either part of their peptide sequence embedded in the hydrophobic region of the membrane or some other covalently attached group such as a GPI anchor that is similarly embedded in the membrane.
The component of the mycolate outer membrane consisting of the gene products having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
The component of the mycolate outer membrane consisting of the gene products having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
The component of the mycolate outer membrane consisting of the gene products having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
The component of mycolate outer 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 mycolate outer 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 mycolate outer 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 mycolate membrane consisting of gene products and protein complexes that are loosely bound to its external surface, but not integrated into the hydrophobic region.
The component of mycolate membrane consisting of gene products and protein complexes that are loosely bound to its external surface, but not integrated into the hydrophobic region.
The component of mycolate membrane consisting of gene products and protein complexes that are loosely bound to its external surface, but not integrated into the hydrophobic region.
Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate.
Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate.
Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate.
Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate.
Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate = 3 diphosphate + all-trans-hexaprenyl diphosphate.
Catalysis of the reaction: (2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate = 3 diphosphate + all-trans-hexaprenyl diphosphate.
Catalysis of the reaction: O-phospho-L-serine + H2O <=> L-serine + phosphate.
Catalysis of the reaction: O-phospho-D-serine + H2O <=> L-serine + phosphate.
Catalysis of the reaction: ditrans,octacis-undecaprenyl phosphate + GDP-alpha-D-mannose = D-mannosyl undecaprenyl phosphate+ GDP.
Catalysis of the reaction: all-trans-undecaprenyl phosphate + GDP-alpha-D-mannose = D-mannosyl undecaprenyl phosphate + GDP.
Catalysis of the reaction: adenosylcobinamide + GTP = adenosylcobinamide phosphate + GDP + H+.
Catalysis of the reaction: adenosylcobinamide + ATP = adenosylcobinamide phosphate + ADP + H+.
Catalysis of the reaction: ATP + CMP = ADP + CDP.
Catalysis of the reaction: ATP + dCMP = ADP + dCDP.
Catalysis of the reaction: ATP + undecaprenol + all-trans-undecaprenyl phosphate + ADP + H+.
Catalysis of the reaction: di-trans, octa-cis-undecaprenol + ATP = di-trans,octa-cis-undecaprenyl phosphate + ADP + H+.
Catalysis of the reaction: ethylnitronate + FMNH(2) + O(2) = acetaldehyde + FMN + H(2)O + H(+) + nitrite.
Interacting selectively and non-covalently with a protein upon poly-ubiquitination formed by linkages between lysine residues at position 48 in the target protein.
An Isw1 complex that binds DNA and has nucleosome-stimulated ATPase activity. In S. cerevisiae, contains an Isw1p ATPase subunit in complex with Ioc3p.
An Isw1 complex that binds DNA and has nucleosome-stimulated ATPase activity. In S. cerevisiae, contains an Isw1p ATPase subunit in complex with Ioc2p and Ioc4p.
A homeostatic process in which the lens is maintained in a highly refractive, transparent state to allow for optimal focusing of light on the retina.
A homeostatic process in which the lens is maintained in a highly refractive, transparent state to allow for optimal focusing of light on the retina.
Catalysis of the reaction: acetyl-CoA + H2O + oxaloacetate = citrate + CoA.
Catalysis of the reaction: (R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+.
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out).
Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out).
Catalysis of the reaction: 3'-phosphoadenylyl sulfate + dermatan = adenosine 3',5'-bisphosphate + dermatan 6'-sulfate.
A process in which a calcium ion (Ca2+) is transported from the cytosol, into the mitochondrial matrix.
A process in which a calcium ion (Ca2+) is transported from the cytosol, into the mitochondrial matrix.
A process in which a calcium ion (Ca2+) is transported from the cytosol, into the mitochondrial matrix.
A process in which a calcium ion (Ca2+) is transported from the cytosol, into the mitochondrial matrix.
The self-renewing division of a neuronal stem cell.
The process in which an undifferentiated cell acquires the features of a myofibroblast 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 the accumulation of sugar-phosphate.
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 the accumulation of glucose-phosphate.
The end of a microtubule that does not preferentially grow (polymerize).
Cleavage of the 5'-cap of a nuclear-transcribed mRNA that has been modified by the enzymatic addition of a sequence of uridylyl residues (polyuridylation) at the 3' end.
Methylation of the 2'-O-ribose of the first or second transcribed nucleotide of a 5'-capped mRNA.
An endosomal sorting complex involved in membrane fission processes related to sorting of multivesicular bodies (MVB) in the endocytic pathway, cytokinesis and viral budding among other processes.
An RNA interference where the silencing signal spreads along the target mRNA in a 5' or 3' direction, outside of the initial target sequence.
A protein complex that has growth factor activity.
Catalysis of the transfer of a iron-sulfur cluster from one compound (donor) to another (acceptor).
Catalysis of the reaction: L-methionine (S)-S-oxide + thioredoxin -> L-methionine + thioredoxin disulfide + H2O.
A cytoplasmic, non-membrane bound granule of, at least, keratinocyte. Associated to keratin intermediate filaments and partially crosslinked to the cell envelope.
Interacting selectively and non-covalently with a hepatocyte growth factor.
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 stress acting at the cell envelope.
Interacting selectively and non-covalently with a BLOC-2 complex, a protein complex required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.
An extrinsic apoptotic signaling pathway initiated by the binding of the ligand TRAIL (tumor necrosis factor-related apoptosis-inducing ligand) to a death receptor on the cell surface.
An extrinsic apoptotic signaling pathway initiated by the binding of the ligand TRAIL (tumor necrosis factor-related apoptosis-inducing ligand) to a death receptor on the cell surface.
An extrinsic apoptotic signaling pathway initiated by the binding of the ligand TRAIL (tumor necrosis factor-related apoptosis-inducing ligand) to a death receptor on the cell surface.
Combining with the ligand TRAIL (tumor necrosis factor-related apoptosis-inducing ligand) and transmitting the signal from one side of the plasma membrane to the other to initiate apoptotic cell death.
A ribonucleoprotein granule located in the cytoplasm.
The trafficking of synaptic vesicles from the pre-synaptic membrane so the vesicle can dock and prime for another round of exocytosis and neurotransmitter release. Recycling occurs after synaptic vesicle exocytosis, and is necessary to replenish presynaptic vesicle pools, sustain transmitter release and preserve the structural integrity of the presynaptic membrane. Recycling can occur following transient fusion with the presynaptic membrane (kiss and run), or via endocytosis of presynaptic membrane.
The trafficking of synaptic vesicles from the pre-synaptic membrane so the vesicle can dock and prime for another round of exocytosis and neurotransmitter release. Recycling occurs after synaptic vesicle exocytosis, and is necessary to replenish presynaptic vesicle pools, sustain transmitter release and preserve the structural integrity of the presynaptic membrane. Recycling can occur following transient fusion with the presynaptic membrane (kiss and run), or via endocytosis of presynaptic membrane.
Synaptic vesicle recycling where vesicles endocytose via clathrin-coated pits, re-acidify, and refill with neurotransmitters after passing through an endosomal intermediate.
Synaptic vesicle recycling where vesicles endocytose via clathrin-coated pits, re-acidify, and refill with neurotransmitters after passing through an endosomal intermediate.
Catalysis of the reaction: 5-hydroxy-L-tryptophan + H+ = CO2 + serotonin.
Catalysis of the reaction: L-dopa + H+ = CO2 + dopamine.
Catalysis of the reaction: L-dopa + H+ = CO2 + dopamine.
Catalysis of the reaction: L-dopa + H+ = CO2 + dopamine.
Catalysis of the reaction: L-tryptophan + H+ = CO2 + tryptamine.
Interacts with and increases tyrosine 3-monooxygenase (tyrosine hydroxylase) activity.
Interacts with and increases tyrosine 3-monooxygenase (tyrosine hydroxylase) activity.
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 glyoxal stimulus.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of interaction between host proteins.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of interaction between host proteins.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of interaction between host proteins.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of interaction between host proteins.
Any biological process that results in permanent cessation of all vital functions of a cell upon exposure to an oxidative stress stimulus.
Any biological process that results in permanent cessation of all vital functions of a cell upon exposure to hydrogen peroxide (H2O2).
Any biological process that results in permanent cessation of all vital functions of a cell upon exposure to hydrogen peroxide (H2O2).
Any biological process that results in permanent cessation of all vital functions of a neuron upon exposure to an oxidative stress stimulus.
Any biological process that results in permanent cessation of all vital functions of a neuron upon exposure to an oxidative stress stimulus.
Any biological process that results in permanent cessation of all vital functions of a neuron upon exposure to hydrogen peroxide (H2O2).
Any biological process that results in permanent cessation of all vital functions of a neuron upon exposure to hydrogen peroxide (H2O2).
Any biological process that results in permanent cessation of all vital functions of a neuron upon exposure to hydrogen peroxide (H2O2).
The region of a neuron that includes the cell body (cell soma) and dendrite(s), but excludes the axon.
Interacts with and increases L-dopa decarboxylase activity.
Interacts with, and stops, prevents or reduces the activity of a peroxidase.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron. The pathway is induced in response to oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron. The pathway is induced in response to oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron. The pathway is induced in response to oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to hydrogen peroxide (H2O2).
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to hydrogen peroxide (H2O2).
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to hydrogen peroxide (H2O2).
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to hydrogen peroxide (H2O2).
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron in response to hydrogen peroxide.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron in response to hydrogen peroxide.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron in response to hydrogen peroxide.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron in response to hydrogen peroxide.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron in response to hydrogen peroxide.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron. The pathway is induced in response to a stimulus indicating endoplasmic reticulum (ER) stress, and ends when the execution phase of apoptosis is triggered. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron. The pathway is induced in response to a stimulus indicating endoplasmic reticulum (ER) stress, and ends when the execution phase of apoptosis is triggered. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron. The pathway is induced in response to a stimulus indicating endoplasmic reticulum (ER) stress, and ends when the execution phase of apoptosis is triggered. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a neuron. The pathway is induced in response to a stimulus indicating endoplasmic reticulum (ER) stress, and ends when the execution phase of apoptosis is triggered. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
The characteristic movement of trunk neural crest cells from the neural tube to other locations in the vertebrate embryo.
The movement of trunk neural crest cells from the neural tube, travelling dorso-laterally into the ectoderm and continuing toward the ventral midline of the belly. These migrating trunk neural crest cells become melanocytes, the melanin-forming pigment cells.
The movement of trunk neural crest cells from the neural tube, travelling ventrally through the anterior half of each sclerotome. Trunk neural crest cells that remain in the sclerotome form the dorsal root ganglia containing the sensory neurons. Trunk neural crest cells that continue more ventrally form the sympathetic ganglia, the adrenal medulla, and the nerve clusters surrounding the aorta.
The movement of trunk neural crest cells from the neural tube, travelling ventrally through the anterior half of each sclerotome. Trunk neural crest cells that remain in the sclerotome form the dorsal root ganglia containing the sensory neurons. Trunk neural crest cells that continue more ventrally form the sympathetic ganglia, the adrenal medulla, and the nerve clusters surrounding the aorta.
The movement of trunk neural crest cells from the neural tube, travelling ventrally through the anterior half of each sclerotome. Trunk neural crest cells that remain in the sclerotome form the dorsal root ganglia containing the sensory neurons. Trunk neural crest cells that continue more ventrally form the sympathetic ganglia, the adrenal medulla, and the nerve clusters surrounding the aorta.
Interacts with, and stops, prevents or reduces the activity of nitric oxide synthase.
Interacts with, and stops, prevents or reduces the activity of nitric oxide synthase.
A heterodimeric protein complex that is composed of the transcription factor CHOP (GADD153) and a member of the C/EBP family of transcription factors.
A heterodimeric protein complex that is composed of the transcription factor CHOP (GADD153) and a member of the C/EBP family of transcription factors.
A heterodimeric protein complex that is composed of the transcription factor CHOP (GADD153) and a member of the C/EBP family of transcription factors.
A heterodimeric protein complex that is composed of the transcription factor CHOP (GADD153) and a member of the C/EBP family of transcription factors.
The chemical reactions and pathways resulting in the formation of neuromelanin. Neuromelanin is a polymer of 5,6-dihydroxyindole monomers.
The chemical reactions and pathways resulting in the formation of neuromelanin. Neuromelanin is a polymer of 5,6-dihydroxyindole monomers.
The chemical reactions and pathways resulting in the formation of neuromelanin. Neuromelanin is a polymer of 5,6-dihydroxyindole monomers.
The chemical reactions and pathways resulting in the formation of neuromelanin. Neuromelanin is a polymer of 5,6-dihydroxyindole monomers.
Modulation of the frequency, rate or extent of translation as a result of endoplasmic reticulum stress.
Any process that modulates the frequency, rate or extent of translation initiation, as a result of endoplasmic reticulum stress.
The addition of a phosphate group on to the translation initiation factor eIF2alpha, as a result of endoplasmic reticulum stress.
The addition of a phosphate group on to the translation initiation factor eIF2alpha, as a result of endoplasmic reticulum stress.
Any process that activates, or increases the frequency, rate or extent of translation as a result of endoplasmic reticulum stress.
Any process that activates, or increases the frequency, rate or extent of translation initiation as a result of endoplasmic reticulum stress.
Any process that stops, prevents, or reduces the frequency, rate or extent of translation initiation as a result of endoplasmic reticulum stress.
Any process that modulates the frequency, rate or extent of translation initiation in response to stress by the dephosphorylation of eIF2 alpha.
The removal of a phosphate group from the translation initiation factor eIF2alpha, as a result of endoplasmic reticulum stress.
The removal of a phosphate group from the translation initiation factor eIF2alpha, as a result of endoplasmic reticulum stress.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor PERK (PKR-like ER kinase). Begins with activation of PERK in response to endoplasmic reticulum (ER) stress and ends with regulation of a downstream cellular process, e.g. transcription. The main substrate of PERK is the translation initiation factor eIF2alpha. Serine-phosphorylation of eIF2alpha by PERK inactivates eIF2alpha and inhibits general protein translation. In addition, eIF2alpha phosphorylation preferentially increases the translation of selective mRNAs such as ATF4 (activating transcription factor 4), which up regulates a subset of UPR genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity.
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity.
A dimeric protein complex that contains the co-factors for the ATPase VCP/p97 (Cdc48p in budding yeast). In mammals, this complex consists of UFD1L (UFD1) and NPLOC4 (NPL4). In budding yeast, the complex is a dimer of Ufd1p and Npl4p.
A dimeric protein complex that contains the co-factors for the ATPase VCP/p97 (Cdc48p in budding yeast). In mammals, this complex consists of UFD1L (UFD1) and NPLOC4 (NPL4). In budding yeast, the complex is a dimer of Ufd1p and Npl4p.
A dimeric protein complex that contains the co-factors for the ATPase VCP/p97 (Cdc48p in budding yeast). In mammals, this complex consists of UFD1L (UFD1) and NPLOC4 (NPL4). In budding yeast, the complex is a dimer of Ufd1p and Npl4p.
A dimeric protein complex that contains the co-factors for the ATPase VCP/p97 (Cdc48p in budding yeast). In mammals, this complex consists of UFD1L (UFD1) and NPLOC4 (NPL4). In budding yeast, the complex is a dimer of Ufd1p and Npl4p.
A dimeric protein complex that contains the co-factors for the ATPase VCP/p97 (Cdc48p in budding yeast). In mammals, this complex consists of UFD1L (UFD1) and NPLOC4 (NPL4). In budding yeast, the complex is a dimer of Ufd1p and Npl4p.
A protein complex containing, in mammals, Derlin-1 and VCP-interacting membrane protein (VIMP). The complex links the p97/VCP-containing ATPase complex with Derlin-1 during translocation of protein substrates from the endoplasmic reticulum to the cytosol for degradation by the cytosolic proteasome.
The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The joining of two lipid bilayers that surround the Golgi apparatus to form a single Golgi membrane.
The joining of two lipid bilayers that surround the Golgi apparatus to form a single Golgi membrane.
Combining with prosaposin to initiate a change in cell activity. Prosaposin is the glycoprotein precursor of four cleavage products (saposins A, B, C and D).
Maintaining a protein in an unfolded, soluble state.
The removal of one or more mannose residues from a mannosylated protein.
The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein.
The removal of one or more alpha 1,2-linked mannose residues from a mannosylated protein.
The removal of an alpha-1,2-linked mannose from the B-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
The removal of an alpha-1,2-linked mannose from the B-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
The removal of an alpha-1,2-linked mannose from the B-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
The removal of an alpha-1,2-linked mannose from the C-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
The removal of an alpha-1,2-linked mannose from the C-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
The removal of an alpha-1,2-linked mannose from the C-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
The removal of the first alpha-1,2-linked mannose from the A-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
The removal of the first alpha-1,2-linked mannose from the A-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
The removal of the first alpha-1,2-linked mannose from the A-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
The removal of the second alpha-1,2-linked mannose from the A-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
The removal of the second alpha-1,2-linked mannose from the A-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
The removal of the second alpha-1,2-linked mannose from the A-chain of a glycoprotein oligosaccharide in the endoplasmic reticulum.
A protein complex that functions in the retrotranslocation step of ERAD (ER-associated protein degradation), and includes at its core Derlin-1 oligomers forming a retrotranslocation channel.
A protein complex that functions in the retrotranslocation step of ERAD (ER-associated protein degradation), and includes at its core Derlin-1 oligomers forming a retrotranslocation channel.
A protein complex that functions in the retrotranslocation step of ERAD (ER-associated protein degradation), and includes at its core Derlin-1 oligomers forming a retrotranslocation channel.
A protein complex that functions in the retrotranslocation step of ERAD (ER-associated protein degradation), and includes at its core Derlin-1 oligomers forming a retrotranslocation channel.
A protein complex that functions in the retrotranslocation step of ERAD (ER-associated protein degradation), and includes at its core Derlin-1 oligomers forming a retrotranslocation channel.
The chemotaxis process that directs the migration of an axon growth cone of a dopaminergic neuron to a specific target site in response to a combination of attractive and repulsive cues.
The chemotaxis process that directs the migration of an axon growth cone of a dopaminergic neuron to a specific target site in response to a combination of attractive and repulsive cues.
The chemotaxis process that directs the migration of an axon growth cone of a dopaminergic neuron to a specific target site in response to a combination of attractive and repulsive cues.
The chemotaxis process that directs the migration of an axon growth cone of a serotonergic neuron to a specific target site in response to a combination of attractive and repulsive cues.
The chemotaxis process that directs the migration of an axon growth cone of a serotonergic neuron to a specific target site in response to a combination of attractive and repulsive cues.
The process in which a dopaminergic neuron growth cone is directed to a specific target site in response to an attractive chemical signal.
The process in which a dopaminergic neuron growth cone is directed to a specific target site in response to an attractive chemical signal.
The process in which a serotonergic neuron growth cone is directed to a specific target site in response to an attractive chemical signal.
The process in which a serotonergic neuron growth cone is directed to a specific target site in response to an attractive chemical signal.
The process in which a dopaminergic neuron growth cone is directed to a specific target site in response to a repulsive chemical cue.
The process in which a dopaminergic neuron growth cone is directed to a specific target site in response to a repulsive chemical cue.
The process in which a serotonergic neuron growth cone is directed to a specific target site in response to a repulsive chemical cue.
The process in which a serotonergic neuron growth cone is directed to a specific target site in response to a repulsive chemical cue.
Cell-cell signaling that mediates the transfer of information from an astrocyte to a dopaminergic neuron.
Cell-cell signaling that mediates the transfer of information from an astrocyte to a dopaminergic neuron.
Cell-cell signaling that mediates the transfer of information from an astrocyte to a dopaminergic neuron.
Cell-cell signaling that mediates the transfer of information from an astrocyte to a dopaminergic neuron.
Any process in which an organism modulates the frequency, rate or extent of protein localisation to the host phagosome. 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 protein localisation to the host phagosome. 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 protein localisation to the host phagosome. 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 protein localisation to the host phagosome. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which an organism activates, maintains or increases the frequency, rate or extent of cytokine secretion in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Catalysis of the removal of a sugar or dicarbonyl from a lysine residue of a glycated protein.
The removal of a sugar or dicarbonyl from a glycated protein.
The removal of a sugar or dicarbonyl from a cysteine residue of a glycated protein.
The removal of a sugar or dicarbonyl from an arginine residue of a glycated protein.
The removal of a sugar or dicarbonyl from a lysine residue of a glycated protein.
The removal of glyoxal from a glycated protein, to form glycolate and a deglycated protein.
The removal of methylglyoxal from a glycated protein, to form lactate and a deglycated protein.
The removal of a sugar or dicarbonyl from glycated glutathione. Glutathione is the tripeptide glutamylcysteinylglycine.
The transfer of information from one cell to another, where an endocrine hormone is transported from the signal-producing cell to the receiving cell via the circulatory system (via blood, lymph or cerebrospinal fluid). The signaling cell and the receiving cell are often distant to each other.
The series of molecular signals generated as a consequence of an opioid receptor binding to one of its physiological ligands.
Any process leading to the attainment of the full functional capacity of a ligand for an epidermal growth factor receptor. The ligand is functional when it can bind to and activate an epidermal growth factor receptor.
The hydrolysis of a peptide bond or bonds within a ligand for the epidermal growth factor receptor, as part of protein maturation, the process leading to the attainment of the full functional capacity of a protein. In Drosophila for example, in the Golgi apparatus of the signal producing cell, Spitz is cleaved within its transmembrane domain to release a functional soluble extracellular fragment.
The hydrolysis of a peptide bond or bonds within a ligand for the epidermal growth factor receptor, as part of protein maturation, the process leading to the attainment of the full functional capacity of a protein. In Drosophila for example, in the Golgi apparatus of the signal producing cell, Spitz is cleaved within its transmembrane domain to release a functional soluble extracellular fragment.
The hydrolysis of a peptide bond or bonds within a ligand for the epidermal growth factor receptor, as part of protein maturation, the process leading to the attainment of the full functional capacity of a protein. In Drosophila for example, in the Golgi apparatus of the signal producing cell, Spitz is cleaved within its transmembrane domain to release a functional soluble extracellular fragment.
The hydrolysis of a peptide bond or bonds within a ligand for the epidermal growth factor receptor, as part of protein maturation, the process leading to the attainment of the full functional capacity of a protein. In Drosophila for example, in the Golgi apparatus of the signal producing cell, Spitz is cleaved within its transmembrane domain to release a functional soluble extracellular fragment.
Combining with a netrin signal and transmitting the signal from one side of the membrane to the other to contribute to the directed movement of a motile cell towards a higher concentration of netrin.
Combining with a netrin signal and transmitting the signal from one side of the membrane to the other to contribute to the directed movement of a motile cell towards a higher concentration of netrin.
A series of molecular events initiated by the binding of a netrin protein to a receptor on the surface of the target cell, and ending with regulation of a downstream cellular process, e.g. transcription. Netrins can act as chemoattractant signals for some cells and chemorepellent signals for others. Netrins also have roles outside of cell and axon guidance.
A series of molecular events initiated by the binding of a netrin protein to a receptor on the surface of the target cell, and ending with regulation of a downstream cellular process, e.g. transcription. Netrins can act as chemoattractant signals for some cells and chemorepellent signals for others. Netrins also have roles outside of cell and axon guidance.
A series of molecular events initiated by the binding of a netrin protein to a receptor on the surface of the target cell, and ending with regulation of a downstream cellular process, e.g. transcription. Netrins can act as chemoattractant signals for some cells and chemorepellent signals for others. Netrins also have roles outside of cell and axon guidance.
A series of molecular events initiated by the binding of a netrin protein to a receptor on the surface of the target cell, and ending with regulation of a downstream cellular process, e.g. transcription. Netrins can act as chemoattractant signals for some cells and chemorepellent signals for others. Netrins also have roles outside of cell and axon guidance.
The intracellular process in which a signal is passed on to downstream components within the cell via a tumor necrosis factor receptor-associated factor (TRAF). TRAFs are directly or indirectly recruited to the intracellular domains of cell surface receptors, and engage other signaling proteins to transfer the signal from a cell surface receptor to other intracellular signaling components.
The intracellular process in which a signal is passed on to downstream components within the cell via a tumor necrosis factor receptor-associated factor (TRAF). TRAFs are directly or indirectly recruited to the intracellular domains of cell surface receptors, and engage other signaling proteins to transfer the signal from a cell surface receptor to other intracellular signaling components.
The intracellular process in which a signal is passed on to downstream components within the cell via a tumor necrosis factor receptor-associated factor (TRAF). TRAFs are directly or indirectly recruited to the intracellular domains of cell surface receptors, and engage other signaling proteins to transfer the signal from a cell surface receptor to other intracellular signaling components.
The intracellular process in which a signal is passed on to downstream components within the cell via a tumor necrosis factor receptor-associated factor (TRAF). TRAFs are directly or indirectly recruited to the intracellular domains of cell surface receptors, and engage other signaling proteins to transfer the signal from a cell surface receptor to other intracellular signaling components.
The intracellular process in which a signal is passed on to downstream components within the cell via a tumor necrosis factor receptor-associated factor (TRAF). TRAFs are directly or indirectly recruited to the intracellular domains of cell surface receptors, and engage other signaling proteins to transfer the signal from a cell surface receptor to other intracellular signaling components.
The intracellular process in which a signal is passed on to downstream components within the cell via a tumor necrosis factor receptor-associated factor (TRAF). TRAFs are directly or indirectly recruited to the intracellular domains of cell surface receptors, and engage other signaling proteins to transfer the signal from a cell surface receptor to other intracellular signaling components.
Any process that modulates the frequency, rate or extent of signal transduction by the movement of a signaling receptor from the plasma membrane to the inside of the cell. Receptor internalization can have a positive or negative effect on a signaling pathway.
Any process in which the internalization of a signaling receptor activates or increases the frequency, rate or extent of signal transduction. Receptor internalization can enhance signaling by concentrating signaling molecules in one location, or by moving a ligand-activated receptor to the location of downstream signaling proteins. Endosomes for example can serve as important intracellular signaling platforms.
Any process in which internalization of a signaling receptor stops, prevents, or reduces the frequency, rate or extent of signal transduction. Receptor internalization can attenuate or reduce the strength of signaling by reducing the concentration of cell surface receptors available to ligands.
Any process in which internalization of a Wnt receptor stops, prevents, or reduces the frequency, rate or extent of Wnt signal transduction.
Any process in which internalization of a Wnt receptor stops, prevents, or reduces the frequency, rate or extent of Wnt signal transduction.
Any process in which internalization of a Wnt receptor stops, prevents, or reduces the frequency, rate or extent of Wnt signal transduction.
Any process in which internalization of a Wnt receptor stops, prevents, or reduces the frequency, rate or extent of Wnt signal transduction.
Any process in which internalization of a Wnt receptor stops, prevents, or reduces the frequency, rate or extent of Wnt signal transduction.
Any process in which internalization of a Wnt receptor activates or increases the frequency, rate or extent of the Wnt signaling pathway.
Any process in which internalization of a Wnt receptor activates or increases the frequency, rate or extent of the Wnt signaling pathway.
Any process in which internalization of a Wnt receptor activates or increases the frequency, rate or extent of the Wnt signaling pathway.
Any process in which internalization of a Wnt receptor activates or increases the frequency, rate or extent of the Wnt signaling pathway.
Any process in which internalization of a Wnt receptor activates or increases the frequency, rate or extent of the Wnt signaling pathway.
Any process in which internalization of an insulin receptor stops, prevents, or reduces the frequency, rate or extent of insulin receptor signal transduction. Internalization of insulin in association with its receptor clears insulin from the circulation and is necessary for subsequent insulin dissociation from the receptor and insulin degradation.
Any process in which internalization of an insulin receptor stops, prevents, or reduces the frequency, rate or extent of insulin receptor signal transduction. Internalization of insulin in association with its receptor clears insulin from the circulation and is necessary for subsequent insulin dissociation from the receptor and insulin degradation.
Any process in which internalization of an insulin receptor activates or increases the frequency, rate or extent of the insulin receptor signaling pathway. Endocytosis of activated receptors can concentrate receptors within endosomes and allow the insulin receptor to phosphorylate substrates that are spatially distinct from those accessible at the plasma membrane.
A receptor-mediated endocytosis process that results in the movement of an insulin receptor from the plasma membrane to the inside of the cell.
A receptor-mediated endocytosis process that results in the movement of a Wnt receptor from the plasma membrane to the inside of the cell.
The chemical reactions and pathways resulting in the breakdown of a Wnt receptor. Internalized Wnt receptors can be recycled to the plasma membrane or sorted to lysosomes for protein degradation.
The chemical reactions and pathways resulting in the breakdown of a Wnt receptor. Internalized Wnt receptors can be recycled to the plasma membrane or sorted to lysosomes for protein degradation.
The chemical reactions and pathways resulting in the breakdown of a Wnt receptor. Internalized Wnt receptors can be recycled to the plasma membrane or sorted to lysosomes for protein degradation.
The chemical reactions and pathways resulting in the breakdown of a Wnt receptor. Internalized Wnt receptors can be recycled to the plasma membrane or sorted to lysosomes for protein degradation.
The chemical reactions and pathways resulting in the breakdown of a Wnt receptor. Internalized Wnt receptors can be recycled to the plasma membrane or sorted to lysosomes for protein degradation.
The process that results in the return of a Wnt receptor to an active state at the plasma membrane. An active state is when the receptor is ready to receive a Wnt signal. Internalized Wnt receptors can be recycled to the plasma membrane or sorted to lysosomes for protein degradation.
The process that results in the return of an insulin receptor to an active state at the plasma membrane. An active state is when the receptor is ready to receive an insulin signal. Internalized insulin receptors can be recycled to the plasma membrane or sorted to lysosomes for protein degradation.
Combining with the fat-cell specific hormone leptin and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with an odorant and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with an odorant and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with an odorant and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with an odorant and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with the secreted glycoprotein reelin, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
A series of molecular signals initiated by the binding of reelin (a secreted glycoprotein) to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of reelin (a secreted glycoprotein) to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of reelin (a secreted glycoprotein) to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of apolipoprotein A-I to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, where the signal is passed on via the MAPKKK cascade.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, where the signal is passed on via the MAPKKK cascade.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, where the signal is passed on via the MAPKKK cascade.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, where the signal is passed on via the MAPKKK cascade.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, where the signal is passed on via the MAPKKK cascade.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, where the signal is passed on via the JNK cascade.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, where the signal is passed on via the JNK cascade.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, where the signal is passed on via the JNK cascade.
The signaling process in which G protein-coupled receptor signaling is brought to an end. For example, through the action of GTPase-activating proteins (GAPs) that act to accelerate hydrolysis of GTP to GDP on G-alpha proteins, thereby terminating the transduced signal.
The signaling process in which G protein-coupled receptor signaling is brought to an end. For example, through the action of GTPase-activating proteins (GAPs) that act to accelerate hydrolysis of GTP to GDP on G-alpha proteins, thereby terminating the transduced signal.
The signaling process in which G protein-coupled receptor signaling is brought to an end. For example, through the action of GTPase-activating proteins (GAPs) that act to accelerate hydrolysis of GTP to GDP on G-alpha proteins, thereby terminating the transduced signal.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a VEGFR on the surface of a cell, which activates or increases the frequency, rate or extent of endothelial cell chemotaxis.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a VEGFR on the surface of a cell, which activates or increases the frequency, rate or extent of endothelial cell chemotaxis.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a VEGFR on the surface of a cell, which activates or increases the frequency, rate or extent of endothelial cell chemotaxis.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a VEGFR on the surface of a cell, which activates or increases the frequency, rate or extent of endothelial cell chemotaxis.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a VEGFR on the surface of a cell, which activates or increases the frequency, rate or extent of endothelial cell chemotaxis.
A series of molecular signals initiated by the absence of a ligand or the withdrawal of a ligand from a receptor.
A series of molecular signals initiated by the absence of a ligand or the withdrawal of a ligand from a receptor.
A series of molecular signals initiated by the absence of a ligand or the withdrawal of a ligand from a receptor.
A series of molecular signals initiated by the absence of a ligand or the withdrawal of a ligand from a receptor.
A series of molecular signals initiated by the absence of a ligand or the withdrawal of a ligand from a receptor.
A series of molecular signals initiated by the absence of a ligand or the withdrawal of a ligand from a receptor.
A series of molecular signals beginning with a consequence of a G protein-coupled receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex, where the G protein-coupled receptor is not bound to an agonist.
A series of molecular signals beginning with a consequence of a G protein-coupled receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex, where the G protein-coupled receptor is not bound to an agonist.
A series of molecular signals beginning with a consequence of a G protein-coupled receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex, where the G protein-coupled receptor is not bound to an agonist.
A series of molecular signals beginning with a consequence of a G protein-coupled receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex, where the G protein-coupled receptor is not bound to an agonist.
A protein complex that contains two G protein-coupled receptors.
A protein complex that contains two G protein-coupled receptors.
A protein complex that contains two G protein-coupled receptors.
A protein complex that contains two G protein-coupled receptors (GPCRs) of the same subtype. Formation of a GPCR homodimer may be important for the transport of newly formed receptors to the cell surface, and the function of the receptor.
A protein complex that contains two G protein-coupled receptors (GPCRs) of the same subtype. Formation of a GPCR homodimer may be important for the transport of newly formed receptors to the cell surface, and the function of the receptor.
A protein complex that contains two G protein-coupled receptors (GPCRs) of the same subtype. Formation of a GPCR homodimer may be important for the transport of newly formed receptors to the cell surface, and the function of the receptor.
A protein complex that contains two G protein-coupled receptors (GPCRs) of different subtypes. Formation of a GPCR heterodimer may alter the functional property of the GPCR.
A protein complex that contains two G protein-coupled receptors (GPCRs) of different subtypes. Formation of a GPCR heterodimer may alter the functional property of the GPCR.
A protein complex that contains two G protein-coupled receptors (GPCRs) of different subtypes. Formation of a GPCR heterodimer may alter the functional property of the GPCR.
Inhibition of one protomer of a G protein-coupled receptor (GPCR) heterodimer by the associated subunit. For example, agonist activation of one cytokine receptor can prevent activation of its associated cytokine receptor subunit.
A series of molecular signals initiated by the binding of interleukin-5 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 interleukin-5 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
The regulated release of transforming growth factor-beta (TGF-beta) from a cell into the extracellular region. TGF-beta is mostly secreted as a large latent TGF-beta complex (LLC) containing latency-associated proteins (LAPs) derived from the N-terminal region of the TGF-beta gene product, dimeric TGF-beta and latent TGF-beta binding proteins (LTBPs).
The regulated release of transforming growth factor-beta (TGF-beta) from a cell into the extracellular region. TGF-beta is mostly secreted as a large latent TGF-beta complex (LLC) containing latency-associated proteins (LAPs) derived from the N-terminal region of the TGF-beta gene product, dimeric TGF-beta and latent TGF-beta binding proteins (LTBPs).
A protein complex containing latency-associated proteins (LAPs), mature disulphide-linked dimeric TGF-beta, and latent TGF-beta binding proteins (LTBPs). TGF-beta is mostly secreted as part of the large latent complex, and must be subsequently released from the LLC in order to bind to cell surface receptors.
A protein complex containing latency-associated proteins (LAPs), mature disulphide-linked dimeric TGF-beta, and latent TGF-beta binding proteins (LTBPs). TGF-beta is mostly secreted as part of the large latent complex, and must be subsequently released from the LLC in order to bind to cell surface receptors.
Combining with a glucocorticoid and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with a glucocorticoid and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with a glucocorticoid and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with a glucocorticoid and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with estrogen and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with estrogen and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription by RNA polymerase II.
Combining with estrogen and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with an RNA polymerase II transcription factor, which may be a single protein or a complex, in order to modulate transcription. For example, estrogen-bound receptors can bind to transcription factor complexes to regulate transcription of genes whose promoters do not contain estrogen response elements.
Combining with estrogen and transmitting the signal to the transcriptional machinery by interacting selectively and non-covalently with an RNA polymerase II transcription factor, which may be a single protein or a complex, in order to modulate transcription. For example, estrogen-bound receptors can bind to transcription factor complexes to regulate transcription of genes whose promoters do not contain estrogen response elements.
Combining with estrogen and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
The controlled release of a member of the BMP family of proteins from a cell.
The controlled release of a member of the BMP family of proteins from a cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the BMP signaling pathway by stopping, preventing or reducing the frequency, rate or extent of secretion of a member of the BMP family of proteins from the signaling cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the BMP signaling pathway by stopping, preventing or reducing the frequency, rate or extent of secretion of a member of the BMP family of proteins from the signaling cell.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
Combining with a tumor necrosis factor ligand superfamily member 11 (TNFSF11) and transmitting the signal across the cell membrane to initiate a change in cell activity or function.
Combining with a tumor necrosis factor ligand superfamily member 11 (TNFSF11) and transmitting the signal across the cell membrane to initiate a change in cell activity or function.
A homodimeric protein complex containing two IkappaB kinase (IKK) alpha subunits.
A homodimeric protein complex containing two IkappaB kinase (IKK) alpha subunits.
A homodimeric protein complex containing two IkappaB kinase (IKK) alpha subunits.
A homodimeric protein complex containing two IkappaB kinase (IKK) alpha subunits.
A homodimeric protein complex containing two IkappaB kinase (IKK) alpha subunits.
Any intracellular signal transduction in which the signal is passed on within the cell by nitric oxide (NO) activating soluble guanylyl cyclase (sGC). Includes synthesis of nitric oxide, guanylyl cyclase activity, and downstream effectors that further transmit the signal within the cell following activation by cGMP.
Any intracellular signal transduction in which the signal is passed on within the cell by nitric oxide (NO) activating soluble guanylyl cyclase (sGC). Includes synthesis of nitric oxide, guanylyl cyclase activity, and downstream effectors that further transmit the signal within the cell following activation by cGMP.
Any intracellular signal transduction in which the signal is passed on within the cell by nitric oxide (NO) activating soluble guanylyl cyclase (sGC). Includes synthesis of nitric oxide, guanylyl cyclase activity, and downstream effectors that further transmit the signal within the cell following activation by cGMP.
Any intracellular signal transduction in which the signal is passed on within the cell by nitric oxide (NO) activating soluble guanylyl cyclase (sGC). Includes synthesis of nitric oxide, guanylyl cyclase activity, and downstream effectors that further transmit the signal within the cell following activation by cGMP.
The process in which a signal is passed on to downstream components within the cell through the NIK-dependent processing and activation of NF-KappaB. Begins with activation of the NF-KappaB-inducing kinase (NIK), which in turn phosphorylates and activates IkappaB kinase alpha (IKKalpha). IKKalpha phosphorylates the NF-Kappa B2 protein (p100) leading to p100 processing and release of an active NF-KappaB (p52).
The process in which a signal is passed on to downstream components within the cell through the NIK-dependent processing and activation of NF-KappaB. Begins with activation of the NF-KappaB-inducing kinase (NIK), which in turn phosphorylates and activates IkappaB kinase alpha (IKKalpha). IKKalpha phosphorylates the NF-Kappa B2 protein (p100) leading to p100 processing and release of an active NF-KappaB (p52).
The process in which a signal is passed on to downstream components within the cell through the NIK-dependent processing and activation of NF-KappaB. Begins with activation of the NF-KappaB-inducing kinase (NIK), which in turn phosphorylates and activates IkappaB kinase alpha (IKKalpha). IKKalpha phosphorylates the NF-Kappa B2 protein (p100) leading to p100 processing and release of an active NF-KappaB (p52).
The process in which a signal is passed on to downstream components within the cell through the NIK-dependent processing and activation of NF-KappaB. Begins with activation of the NF-KappaB-inducing kinase (NIK), which in turn phosphorylates and activates IkappaB kinase alpha (IKKalpha). IKKalpha phosphorylates the NF-Kappa B2 protein (p100) leading to p100 processing and release of an active NF-KappaB (p52).
The process in which a signal is passed on to downstream components within the cell through the NIK-dependent processing and activation of NF-KappaB. Begins with activation of the NF-KappaB-inducing kinase (NIK), which in turn phosphorylates and activates IkappaB kinase alpha (IKKalpha). IKKalpha phosphorylates the NF-Kappa B2 protein (p100) leading to p100 processing and release of an active NF-KappaB (p52).
The process in which a signal is passed on to downstream components within the cell through the NIK-dependent processing and activation of NF-KappaB. Begins with activation of the NF-KappaB-inducing kinase (NIK), which in turn phosphorylates and activates IkappaB kinase alpha (IKKalpha). IKKalpha phosphorylates the NF-Kappa B2 protein (p100) leading to p100 processing and release of an active NF-KappaB (p52).
Combining with collagen and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity by catalysis of the reaction: ATP + a protein-L-tyrosine = ADP + a protein-L-tyrosine phosphate.
Combining with collagen and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity by catalysis of the reaction: ATP + a protein-L-tyrosine = ADP + a protein-L-tyrosine phosphate.
A series of molecular signals initiated by the binding of collagen to a receptor on the surface of the target cell where the receptor possesses tyrosine kinase activity. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of collagen to a receptor on the surface of the target cell where the receptor possesses tyrosine kinase activity. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of collagen to a receptor on the surface of the target cell where the receptor possesses tyrosine kinase activity. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of collagen to a receptor on the surface of the target cell where the receptor possesses tyrosine kinase activity. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
Combining with a collagen and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
A series of molecular signals initiated by collagen binding to a cell surface receptor, and ending with regulation of a downstream cellular process, e.g. transcription.
An intracellular protein kinase cascade containing at least a p38 MAPK, a MAPKK and a MAP3K. The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
An intracellular protein kinase cascade containing at least a p38 MAPK, a MAPKK and a MAP3K. The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell.
Catalysis of the reaction: protein + ATP = protein phosphate + ADP by a mitogen-activated protein kinase, as part of a MAPK signaling cascade that contributes to an innate immune response.
Catalysis of the reaction: a phosphorylated MAP kinase + H2O = a MAP kinase + phosphate, where the MAP kinase (MAPK) is part of a MAPK signaling cascade that contributes to an innate immune response.
The phosphorylation by a protein of one or more of its own tyrosine amino acid residues, or a tyrosine residue on an identical protein.
The phosphorylation by a protein of one or more of its own tyrosine amino acid residues, or a tyrosine residue on an identical protein.
The phosphorylation by a protein of one or more of its own tyrosine amino acid residues, or a tyrosine residue on an identical protein.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a receptor on the surface of the target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a receptor on the surface of the target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a receptor on the surface of the target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Interacting selectively and non-covalently with a vascular endothelial growth factor.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to a platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to a platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to a platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to a platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to an alpha-type platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to an alpha-type platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to an alpha-type platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to an alpha-type platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to an alpha-type platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to a beta-type platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to a beta-type platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to a beta-type platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to a beta-type platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to a beta-type platelet-derived growth factor receptor (PDGFR) 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 vascular endothelial growth factor (VEGF) to a receptor on the surface of a cell, which activates or increases the frequency, rate or extent of the orderly movement of a cell from one site to another.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a receptor on the surface of a cell, which activates or increases the frequency, rate or extent of the orderly movement of a cell from one site to another.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a receptor on the surface of a cell, which activates or increases the frequency, rate or extent of the orderly movement of a cell from one site to another.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a receptor on the surface of a cell, which activates or increases the frequency, rate or extent of the orderly movement of a cell from one site to another.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a platelet-derived growth factor receptor (PDGFR) on the surface of a cell, which activates or increases the frequency, rate or extent of the orderly movement of a cell from one site to another.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a platelet-derived growth factor receptor (PDGFR) on the surface of a cell, which activates or increases the frequency, rate or extent of the orderly movement of a cell from one site to another.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a platelet-derived growth factor receptor (PDGFR) on the surface of a cell, which activates or increases the frequency, rate or extent of the orderly movement of a cell from one site to another.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a platelet-derived growth factor receptor (PDGFR) on the surface of a cell, which activates or increases the frequency, rate or extent of cell proliferation.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a platelet-derived growth factor receptor (PDGFR) on the surface of a cell, which activates or increases the frequency, rate or extent of cell proliferation.
A series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to a platelet-derived growth factor receptor (PDGFR) on the surface of a cell, which activates or increases the frequency, rate or extent of cell proliferation.
A series of molecular signals initiated by the binding of a nodal protein to an activin receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a nodal protein to an activin receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of the Fc portion of an immunoglobulin to an Fc receptor on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription. The Fc portion of an immunoglobulin is its C-terminal constant region.
A series of molecular signals initiated by the binding of the Fc portion of immunoglobulin G (IgG) to an Fc-gamma receptor on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription. The Fc portion of an immunoglobulin is its C-terminal constant region.
A series of molecular signals initiated by the binding of the Fc portion of immunoglobulin E (IgE) to an Fc-epsilon receptor on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription. The Fc portion of an immunoglobulin is its C-terminal constant region.
An Fc-gamma receptor signaling pathway that contributes to the endocytic engulfment of external particulate material by phagocytes.
An Fc-gamma receptor signaling pathway that contributes to the endocytic engulfment of external particulate material by phagocytes.
An Fc-gamma receptor signaling pathway that contributes to the endocytic engulfment of external particulate material by phagocytes.
An Fc-gamma receptor signaling pathway that contributes to the endocytic engulfment of external particulate material by phagocytes.
An Fc-epsilon receptor signaling pathway that results in the change in morphology and behavior of a mast cell resulting from exposure to a cytokine, chemokine, soluble factor, or to (at least in mammals) an antigen which the mast cell has specifically bound via IgE bound to Fc-epsilonRI receptors.
An Fc-epsilon receptor signaling pathway that results in the change in morphology and behavior of a mast cell resulting from exposure to a cytokine, chemokine, soluble factor, or to (at least in mammals) an antigen which the mast cell has specifically bound via IgE bound to Fc-epsilonRI receptors.
An Fc-epsilon receptor signaling pathway that results in the change in morphology and behavior of a mast cell resulting from exposure to a cytokine, chemokine, soluble factor, or to (at least in mammals) an antigen which the mast cell has specifically bound via IgE bound to Fc-epsilonRI receptors.
Binding to a bone morphogenetic protein (BMP) in the extracellular region, and inhibiting BMP signaling by preventing BMP from binding to its cell surface receptor.
Binding to a bone morphogenetic protein (BMP) in the extracellular region, and inhibiting BMP signaling by preventing BMP from binding to its cell surface receptor.
The aggregation, arrangement and bonding together of a set of components to form a complex containing a type II activin receptor, a type I activin receptor, and a coreceptor of the EGF-CFC family (e.g. Cripto or Cryptic, in mammals).
The aggregation, arrangement and bonding together of a set of components to form a complex containing a type II activin receptor, a type I activin receptor, and a coreceptor of the EGF-CFC family (e.g. Cripto or Cryptic, in mammals).
Interacting selectively and non-covalently with a nodal protein, a member of the transforming growth factor-beta superfamily.
Binding to a nodal protein in the extracellular region, and inhibiting nodal signaling by preventing nodal from binding to its cell surface receptor.
Binding to a nodal protein in the extracellular region, and inhibiting nodal signaling by preventing nodal from binding to its cell surface receptor.
Binding to a nodal protein in the extracellular region, and inhibiting nodal signaling by preventing nodal from binding to its cell surface receptor.
Interacting with an activin receptor complex to reduce the action of another ligand, the agonist. A receptor antagonist does not initiate signaling upon binding to a receptor, but instead blocks an agonist from binding to the receptor.
Interacting with an activin receptor to reduce the action of the agonist nodal. A receptor antagonist does not initiate signaling upon binding to a receptor, but instead blocks an agonist from binding to the receptor.
Interacting with an activin receptor to reduce the action of the agonist nodal. A receptor antagonist does not initiate signaling upon binding to a receptor, but instead blocks an agonist from binding to the receptor.
A protein complex containing at least a type II activin receptor, a type I activin receptor, and a coreceptor (EGF-CFC protein) such as Cripto or Cryptic. Nodal receptor complexes are capable of binding a nodal protein and transducing the signal into the cell.
Binding to a transforming growth factor-beta (TGFbeta) protein in the extracellular region, and inhibiting TGFbeta signaling by preventing TGFbeta from binding to its cell surface receptor.
Binding to a transforming growth factor-beta (TGFbeta) protein in the extracellular region, and inhibiting TGFbeta signaling by preventing TGFbeta from binding to its cell surface receptor.
Interacting selectively and non-covalently with choriogonadotropin hormone, a heterodimer, with an alpha subunit identical to that of luteinizing hormone (LH), follicle-stimulating hormone (FSH) and thyroid-stimulating hormone (TSH), and a unique beta subunit.
Interacting selectively and non-covalently with choriogonadotropin hormone, a heterodimer, with an alpha subunit identical to that of luteinizing hormone (LH), follicle-stimulating hormone (FSH) and thyroid-stimulating hormone (TSH), and a unique beta subunit.
A series of molecular signals initiated by the binding of a nodal protein to an activin receptor on the surface of a target cell, which contributes to the establishment of an organism's body plan or part of an organism with respect to the left and right halves.
A series of molecular signals initiated by the binding of a nodal protein to an activin receptor on the surface of a target cell, which contributes to the establishment of an organism's body plan or part of an organism with respect to the left and right halves.
A series of molecular signals initiated by the binding of leptin to a receptor on the surface of a cell, which reduces appetite, the desire or physical craving for food.
A series of molecular signals initiated by the binding of leptin to a receptor on the surface of a cell, which reduces appetite, the desire or physical craving for food.
A series of molecular signals initiated by the binding of leptin to a receptor on the surface of a cell, which reduces appetite, the desire or physical craving for food.
A series of molecular signals initiated by the binding of leptin to a receptor on the surface of a cell, which reduces appetite, the desire or physical craving for food.
A series of molecular signals that starts with the binding of stem cell factor to the tyrosine kinase receptor KIT on the surface of a cell, and ends with regulation of a downstream cellular process, e.g. transcription. Stem cell factor (KIT ligand) binding to the receptor Kit mediates receptor dimerization, activation of its intrinsic tyrosine kinase activity and autophosphorylation. The activated receptor then phosphorylates various substrates, thereby activating distinct signaling cascades within the cell that trigger a change in state or activity of the cell.
A series of molecular signals that starts with the binding of stem cell factor to the tyrosine kinase receptor KIT on the surface of a cell, and ends with regulation of a downstream cellular process, e.g. transcription. Stem cell factor (KIT ligand) binding to the receptor Kit mediates receptor dimerization, activation of its intrinsic tyrosine kinase activity and autophosphorylation. The activated receptor then phosphorylates various substrates, thereby activating distinct signaling cascades within the cell that trigger a change in state or activity of the cell.
A series of molecular signals that starts with the binding of stem cell factor to the tyrosine kinase receptor KIT on the surface of a cell, and ends with regulation of a downstream cellular process, e.g. transcription. Stem cell factor (KIT ligand) binding to the receptor Kit mediates receptor dimerization, activation of its intrinsic tyrosine kinase activity and autophosphorylation. The activated receptor then phosphorylates various substrates, thereby activating distinct signaling cascades within the cell that trigger a change in state or activity of the cell.
A series of molecular signals that starts with the binding of stem cell factor to the tyrosine kinase receptor KIT on the surface of a cell, and ends with regulation of a downstream cellular process, e.g. transcription. Stem cell factor (KIT ligand) binding to the receptor Kit mediates receptor dimerization, activation of its intrinsic tyrosine kinase activity and autophosphorylation. The activated receptor then phosphorylates various substrates, thereby activating distinct signaling cascades within the cell that trigger a change in state or activity of the cell.
A series of molecular signals initiated by the binding of interleukin-2 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 interleukin-2 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 interleukin-7 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 interleukin-7 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 interleukin-8 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 interleukin-8 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 interleukin-9 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 interleukin-9 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 interleukin-21 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 interleukin-21 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 the C-C chemokine CCL19 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 the C-C chemokine CCL19 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 the C-C chemokine CCL19 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 the C-C chemokine CCL21 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 the C-C chemokine CCL21 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 the C-C chemokine CCL21 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Combining with the C-C motif chemokine 19 (CCL19) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
A series of molecular signals initiated by a the C-C chemokine type 7 receptor on the surface of a cell binding to one of it's physiological ligands, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by a the C-C chemokine type 7 receptor on the surface of a cell binding to one of it's physiological ligands, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of the C-C chemokine CCL19 to a C-C chemokine type 7 receptor (CCR7) 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 the C-C chemokine CCL21 to a C-C chemokine type 7 receptor (CCR7) on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Combining with the C-C motif chemokine 21 (CCL21) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with the C-C motif chemokine 5 (CCL5) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with the C-C motif chemokine 5 (CCL5) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with the C-C motif chemokine 5 (CCL5) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
A series of molecular signals initiated by the binding of a heterodimeric TLR1:TLR2 complex to one of it's physiological ligands, followed by transmission of the signal by the activated receptor, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a heterodimeric TLR1:TLR2 complex to one of it's physiological ligands, followed by transmission of the signal by the activated receptor, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a heterodimeric TLR6:TLR2 complex to one of it's physiological ligands, followed by transmission of the signal by the activated receptor, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a heterodimeric TLR6:TLR2 complex to one of it's physiological ligands, followed by transmission of the signal by the activated receptor, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a ligand to a member of the ERBB family of receptor tyrosine kinases 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 binding of a ligand to a member of the ERBB family of receptor tyrosine kinases 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 binding of a ligand to a member of the ERBB family of receptor tyrosine kinases 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 binding of a ligand to a member of the ERBB family of receptor tyrosine kinases 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 binding of a ligand to a member of the ERBB family of receptors on the surface of a cell, where the signal is transmitted by ERBB2. The pathway ends with regulation of a downstream cellular process, e.g. transcription. ERBB2 receptors are themselves unable to bind to ligands, but act as a signal-amplifying tyrosine kinase within a heterodimeric pair.
A series of molecular signals initiated by binding of a ligand to a member of the ERBB family of receptors on the surface of a cell, where the signal is transmitted by ERBB2. The pathway ends with regulation of a downstream cellular process, e.g. transcription. ERBB2 receptors are themselves unable to bind to ligands, but act as a signal-amplifying tyrosine kinase within a heterodimeric pair.
A series of molecular signals initiated by binding of a ligand to a member of the ERBB family of receptors on the surface of a cell, where the signal is transmitted by ERBB2. The pathway ends with regulation of a downstream cellular process, e.g. transcription. ERBB2 receptors are themselves unable to bind to ligands, but act as a signal-amplifying tyrosine kinase within a heterodimeric pair.
A series of molecular signals initiated by binding of a ligand to a member of the ERBB family of receptors on the surface of a cell, where the signal is transmitted by ERBB2. The pathway ends with regulation of a downstream cellular process, e.g. transcription. ERBB2 receptors are themselves unable to bind to ligands, but act as a signal-amplifying tyrosine kinase within a heterodimeric pair.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB3 on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription. ERBB3 receptors have impaired kinase activity and rely on the kinase activity of the heterodimer partner for activation and signal transmission.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB3 on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription. ERBB3 receptors have impaired kinase activity and rely on the kinase activity of the heterodimer partner for activation and signal transmission.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB3 on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription. ERBB3 receptors have impaired kinase activity and rely on the kinase activity of the heterodimer partner for activation and signal transmission.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB4 on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB4 on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB4 on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
Combining with a neuregulin, a member of the EGF family of growth factors, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with a neuregulin, a member of the EGF family of growth factors, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with a neuregulin, a member of the EGF family of growth factors, 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 neuregulin, a member of the EGF family of growth factors.
A series of molecular signals initiated by binding of a ligand to a ERBB3 receptor on the surface of a cell, followed by transmission of the signal by a heterodimeric complex of ERBB2 and ERBB3. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as ERBB3. ERBB3 also has impaired kinase activity and relies on ERBB2 for activation and signal transmission.
A series of molecular signals initiated by binding of a ligand to a ERBB3 receptor on the surface of a cell, followed by transmission of the signal by a heterodimeric complex of ERBB2 and ERBB3. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as ERBB3. ERBB3 also has impaired kinase activity and relies on ERBB2 for activation and signal transmission.
A series of molecular signals initiated by binding of a ligand to an epidermal growth factor receptor (EGFR/ERBB1) on the surface of a cell, followed by transmission of the signal by a heterodimeric complex of ERBB2 and EGFR. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as EGFR.
A series of molecular signals initiated by binding of a ligand to an epidermal growth factor receptor (EGFR/ERBB1) on the surface of a cell, followed by transmission of the signal by a heterodimeric complex of ERBB2 and EGFR. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as EGFR.
A series of molecular signals initiated by binding of a ligand to a ERBB4 receptor on the surface of a cell, followed by transmission of the signal by a heterodimeric complex of ERBB2 and ERBB4. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as ERBB4.
A series of molecular signals initiated by binding of a ligand to a ERBB4 receptor on the surface of a cell, followed by transmission of the signal by a heterodimeric complex of ERBB2 and ERBB4. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as ERBB4.
A series of molecular signals transmitted by a heterodimeric complex of the tyrosine kinase receptors ERBB3 and ERBB4. The pathway begins with binding of a ligand to either cell surface receptor, or the dimeric receptor complex, and ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals transmitted by a heterodimeric complex of the tyrosine kinase receptors ERBB3 and ERBB4. The pathway begins with binding of a ligand to either cell surface receptor, or the dimeric receptor complex, and ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals transmitted by a heterodimeric complex of the tyrosine kinase receptors EGFR (epidermal growth factor receptor/ERBB1) and ERBB4. The pathway begins with binding of a ligand to either cell surface receptor, or the dimeric receptor complex, and ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals transmitted by a heterodimeric complex of the tyrosine kinase receptors EGFR (epidermal growth factor receptor/ERBB1) and ERBB4. The pathway begins with binding of a ligand to either cell surface receptor, or the dimeric receptor complex, and ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals transmitted by a heterodimeric complex of the tyrosine kinase receptors EGFR (epidermal growth factor receptor/ERBB1) and ERBB4. The pathway begins with binding of a ligand to either cell surface receptor, or the dimeric receptor complex, and ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB4, followed by ligand-induced homodimerization of ERBB4 and transmission of the signal into the cell by the homodimeric ERBB4 complex. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB4, followed by ligand-induced homodimerization of ERBB4 and transmission of the signal into the cell by the homodimeric ERBB4 complex. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB4, followed by ligand-induced homodimerization of ERBB4 and transmission of the signal into the cell by the homodimeric ERBB4 complex. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
A heterodimeric complex between the tyrosine kinase receptors ERBB4 (also called HER4) and epidermal growth factor receptor (EGFR/ERBB1).
A heterodimeric complex between the tyrosine kinase receptors ERBB4 (also called HER4) and epidermal growth factor receptor (EGFR/ERBB1).
A heterodimeric complex between the tyrosine kinase receptors ERBB4 (also called HER4) and ERBB3 (also called HER3). ERBB3 has impaired kinase activity so relies on the kinase activity of its heterodimer partner for activation and signal transmission.
A heterodimeric complex between the tyrosine kinase receptors ERBB4 (also called HER4) and ERBB3 (also called HER3). ERBB3 has impaired kinase activity so relies on the kinase activity of its heterodimer partner for activation and signal transmission.
A homodimeric complex containing two monomers of the tyrosine kinase receptor ERBB4 (also called HER4).
A heterodimeric complex between the tyrosine kinase receptor ERBB2 and a ligand-activated epidermal growth factor receptor (EGFR/ERBB1). ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as EGFR.
A heterodimeric complex between the tyrosine kinase receptor ERBB2 and a ligand-activated epidermal growth factor receptor (EGFR/ERBB1). ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as EGFR.
A heterodimeric complex between the tyrosine kinase receptor ERBB2 and a ligand-activated receptor ERBB3. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as ERBB3.
A heterodimeric complex between the tyrosine kinase receptor ERBB2 and a ligand-activated receptor ERBB3. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as ERBB3.
A heterodimeric complex between the tyrosine kinase receptor ERBB2 and a ligand-activated receptor ERBB4. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as ERBB4.
A heterodimeric complex between the tyrosine kinase receptor ERBB2 and a ligand-activated receptor ERBB4. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as ERBB4.
A series of molecular signals initiated by the binding of the cytokine macrophage colony-stimulating factor (M-CSF) 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 the cytokine macrophage colony-stimulating factor (M-CSF) 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 the chemokine CXCL12 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 the chemokine CXCL12 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 the chemokine CXCL12 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 the chemokine CXCL12 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Combining with the C-X-C motif chemokine 12 (CXCL12) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with the C-X-C motif chemokine 12 (CXCL12) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with the C-X-C motif chemokine 12 (CXCL12) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with the C-X-C motif chemokine 12 (CXCL12) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with the C-X-C motif chemokine 12 (CXCL12) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
A series of molecular signals initiated by the binding of the C-C chemokine CCL2 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Combining with the C-C motif chemokine 2 (CCL2) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
A series of molecular signals initiated by a the C-C chemokine type 2 receptor (CCR2) on the surface of a cell binding to one of it's physiological ligands, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of the C-C chemokine CCL2 to a C-C chemokine type 2 receptor (CCR2) 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 a the C-C chemokine type 2 receptor (CCR4) on the surface of a cell binding to one of it's physiological ligands, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by a the C-C chemokine type 2 receptor (CCR4) on the surface of a cell binding to one of it's physiological ligands, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of the C-C chemokine CCL2 to a C-C chemokine type 4 receptor (CCR4) 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 interleukin-11 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 interleukin-11 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 interleukin-23 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 interleukin-23 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 interleukin-3 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 interleukin-3 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 the cytokine granulocyte macrophage colony-stimulating factor (GM-CSF) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. GM-CSF binds to a heterodimer receptor (CSF2R) consisting of an alpha ligand-binding subunit, and a common beta subunit that is shared with other cytokine receptors.
A series of molecular signals initiated by the binding of the cytokine granulocyte macrophage colony-stimulating factor (GM-CSF) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. GM-CSF binds to a heterodimer receptor (CSF2R) consisting of an alpha ligand-binding subunit, and a common beta subunit that is shared with other cytokine receptors.
A series of molecular signals initiated by the binding of the cytokine granulocyte macrophage colony-stimulating factor (GM-CSF) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. GM-CSF binds to a heterodimer receptor (CSF2R) consisting of an alpha ligand-binding subunit, and a common beta subunit that is shared with other cytokine receptors.
A series of molecular signals initiated by the binding of the cytokine granulocyte macrophage colony-stimulating factor (GM-CSF) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. GM-CSF binds to a heterodimer receptor (CSF2R) consisting of an alpha ligand-binding subunit, and a common beta subunit that is shared with other cytokine receptors.
A series of molecular signals initiated by the binding of the cytokine granulocyte macrophage colony-stimulating factor (GM-CSF) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. GM-CSF binds to a heterodimer receptor (CSF2R) consisting of an alpha ligand-binding subunit, and a common beta subunit that is shared with other cytokine receptors.
A series of molecular signals initiated by the binding of the cytokine granulocyte colony-stimulating factor (G-CSF) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. G-CSF binds to the receptor (CSF3R).
A series of molecular signals initiated by the binding of the cytokine granulocyte colony-stimulating factor (G-CSF) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. G-CSF binds to the receptor (CSF3R).
A series of molecular signals initiated by the binding of the cytokine granulocyte colony-stimulating factor (G-CSF) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. G-CSF binds to the receptor (CSF3R).
A series of molecular signals initiated by the binding of the cytokine granulocyte colony-stimulating factor (G-CSF) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. G-CSF binds to the receptor (CSF3R).
A series of molecular signals initiated by the binding of the cytokine granulocyte colony-stimulating factor (G-CSF) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. G-CSF binds to the receptor (CSF3R).
A series of molecular signals initiated by a the C-X-C chemokine type 4 receptor on the surface of a cell binding to one of it's physiological ligands, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of the C-X-C chemokine CXCL12 to a C-X-C chemokine type 4 receptor (CXCR4) 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 the peptide hormone prolactin 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 the peptide hormone prolactin 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 erythropoietin (EPO) to the erythropoietin receptor (EPO-R) 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 erythropoietin (EPO) to the erythropoietin receptor (EPO-R) 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 thrombopoietin to the thrombopoietin 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 thrombopoietin to the thrombopoietin 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 thrombopoietin to the thrombopoietin receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Combining with the glycoprotein thrombopoietin and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
A series of molecular signals initiated by the binding of oncostatin-M (OSM) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. OSM can signal via at least two different receptors (a specific receptor and a LIF receptor) to activate different downstream signal transduction pathways.
A series of molecular signals initiated by the binding of oncostatin-M (OSM) to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. OSM can signal via at least two different receptors (a specific receptor and a LIF receptor) to activate different downstream signal transduction pathways.
The series of molecular signals generated as a consequence of angiotensin II binding to an angiotensin receptor on the surface of the cell, and proceeding with the activated receptor transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity. Ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of angiotensin II binding to an angiotensin receptor on the surface of the cell, and proceeding with the activated receptor transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity. Ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of angiotensin II binding to an angiotensin receptor on the surface of the cell, and proceeding with the activated receptor transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity. Ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to one of its physiological ligands, where the signal is passed on within the cell via activation of the transcription factor NF-kappaB.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to one of its physiological ligands, where the signal is passed on within the cell via I-kappaB-kinase (IKK)-dependent activation of the transcription factor NF-kappaB.
The series of molecular signals generated as a consequence of an epidermal growth factor receptor binding to one of its physiological ligands, where the signal is passed on within the cell via I-kappaB-kinase (IKK)-dependent activation of the transcription factor NF-kappaB.
The series of molecular signals generated as a consequence of a somatostatin receptor (SSTR) binding to one of its physiological ligands and transmitting the signal to a heterotrimeric G-protein complex. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of a somatostatin receptor (SSTR) binding to one of its physiological ligands and transmitting the signal to a heterotrimeric G-protein complex. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of the peptide somatostatin (SST) binding to a somatostatin receptor (SSTR). The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of the peptide somatostatin (SST) binding to a somatostatin receptor (SSTR). The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of the peptide somatostatin (SST) binding to a somatostatin receptor (SSTR). The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of the peptide somatostatin (SST) binding to a somatostatin receptor (SSTR). The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of the peptide somatostatin (SST) binding to a somatostatin receptor (SSTR). The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of the peptide somatostatin (SST) binding to a somatostatin receptor (SSTR). The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of a cannabinoid binding to a cell surface receptor. The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription. Cannabinoids are a class of diverse chemical compounds that include the endocannabinoids and the phytocannabinoids.
The series of molecular signals generated as a consequence of a cannabinoid binding to a cell surface receptor. The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription. Cannabinoids are a class of diverse chemical compounds that include the endocannabinoids and the phytocannabinoids.
The series of molecular signals generated as a consequence of a cannabinoid binding to a cell surface receptor. The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription. Cannabinoids are a class of diverse chemical compounds that include the endocannabinoids and the phytocannabinoids.
A series of molecular signals initiated by the binding of interleukin-33 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 interleukin-33 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 interleukin-33 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 interleukin-33 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 interleukin-17A 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 interleukin-17A 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 interleukin-17A 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 interleukin-17A to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Combining with the cytokine interleukin-17A and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Any process that stops, prevents or reduces the frequency, rate or extent of the SREBP signaling pathway in response to an increase in oxygen levels.
Any process that stops, prevents or reduces the frequency, rate or extent of the SREBP signaling pathway in response to an increase in oxygen levels.
Any process that activates or increases the frequency, rate or extent of the SREBP signaling pathway in response to a decrease in oxygen levels.
Any process that activates or increases the frequency, rate or extent of the SREBP signaling pathway in response to a decrease in oxygen levels.
Interacting with a death receptor such that the proportion of death receptors in an active form is increased. Ligand binding to a death receptor often induces a conformational change to activate the receptor.
A series of molecular signals generated as a consequence of a the C5a component of the complement pathway binding to a complement receptor, and ending with regulation of a downstream cellular process. C5a is a peptide derived from the C5 complement factor.
A series of molecular signals initiated by the binding of a neurotrophin to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription. Neurotrophins are a family of secreted growth factors that induce the survival, development, and function of neurons.
A series of molecular signals initiated by the binding of nerve growth factor (NGF) to a receptor on the surface of the target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of nerve growth factor (NGF) to a receptor on the surface of the target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Combining with a bile acid and transmitting the signal to initiate a change in cell activity. A bile acid is any member of a group of steroid carboxylic acids occurring in bile.
Combining with an extracellular bile acid and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with an extracellular bile acid and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
Combining with an extracellular bile acid and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
A series of molecular signals initiated by the binding of a bile acid to a receptor, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by binding of a bile acid 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 a bile acid binding to an receptor located within a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Combining with lithocholic acid and transmitting the signal to initiate a change in cell activity.
Combining with a pathogen-associated molecular pattern (PAMP), a structure conserved among microbial species, or damage-associated molecular pattern (DAMP), an endogenous molecule released from damaged cells), to initiate a change in cell activity.
The series of molecular signals generated as a consequence of cholecystokinin binding to a receptor on the surface of the cell, and proceeding with the activated receptor transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity. Ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of cholecystokinin binding to a receptor on the surface of the cell, and proceeding with the activated receptor transmitting the signal to a heterotrimeric G-protein complex to initiate a change in cell activity. Ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of an extracellular ligand to a neuropilin protein on the surface of a target cell, followed by transmission of the signal, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of vascular endothelial growth factor (VEGF) to a neuropilin protein on the surface of a target cell, followed by transmission of the signal, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of vascular endothelial growth factor (VEGF) to a neuropilin protein on the surface of a target cell, followed by transmission of the signal, and ending with regulation of a downstream cellular process, e.g. transcription.
Interacting selectively and non-covalently with a member of the neuropilin family.
Interacting selectively and non-covalently with a member of the neuropilin family.
Interacting selectively and non-covalently with a member of the neuropilin family.
The series of molecular signals generated as a consequence of a gastric inhibitory peptide (GIP) binding to a cell surface receptor. The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of a gastric inhibitory peptide (GIP) binding to a cell surface receptor. The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of a gastric inhibitory peptide (GIP) binding to a cell surface receptor. The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of thromboxane A2 binding to a cell surface receptor. The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of thromboxane A2 binding to a cell surface receptor. The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of thyroid-stimulating hormone (thyrotropin) binding to a cell surface receptor. The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
The series of molecular signals generated as a consequence of thyroid-stimulating hormone (thyrotropin) binding to a cell surface receptor. The pathway proceeds with the receptor transmitting the signal to a heterotrimeric G-protein complex and ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of urokinase plasminogen activator to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of a type III interferon to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. Interferon lambda is the only member of the type III interferon found so far.
A series of molecular signals initiated by the binding of a type III interferon to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. Interferon lambda is the only member of the type III interferon found so far.
A heterodimeric protein complex that binds a type I interferon and transmits the signal across the membrane into the cell. Consists of an alpha subunit (IFNAR1) and a beta subunit (IFNAR2).
Combining with auxin and transmitting the signal in the cell to initiate a change in cell activity. Auxin is a plant hormone (phytohormone).
Combining with ethylene and transmitting the signal in the cell to initiate a change in cell activity.
Combining with ethylene and transmitting the signal in the cell to initiate a change in cell activity.
Combining with ethylene and transmitting the signal within the cell to initiate a change in cell activity by catalysis of the reaction: ATP + a protein-L-histidine = ADP + a protein-L-histidine phosphate.
A protein complex that contains at least TOR (target of rapamycin) in complex with other signaling components. Mediates the phosphorylation and activation of downstream signaling components including PKB (AKT) or S6K.
A protein complex that contains at least TOR (target of rapamycin) in complex with other signaling components. Mediates the phosphorylation and activation of downstream signaling components including PKB (AKT) or S6K.
A protein complex that contains at least TOR (target of rapamycin) in complex with other signaling components. Mediates the phosphorylation and activation of downstream signaling components including PKB (AKT) or S6K.
A series of intracellular molecular signals mediated by TORC1; TOR (target of rapamycin) in complex with at least Raptor (regulatory-associated protein of TOR), or orthologs of, and other signaling components.
A series of intracellular molecular signals mediated by TORC2; TOR (rapamycin-insensitive companion of TOR) in complex with at least Rictor (regulatory-associated protein of TOR), or orthologs of, and other signaling components.
The process in which regions of the embryo are delineated into the area in which the pronephric kidney will develop.
The process in which the proximal tubule of the pronephric nephron acquires its identity.
The process in which the tubules arranged along the proximal/distal axis of the pronephric nephron acquire their identity.
The developmental process pertaining to the initial formation of a pronephric nephron tubule from unspecified parts. A pronephric nephron tubule is an epithelial tube that is part of a nephron in the pronephros.
The developmental process pertaining to the initial formation of a pronephric nephron tubule from unspecified parts. A pronephric nephron tubule is an epithelial tube that is part of a nephron in the pronephros.
The process in which the anatomical structures of the pronephric nephron are generated and organized. A pronephric nephron is the functional unit of the pronephros.
The process in which the anatomical structures of a pronephric nephron tubule are generated and organized from an epithelium. A pronephric nephron tubule is an epithelial tube that is part of the pronephric nephron.
The process whose specific outcome is the progression of the rectal diverticulum over time, from its formation to the mature structure. The rectal diverticulum is an outgrowth of the cloaca and links the pronephric kidney to the exterior.
The process in which the distal tubule of the pronephric nephron acquires its identity.
The process in which the anatomical structures of a pronephric nephron proximal tubule are generated and organized. A pronephric nephron tubule is an epithelial tube that is part of the pronephros.
The process whose specific outcome is the progression of the pronephric sinus over time, from its formation to the mature structure. The pronephric sinus is an ill-defined capillary network that lies between the pronephric tubules.
The process in which the anatomical structures of a pronephric nephron distal tubule are generated and organized. A pronephric nephron tubule is an epithelial tube that is part of the pronephros.
The process in which relatively unspecialized cells acquire specialized structural and/or functional features that characterize the cells of the pronephros as it progresses from its formation to the mature state.
The multiplication or reproduction of cells, resulting in the expansion of the population in the pronephros.
Any process that mediates the transfer of information from one cell to another and contributes to the progression of the pronephros over time, from its formation to the mature organ.
Any process that mediates the transfer of information from one cell to another and contributes to the progression of the pronephros over time, from its formation to the mature organ.
Any developmental process that results in the creation of defined areas or spaces within the pronephros to which cells respond and eventually are instructed to differentiate.
The process whose specific outcome is the progression of the nephrostome over time, from its formation to the mature structure. The nephrostome is the opening of the pronephros into the body cavity.
The process whose specific outcome is the progression of the pronephric nephron over time, from its formation to the mature structure. A pronephric nephron is the functional unit of the pronephros.
The process whose specific outcome is the progression of a pronephric nephron tubule over time, from its formation to the mature structure. The pronephric nephron tubule is an epithelial tube that is part of the pronephric nephron and connects the filtration unit (glomerulus or glomus) of the pronephros to the pronephric duct.
The progression of the glomerulus of the pronephric kidney over time from its initial formation until its mature state. The pronephric glomerulus is part of the pronephric nephron and is restricted to one body segment.
The process whose specific outcome is the progression of the pronephric duct over time, from its formation to the mature structure. The pronephric duct collects the filtrate from the pronephric tubules and opens to the exterior of the pronephric kidney.
The process in which the anatomical structures of the pronephric duct are generated and organized. The pronephric duct collects the filtrate from the pronephric tubules and opens to the exterior of the kidney.
Any viral process that results in the inhibition of host cell type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any viral process that results in the inhibition of host cell type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any viral process that results in the inhibition of host cell type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of type I interferon-mediated signaling in the host organism. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of type I interferon-mediated signaling in the host organism. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of type I interferon-mediated signaling in the host organism. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of type I interferon-mediated signaling in the host organism. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the innate immune response of the host organism, the host's first line of defense.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the innate immune response of the host organism, the host's first line of defense.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the innate immune response of the host organism, the host's first line of defense.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the innate immune response of the host organism, the host's first line of defense.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the adaptive immune response of the host organism, an immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory).
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the adaptive immune response of the host organism, an immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory).
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the adaptive immune response of the host organism, an immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory).
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the adaptive immune response of the host organism, an immune response based on directed amplification of specific receptors for antigen produced through a somatic diversification process, and allowing for enhanced response to subsequent exposures to the same antigen (immunological memory).
Any viral process that inhibits a host antigen-presenting cell expressing a peptide antigen on its cell surface in association with an MHC class II protein complex.
The process in which a virus effects a change in the function of a host protein via a direct interaction.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host protein.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host protein.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host protein.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host protein.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host protein.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host protein.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host receptor.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host receptor.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host receptor.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host receptor.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host receptor.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host receptor.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host pattern recognition receptor. A pattern recognition receptor combines with a molecular pattern based on a repeating or polymeric structure, such as a polysaccharide or peptidoglycan, to initiate a change in cell activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host pattern recognition receptor. A pattern recognition receptor combines with a molecular pattern based on a repeating or polymeric structure, such as a polysaccharide or peptidoglycan, to initiate a change in cell activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host pattern recognition receptor. A pattern recognition receptor combines with a molecular pattern based on a repeating or polymeric structure, such as a polysaccharide or peptidoglycan, to initiate a change in cell activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host pattern recognition receptor. A pattern recognition receptor combines with a molecular pattern based on a repeating or polymeric structure, such as a polysaccharide or peptidoglycan, to initiate a change in cell activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host pattern recognition receptor. A pattern recognition receptor combines with a molecular pattern based on a repeating or polymeric structure, such as a polysaccharide or peptidoglycan, to initiate a change in cell activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host pattern recognition receptor. A pattern recognition receptor combines with a molecular pattern based on a repeating or polymeric structure, such as a polysaccharide or peptidoglycan, to initiate a change in cell activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host ATP-dependent RNA helicase activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host ATP-dependent RNA helicase activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host ATP-dependent RNA helicase activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host ATP-dependent RNA helicase activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host interferon receptor.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host interferon receptor.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host interferon receptor.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host interferon receptor.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host interferon receptor.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host protein tyrosine kinase activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host protein tyrosine kinase activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host protein tyrosine kinase activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host protein tyrosine kinase activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host enzyme activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host enzyme activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host enzyme activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host enzyme activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the JAK-STAT signal cascade in the host organism.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the JAK-STAT signal cascade in the host organism.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the JAK-STAT signal cascade in the host organism.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the JAK-STAT signal cascade in the host organism.
The process in which a virus effects a change in host enzyme activity.
The process in which a virus effects a change in host enzyme activity.
The process in which a virus effects a change in host enzyme activity.
The process in which a virus effects a change in host protein serine/threonine phosphatase activity.
The process in which a virus effects a change in host protein serine/threonine phosphatase activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host cytokine activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host cytokine activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host cytokine activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host cytokine activity.
Any process in which a virus effect a change in the frequency, rate or extent of autophagy in the host.
Any process in which a virus activates or increases the frequency, rate or extent of autophagy in the host.
Any process in which a virus activates or increases the frequency, rate or extent of autophagy in the host.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of autophagy in the host.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of autophagy in the host.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of autophagy in the host.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of movement of mRNA from the nucleus to the cytoplasm in the host organism.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of movement of mRNA from the nucleus to the cytoplasm in the host organism.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of movement of mRNA from the nucleus to the cytoplasm in the host organism.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of movement of mRNA from the nucleus to the cytoplasm in the host organism.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host RNA polymerase II activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host RNA polymerase II activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host RNA polymerase II activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of mRNA processing in the host cell. mRNA processing is the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of mRNA processing in the host cell. mRNA processing is the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of mRNA processing in the host cell. mRNA processing is the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of mRNA processing in the host cell. mRNA processing is the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
Any process in which a virus effects a change in the organization of chromatin in the host.
Any process in which a virus effects a change in the organization of chromatin in the host.
Any process in which a virus effects a change in the organization of chromatin in the host.
Any process in which a virus effects a change in the organization of chromatin in the host.
Any process in which a virus modulates the frequency, rate or extent of apoptosis of infected host cells.
Any process in which a virus modulates the frequency, rate or extent of apoptosis of infected host cells.
Any process in which a virus modulates the frequency, rate or extent of apoptosis of infected host cells.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of TRAF-mediated signal transduction in the host.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of TRAF-mediated signal transduction in the host.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of TRAF-mediated signal transduction in the host.
Any series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. RIG-I detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. RIG-I detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. RIG-I detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. MDA-5 detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. MDA-5 detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. MDA-5 detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. MDA-5 detects RNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any process that modulates the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm.
Any process that modulates the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm.
Any process that stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm.
Any process that stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm.
Any process that stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm.
Any process that modulates the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA.
Any process that modulates the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA.
Any process that modulates the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA.
Any process that modulates the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA.
Any process that modulates the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA.
Any process that modulates the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA.
Any process that modulates the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) RIG-1 (also known as DDX58) binding to viral RNA. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. This is a mechanism by which the virus evades the host innate immune response.
Any process in which a virus stops, prevents, or reduces the activity of RIG-1 (also known as DDX58). The cytoplasmic pattern recognition RIG-I recognizes viral RNA synthesized during active viral replication and signals to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any process in which a virus stops, prevents, or reduces the activity of RIG-1 (also known as DDX58). The cytoplasmic pattern recognition RIG-I recognizes viral RNA synthesized during active viral replication and signals to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any process in which a virus stops, prevents, or reduces the activity of RIG-1 (also known as DDX58). The cytoplasmic pattern recognition RIG-I recognizes viral RNA synthesized during active viral replication and signals to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any process in which a virus stops, prevents, or reduces the activity of MAVS (mitochondrial antiviral signaling protein), a signal transducer that lies downstream of the viral RNA receptors MDA-5 and RIG-I to coordinate host innate immune responses.
Any process in which a virus stops, prevents, or reduces the activity of MAVS (mitochondrial antiviral signaling protein), a signal transducer that lies downstream of the viral RNA receptors MDA-5 and RIG-I to coordinate host innate immune responses.
Any process in which a virus stops, prevents, or reduces the activity of a host TRAF (tumor necrosis factor receptor-associated factor) protein. TRAFs are intracellular signal transducers that lie downstream of receptors including RIG-I, MDA-5 and Toll-like receptors (TLR) and transfer the signal to other intracellular signaling components.
Any process in which a virus stops, prevents, or reduces the activity of host IRF3 (interferon regulatory factor-3), a transcription factor in the RIG-I/MDA-5 signaling pathway. Viral infection triggers phosphorylation of cytoplasmic IRF3, which allows IRF3 to form a homodimer, migrate to the nucleus, and activate transcription of IFN-alpha and IFN-beta genes.
Any process in which a virus stops, prevents, or reduces the activity of host IRF3 (interferon regulatory factor-3), a transcription factor in the RIG-I/MDA-5 signaling pathway. Viral infection triggers phosphorylation of cytoplasmic IRF3, which allows IRF3 to form a homodimer, migrate to the nucleus, and activate transcription of IFN-alpha and IFN-beta genes.
Any process in which a virus stops, prevents, or reduces the activity of host IRF3 (interferon regulatory factor-3), a transcription factor in the RIG-I/MDA-5 signaling pathway. Viral infection triggers phosphorylation of cytoplasmic IRF3, which allows IRF3 to form a homodimer, migrate to the nucleus, and activate transcription of IFN-alpha and IFN-beta genes.
Interacting selectively and non-covalently with RIG-I, a cytosolic pattern recognition receptor that initiates an antiviral signaling pathway upon binding to viral RNA.
Interacting selectively and non-covalently with RIG-I, a cytosolic pattern recognition receptor that initiates an antiviral signaling pathway upon binding to viral RNA.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host chemokine activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host chemokine activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host chemokine activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host chemokine activity.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host chemokine activity.
Any process in which a virus stops, prevents, or reduces the activity of MDA-5 (also known as IFIH1). The cytoplasmic pattern recognition receptor MDA-5 detects dsRNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Any process in which a virus stops, prevents, or reduces the activity of MDA-5 (also known as IFIH1). The cytoplasmic pattern recognition receptor MDA-5 detects dsRNA synthesized during active viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines.
Interacting selectively and non-covalently with MDA-5, a cytosolic pattern recognition receptor that initiates an antiviral signaling pathway upon binding to viral dsRNA.
Any process in which a virus stops, prevents, or reduces the activity of host IRF7 (interferon regulatory factor-7), a transcription factor in the RIG-I/MDA-5 signaling pathway. Viral infection triggers phosphorylation of cytoplasmic IRF7, which allows IRF7 to form a homodimer, migrate to the nucleus, and activate transcription of IFN-alpha and IFN-beta genes.
Any process in which a virus stops, prevents, or reduces the activity of host IRF7 (interferon regulatory factor-7), a transcription factor in the RIG-I/MDA-5 signaling pathway. Viral infection triggers phosphorylation of cytoplasmic IRF7, which allows IRF7 to form a homodimer, migrate to the nucleus, and activate transcription of IFN-alpha and IFN-beta genes.
Any process in which a virus stops, prevents, or reduces the activity of host IRF7 (interferon regulatory factor-7), a transcription factor in the RIG-I/MDA-5 signaling pathway. Viral infection triggers phosphorylation of cytoplasmic IRF7, which allows IRF7 to form a homodimer, migrate to the nucleus, and activate transcription of IFN-alpha and IFN-beta genes.
Any process in which a virus stops, prevents, or reduces the activity of host IRF9 (interferon regulatory factor-9), a transcription factor involved in the innate immune response. Viral infection triggers binding of IRF9 to phosphorylated STAT1 and STAT2, forming the ISGF3 complex. The ISGF3 complex migrates to the nucleus and activates transcription of IFN-responsive genes.
Any process in which a virus stops, prevents, or reduces the activity of host IRF9 (interferon regulatory factor-9), a transcription factor involved in the innate immune response. Viral infection triggers binding of IRF9 to phosphorylated STAT1 and STAT2, forming the ISGF3 complex. The ISGF3 complex migrates to the nucleus and activates transcription of IFN-responsive genes.
Any process in which a virus stops, prevents, or reduces the activity of host IRF9 (interferon regulatory factor-9), a transcription factor involved in the innate immune response. Viral infection triggers binding of IRF9 to phosphorylated STAT1 and STAT2, forming the ISGF3 complex. The ISGF3 complex migrates to the nucleus and activates transcription of IFN-responsive genes.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host STAT (signal transducer and activator of transcription) activity. STATs are SH2 domain-containing proteins which lie downstream of many signaling receptors. Upon phosphorylation by JAKs, STAT proteins hetero- or homo-dimerize and translocate to the nucleus to activate transcription of target genes.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host STAT (signal transducer and activator of transcription) activity. STATs are SH2 domain-containing proteins which lie downstream of many signaling receptors. Upon phosphorylation by JAKs, STAT proteins hetero- or homo-dimerize and translocate to the nucleus to activate transcription of target genes.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host STAT1 (signal transducer and activator of transcription-1) activity. STATs are SH2 domain-containing proteins which lie downstream of many signaling receptors. Upon phosphorylation by JAKs, STAT proteins hetero- or homo-dimerize and translocate to the nucleus to activate transcription of target genes.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host STAT1 (signal transducer and activator of transcription-1) activity. STATs are SH2 domain-containing proteins which lie downstream of many signaling receptors. Upon phosphorylation by JAKs, STAT proteins hetero- or homo-dimerize and translocate to the nucleus to activate transcription of target genes.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host STAT2 (signal transducer and activator of transcription-2) activity. STATs are SH2 domain-containing proteins which lie downstream of many signaling receptors. Upon phosphorylation by JAKs, STAT proteins hetero- or homo-dimerize and translocate to the nucleus to activate transcription of target genes.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host STAT2 (signal transducer and activator of transcription-2) activity. STATs are SH2 domain-containing proteins which lie downstream of many signaling receptors. Upon phosphorylation by JAKs, STAT proteins hetero- or homo-dimerize and translocate to the nucleus to activate transcription of target genes.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of complement activation. The activation of complement involves the sequential proteolysis of proteins to generate enzymes with catalytic activities. The biological functions of the complement include opsonization, inflammation, lysis of immune complexes, or enhancement of the humoral immune response. For example, the virus complement control protein (VCP) of vaccinia virus, and the complement control protein of herpesvirus inhibit C3 convertase.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of complement activation. The activation of complement involves the sequential proteolysis of proteins to generate enzymes with catalytic activities. The biological functions of the complement include opsonization, inflammation, lysis of immune complexes, or enhancement of the humoral immune response. For example, the virus complement control protein (VCP) of vaccinia virus, and the complement control protein of herpesvirus inhibit C3 convertase.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of complement activation. The activation of complement involves the sequential proteolysis of proteins to generate enzymes with catalytic activities. The biological functions of the complement include opsonization, inflammation, lysis of immune complexes, or enhancement of the humoral immune response. For example, the virus complement control protein (VCP) of vaccinia virus, and the complement control protein of herpesvirus inhibit C3 convertase.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host TYK2 (tyrosine kinase 2) activity. TYK2 is an intracellular signal-transducing tyrosine kinase that associates with the cytoplasmic tails of cytokine receptors and transmits the cytokine signal by phosphorylating receptor subunits.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host JAK1 (Janus Kinase 1) activity. In the host, binding of a ligand to a receptor triggers activation of JAK proteins, which phosphorylate tyrosine residues on the receptor creating sites for STAT proteins to bind, which are in turn phosphorylated and activated by JAK proteins. By blocking JAK1 activity, many viruses block the host signal transduction pathway.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host JAK1 (Janus Kinase 1) activity. In the host, binding of a ligand to a receptor triggers activation of JAK proteins, which phosphorylate tyrosine residues on the receptor creating sites for STAT proteins to bind, which are in turn phosphorylated and activated by JAK proteins. By blocking JAK1 activity, many viruses block the host signal transduction pathway.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host JAK1 (Janus Kinase 1) activity. In the host, binding of a ligand to a receptor triggers activation of JAK proteins, which phosphorylate tyrosine residues on the receptor creating sites for STAT proteins to bind, which are in turn phosphorylated and activated by JAK proteins. By blocking JAK1 activity, many viruses block the host signal transduction pathway.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host JAK1 (Janus Kinase 1) activity. In the host, binding of a ligand to a receptor triggers activation of JAK proteins, which phosphorylate tyrosine residues on the receptor creating sites for STAT proteins to bind, which are in turn phosphorylated and activated by JAK proteins. By blocking JAK1 activity, many viruses block the host signal transduction pathway.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host JAK1 (Janus Kinase 1) activity. In the host, binding of a ligand to a receptor triggers activation of JAK proteins, which phosphorylate tyrosine residues on the receptor creating sites for STAT proteins to bind, which are in turn phosphorylated and activated by JAK proteins. By blocking JAK1 activity, many viruses block the host signal transduction pathway.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host JAK1 (Janus Kinase 1) activity. In the host, binding of a ligand to a receptor triggers activation of JAK proteins, which phosphorylate tyrosine residues on the receptor creating sites for STAT proteins to bind, which are in turn phosphorylated and activated by JAK proteins. By blocking JAK1 activity, many viruses block the host signal transduction pathway.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host JAK1 (Janus Kinase 1) activity. In the host, binding of a ligand to a receptor triggers activation of JAK proteins, which phosphorylate tyrosine residues on the receptor creating sites for STAT proteins to bind, which are in turn phosphorylated and activated by JAK proteins. By blocking JAK1 activity, many viruses block the host signal transduction pathway.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host ubiquitin-like protein ISG15 activity. ISG15 is a ubiquitin-like protein that is conjugated to lysine residues on various target proteins. Viruses escape from the antiviral activity of ISG15 by using different mechanisms; the influenza B virus NS1 protein for instance blocks the covalent linkage of ISG15 to its target proteins by directly interacting with ISG15. The papain-like protease from the coronavirus cleaves ISG15 derivatives.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host PKR (protein kinase regulated by RNA) activity. Activation of PKR involves dsRNA binding followed by autophosphorylation. Phosphorylated PKR can then phosphorylate downstream targets such as the translation initiation factor eIF2 to inhibit protein synthesis. Viruses encode a number of mechanisms to inhibit the host antiviral response via PKR, including direct interaction with PKR, promoting degradation of PKR or altering the subcellular location of PKR.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host protein kinase activity.
A series of reactions in which a signal is passed on to downstream proteins within the cell via PKR, an intracellular protein kinase that is activated by stress signals or upon binding to double-stranded RNA (dsRNA), followed by autophosphorylation. PKR plays a role in the antiviral response, phosphorylating proteins such as the translation initiation factor eIF2 to inhibit protein synthesis during viral infection. Begins with activation of PKR activity, and ends with regulation of a downstream cellular process, e.g. regulation of transcription or inhibition of translation.
A series of reactions in which a signal is passed on to downstream proteins within the cell via PKR, an intracellular protein kinase that is activated by stress signals or upon binding to double-stranded RNA (dsRNA), followed by autophosphorylation. PKR plays a role in the antiviral response, phosphorylating proteins such as the translation initiation factor eIF2 to inhibit protein synthesis during viral infection. Begins with activation of PKR activity, and ends with regulation of a downstream cellular process, e.g. regulation of transcription or inhibition of translation.
The process in which a virus effects a change in host protein phosphatase-1 (PP1) activity, a serine/threonine phosphatase. Different viruses modulate host PP1 activity to remove phosphates from various cellular substrates and downregulate the host's antiviral response.
The process in which a virus effects a change in host protein phosphatase-1 (PP1) activity, a serine/threonine phosphatase. Different viruses modulate host PP1 activity to remove phosphates from various cellular substrates and downregulate the host's antiviral response.
Any process in which a virus stops, prevents, or reduces the activity of host tetherin activity. Tetherin (also known as BST2) is an alpha interferon-inducible cellular factor that impairs the release of many enveloped viruses. By blocking tetherin activity, many viruses circumvent its antiviral effects.
Any process in which a virus stops, prevents, or reduces the activity of host tetherin activity. Tetherin (also known as BST2) is an alpha interferon-inducible cellular factor that impairs the release of many enveloped viruses. By blocking tetherin activity, many viruses circumvent its antiviral effects.
Any viral process that inhibits a host antigen-presenting cell expressing a peptide antigen on its cell surface in association with an MHC protein complex.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host tapasin (TAP binding protein/TAPBP) activity. Tapasin is a type I transmembrane protein essential for the optimal expression of stable MHC class I molecules on the host cell surface. By inhibiting host tapasin activity, viruses can prevent presentation of their antigens at the cell surface, and thereby evade the host anti-viral immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host tapasin (TAP binding protein/TAPBP) activity. Tapasin is a type I transmembrane protein essential for the optimal expression of stable MHC class I molecules on the host cell surface. By inhibiting host tapasin activity, viruses can prevent presentation of their antigens at the cell surface, and thereby evade the host anti-viral immune response.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host tapasin (TAP binding protein/TAPBP) activity. Tapasin is a type I transmembrane protein essential for the optimal expression of stable MHC class I molecules on the host cell surface. By inhibiting host tapasin activity, viruses can prevent presentation of their antigens at the cell surface, and thereby evade the host anti-viral immune response.
Any viral process that decreases the rate or extent of progression from G2 phase to M phase of the host mitotic cell cycle.
Any viral process which decreases the rate or extent of a host cell leaving M phase of the cell cycle. M phase is the part of the mitotic cell cycle during which mitosis and cytokinesis take place.
Any endoribonuclease activity that contributes to the viral-induced catabolism of host mRNA.
The process in which a virus increases the frequency, rate or extent of the breakdown of host messenger RNA (mRNA).
The process in which a virus increases the frequency, rate or extent of the breakdown of host messenger RNA (mRNA).
The process in which a virus increases the frequency, rate or extent of the breakdown of host messenger RNA (mRNA).
The process in which a virus increases the frequency, rate or extent of the breakdown of host messenger RNA (mRNA).
The process in which a virus increases the frequency, rate or extent of the breakdown of host messenger RNA (mRNA).
Any viral process that modulates the frequency, rate or extent of dephosphorylation of a host protein.
Any viral process that activates or increases the frequency, rate or extent of host endoribonuclease activity.
Any process in which a host pre-mRNA or mRNA molecule is cleaved at specific sites or in a regulated manner by a viral endoribonuclease.
Any process in which a host pre-mRNA or mRNA molecule is cleaved at specific sites or in a regulated manner by a viral endoribonuclease.
The process in which a virus increases the frequency, rate or extent of the breakdown of host nuclear-transcribed mRNAs that begins with endonucleolytic cleavage (by either a host or a viral RNAse) to generate unprotected ends.
The process in which a virus increases the frequency, rate or extent of the breakdown of host nuclear-transcribed mRNAs that begins with endonucleolytic cleavage (by either a host or a viral RNAse) to generate unprotected ends.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the assembly of the RNA polymerase II preinitiation complex (PIC) at an RNA polymerase II promoter region of a host DNA template.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the assembly of the RNA polymerase II preinitiation complex (PIC) at an RNA polymerase II promoter region of a host DNA template.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the assembly of the RNA polymerase II preinitiation complex (PIC) at an RNA polymerase II promoter region of a host DNA template.
Any process in which a virus prevents or reduces the frequency, rate or extent of translation of host mRNA.
Any process in which a virus prevents or reduces the frequency, rate or extent of translation of host mRNA.
Any process in which a virus prevents or reduces the frequency, rate or extent of translation of host mRNA.
Any process in which a virus prevents or reduces the frequency, rate or extent of host translation initiation, the host process preceding formation of the peptide bond between the first two amino acids of a protein.
Any process in which a virus prevents or reduces the frequency, rate or extent of activity of a host translation initiation factor.
Any process in which a virus prevents or reduces the frequency, rate or extent of activity of a host translation initiation factor.
Any process in which a virus prevents or reduces the frequency, rate or extent of activity of a host translation initiation factor.
Any process in which a virus prevents or reduces the frequency, rate or extent of activity of a host translation initiation factor.
Any viral process that modulates the frequency, rate or extent of phosphorylation of viral or host proteins in a host.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of phosphorylation of viral or host proteins in a host.
Any process in which a virus activates or increases the frequency, rate or extent of phosphorylation of viral or host proteins in a host.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=1 symmetry. The T=1 capsid is composed of 12 pentameric capsomeres.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=2 symmetry. The T=2 capsid is composed of 12 pentameric dimers.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=3 symmetry. The T=3 capsid is composed of 12 pentameric and 20 hexameric capsomeres.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with pseudo T=3 symmetry. The T=pseudo3 capsid is composed of 12 pentameric and 20 hexameric capsomeres.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=4 symmetry. The T=4 capsid is composed of 12 pentameric and 30 hexameric capsomeres.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=7 symmetry. The T=7 capsid is composed of 12 pentameric and 60 hexameric capsomeres.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=13 symmetry. The T=13 capsid is composed of 12 pentameric and 120 hexameric capsomeres.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=16 symmetry. The T=16 capsid is composed of 12 pentameric and 150 hexameric capsomeres.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=25 symmetry. The T=25 capsid is composed of 12 pentameric and 240 hexameric capsomeres.
The outer layer of a double or triple concentric icosahedral capsid. Outer capsids are part of reoviridae and cystoviridae virions.
The inner layer of a double or triple concentric icosahedral capsid. Inner capsids are part of reoviridae and cystoviridae virions.
The intermediate layer of a triple concentric icosahedral capsid. Intermediate capsids are part of reoviridae virions.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=147 symmetry. T=147 icosahedral capsid is composed of 12 pentameric and 1460 hexameric capsomeres for a total of 8820 capsid proteins.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=169 symmetry. T=169 icosahedral capsid is composed of 12 pentameric and 1680 hexameric capsomeres for a total of 10140 capsid proteins.
The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=219 symmetry. T=219 icosahedral capsid is composed of 12 pentameric and 2180 hexameric capsomeres for a total of 13140 capsid proteins.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive movement along a single- or double-stranded RNA molecule.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive movement along a single- or double-stranded DNA molecule, that contributes to the packing of viral DNA into a capsid.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive movement along a single- or double-stranded DNA molecule, that contributes to the packing of viral DNA into a capsid.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive movement along a single- or double-stranded RNA molecule, which contributes to the packaging of viral RNA into a nucleocapsid.
Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive movement along a single- or double-stranded RNA molecule, which contributes to the packaging of viral RNA into a nucleocapsid.
Any process mediated by a virus that results in the death of a cell in the host organism.
Any process mediated by a virus that results in the death of a cell in the host organism.
The viral-killing of a host cell by a pre-existing virus in response to a subsequent infection of the host cell by second virus.
The viral-killing of a host cell by a pre-existing virus in response to a subsequent infection of the host cell by second virus.
The viral-killing of a host cell by a pre-existing virus in response to a subsequent infection of the host cell by second virus.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of peptidoglycan biosynthesis in the host organism. Peptidoglycans are any of a class of glycoconjugates found in bacterial cell walls.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of cell wall biogenesis in the host organism. Cell wall biogenesis includes the biosynthesis of constituent macromolecules, and the assembly and arrangement of these constituent parts.
The breakdown of host DNA, deoxyribonucleic acid, by a virus.
The process by which a virion attaches to a host cell by binding to a lipopolysaccharide (LPS) on the host cell surface.
The process by which a virion attaches to a host cell by binding to a lipopolysaccharide (LPS) on the host cell surface.
The process by which a virion attaches to a host cell by binding to a lipopolysaccharide (LPS) on the host cell surface.
The prevention or delay of host cell lysis by a pre-existing virus in response to a subsequent infection of the host cell by second virus.
The prevention or delay of host cell lysis by a pre-existing virus in response to a subsequent infection of the host cell by second virus.
The killing by a virus of host cell by cytolysis, caused by a virus stopping, preventing, or reducing peptidoglycan biosynthesis in the host organism. Peptidoglycans are any of a class of glycoconjugates found in bacterial cell walls.
The lipid bilayer of a virion contained inside the protein capsid.
The region of a virion in which the nucleic acid is confined.
The region of a host cell that contains the viral genome.
Any process in which a virus stops, prevents, or reduces the activity of host NF-kappaB activity.
Any viral process that modulates the frequency, rate or extent of the host cell G1/S transition checkpoint.
Any viral process that modulates the frequency, rate or extent of the host cell G0/G1 transition checkpoint.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host poly(A)-binding protein (PABP) activity. PABP binds to the poly(A) tail of mRNA to facilitate translation.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host poly(A)-binding protein (PABP) activity. PABP binds to the poly(A) tail of mRNA to facilitate translation.
Any process in which a virus modulates the frequency, rate or extent of protein ubiquitination in the host organism. Ubiquitination is the process in which one or more ubiquitin groups are added to a protein.
The process in which a virus effects a change in host ubiquitin-protein ligase activity. Ubiquitin-protein ligase activity catalyzes the reaction: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host caspase activity. Caspases are cysteine-type endopeptidases which contribute to the apoptotic process.
Any process in which a virus increases the frequency, rate or extent of host cysteine-type endopeptidase activity (also called caspase activity) which contributes to the apoptotic process.
Any process in which a virus increases the frequency, rate or extent of host cysteine-type endopeptidase activity (also called caspase activity) which contributes to the apoptotic process.
Any process in which a virus starts, promotes, or enhances the activity of the host transcription factor NF-kappaB.
Any process in which a virus stops, prevents, or reduces the activity of host DNA-dependent transcription; the cellular synthesis of RNA on a template of DNA. Viral proteins can interfere with either host RNA polymerase or with transcription factors.
Any process in which a virus stops, prevents, or reduces the activity of host DNA-dependent transcription; the cellular synthesis of RNA on a template of DNA. Viral proteins can interfere with either host RNA polymerase or with transcription factors.
Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
The process in which a virus effects a change in gene expression in its host organism. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein. Some protein processing events may be included when they are required to form an active form of a product from an inactive precursor form.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of gene expression in the host organism. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein. Some protein processing events may be included when they are required to form an active form of a product from an inactive precursor form.
A protein complex containing TBK1 (TANK-binding kinase 1), IKBKE (I-Kappa-B kinase epsilon/IKKE/IKK-epsilon) and the DEAD box family RNA helicase DDX3.
The action of a molecule that contributes to the structural integrity of a virion.
The outer, i.e. cytoplasm-facing in a cellular organelle, lipid bilayer of an organelle envelope, occurring in a host cell.
A lipid bilayer that forms the outermost layer of the cell envelope, occurring in a host cell.
A lipid bilayer that forms the outermost layer of the cell envelope, occurring in a host cell.
Merging of the virion membrane and a host membrane (host plasma membrane or host organelle membrane) that is involved in the uptake of a virus into a host cell.
Merging of the virion membrane and a host membrane (host plasma membrane or host organelle membrane) that is involved in the uptake of a virus into a host cell.
Merging of the virion membrane and a host membrane (host plasma membrane or host organelle membrane) that is involved in the uptake of a virus into a host cell.
The viral-induced lysis of an organelle (endosome, lysosome, or caveosome) that is involved in the uptake of a virus into a host cell. Occurs once the virus is within the organelle, and results in transfer of the viral contents from the organelle compartment into the cytoplasm.
The viral-induced lysis of an organelle (endosome, lysosome, or caveosome) that is involved in the uptake of a virus into a host cell. Occurs once the virus is within the organelle, and results in transfer of the viral contents from the organelle compartment into the cytoplasm.
The viral-induced lysis of an organelle (endosome, lysosome, or caveosome) that is involved in the uptake of a virus into a host cell. Occurs once the virus is within the organelle, and results in transfer of the viral contents from the organelle compartment into the cytoplasm.
The viral-induced lysis of an organelle (endosome, lysosome, or caveosome) that is involved in the uptake of a virus into a host cell. Occurs once the virus is within the organelle, and results in transfer of the viral contents from the organelle compartment into the cytoplasm.
Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm.
Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm.
Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm.
Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm.
Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm.
The process by which a virion attaches to a host cell by binding to a pilus on the host cell surface. Pili are retractile filaments that protrude from gram-negative bacteria. Filamentous viruses can attach to the pilus tip, whereas icosahedral viruses can attach to the pilus side.
The process by which a virion attaches to a host cell by binding to a pilus on the host cell surface. Pili are retractile filaments that protrude from gram-negative bacteria. Filamentous viruses can attach to the pilus tip, whereas icosahedral viruses can attach to the pilus side.
The process by which a virion attaches to a host cell by binding to a pilus on the host cell surface. Pili are retractile filaments that protrude from gram-negative bacteria. Filamentous viruses can attach to the pilus tip, whereas icosahedral viruses can attach to the pilus side.
The process by which a virion attaches to a host cell by binding to a pilus on the host cell surface. Pili are retractile filaments that protrude from gram-negative bacteria. Filamentous viruses can attach to the pilus tip, whereas icosahedral viruses can attach to the pilus side.
The uptake of a virus or viral genetic material into a host cell which occurs through retraction of a virion-bound pilus.
The uptake of a virus or viral genetic material into a host cell which occurs through retraction of the virion-bound pilus, followed by entry of the viral genome into the host cell through the pilus basal pore. Filamentous bacteriophages absorb to the tip of the F-pili and can enter the bacterial cell in this way.
The uptake of a virus into a host cell which occurs via retraction of the viral-bound pilus to bring the virus in contact with the host cell membrane, followed by fusion of the bacteriophage membrane with the host outer membrane.
A turret-like appendage formed at the vertices of an icosahedral capsid.
Any process by which a virus avoids the effects mediated by the host organism's natural killer (NK) cells.
Any process by which a virus avoids the effects mediated by the host organism's natural killer (NK) cells.
Any process by which a virus avoids the effects mediated by the host organism's natural killer (NK) cells.
Any process by which a virus avoids the effects mediated by the host organism's natural killer (NK) cells.
Any process by which a virus avoids the effects mediated by the host organism's natural killer (NK) cells.
Any process by which a virus avoids the effects mediated by the host organism's natural killer (NK) cells.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of natural killer cell activation in the host.
Any process by which a virus avoids the effects mediated by the host organism's dendritic cells.
Any process by which a virus avoids the effects mediated by the host organism's dendritic cells.
Any process by which a virus avoids the effects mediated by the host organism's dendritic cells.
The directed movement of the viral genome or a viral particle out of the host cell nucleus.
The directed movement of the viral genome or a viral particle out of the host cell nucleus through the nuclear pore.
The directed movement of the viral genome or a viral particle out of the host cell nucleus through the nuclear pore.
The directed movement of the viral genome or a viral particle out of the host cell nucleus through the nuclear pore.
The directed movement of the viral genome or a viral particle out of the host cell nucleus that involves disruption of the nuclear membrane envelope by the virus.
Ejection by a non-enveloped prokaryotic virus of its genome into the host cytoplasm. Caudovirales carry an ejection apparatus that can be long and contractile, long and noncontractile, or short, and is able to penetrate the host cell envelope to deliver the viral genome into the host cell cytoplasm.
Ejection by a non-enveloped prokaryotic virus of its genome into the host cytoplasm. Caudovirales carry an ejection apparatus that can be long and contractile, long and noncontractile, or short, and is able to penetrate the host cell envelope to deliver the viral genome into the host cell cytoplasm.
A crystalline protein matrix surrounding the nucleocapsids of some insect viruses after their release in the environment. Produced in the host cell, the occlusion body protects the infectious virion after death of the host.
The directed movement of a virus, or part of a virus, towards the host cell nucleus using actin filaments.
The directed movement of a virus, or part of a virus, towards the host cell nucleus using actin filaments.
A process of unidirectional viral DNA replication that takes place on a circular DNA to rapidly produce numerous copies of the viral genome. Involves creating a nick in one strand of the circular DNA molecule at the origin of replication. DNA is then synthesized by DNA polymerase. Using the non-nicked strand as a template, replication proceeds around the circular DNA molecule, displacing the nicked strand as single-stranded DNA.
A rolling circle viral DNA replication that begins with a double-stranded viral DNA genome.
A rolling circle viral DNA replication that begins with a single-stranded viral DNA genome.
A viral DNA replication process where a 3' hairpin structure in the viral single-stranded DNA (ssDNA) template serves as a primer for host enzymes to synthesize DNA.
A viral DNA replication process where replication occurs in both directions from the starting point. This creates two replication forks, moving in opposite directions.
A viral DNA replication process where only one strand is replicated at once, and which releases a single stranded DNA (ssDNA).
A DNA replication process that uses viral RNA as a template for RNA-dependent DNA polymerases (e.g. reverse transcriptase) that synthesize the new strands.
A DNA replication process that uses viral RNA as a template for RNA-dependent DNA polymerases (e.g. reverse transcriptase) that synthesize the new strands.
A DNA replication process that uses viral RNA as a template for RNA-dependent DNA polymerases (e.g. reverse transcriptase) that synthesize the new strands.
A viral genome replication process where the template genome is negative stranded, single stranded RNA ((-)ssRNA).
A viral genome replication process where the template genome is positive stranded, single stranded RNA ((+)ssRNA). Replication of the positive strand leads to dsRNA formation, which in turn is transcribed into positive single stranded RNA.
A viral genome replication process where the template genome is double stranded RNA (dsRNA). Genomic dsRNA is first transcribed into single-stranded (ss) mRNA, which is then replicated to ds-genomic RNA.
A viral genome replication where the template is single-stranded RNA (ssRNA), and which proceeds via a double stranded DNA (dsDNA) intermediate molecule. Viral genomic RNA is first reverse transcribed into dsDNA, which integrates into the host chromosomal DNA, where it is transcribed by host RNA polymerase II.
A viral genome replication where the template is single-stranded RNA (ssRNA), and which proceeds via a double stranded DNA (dsDNA) intermediate molecule. Viral genomic RNA is first reverse transcribed into dsDNA, which integrates into the host chromosomal DNA, where it is transcribed by host RNA polymerase II.
A viral genome replication where the template is single-stranded RNA (ssRNA), and which proceeds via a double stranded DNA (dsDNA) intermediate molecule. Viral genomic RNA is first reverse transcribed into dsDNA, which integrates into the host chromosomal DNA, where it is transcribed by host RNA polymerase II.
The replication of a viral DNA genome.
The replication of a viral DNA genome.
The replication of a viral DNA genome.
The replication of a viral DNA genome.
The replication of a viral RNA genome.
A transcription process that uses a viral DNA as a template.
A transcription process that uses viral RNA as a template.
A viral transcription process that uses negative stranded (-) single stranded (ss) RNA as a template.
Polyadenylation of viral mRNA through a polymerase stuttering mechanism. The stop signal present at the end of each gene comprises a stretch of uridine on which the viral polymerase acquires a stuttering behavior: after each adenine inserted, the polymerase moves back one nucleotide along with the mRNA. It resumes transcription adding a new adenine, then again moves back, thereby producing a polyA tail.
Methylation of the 2'-O-ribose of the first or second transcribed nucleotide of a viral mRNA. Methylation allows evasion of the host innate immune response, which degrades cap0 (non-methylated) mRNAs.
Fusion of a viral primary envelope with the host outer nuclear membrane during nuclear egress. The transitory primary envelope is acquired by the virus as it buds at the inner nuclear membrane and gains access to the perinuclear space. This membrane is lost by fusing with the host outer nuclear membrane during nuclear exit.
Fusion of a viral primary envelope with the host outer nuclear membrane during nuclear egress. The transitory primary envelope is acquired by the virus as it buds at the inner nuclear membrane and gains access to the perinuclear space. This membrane is lost by fusing with the host outer nuclear membrane during nuclear exit.
The directed movement of the viral genome or a viral particle towards the cell periphery using host microtubules. Mostly used by viruses that replicate their genome near or in the nucleus to allows newly assembled viral progeny to reach the plasma membrane.
Viral budding which uses a host ESCRT protein complex, or complexes, to mediate the budding process.
Viral budding which uses a host ESCRT protein complex, or complexes, to mediate the budding process.
The cellular metabolic process in which a cell duplicates one or more molecules of RNA.
A viral translation initiation mechanism where ribosomes are loaded onto viral mRNA at the 5'-cap structure and start scanning for a short distance before by-passing the large internal leader region and initiating at a downstream start site.
The continuation of translation of a viral mRNA beyond a stop codon by the use of a special tRNA that recognizes the UAG and UGA codons as modified amino acids, rather than as termination codons.
The continuation of translation of a viral mRNA beyond a stop codon by the use of a special tRNA that recognizes the UAG and UGA codons as modified amino acids, rather than as termination codons.
Interacting selectively and non-covalently with a coreceptor. A coreceptor acts in cooperation with a primary receptor to transmit a signal within the cell.
The aggregation, arrangement and bonding together of a set of components by a virus to form a pore complex in a membrane of a host organism.
The aggregation, arrangement and bonding together of a set of components by a virus to form a pore complex in a membrane of a host organism.
The assembly of a virus capsid that occurs in the nucleus. The assembly of large icosahedral shells for herpesviridae and adenoviridae requires structural proteins that act as chaperones for assembly.
The assembly of a virus capsid that occurs in the cytoplasm.
The assembly of an icosahedral viral capsid in the cytoplasm. Often occurs by assembling around the viral genome.
The assembly of a helical viral capsid in the cytoplasm. Occurs by assembling around the viral genome.
Any viral process that activates or increases the frequency, rate or extent of host catalytic activity.
An intracellular compartment in a host cell which increases the efficiency of viral replication and/or assembly, and shields the virus from host defenses. Viral factories can be either cytoplasmic or nuclear and often arise from extensive rearrangement of host cell cytoskeletal and/or cell membrane compartments.
A viral factory located in the cytoplasm of a host cell.
A viral factory located in the nucleus of a host cell.
A cytoplasmic viral factory that is electron dense due to high levels of viral RNA. Produced by nucleo-cytoplasmic large DNA viruses (NCLDV) like Poxviridae, Asfarviridae and Iridoviridae, and dsRNA viruses like Reoviridae.
A cytoplasmic viral factory which is a 50-400nm diameter membrane invagination. Spherules can appear on several enveloped cellular components depending on the virus.
A cytoplasmic viral factory that consists of a double-membrane bound vesicle. Has a diameter of 200-300nm and is derived from the endoplasmic reticulum or Golgi apparatus. Produced by Picornaviridae, Nidovirales, Arteriviridae and Coronaviridae.
A cytoplasmic viral factory derived from the Golgi in which Bunyaviridae replication takes place. Tubes are membranous structures close to the assembly and budding sites, and their function may be to connect viral replication and morphogenesis inside viral factories.
A nuclear viral factory formed by Baculoviruses. A vesicular structure in which virions are assembled.
A nuclear viral factory formed at the periphery of the host cell nucleus by Baculoviruses.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of toll-like receptor (TLR) signaling in the host organism.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of toll-like receptor (TLR) signaling in the host organism.
Any process in which a virus stops, prevents, or reduces the activity of the host serine/threonine kinase TBK1.
Any process in which a virus stops, prevents, or reduces the activity of the host I-kappa-B kinase epsilon (IKBKE/IKK-epsilon/IKK-E).
The cell cycle process in which the directed movement of the mitotic spindle to a specific location in the cell occurs.
The cell cycle process in which the directed movement of the mitotic spindle to a specific location in the cell occurs.
The cell cycle process in which the directed movement of the mitotic spindle to a specific location in the cell occurs.
The cell cycle process in which the directed movement of the mitotic spindle to a specific location in the cell occurs.
The cell cycle process in which the directed movement of the mitotic spindle to a specific location in the cell occurs.
The cell cycle process in which the directed movement of the mitotic spindle to a specific location in the cell occurs.
The cell cycle process in which the directed movement of the mitotic spindle to a specific location in the cell occurs.
The cell cycle process in which the directed movement of the mitotic spindle to a specific location in the cell occurs.
The cell cycle process in which the directed movement of the mitotic spindle to a specific location in the cell occurs.
The cell cycle process in which the directed movement of the mitotic spindle to a specific location in the cell occurs.
The cell cycle process in which the directed movement of the mitotic spindle to a specific location in the cell occurs.
Attaching of a collagen and cuticulin-based cuticle to the epithelium underlying it. An example of this process is found in Caenorhabditis elegans.
Attaching of a chitin-containing cuticle to the epithelium underlying it. An example of this process is found in Drosophila melanogaster.
Any process that modulates the frequency, rate or extent of the growth of all or part of an organism so that it occurs at its proper speed, either globally or in a specific part of the organism's development.
Any process that modulates the rate of growth of all or part of an organism.
Any process that increases the rate of growth of all or part of an organism.
Any process that increases the rate of growth of all or part of an organism.
Any process that increases the rate of growth of all or part of an organism.
Any process that increases the rate of growth of all or part of an organism.
Any process that increases the rate of growth of all or part of an organism.
Self-propelled movement of a cell or organism from one location to another.
Any process that modulates the frequency, rate or extent of locomotion of a cell or organism.
Any process that stops, prevents, or reduces the frequency, rate or extent of locomotion of a cell or organism.
Any process that stops, prevents, or reduces the frequency, rate or extent of locomotion of a cell or organism.
Any process that stops, prevents, or reduces the frequency, rate or extent of locomotion of a cell or organism.
Any process that stops, prevents, or reduces the frequency, rate or extent of locomotion of a cell or organism.
Any process that modulates the frequency, rate or extent of growth of the body of an organism so that it reaches its usual body size.
Any process that modulates the frequency, rate or extent of growth of the body of an organism so that it reaches its usual body size.
Any process that stops, prevents, or reduces the frequency, rate or extent of growth of an organism to reach its usual body size.
Any process that stops, prevents, or reduces the frequency, rate or extent of growth of an organism to reach its usual body size.
The first few specialized divisions of an activated animal egg.
Any process that activates or increases the frequency, rate or extent of locomotion of a cell or organism.
Any process that activates or increases the frequency, rate or extent of locomotion of a cell or organism.
Any process that activates or increases the frequency, rate or extent of locomotion of a cell or organism.
Any process that activates or increases the frequency, rate or extent of locomotion of a cell or organism.
Any process that activates or increases the frequency, rate or extent of locomotion of a cell or organism.
Any process that activates or increases the frequency, rate or extent of growth of an organism to reach its usual body size.
Any process that activates or increases the frequency, rate or extent of growth of an organism to reach its usual body size.
Any process that activates or increases the frequency, rate or extent of embryonic development.
Any process that activates or increases the frequency, rate or extent of embryonic development.
Any process that activates or increases the frequency, rate or extent of embryonic development.
Any process that activates or increases the frequency, rate or extent of embryonic development.
Any process that activates or increases the frequency, rate or extent of embryonic development.
Any process that modulates the frequency, rate or extent of meiotic nuclear division, the process in which the nucleus of a diploid cell divides twice forming four haploid cells, one or more of which usually function as gametes.
The determination of sex and sexual phenotype in the germ line of a hermaphrodite.
The determination of female sex and sexual phenotype in the germ-line of the hermaphrodite.
The process whose specific outcome is the progression of the dauer larva over time, through the facultative diapause of the dauer (enduring) larval stage, with specialized traits adapted for dispersal and long-term survival, with elevated stress resistance and without feeding.
The process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult.
Any process that activates or increases the frequency, rate or extent of development of the vulva. Vulval development is the process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult.
Any process that activates or increases the frequency, rate or extent of development of the vulva. Vulval development is the process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult.
Any process that activates or increases the frequency, rate or extent of development of the vulva. Vulval development is the process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult.
Any process that activates or increases the frequency, rate or extent of development of the vulva. Vulval development is the process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult.
Any process that activates or increases the frequency, rate or extent of development of the vulva. Vulval development is the process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult.
Any process that stops, prevents, or reduces the frequency, rate or extent of development of the vulva. Vulval development is the process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult.
Any process that stops, prevents, or reduces the frequency, rate or extent of development of the vulva. Vulval development is the process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult.
Any process that stops, prevents, or reduces the frequency, rate or extent of development of the vulva. Vulval development is the process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult.
Any process that stops, prevents, or reduces the frequency, rate or extent of development of the vulva. Vulval development is the process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult.
Any process that modulates the frequency, rate or extent of development of the vulva. Vulval development is the process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult.
Any process that modulates the frequency, rate or extent of gene expression; the process is mitotically or meiotically heritable, or is stably self-propagated in the cytoplasm of a resting cell, and does not entail a change in DNA sequence.
Any heritable epigenetic process that modulates the frequency, rate or extent of protein function by self-perpetuating conformational conversions of normal proteins in healthy cells. This is distinct from, though mechanistically analogous to, disease states associated with prion propagation and amyloidogenesis. A single protein, if it carries a glutamine/asparagine-rich ('prion') domain, can sometimes stably exist in at least two distinct physical states, each associated with a different phenotype; propagation of one of these traits is achieved by a self-perpetuating change in the protein from one form to the other, mediated by conformational changes in the glutamine/asparagine-rich domain. Prion domains are both modular and transferable to other proteins, on which they can confer a heritable epigenetic alteration of function; existing bioinformatics data indicate that they are rare in non-eukarya, but common in eukarya.
The covalent alteration of one or more nucleotides within snRNA, resulting in a change in the properties of the snRNA.
The process in which the anatomical structures of the post-embryonic soma are generated and organized.
Any process, mediated by small non-coding RNAs, that stops, prevents or reduces the rate that mRNAs are effectively translated into protein.
Any process, mediated by small non-coding RNAs, that stops, prevents or reduces the rate that mRNAs are effectively translated into protein.
Any process, mediated by small non-coding RNAs, that stops, prevents or reduces the rate that mRNAs are effectively translated into protein.
Any process, mediated by small non-coding RNAs, that stops, prevents or reduces the rate that mRNAs are effectively translated into protein.
Any process that modulates the consistent predetermined time point at which an integrated living unit or organism progresses from an initial condition to a later condition and the rate at which this time point is reached.
Any process that modulates the consistent predetermined time point at which an integrated living unit or organism progresses from an initial condition to a later condition and the rate at which this time point is reached.
Any process that modulates the consistent predetermined time point at which an integrated living unit or organism progresses from an initial condition to a later condition and the rate at which this time point is reached.
The process whose specific outcome is the progression of the hermaphrodite genitalia over time, from formation to the mature structures.
Any process that modulates the frequency, rate or extent of fibroblast growth factor receptor signaling pathway activity.
Any process that modulates the frequency, rate or extent of fibroblast growth factor receptor signaling pathway activity.
Any process that modulates the frequency, rate or extent of fibroblast growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of fibroblast growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of fibroblast growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of fibroblast growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of fibroblast growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of fibroblast growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of fibroblast growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of fibroblast growth factor receptor signaling pathway activity.
The cell cycle process in which two small cells are generated, as byproducts destined to degenerate, as a result of the first and second meiotic divisions of a primary oocyte during its development to a mature ovum. One polar body is formed in the first division of meiosis and the other in the second division; at each division, the cytoplasm divides unequally, so that the polar body is of much smaller size than the developing oocyte. At the second division in which a polar body is formed, the polar body and the developing oocyte each contain a haploid set of chromosomes.
Migration of a cell in a multicellular organism that, having changed its location, is required to induce normal properties in one or more cells at its new location. An example of this would be the distal tip cells of Caenorhabditis elegans.
Behavior that is dependent upon the sensation of temperature.
Behavior that is dependent upon the sensation of temperature.
Behavior that is dependent upon the sensation of temperature.
The directed movement of peptides or proteins produced by an organism to a location inside its host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The determination of sex and sexual phenotypes in a hermaphroditic organism's soma. An example of this is found in Caenorhabditis elegans.
Promotion of male sex and sexual phenotypes in the hermaphroditic nematode soma. An example of this is found in Caenorhabditis elegans.
Promotion of female sex and sexual phenotypes in the hermaphroditic soma. An example of this is found in Caenorhabditis elegans.
The determination of male sex and sexual phenotype in the germ-line of the hermaphrodite. An example of this is found in Caenorhabditis elegans.
Interacting selectively and non-covalently with interleukin-18.
Combining with interleukin-18 and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with interleukin-18 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 interleukin-15.
Combining with interleukin-15 and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with interleukin-15 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 interleukin-16.
Combining with interleukin-16 and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with interleukin-16 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 interleukin-19.
Combining with interleukin-19 and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with interleukin-19 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 interleukin-20.
Combining with interleukin-20 and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with interleukin-20 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 interleukin-22.
Combining with interleukin-22 and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with interleukin-22 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 interleukin-23.
Combining with interleukin-23 and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with interleukin-23 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 the granulocyte macrophage colony-stimulating factor complex.
Interacting selectively and non-covalently with the granulocyte macrophage colony-stimulating factor complex.
Interacting selectively and non-covalently with the granulocyte macrophage colony-stimulating factor complex.
A protein complex that binds interleukin-12 and that consists of, at a minimum, a dimeric interleukin and its two receptor subunits as well as optional additional kinase subunits.
A protein complex that binds interleukin-12 and that consists of, at a minimum, a dimeric interleukin and its two receptor subunits as well as optional additional kinase subunits.
Regulated re-replication of DNA within a single cell cycle, resulting in an increased cell ploidy. An example of this process occurs in the synthesis of Drosophila salivary gland cell polytene chromosomes.
Regulated re-replication of DNA within a single cell cycle, resulting in an increased cell ploidy. An example of this process occurs in the synthesis of Drosophila salivary gland cell polytene chromosomes.
A membrane-bounded organelle as it is found in the host cell in which chromosomes are housed and replicated. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Stops, prevents or reduces the activity of any enzyme that catalyzes the hydrolysis of ATP to ADP and orthophosphate.
Stops, prevents or reduces the activity of a peptidyl-dipeptidase. Peptidyl-dipeptidase activity catalyzes the release of C-terminal dipeptides from a polypeptide chain.
The chemical reactions and pathways resulting in the formation of chemokines, any member of a family of small chemotactic cytokines; their name is derived from their ability to induce directed chemotaxis in nearby responsive cells. All chemokines possess a number of conserved cysteine residues involved in intramolecular disulfide bond formation. Some chemokines are considered pro-inflammatory and can be induced during an immune response to recruit cells of the immune system to a site of infection, while others are considered homeostatic and are involved in controlling the migration of cells during normal processes of tissue maintenance or development. Chemokines are found in all vertebrates, some viruses and some bacteria.
The chemical reactions and pathways resulting in the formation of chemokines, any member of a family of small chemotactic cytokines; their name is derived from their ability to induce directed chemotaxis in nearby responsive cells. All chemokines possess a number of conserved cysteine residues involved in intramolecular disulfide bond formation. Some chemokines are considered pro-inflammatory and can be induced during an immune response to recruit cells of the immune system to a site of infection, while others are considered homeostatic and are involved in controlling the migration of cells during normal processes of tissue maintenance or development. Chemokines are found in all vertebrates, some viruses and some bacteria.
The chemical reactions and pathways resulting in the formation of chemokines, any member of a family of small chemotactic cytokines; their name is derived from their ability to induce directed chemotaxis in nearby responsive cells. All chemokines possess a number of conserved cysteine residues involved in intramolecular disulfide bond formation. Some chemokines are considered pro-inflammatory and can be induced during an immune response to recruit cells of the immune system to a site of infection, while others are considered homeostatic and are involved in controlling the migration of cells during normal processes of tissue maintenance or development. Chemokines are found in all vertebrates, some viruses and some bacteria.
The chemical reactions and pathways resulting in the formation of chemokines, any member of a family of small chemotactic cytokines; their name is derived from their ability to induce directed chemotaxis in nearby responsive cells. All chemokines possess a number of conserved cysteine residues involved in intramolecular disulfide bond formation. Some chemokines are considered pro-inflammatory and can be induced during an immune response to recruit cells of the immune system to a site of infection, while others are considered homeostatic and are involved in controlling the migration of cells during normal processes of tissue maintenance or development. Chemokines are found in all vertebrates, some viruses and some bacteria.
The modification of a C-terminal peptidyl-lysine to form peptidyl-L-lysine methyl ester.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
The methylation of peptidyl-L-histidine to form peptidyl-L-3'-methyl-L-histidine (otherwise known as pi-methylhistidine, pros-methylhistidine).
The methylation of peptidyl-L-histidine to form peptidyl-L-3'-methyl-L-histidine (otherwise known as pi-methylhistidine, pros-methylhistidine).
The methylation of peptidyl-L-histidine to form peptidyl-L-1'-methyl-L-histidine (otherwise known as tau-methylhistidine, tele-methylhistidine).
The methylation of peptidyl-L-histidine to form peptidyl-L-1'-methyl-L-histidine (otherwise known as tau-methylhistidine, tele-methylhistidine).
The incorporation of vanadium a metallo-sulfur cluster such as VFe(7-8)S(n).
The incorporation of a metal into a metallo-molybdopterin complex.
The incorporation of tungsten into a tungsten-molybdopterin complex.
The directed movement of substances that are in liquid form in normal living conditions 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 fluid across epithelia.
The chemical reactions and pathways involving 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 involving 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 involving 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 formation 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 formation 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 formation 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 formation 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 formation 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 formation 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 behavior of an organism in response to an odor.
The behavior of an organism in response to an odor.
The behavior of an organism in response to an odor.
The behavior of an organism in response to an odor.
The behavior of an organism in response to an odor.
The behavior of an organism in response to an odor.
Any process involved in the maintenance of an internal steady state of acyl-CoA within a cell or between a cell and its external environment.
The assembly and arrangement of a rhabdomere within a cell. The rhabdomere is the organelle on the apical surface of a photoreceptor cell that contains the visual pigments.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving dopamine.
Catalysis of the reaction: S-adenosyl-L-methionine + histone = S-adenosyl-L-homocysteine + methyl-histone. Histone methylation generally occurs on either an arginine or lysine residue.
Providing the environmental signal that initiates the directed movement of a motile cell or organism towards a higher concentration of that signal.
Any process that modulates the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
Any process that modulates the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
Any process that modulates the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
The series of events that restore integrity to a damaged tissue, following an injury.
Any process that results in an increase in the efficacy of transmission at a neuromuscular synapse.
The process that results in the generation of glial cells. This includes the production of glial progenitors and their differentiation into mature glia.
Growth of glial cells, non-neuronal cells that provide support and nutrition, maintain homeostasis, form myelin, and participate in signal transmission in the nervous system.
Glial cell growth that occurs in the perineurium, a cell layer that ensheaths projections of peripheral nerves, such as motor axons.
The specification of polarized ommatidia. Ommatidia occur in two chiral forms. The trapezoidal arrangement of photoreceptors in the dorsal part of the eye is the mirror image of that in the ventral part.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving pteridine.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving catecholamines.
Maintenance of the oocyte nucleus in a particular position within the cell during the establishment and maintenance of the axes of the oocyte. An example of this process is found In Drosophila melanogaster.
Maintenance of the oocyte nucleus in a particular position within the cell during the establishment and maintenance of the axes of the oocyte. An example of this process is found In Drosophila melanogaster.
Maintenance of the oocyte nucleus in a particular position within the cell during the establishment and maintenance of the axes of the oocyte. An example of this process is found In Drosophila melanogaster.
Maintenance of the oocyte nucleus in a particular position within the cell during the establishment and maintenance of the axes of the oocyte. An example of this process is found In Drosophila melanogaster.
Maintenance of the oocyte nucleus in a particular position within the cell during the establishment and maintenance of the axes of the oocyte. An example of this process is found In Drosophila melanogaster.
Maintenance of the oocyte nucleus in a particular position within the cell during the establishment and maintenance of the axes of the oocyte. An example of this process is found In Drosophila melanogaster.
Maintenance of the oocyte nucleus in a particular position within the cell during the establishment and maintenance of the axes of the oocyte. An example of this process is found In Drosophila melanogaster.
Maintenance of the oocyte nucleus in a particular position within the cell during the establishment and maintenance of the axes of the oocyte. An example of this process is found In Drosophila melanogaster.
Maintenance of the oocyte nucleus in a particular position within the cell during the establishment and maintenance of the axes of the oocyte. An example of this process is found In Drosophila melanogaster.
Maintenance of the oocyte nucleus in a particular position within the cell during the establishment and maintenance of the axes of the oocyte. An example of this process is found In Drosophila melanogaster.
Combining with a leucokinin, any of several octapeptide hormones found in insects, and transmitting the signal to initiate a change in cell activity.
The bidirectional movement of large protein complexes along microtubules within a cilium, mediated by motor proteins.
The bidirectional movement of large protein complexes along microtubules within a cilium, mediated by motor proteins.
The bidirectional movement of large protein complexes along microtubules within a cilium, mediated by motor proteins.
The bidirectional movement of large protein complexes along microtubules within a cilium, mediated by motor proteins.
The bidirectional movement of large protein complexes along microtubules within a cilium, mediated by motor proteins.
The migration of individual cells within the blastocyst to help establish the multi-layered body plan of the organism (gastrulation). For example, the migration of cells from the surface to the interior of the embryo (ingression).
The incorporation of nickel into a nickel-iron-sulfur cluster via pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide, found in carbon monoxide dehydrogenase.
The glycosylation of peptidyl-amino acids through a phosphoester bond forming, for example, GlcNAc-alpha-1-P-Ser residues.
The glycosylation of peptidyl-amino acids through a phosphoester bond forming, for example, GlcNAc-alpha-1-P-Ser residues.
The glycosylation of peptidyl-serine through a phosphoester bond forming, for example, GlcNAc-alpha-1-P-Ser residues.
The self-renewing division of a germline stem cell to produce a daughter stem cell and a daughter germ cell, which will divide to form the gametes.
The self-renewing division of a germline stem cell to produce a daughter stem cell and a daughter germ cell, which will divide to form the gametes.
The chemical reactions and pathways involving glycosylsphingolipidinositol (GSI) anchors, which attach membrane proteins to the lipid bilayer of the cell membrane.
The chemical reactions and pathways involving glycosylsphingolipidinositol (GSI) anchors, which attach membrane proteins to the lipid bilayer of the cell membrane.
The chemical reactions and pathways involving glycosylsphingolipidinositol (GSI) anchors, which attach membrane proteins to the lipid bilayer of the cell membrane.
The chemical reactions and pathways resulting in the formation of a glycosylsphingolipidinositol (GSI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The sphingolipid group is linked, via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via a ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GSI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylsphingolipidinositol (GSI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The sphingolipid group is linked, via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via a ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GSI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylsphingolipidinositol (GSI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The sphingolipid group is linked, via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via a ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GSI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylsphingolipidinositol (GSI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The sphingolipid group is linked, via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via a ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GSI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylsphingolipidinositol (GSI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The sphingolipid group is linked, via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via a ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GSI anchors have variants on this canonical linkage.
The chemical reactions and pathways resulting in the formation of a glycosylsphingolipidinositol (GSI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The sphingolipid group is linked, via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via a ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GSI anchors have variants on this canonical linkage.
Catalysis of the transfer of a methyl group to an acceptor molecule; dependent on the presence of 5,10-methylenetetrahydrofolate.
Catalysis of the transfer of a methyl group to an acceptor molecule; dependent on the presence of 5-methyltetrahydrofolate.
Catalysis of the transfer of a methyl group to an acceptor molecule; dependent on the presence of 5-methyltetrahydropteroyltri-L-glutamate.
Catalysis of the transfer of a methyl group to an acceptor molecule, dependent on the presence of 5-methyl-5,6,7,8-tetrahydromethanopterin.
An immune response which is associated with resistance to intracellular bacteria, fungi, and protozoa, and pathological conditions such as arthritis, and which is typically orchestrated by the production of particular cytokines by T-helper 1 cells, most notably interferon-gamma, IL-2, and lymphotoxin.
The chemical reactions and pathways resulting in the formation of cytokines, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity.
The chemical reactions and pathways resulting in the formation of cytokines, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity.
The chemical reactions and pathways resulting in the formation of cytokines, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity.
The chemical reactions and pathways resulting in the formation of cytokines, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity.
The chemical reactions and pathways resulting in the formation of cytokines, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity.
The chemical reactions and pathways resulting in the formation of cytokines, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity.
The chemical reactions and pathways resulting in the formation of interleukin-12.
The chemical reactions and pathways resulting in the formation of interleukin-12.
The chemical reactions and pathways resulting in the formation of interleukin-12.
The chemical reactions and pathways resulting in the formation of interleukin-12.
The chemical reactions and pathways resulting in the formation of interleukin-12.
The chemical reactions and pathways resulting in the formation of interleukin-12.
The chemical reactions and pathways resulting in the formation of interleukin-10.
The chemical reactions and pathways resulting in the formation of interleukin-10.
The chemical reactions and pathways resulting in the formation of interleukin-10.
The chemical reactions and pathways resulting in the formation of interleukin-10.
The chemical reactions and pathways resulting in the formation of interleukin-10.
The chemical reactions and pathways resulting in the formation of interleukin-10.
An immune response which is associated with resistance to extracellular organisms such as helminths and pathological conditions such as allergy, which is orchestrated by the production of particular cytokines, most notably IL-4, IL-5, IL-10, and IL-13, by any of a variety of cell types including T-helper 2 cells, eosinophils, basophils, mast cells, and nuocytes, resulting in enhanced production of certain antibody isotypes and other effects.
An immune response which is associated with resistance to extracellular organisms such as helminths and pathological conditions such as allergy, which is orchestrated by the production of particular cytokines, most notably IL-4, IL-5, IL-10, and IL-13, by any of a variety of cell types including T-helper 2 cells, eosinophils, basophils, mast cells, and nuocytes, resulting in enhanced production of certain antibody isotypes and other effects.
The process in which a relatively unspecialized thymocyte acquires specialized features of a T-helper cell.
The process in which a relatively unspecialized thymocyte acquires specialized features of a T-helper cell.
The chemical reactions and pathways resulting in the formation of interleukin-2.
The chemical reactions and pathways resulting in the formation of interleukin-2.
The chemical reactions and pathways resulting in the formation of interleukin-2.
The chemical reactions and pathways resulting in the formation of interleukin-2.
The chemical reactions and pathways resulting in the formation of interleukin-2.
The chemical reactions and pathways resulting in the formation of interleukin-2.
The chemical reactions and pathways resulting in the formation of interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
The chemical reactions and pathways resulting in the formation of interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
The chemical reactions and pathways resulting in the formation of interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
The chemical reactions and pathways resulting in the formation of interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
The chemical reactions and pathways resulting in the formation of interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
The chemical reactions and pathways resulting in the formation of interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
The chemical reactions and pathways resulting in the formation of interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
The chemical reactions and pathways resulting in the formation of interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
The chemical reactions and pathways resulting in the formation of interleukin-4.
The chemical reactions and pathways resulting in the formation of interleukin-4.
The chemical reactions and pathways resulting in the formation of interleukin-4.
The chemical reactions and pathways resulting in the formation of interleukin-4.
The chemical reactions and pathways resulting in the formation of interleukin-4.
The chemical reactions and pathways resulting in the formation of interleukin-4.
The chemical reactions and pathways resulting in the formation of interleukin-4.
The expansion of a T cell population by cell division. Follows T cell activation.
The expansion of a T cell population by cell division. Follows T cell activation.
The expansion of a T cell population by cell division. Follows T cell activation.
The expansion of a T cell population by cell division. Follows T cell activation.
The expansion of a B cell population by cell division. Follows B cell activation.
The expansion of a B cell population by cell division. Follows B cell activation.
The expansion of a B cell population by cell division. Follows B cell activation.
The expansion of a B cell population by cell division. Follows B cell activation.
Any process that activates or increases the rate or extent of T cell proliferation.
Any process that activates or increases the rate or extent of T cell proliferation.
Any process that activates or increases the rate or extent of T cell proliferation.
Any process that activates or increases the rate or extent of T cell proliferation.
Any process that activates or increases the rate or extent of T cell proliferation.
Any process that activates or increases the rate or extent of T cell proliferation.
Any process that activates or increases the rate or extent of T cell proliferation.
Any process that activates or increases the rate or extent of resting T cell proliferation.
Any process that activates or increases the rate or extent of resting T cell proliferation.
Any process that activates or increases the rate or extent of resting T cell proliferation.
Any process that activates or increases the rate or extent of resting T cell proliferation.
Any process that activates or increases the rate or extent of resting T cell proliferation.
Any process that activates or increases the rate or extent of resting T cell proliferation.
Any process that activates or increases the rate or extent of resting T cell proliferation.
Any process that activates or increases the rate or extent of resting T cell proliferation.
Any process that activates or increases the rate or extent of resting T cell proliferation.
Any process that activates or increases the rate or extent of activated T cell proliferation.
Any process that activates or increases the rate or extent of activated T cell proliferation.
Any process that activates or increases the rate or extent of activated T cell proliferation.
Any process that activates or increases the rate or extent of activated T cell proliferation.
Any process that activates or increases the rate or extent of activated T cell proliferation.
Any process that activates or increases the rate or extent of activated T cell proliferation.
Any process that activates or increases the rate or extent of activated T cell proliferation.
Any process that activates or increases the rate or extent of activated T cell proliferation.
A T cell receptor complex in which the TCR heterodimer comprises alpha and beta chains, associated with the CD3 complex; recognizes a complex consisting of an antigen-derived peptide bound to a class I or class II MHC protein.
A T cell receptor complex in which the TCR heterodimer comprises alpha and beta chains, associated with the CD3 complex; recognizes a complex consisting of an antigen-derived peptide bound to a class I or class II MHC protein.
A T cell receptor complex in which the TCR heterodimer comprises alpha and beta chains, associated with the CD3 complex; recognizes a complex consisting of an antigen-derived peptide bound to a class I or class II MHC protein.
A T cell receptor complex in which the TCR heterodimer comprises alpha and beta chains, associated with the CD3 complex; recognizes a complex consisting of an antigen-derived peptide bound to a class I or class II MHC protein.
A T cell receptor complex in which the TCR heterodimer comprises gamma and delta chains, associated with the CD3 complex; recognizes antigen directly, without a requirement for processing and presentation by an MHC protein.
A T cell receptor complex in which the TCR heterodimer comprises gamma and delta chains, associated with the CD3 complex; recognizes antigen directly, without a requirement for processing and presentation by an MHC protein.
A T cell receptor complex in which the TCR heterodimer comprises gamma and delta chains, associated with the CD3 complex; recognizes antigen directly, without a requirement for processing and presentation by an MHC protein.
A T cell receptor complex in which the TCR heterodimer comprises gamma and delta chains, associated with the CD3 complex; recognizes antigen directly, without a requirement for processing and presentation by an MHC protein.
The chemical reactions and pathways involving cytokines, any of a group of proteins or glycoproteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
The change in morphology and behavior of a mature or immature T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
The change in morphology and behavior of a mature or immature B cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
The change in morphology and behavior of a mature or immature B cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
The change in morphology and behavior of a mature or immature B cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific.
A change in morphology and behavior of a macrophage resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor.
The change in morphology and behavior of a monocyte resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor.
The change in morphology and behavior of an endothelial cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor.
The change in morphology and behavior of a neutrophil resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor.
The chemical reactions and pathways involving alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways involving alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways involving alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways resulting in the formation of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways resulting in the formation of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways resulting in the formation of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways resulting in the formation of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways resulting in the formation of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways resulting in the formation of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways resulting in the breakdown of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways resulting in the breakdown of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways resulting in the breakdown of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways resulting in the breakdown of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
The chemical reactions and pathways resulting in the breakdown of alginic acid, a hydrophilic polysaccharide occurring in, for example, the cell walls of brown algae (brown seaweeds).
Catalysis of the splitting and linkage of glucan molecules, resulting in glucan chain elongation.
Catalysis of the splitting and linkage of (1->3)-beta-D-glucan molecules, resulting in (1->3)-beta-D-glucan chain elongation.
The addition of a galactose molecule to a protein amino acid.
The chemical reactions and pathways involving nitrates, inorganic or organic salts and esters of nitric acid.
Any process that modulates the frequency, rate or extent of cell proliferation.
The nitrogen metabolic process that encompasses the uptake of nitrate from the environment and reduction to ammonia, and results in the incorporation of nitrogen derived from nitrate into cellular substances.
Any process that modulates the frequency, rate or extent of T cell proliferation.
Any process that modulates the frequency, rate or extent of T cell proliferation.
Any process that modulates the frequency, rate or extent of T cell proliferation.
Any process that stops, prevents or reduces the rate or extent of T cell proliferation.
Any process that stops, prevents or reduces the rate or extent of T cell proliferation.
Any process that stops, prevents or reduces the rate or extent of T cell proliferation.
Any process that stops, prevents or reduces the rate or extent of T cell proliferation.
Any process that stops, prevents or reduces the rate or extent of T cell proliferation.
Any process that stops, prevents or reduces the rate or extent of T cell proliferation.
Any process that stops, prevents or reduces the rate or extent of T cell proliferation.
Catalysis of the reaction: thiamine phosphate + H2O = thiamine + phosphate.
Catalysis of the reaction: thiamine phosphate + H2O = thiamine + phosphate.
Catalysis of the reaction: thiamine phosphate + H2O = thiamine + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Catalysis of the reaction: D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
The chemical reactions and pathways involving neurotransmitters, any of a group of substances that are released on excitation from the axon terminal of a presynaptic neuron of the central or peripheral nervous system and travel across the synaptic cleft to either excite or inhibit the target cell.
Interacting selectively and non-covalently with an unprocessed ribosomal RNA transcript.
The chemical reactions and pathways resulting in the breakdown of any of a group of substances that are released on excitation from the axon terminal of a presynaptic neuron of the central or peripheral nervous system and travel across the synaptic cleft to either excite or inhibit the target cell.
The chemical reactions and pathways resulting in the breakdown of any of a group of substances that are released on excitation from the axon terminal of a presynaptic neuron of the central or peripheral nervous system and travel across the synaptic cleft to either excite or inhibit the target cell.
The chemical reactions and pathways resulting in the breakdown of any of a group of substances that are released on excitation from the axon terminal of a presynaptic neuron of the central or peripheral nervous system and travel across the synaptic cleft to either excite or inhibit the target cell.
The cell cycle process in which double-strand breaks are generated at defined hotspots throughout the genome during meiosis I. This results in the initiation of meiotic recombination.
During meiosis, the aggregation, arrangement and bonding together of strand exchange proteins (recombinases) to form small, electron dense structures in association with meiotic chromosomes during leptotene and zygotene.
During meiosis, the aggregation, arrangement and bonding together of strand exchange proteins (recombinases) to form small, electron dense structures in association with meiotic chromosomes during pachytene. Involved in the catalysis crossing over.
The formation of bonds from two or more atoms within the same ligand to a metal atom in complexes in which the metal is part of a ring.
The formation of bonds from two or more atoms within the same ligand to a metal atom in complexes in which the metal is part of a ring.
The fusion of two vacuole membranes to form a single vacuole.
The fusion of two vacuole membranes to form a single vacuole.
The fusion of two vacuole membranes to form a single vacuole.
The fusion of two vacuole membranes to form a single vacuole.
The fusion of two vacuole membranes to form a single vacuole.
The directed movement of membrane-bounded vesicles from endosomes back to the trans-Golgi network where they are recycled for further rounds of transport.
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. 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.
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. 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.
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. 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.
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. 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.
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. 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.
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 glucose.
A process of DNA recombination occurring within a plasmid or between plasmids and other plasmids or DNA molecules.
An organelle found in cnidoblast (nematoblast) cells. When matured, these stinging organelles store toxins and can deliver them when the cnidocil (a short extension of the cnidocyst) is stimulated by a prey or another stimulus.
The reverse transcription of an RNA molecule followed by recombination between the resultant cDNA and its homologous chromosomal allele.
The chemical reactions and pathways involving any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids.
The chemical reactions and pathways resulting in the formation of any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids.
The chemical reactions and pathways resulting in the formation of any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids.
The chemical reactions and pathways resulting in the formation of any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids.
The chemical reactions and pathways resulting in the formation of any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids.
The chemical reactions and pathways resulting in the breakdown of any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids.
The chemical reactions and pathways resulting in the breakdown of any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids.
The chemical reactions and pathways resulting in the breakdown of any conjugated, water-soluble protein in which the covalently attached nonprotein group consists of a lipid or lipids.
The chemical reactions and pathways resulting in the covalent alteration of one or more amino acid or lipid residues occurring in a lipoprotein, any conjugated, water-soluble protein in which the nonprotein group consists of a lipid or lipids.
The modification of a lipoprotein by oxidation of one or more amino acids or the lipid group.
Interacting selectively and non-covalently with the beta subunit of interleukin-12.
Interacting selectively and non-covalently with the beta subunit of interleukin-12.
Interacting selectively and non-covalently with the beta subunit of interleukin-12.
Interacting selectively and non-covalently with the beta subunit of interleukin-12.
Interacting selectively and non-covalently with the alpha subunit of interleukin-12.
Interacting selectively and non-covalently with the alpha subunit of interleukin-12.
Interacting selectively and non-covalently with the alpha subunit of interleukin-12.
Interacting selectively and non-covalently with the alpha subunit of interleukin-12.
Interacting selectively and non-covalently with a neurotransmitter, any chemical substance that is capable of transmitting (or inhibiting the transmission of) a nerve impulse from a neuron to another cell.
Interacting selectively and non-covalently with acetylcholine, an acetic acid ester of the organic base choline that functions as a neurotransmitter, released at the synapses of parasympathetic nerves and at neuromuscular junctions.
The chemical reactions and pathways resulting in the breakdown of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.
The chemical reactions and pathways resulting in the breakdown of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.
The chemical reactions and pathways resulting in the breakdown of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.
The chemical reactions and pathways resulting in the breakdown of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.
The chemical reactions and pathways resulting in the breakdown of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.
The chemical reactions and pathways involving heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.
The chemical reactions and pathways involving heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.
The chemical reactions and pathways involving heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.
Interacting selectively and non-covalently with a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class.
Either of the lipid bilayers that surround a plastid and form the plastid envelope.
Catalysis of the transfer of acyl groups from an acyl-CoA to lysophosphatidic acid to form phosphatidic acid.
Any process that modulates the frequency, rate or extent of spore formation.
Any process that stops, prevents, or reduces the frequency, rate or extent of sporulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of sporulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of sporulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of sporulation.
The continuous network of membranes encompassing the nuclear outer membrane and the endoplasmic reticulum membrane.
The continuous network of membranes encompassing the nuclear outer membrane and the endoplasmic reticulum membrane.
The continuous network of membranes encompassing the nuclear outer membrane and the endoplasmic reticulum membrane.
The continuous network of membranes encompassing the nuclear outer membrane and the endoplasmic reticulum membrane.
The continuous network of membranes encompassing the nuclear outer membrane and the endoplasmic reticulum membrane.
The continuous network of membranes encompassing the nuclear outer membrane and the endoplasmic reticulum membrane.
The continuous network of membranes encompassing the nuclear outer membrane and the endoplasmic reticulum membrane.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
The chemical reactions and pathways resulting in the breakdown of a xenobiotic compound, a compound foreign to living organisms. Used of chemical compounds, e.g. a xenobiotic chemical, such as a pesticide.
The chemical reactions and pathways resulting in the breakdown of a xenobiotic compound, a compound foreign to living organisms. Used of chemical compounds, e.g. a xenobiotic chemical, such as a pesticide.
The chemical reactions and pathways resulting in the breakdown of a xenobiotic compound, a compound foreign to living organisms. Used of chemical compounds, e.g. a xenobiotic chemical, such as a pesticide.
The chemical reactions and pathways resulting in the formation of nicotine, (S)(-)-3-(1-methyl-2-pyrrolidinyl)pyridine.
The chemical reactions and pathways resulting in the formation of nicotine, (S)(-)-3-(1-methyl-2-pyrrolidinyl)pyridine.
The chemical reactions and pathways resulting in the formation of nicotine, (S)(-)-3-(1-methyl-2-pyrrolidinyl)pyridine.
The chemical reactions and pathways resulting in the formation of nicotine, (S)(-)-3-(1-methyl-2-pyrrolidinyl)pyridine.
The chemical reactions and pathways involving any of a class of organic compounds that contain the carbonyl group, CO, and in which the carbonyl group is bonded only to carbon atoms, as carried out by individual cells. The general formula for a ketone is RCOR, where R and R are alkyl or aryl groups.
The chemical reactions and pathways resulting in the formation of ketones, a class of organic compounds that contain the carbonyl group, CO, and in which the carbonyl group is bonded only to carbon atoms. The general formula for a ketone is RCOR, where R and R are alkyl or aryl groups.
The chemical reactions and pathways resulting in the formation of ketones, a class of organic compounds that contain the carbonyl group, CO, and in which the carbonyl group is bonded only to carbon atoms. The general formula for a ketone is RCOR, where R and R are alkyl or aryl groups.
The chemical reactions and pathways resulting in the formation of ketones, a class of organic compounds that contain the carbonyl group, CO, and in which the carbonyl group is bonded only to carbon atoms. The general formula for a ketone is RCOR, where R and R are alkyl or aryl groups.
The chemical reactions and pathways resulting in the formation of ketones, a class of organic compounds that contain the carbonyl group, CO, and in which the carbonyl group is bonded only to carbon atoms. The general formula for a ketone is RCOR, where R and R are alkyl or aryl groups.
The chemical reactions and pathways resulting in the breakdown of ketones, a class of organic compounds that contain the carbonyl group, CO, and in which the carbonyl group is bonded only to carbon atoms. The general formula for a ketone is RCOR, where R and R are alkyl or aryl groups.
The chemical reactions and pathways resulting in the breakdown of ketones, a class of organic compounds that contain the carbonyl group, CO, and in which the carbonyl group is bonded only to carbon atoms. The general formula for a ketone is RCOR, where R and R are alkyl or aryl groups.
The chemical reactions and pathways resulting in the breakdown of ketones, a class of organic compounds that contain the carbonyl group, CO, and in which the carbonyl group is bonded only to carbon atoms. The general formula for a ketone is RCOR, where R and R are alkyl or aryl groups.
The chemical reactions and pathways resulting in the breakdown of formate, also known as methanoate, the anion HCOO- derived from methanoic (formic) acid.
The chemical reactions and pathways resulting in the breakdown of formate, also known as methanoate, the anion HCOO- derived from methanoic (formic) acid.
The chemical reactions and pathways resulting in the breakdown of formate, also known as methanoate, the anion HCOO- derived from methanoic (formic) acid.
The chemical reactions and pathways resulting in the breakdown of formate, also known as methanoate, the anion HCOO- derived from methanoic (formic) acid.
The chemical reactions and pathways resulting in the breakdown of formate, also known as methanoate, the anion HCOO- derived from methanoic (formic) acid.
The chemical reactions and pathways resulting in the breakdown of xylene, a mixture of three colorless, aromatic hydrocarbon liquids, ortho-, meta- and para-xylene.
The chemical reactions and pathways resulting in the breakdown of xylene, a mixture of three colorless, aromatic hydrocarbon liquids, ortho-, meta- and para-xylene.
The chemical reactions and pathways resulting in the breakdown of xylene, a mixture of three colorless, aromatic hydrocarbon liquids, ortho-, meta- and para-xylene.
The chemical reactions and pathways resulting in the breakdown of m-xylene, 1,3-dimethylbenzene, a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of m-xylene, 1,3-dimethylbenzene, a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of m-xylene, 1,3-dimethylbenzene, a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of m-xylene, 1,3-dimethylbenzene, a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of m-xylene, 1,3-dimethylbenzene, a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of o-xylene, (1,2-dimethylbenzene) a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of o-xylene, (1,2-dimethylbenzene) a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of o-xylene, (1,2-dimethylbenzene) a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of o-xylene, (1,2-dimethylbenzene) a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of o-xylene, (1,2-dimethylbenzene) a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of p-xylene (1,4-dimethylbenzene), a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of p-xylene (1,4-dimethylbenzene), a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of p-xylene (1,4-dimethylbenzene), a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of p-xylene (1,4-dimethylbenzene), a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of p-xylene (1,4-dimethylbenzene), a colorless, liquid aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of 1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane (DDT), a chlorinated broad spectrum contact insecticide.
The chemical reactions and pathways resulting in the breakdown of 1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane (DDT), a chlorinated broad spectrum contact insecticide.
The chemical reactions and pathways resulting in the breakdown of 1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane (DDT), a chlorinated broad spectrum contact insecticide.
The chemical reactions and pathways resulting in the breakdown of 1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane (DDT), a chlorinated broad spectrum contact insecticide.
The chemical reactions and pathways resulting in the breakdown of 1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane (DDT), a chlorinated broad spectrum contact insecticide.
The chemical reactions and pathways resulting in the formation of vanillin, an aromatic hydrocarbon which occurs naturally in black vanilla bean pods.
The chemical reactions and pathways resulting in the formation of vanillin, an aromatic hydrocarbon which occurs naturally in black vanilla bean pods.
The chemical reactions and pathways resulting in the formation of vanillin, an aromatic hydrocarbon which occurs naturally in black vanilla bean pods.
The chemical reactions and pathways resulting in the formation of vanillin, an aromatic hydrocarbon which occurs naturally in black vanilla bean pods.
The chemical reactions and pathways resulting in the formation of vanillin, an aromatic hydrocarbon which occurs naturally in black vanilla bean pods.
The chemical reactions and pathways resulting in the formation of vanillin, an aromatic hydrocarbon which occurs naturally in black vanilla bean pods.
The chemical reactions and pathways resulting in the breakdown of vanillin, an aromatic hydrocarbon which occurs naturally in black vanilla bean pods.
The chemical reactions and pathways resulting in the breakdown of vanillin, an aromatic hydrocarbon which occurs naturally in black vanilla bean pods.
The chemical reactions and pathways resulting in the breakdown of vanillin, an aromatic hydrocarbon which occurs naturally in black vanilla bean pods.
The chemical reactions and pathways resulting in the breakdown of vanillin, an aromatic hydrocarbon which occurs naturally in black vanilla bean pods.
The chemical reactions and pathways resulting in the breakdown of vanillin, an aromatic hydrocarbon which occurs naturally in black vanilla bean pods.
The chemical reactions and pathways involving methylmercury (MeHg+), a highly toxic organometal which can accumulate in tissues, particularly in fish species.
The chemical reactions and pathways resulting in the formation of methylmercury (MeHg+), a highly toxic organometal.
The chemical reactions and pathways resulting in the formation of methylmercury (MeHg+), a highly toxic organometal.
The chemical reactions and pathways resulting in the formation of methylmercury (MeHg+), a highly toxic organometal.
The chemical reactions and pathways resulting in the formation of methylmercury (MeHg+), a highly toxic organometal.
The chemical reactions and pathways resulting in the breakdown of methylmercury (MeHg+), a highly toxic organometal.
The chemical reactions and pathways resulting in the breakdown of methylmercury (MeHg+), a highly toxic organometal.
The chemical reactions and pathways resulting in the breakdown of methylmercury (MeHg+), a highly toxic organometal.
The chemical reactions and pathways resulting in the formation of quinate, the anion of quinic acid.
The chemical reactions and pathways resulting in the formation of quinate, the anion of quinic acid.
The chemical reactions and pathways resulting in the formation of quinate, the anion of quinic acid.
The chemical reactions and pathways resulting in the formation of quinate, the anion of quinic acid.
The chemical reactions and pathways resulting in the formation of quinate, the anion of quinic acid.
The chemical reactions and pathways resulting in the formation of quinate, the anion of quinic acid.
The chemical reactions and pathways resulting in the breakdown of gallate, the anion of gallic acid, in the presence of oxygen.
The chemical reactions and pathways resulting in the breakdown of gallate, the anion of gallic acid, in the presence of oxygen.
The chemical reactions and pathways resulting in the breakdown of gallate, the anion of gallic acid, in the presence of oxygen.
The chemical reactions and pathways resulting in the breakdown of gallate, the anion of gallic acid, in the presence of oxygen.
The chemical reactions and pathways resulting in the breakdown of gallate, the anion of gallic acid, in the presence of oxygen.
The chemical reactions and pathways involving chlorinated hydrocarbons, any hydrocarbon with one or more chlorine atoms attached to it.
The chemical reactions and pathways involving halogenated hydrocarbons, any hydrocarbon with one or more halogen atoms attached to it. Halogens include fluorine, chlorine, bromine and iodine.
The chemical reactions and pathways involving nylon, a polymer where the main polymer chain comprises recurring amide groups; these compounds are generally formed from combinations of diamines, diacids and amino acids.
The chemical reactions and pathways involving cyanuric acid, a suspected gastrointestinal or liver toxicant, and a potential degradation product of triazine herbicides, such as atrazine and simazine. It is widely used for the stabilization of available chlorine in swimming pool water and is also the starting compound for the synthesis of many organic derivatives.
The chemical reactions and pathways resulting in the breakdown of cyanuric acid, a potential degradation product of triazine herbicides.
The chemical reactions and pathways resulting in the breakdown of cyanuric acid, a potential degradation product of triazine herbicides.
The chemical reactions and pathways resulting in the breakdown of cyanuric acid, a potential degradation product of triazine herbicides.
The chemical reactions and pathways involving N-cyclopropylmelamine, a triazine compound commonly used as an insect growth regulator insecticide.
The chemical reactions and pathways involving N-cyclopropylmelamine, a triazine compound commonly used as an insect growth regulator insecticide.
The chemical reactions and pathways involving N-cyclopropylmelamine, a triazine compound commonly used as an insect growth regulator insecticide.
The chemical reactions and pathways resulting in the breakdown of N-cyclopropylmelamine, a triazine compound commonly used as an insecticide.
The chemical reactions and pathways resulting in the breakdown of N-cyclopropylmelamine, a triazine compound commonly used as an insecticide.
The chemical reactions and pathways resulting in the breakdown of N-cyclopropylmelamine, a triazine compound commonly used as an insecticide.
The chemical reactions and pathways resulting in the breakdown of N-cyclopropylmelamine, a triazine compound commonly used as an insecticide.
The chemical reactions and pathways resulting in the breakdown of N-cyclopropylmelamine, a triazine compound commonly used as an insecticide.
The chemical reactions and pathways resulting in the breakdown of toluene, a volatile monoaromatic hydrocarbon found in crude petroleum and petroleum products.
The chemical reactions and pathways resulting in the breakdown of toluene, a volatile monoaromatic hydrocarbon found in crude petroleum and petroleum products.
The chemical reactions and pathways resulting in the breakdown of toluene, a volatile monoaromatic hydrocarbon found in crude petroleum and petroleum products.
The chemical reactions and pathways resulting in the breakdown of any s-triazine compound. These compounds include many pesticides of widespread use in agriculture, and are characterized by a symmetrical hexameric ring consisting of alternating carbon and nitrogen atoms.
The chemical reactions and pathways resulting in the breakdown of any s-triazine compound. These compounds include many pesticides of widespread use in agriculture, and are characterized by a symmetrical hexameric ring consisting of alternating carbon and nitrogen atoms.
The chemical reactions and pathways resulting in the breakdown of any s-triazine compound. These compounds include many pesticides of widespread use in agriculture, and are characterized by a symmetrical hexameric ring consisting of alternating carbon and nitrogen atoms.
The chemical reactions and pathways resulting in the breakdown of chlorinated hydrocarbons, any hydrocarbon with one or more chlorine atoms attached to it.
The chemical reactions and pathways resulting in the breakdown of chlorinated hydrocarbons, any hydrocarbon with one or more chlorine atoms attached to it.
The chemical reactions and pathways resulting in the breakdown of chlorinated hydrocarbons, any hydrocarbon with one or more chlorine atoms attached to it.
The chemical reactions and pathways resulting in the breakdown of halogenated hydrocarbons, any hydrocarbon with one or more halogen atoms attached to it.
The chemical reactions and pathways resulting in the breakdown of halogenated hydrocarbons, any hydrocarbon with one or more halogen atoms attached to it.
The chemical reactions and pathways resulting in the breakdown of halogenated hydrocarbons, any hydrocarbon with one or more halogen atoms attached to it.
The chemical reactions and pathways resulting in the breakdown of styrene, an aromatic hydrocarbon liquid used in the manufacture of polystyrene.
The chemical reactions and pathways resulting in the breakdown of styrene, an aromatic hydrocarbon liquid used in the manufacture of polystyrene.
The chemical reactions and pathways resulting in the breakdown of styrene, an aromatic hydrocarbon liquid used in the manufacture of polystyrene.
The chemical reactions and pathways resulting in the breakdown of propylene, an alkene produced by catalytic or thermal cracking of hydrocarbons or as a by-product of petroleum refining.
The chemical reactions and pathways resulting in the breakdown of propylene, an alkene produced by catalytic or thermal cracking of hydrocarbons or as a by-product of petroleum refining.
The chemical reactions and pathways resulting in the breakdown of propylene, an alkene produced by catalytic or thermal cracking of hydrocarbons or as a by-product of petroleum refining.
The chemical reactions and pathways resulting in the breakdown of orcinol (5-methyl-1,3-benzenediol), an aromatic compound derived from the fermentation of lichen and synthesized by some higher plants.
The chemical reactions and pathways resulting in the breakdown of orcinol (5-methyl-1,3-benzenediol), an aromatic compound derived from the fermentation of lichen and synthesized by some higher plants.
The chemical reactions and pathways resulting in the breakdown of orcinol (5-methyl-1,3-benzenediol), an aromatic compound derived from the fermentation of lichen and synthesized by some higher plants.
The chemical reactions and pathways resulting in the breakdown of orcinol (5-methyl-1,3-benzenediol), an aromatic compound derived from the fermentation of lichen and synthesized by some higher plants.
The chemical reactions and pathways resulting in the breakdown of orcinol (5-methyl-1,3-benzenediol), an aromatic compound derived from the fermentation of lichen and synthesized by some higher plants.
The anaerobic chemical reactions and pathways resulting in the breakdown of octamethylcyclotetrasiloxane into dimethylsilanediol. The former is a tetramer of the latter.
The anaerobic chemical reactions and pathways resulting in the breakdown of octamethylcyclotetrasiloxane into dimethylsilanediol. The former is a tetramer of the latter.
The anaerobic chemical reactions and pathways resulting in the breakdown of octamethylcyclotetrasiloxane into dimethylsilanediol. The former is a tetramer of the latter.
The anaerobic chemical reactions and pathways resulting in the breakdown of octamethylcyclotetrasiloxane into dimethylsilanediol. The former is a tetramer of the latter.
The aerobic chemical reactions and pathways resulting in the breakdown of dimethylsilanediol, the smallest member of the dialkylsilanediols. Dimethylsilanediol is the monomer of polydimethylsiloxane, a compound which can be found in a wide range of industrial and consumer products.
The aerobic chemical reactions and pathways resulting in the breakdown of dimethylsilanediol, the smallest member of the dialkylsilanediols. Dimethylsilanediol is the monomer of polydimethylsiloxane, a compound which can be found in a wide range of industrial and consumer products.
The aerobic chemical reactions and pathways resulting in the breakdown of dimethylsilanediol, the smallest member of the dialkylsilanediols. Dimethylsilanediol is the monomer of polydimethylsiloxane, a compound which can be found in a wide range of industrial and consumer products.
The aerobic chemical reactions and pathways resulting in the breakdown of dimethylsilanediol, the smallest member of the dialkylsilanediols. Dimethylsilanediol is the monomer of polydimethylsiloxane, a compound which can be found in a wide range of industrial and consumer products.
The aerobic chemical reactions and pathways resulting in the breakdown of dimethylsilanediol, the smallest member of the dialkylsilanediols. Dimethylsilanediol is the monomer of polydimethylsiloxane, a compound which can be found in a wide range of industrial and consumer products.
The aerobic chemical reactions and pathways resulting in the breakdown of dimethylsilanediol, the smallest member of the dialkylsilanediols. Dimethylsilanediol is the monomer of polydimethylsiloxane, a compound which can be found in a wide range of industrial and consumer products.
The chemical reactions and pathways involving cresol, a mixture of the aromatic alcohol isoforms o-, p-, and m-cresol, which is obtained from coal tar or petroleum. The isomers are used as disinfectants, textile scouring agents, surfactants and as intermediates in the manufacture of salicylaldehyde, coumarin, and herbicides as well as being a major component of creosote.
The chemical reactions and pathways involving cresol, a mixture of the aromatic alcohol isoforms o-, p-, and m-cresol, which is obtained from coal tar or petroleum. The isomers are used as disinfectants, textile scouring agents, surfactants and as intermediates in the manufacture of salicylaldehyde, coumarin, and herbicides as well as being a major component of creosote.
The chemical reactions and pathways involving cresol, a mixture of the aromatic alcohol isoforms o-, p-, and m-cresol, which is obtained from coal tar or petroleum. The isomers are used as disinfectants, textile scouring agents, surfactants and as intermediates in the manufacture of salicylaldehyde, coumarin, and herbicides as well as being a major component of creosote.
The chemical reactions and pathways resulting in the breakdown of m-cresol (3-hydroxytoluene), the meta-isoform of cresol.
The chemical reactions and pathways resulting in the breakdown of m-cresol (3-hydroxytoluene), the meta-isoform of cresol.
The chemical reactions and pathways resulting in the breakdown of m-cresol (3-hydroxytoluene), the meta-isoform of cresol.
The chemical reactions and pathways resulting in the breakdown of m-cresol (3-hydroxytoluene), the meta-isoform of cresol.
The chemical reactions and pathways resulting in the breakdown of m-cresol (3-hydroxytoluene), the meta-isoform of cresol.
The chemical reactions and pathways resulting in the breakdown of m-cresol (3-hydroxytoluene), the meta-isoform of cresol.
The chemical reactions and pathways resulting in the breakdown of m-cresol (3-hydroxytoluene), the meta-isoform of cresol.
The chemical reactions and pathways involving terpenes, any of a large group of hydrocarbons that are made up of isoprene (C5H8) units which may be cyclic, acyclic or multicyclic, saturated or unsaturated, and may contain various functional groups.
The chemical reactions and pathways involving a phenol, any compound containing one or more hydroxyl groups directly attached to an aromatic carbon ring, in the absence of oxygen.
The chemical reactions and pathways resulting in the breakdown of phenanthrene, a tricyclic aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of phenanthrene, a tricyclic aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of phenanthrene, a tricyclic aromatic hydrocarbon.
The chemical reactions and pathways resulting in the breakdown of 1-aminocyclopropane-1-carboxylate, a natural product found in plant tissues. It is a key intermediate in the biosynthesis of ethylene (ethene), a fruit-ripening hormone in plants.
The chemical reactions and pathways resulting in the breakdown of 1-aminocyclopropane-1-carboxylate, a natural product found in plant tissues. It is a key intermediate in the biosynthesis of ethylene (ethene), a fruit-ripening hormone in plants.
The chemical reactions and pathways resulting in the breakdown of 1-aminocyclopropane-1-carboxylate, a natural product found in plant tissues. It is a key intermediate in the biosynthesis of ethylene (ethene), a fruit-ripening hormone in plants.
The chemical reactions and pathways resulting in the formation of 1-aminocyclopropane-1-carboxylate, a natural product found in plant tissues. It is a key intermediate in the biosynthesis of ethylene (ethene), a fruit-ripening hormone in plants.
The chemical reactions and pathways resulting in the formation of 1-aminocyclopropane-1-carboxylate, a natural product found in plant tissues. It is a key intermediate in the biosynthesis of ethylene (ethene), a fruit-ripening hormone in plants.
The chemical reactions and pathways resulting in the formation of 1-aminocyclopropane-1-carboxylate, a natural product found in plant tissues. It is a key intermediate in the biosynthesis of ethylene (ethene), a fruit-ripening hormone in plants.
The chemical reactions and pathways resulting in the formation of 1-aminocyclopropane-1-carboxylate, a natural product found in plant tissues. It is a key intermediate in the biosynthesis of ethylene (ethene), a fruit-ripening hormone in plants.
The chemical reactions and pathways resulting in the breakdown of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the breakdown of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the breakdown of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the breakdown of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the breakdown of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the breakdown of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the breakdown of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the breakdown of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the breakdown of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the breakdown of compounds derived from amino acids, organic acids containing one or more amino substituents.
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 cocaine stimulus. Cocaine is a crystalline alkaloid obtained from the leaves of the coca plant.
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 chemical 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 chemical stimulus.
The chemical reactions and pathways resulting in the formation of interleukin-1, an interleukin produced mainly by activated macrophages. It is involved in the inflammatory response, and is identified as an endogenous pyrogen.
The chemical reactions and pathways resulting in the formation of interleukin-1, an interleukin produced mainly by activated macrophages. It is involved in the inflammatory response, and is identified as an endogenous pyrogen.
The chemical reactions and pathways resulting in the formation of interleukin-1, an interleukin produced mainly by activated macrophages. It is involved in the inflammatory response, and is identified as an endogenous pyrogen.
The chemical reactions and pathways resulting in the formation of interleukin-1, an interleukin produced mainly by activated macrophages. It is involved in the inflammatory response, and is identified as an endogenous pyrogen.
The chemical reactions and pathways resulting in the formation of interleukin-1, an interleukin produced mainly by activated macrophages. It is involved in the inflammatory response, and is identified as an endogenous pyrogen.
The chemical reactions and pathways resulting in the formation of interleukin-1, an interleukin produced mainly by activated macrophages. It is involved in the inflammatory response, and is identified as an endogenous pyrogen.
The chemical reactions and pathways resulting in the formation of interleukin-3.
The chemical reactions and pathways resulting in the formation of interleukin-3.
The chemical reactions and pathways resulting in the formation of interleukin-3.
The chemical reactions and pathways resulting in the formation of interleukin-3.
The chemical reactions and pathways resulting in the formation of interleukin-3.
The chemical reactions and pathways resulting in the formation of interleukin-3.
The chemical reactions and pathways resulting in the formation of interleukin-5.
The chemical reactions and pathways resulting in the formation of interleukin-5.
The chemical reactions and pathways resulting in the formation of interleukin-5.
The chemical reactions and pathways resulting in the formation of interleukin-5.
The chemical reactions and pathways resulting in the formation of interleukin-5.
The chemical reactions and pathways resulting in the formation of interleukin-5.
The chemical reactions and pathways resulting in the formation of interleukin-6.
The chemical reactions and pathways resulting in the formation of interleukin-6.
The chemical reactions and pathways resulting in the formation of interleukin-6.
The chemical reactions and pathways resulting in the formation of interleukin-6.
The chemical reactions and pathways resulting in the formation of interleukin-6.
The chemical reactions and pathways resulting in the formation of interleukin-6.
The chemical reactions and pathways resulting in the formation of interleukin-7.
The chemical reactions and pathways resulting in the formation of interleukin-7.
The chemical reactions and pathways resulting in the formation of interleukin-7.
The chemical reactions and pathways resulting in the formation of interleukin-7.
The chemical reactions and pathways resulting in the formation of interleukin-7.
The chemical reactions and pathways resulting in the formation of interleukin-7.
The chemical reactions and pathways resulting in the formation of interleukin-8.
The chemical reactions and pathways resulting in the formation of interleukin-8.
The chemical reactions and pathways resulting in the formation of interleukin-8.
The chemical reactions and pathways resulting in the formation of interleukin-8.
The chemical reactions and pathways resulting in the formation of interleukin-8.
The chemical reactions and pathways resulting in the formation of interleukin-8.
The chemical reactions and pathways resulting in the formation of interleukin-9.
The chemical reactions and pathways resulting in the formation of interleukin-9.
The chemical reactions and pathways resulting in the formation of interleukin-9.
The chemical reactions and pathways resulting in the formation of interleukin-9.
The chemical reactions and pathways resulting in the formation of interleukin-9.
The chemical reactions and pathways resulting in the formation of interleukin-9.
The chemical reactions and pathways resulting in the formation of interleukin-11.
The chemical reactions and pathways resulting in the formation of interleukin-11.
The chemical reactions and pathways resulting in the formation of interleukin-11.
The chemical reactions and pathways resulting in the formation of interleukin-11.
The chemical reactions and pathways resulting in the formation of interleukin-11.
The chemical reactions and pathways resulting in the formation of interleukin-11.
The chemical reactions and pathways resulting in the formation of interleukin-13.
The chemical reactions and pathways resulting in the formation of interleukin-13.
The chemical reactions and pathways resulting in the formation of interleukin-13.
The chemical reactions and pathways resulting in the formation of interleukin-13.
The chemical reactions and pathways resulting in the formation of interleukin-13.
The chemical reactions and pathways resulting in the formation of interleukin-13.
The chemical reactions and pathways resulting in the formation of interleukin-14.
The chemical reactions and pathways resulting in the formation of interleukin-14.
The chemical reactions and pathways resulting in the formation of interleukin-14.
The chemical reactions and pathways resulting in the formation of interleukin-14.
The chemical reactions and pathways resulting in the formation of interleukin-14.
The chemical reactions and pathways resulting in the formation of interleukin-14.
The chemical reactions and pathways resulting in the formation of interleukin-15.
The chemical reactions and pathways resulting in the formation of interleukin-15.
The chemical reactions and pathways resulting in the formation of interleukin-15.
The chemical reactions and pathways resulting in the formation of interleukin-15.
The chemical reactions and pathways resulting in the formation of interleukin-15.
The chemical reactions and pathways resulting in the formation of interleukin-15.
The chemical reactions and pathways resulting in the formation of interleukin-16.
The chemical reactions and pathways resulting in the formation of interleukin-16.
The chemical reactions and pathways resulting in the formation of interleukin-16.
The chemical reactions and pathways resulting in the formation of interleukin-16.
The chemical reactions and pathways resulting in the formation of interleukin-16.
The chemical reactions and pathways resulting in the formation of interleukin-16.
The chemical reactions and pathways resulting in the formation of any member of the interleukin-17 family of cytokines.
The chemical reactions and pathways resulting in the formation of any member of the interleukin-17 family of cytokines.
The chemical reactions and pathways resulting in the formation of any member of the interleukin-17 family of cytokines.
The chemical reactions and pathways resulting in the formation of any member of the interleukin-17 family of cytokines.
The chemical reactions and pathways resulting in the formation of any member of the interleukin-17 family of cytokines.
The chemical reactions and pathways resulting in the formation of any member of the interleukin-17 family of cytokines.
The chemical reactions and pathways resulting in the formation of interleukin-19.
The chemical reactions and pathways resulting in the formation of interleukin-19.
The chemical reactions and pathways resulting in the formation of interleukin-19.
The chemical reactions and pathways resulting in the formation of interleukin-19.
The chemical reactions and pathways resulting in the formation of interleukin-19.
The chemical reactions and pathways resulting in the formation of interleukin-19.
The chemical reactions and pathways resulting in the formation of interleukin-20.
The chemical reactions and pathways resulting in the formation of interleukin-20.
The chemical reactions and pathways resulting in the formation of interleukin-20.
The chemical reactions and pathways resulting in the formation of interleukin-20.
The chemical reactions and pathways resulting in the formation of interleukin-20.
The chemical reactions and pathways resulting in the formation of interleukin-20.
The chemical reactions and pathways resulting in the formation of interleukin-21.
The chemical reactions and pathways resulting in the formation of interleukin-21.
The chemical reactions and pathways resulting in the formation of interleukin-21.
The chemical reactions and pathways resulting in the formation of interleukin-21.
The chemical reactions and pathways resulting in the formation of interleukin-21.
The chemical reactions and pathways resulting in the formation of interleukin-21.
The chemical reactions and pathways resulting in the formation of interleukin-22.
The chemical reactions and pathways resulting in the formation of interleukin-22.
The chemical reactions and pathways resulting in the formation of interleukin-22.
The chemical reactions and pathways resulting in the formation of interleukin-22.
The chemical reactions and pathways resulting in the formation of interleukin-22.
The chemical reactions and pathways resulting in the formation of interleukin-22.
The chemical reactions and pathways resulting in the formation of interleukin-23.
The chemical reactions and pathways resulting in the formation of interleukin-23.
The chemical reactions and pathways resulting in the formation of interleukin-23.
The chemical reactions and pathways resulting in the formation of interleukin-23.
The chemical reactions and pathways resulting in the formation of interleukin-23.
The chemical reactions and pathways resulting in the formation of interleukin-23.
The chemical reactions and pathways resulting in the formation of interleukin-18.
The chemical reactions and pathways resulting in the formation of interleukin-18.
The chemical reactions and pathways resulting in the formation of interleukin-18.
The chemical reactions and pathways resulting in the formation of interleukin-18.
The chemical reactions and pathways resulting in the formation of interleukin-18.
The chemical reactions and pathways resulting in the formation of interleukin-18.
Catalysis of the conversion of cobyrinic acid to cobyrinic acid a,c-diamide via the intermediate formation of cobyrinic acid c-monoamide.
The aggregation, arrangement and bonding together of a set of components to form an asexual spore wall, the specialized envelope lying outside the cell membrane of a spore derived from an asexual process. Examples of this process are found in Bacterial and Fungal species.
The aggregation, arrangement and bonding together of a set of components to form a spore wall; a spore wall is the specialized envelope lying outside the cell membrane of a spore.
The aggregation, arrangement and bonding together of a set of components to form a spore wall; a spore wall is the specialized envelope lying outside the cell membrane of a spore.
The aggregation, arrangement and bonding together of a set of components to form a spore wall; a spore wall is the specialized envelope lying outside the cell membrane of a spore.
Any process that results in the repair of damaged RNA.
The regrowth of lost or destroyed tissues.
Coordinated organization of groups of cells in the plane of a follicular epithelium, such that they all orient to similar coordinates.
The maintenance of an established polarized follicular epithelial sheet.
Coordinated organization of groups of cells in the plane of an embryonic epithelium, such that they all orient to similar coordinates.
The maintenance of an established polarized embryonic epithelial sheet.
The maintenance of an established polarized larval imaginal disc epithelium.
Coordinated organization of groups of cells in the plane of a larval imaginal disc epithelium, such that they all orient to similar coordinates.
The chemical reactions and pathways resulting in the formation of granulocyte macrophage colony-stimulating factor, cytokines that act in hemopoiesis by controlling the production, differentiation, and function of two related white cell populations, granulocytes and monocytes-macrophages.
The chemical reactions and pathways resulting in the formation of granulocyte macrophage colony-stimulating factor, cytokines that act in hemopoiesis by controlling the production, differentiation, and function of two related white cell populations, granulocytes and monocytes-macrophages.
The chemical reactions and pathways resulting in the formation of granulocyte macrophage colony-stimulating factor, cytokines that act in hemopoiesis by controlling the production, differentiation, and function of two related white cell populations, granulocytes and monocytes-macrophages.
The chemical reactions and pathways resulting in the formation of granulocyte macrophage colony-stimulating factor, cytokines that act in hemopoiesis by controlling the production, differentiation, and function of two related white cell populations, granulocytes and monocytes-macrophages.
The chemical reactions and pathways resulting in the formation of granulocyte macrophage colony-stimulating factor, cytokines that act in hemopoiesis by controlling the production, differentiation, and function of two related white cell populations, granulocytes and monocytes-macrophages.
The chemical reactions and pathways resulting in the formation of granulocyte macrophage colony-stimulating factor, cytokines that act in hemopoiesis by controlling the production, differentiation, and function of two related white cell populations, granulocytes and monocytes-macrophages.
The chemical reactions and pathways resulting in the formation of granulocyte macrophage colony-stimulating factor, cytokines that act in hemopoiesis by controlling the production, differentiation, and function of two related white cell populations, granulocytes and monocytes-macrophages.
The chemical reactions and pathways resulting in the formation of granulocyte macrophage colony-stimulating factor, cytokines that act in hemopoiesis by controlling the production, differentiation, and function of two related white cell populations, granulocytes and monocytes-macrophages.
The chemical reactions and pathways resulting in the formation of granulocyte macrophage colony-stimulating factor, cytokines that act in hemopoiesis by controlling the production, differentiation, and function of two related white cell populations, granulocytes and monocytes-macrophages.
The aggregation, arrangement and bonding together of the mature ribosome and of its subunits.
The aggregation, arrangement and bonding together of the mature ribosome and of its subunits.
The aggregation, arrangement and bonding together of the large and small ribosomal subunits into a functional ribosome.
The incorporation of molybdenum into a protein via L-serinyl molybdopterin guanine dinucleotide.
The modification of peptidyl-asparagine to form peptidyl-L-beta-methylthioasparagine, typical of bacterial ribosomal protein S12.
The modification of peptidyl-asparagine to form peptidyl-L-beta-methylthioasparagine, typical of bacterial ribosomal protein S12.
The modification of peptidyl-asparagine to form peptidyl-L-beta-methylthioasparagine, typical of bacterial ribosomal protein S12.
Any process in which DNA is protected from damage by, for example, oxidative stress.
Combining with neuropeptide F and transmitting the signal within the cell to initiate a change in cell activity. Neuropeptide F is an arthropod peptide of more than 28 residues (typically 28-45) with a consensus C-terminal RxRFamide (commonly RPRFa, but also RVRFa.
Any process that modulates the frequency, rate or extent of the rupture of cell membranes and the loss of cytoplasm.
Any process that modulates the frequency, rate, or extent of natural killer cell mediated cytotoxicity.
Any process that modulates the frequency, rate, or extent of natural killer cell mediated cytotoxicity.
Any process that modulates the frequency, rate, or extent of natural killer cell mediated cytotoxicity.
Any process that modulates the frequency, rate, or extent of natural killer cell mediated cytotoxicity.
Any process that modulates the frequency, rate, or extent of natural killer cell mediated cytotoxicity.
Any process that modulates the frequency, rate, or extent of natural killer cell mediated cytotoxicity.
Any process that modulates the frequency, rate, or extent of natural killer cell mediated cytotoxicity.
Any process that modulates the frequency, rate, or extent of natural killer cell mediated cytotoxicity.
The process of protecting a cell from natural killer cell mediated cytotoxicity.
The process of protecting a cell from natural killer cell mediated cytotoxicity.
The process of protecting a cell from natural killer cell mediated cytotoxicity.
The process of protecting a cell from natural killer cell mediated cytotoxicity.
The process of protecting a cell from natural killer cell mediated cytotoxicity.
The process of protecting a cell from natural killer cell mediated cytotoxicity.
The process of protecting a cell from natural killer cell mediated cytotoxicity.
The process of causing a cell to become susceptible to natural killer cell mediated cytotoxicity.
The process of causing a cell to become susceptible to natural killer cell mediated cytotoxicity.
The process of causing a cell to become susceptible to natural killer cell mediated cytotoxicity.
The process of causing a cell to become susceptible to natural killer cell mediated cytotoxicity.
The process of causing a cell to become susceptible to natural killer cell mediated cytotoxicity.
The process of causing a cell to become susceptible to natural killer cell mediated cytotoxicity.
The process of causing a cell to become susceptible to natural killer cell mediated cytotoxicity.
A protein complex that contains two proteins (know in several organisms, including Drosophila, as NXF1 and NXF2) and is required for the export of the majority of mRNAs from the nucleus to the cytoplasm; localized in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex; shuttles between the nucleus and the cytoplasm.
A protein complex that contains two proteins (know in several organisms, including Drosophila, as NXF1 and NXF2) and is required for the export of the majority of mRNAs from the nucleus to the cytoplasm; localized in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex; shuttles between the nucleus and the cytoplasm.
A protein complex that contains two proteins (know in several organisms, including Drosophila, as NXF1 and NXF2) and is required for the export of the majority of mRNAs from the nucleus to the cytoplasm; localized in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex; shuttles between the nucleus and the cytoplasm.
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a large ribosomal subunit; includes transport to the sites of protein synthesis.
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a small ribosomal subunit; includes transport to the sites of protein synthesis.
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA via processes such as template switching, which does not remove the replication-blocking lesions but does not increase the endogenous mutation rate.
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA via processes such as template switching, which does not remove the replication-blocking lesions but does not increase the endogenous mutation rate.
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.
The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.
Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds.
Catalysis of the reaction: NH3 + 2 H2O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H+.
Catalysis of the reaction: NH3 + 2 H2O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H+.
Catalysis of the reaction: NH3 + 2 H2O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H+.
Catalysis of the reaction: NH3 + 2 H2O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H+.
Catalysis of the reaction: NH3 + 2 H2O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H+.
Interacting selectively and non-covalently with a receptor on the host cell surface.
Interacting selectively and non-covalently with a receptor on the host cell surface.
Catalysis of the addition of the first 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(9)GlcNAc(2)-PP-Dol.
Catalysis of the reaction: (R)-mevalonate + CoA + 2 NAD(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH.
Catalysis of the reaction: (R)-mevalonate + CoA + 2 NAD(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH.
Catalysis of the reaction: (R)-mevalonate + CoA + 2 NAD(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH.
Catalysis of the reaction: (R)-mevalonate + CoA + 2 NAD(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH.
Catalysis of the reaction: (R)-mevalonate + CoA + 2 NAD(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH.
Catalysis of the reaction: (R)-mevalonate + CoA + 2 NAD(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH.
Catalysis of the reaction: (R)-mevalonate + CoA + 2 NAD(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH.
Catalysis of the reaction: (R)-mevalonate + CoA + 2 NAD(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH.
Catalysis of the addition of the second 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 Glc(1)Man(9)GlcNAc(2)-PP-Dol.
Catalysis of the introduction of a trans double bond between C4 and C5 of the long chain base region of a sphingolipid. Sphingolipids are composed of a long chain base (LCB) amide-linked to a very long chain fatty acid.
Catalysis of the transfer of a xylosyl group to an acceptor molecule, typically another carbohydrate or a lipid.
Catalysis of the reaction: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate.
Catalysis of the reaction: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate.
Interacting selectively and non-covalently with major histocompatibility complex molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
Interacting selectively and non-covalently with major histocompatibility complex molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
Interacting selectively and non-covalently with major histocompatibility complex class I molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
Interacting selectively and non-covalently with major histocompatibility complex class I molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
Interacting selectively and non-covalently with major histocompatibility complex class I molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
Interacting selectively and non-covalently with major histocompatibility complex class I molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
Interacting selectively and non-covalently with major histocompatibility complex class I molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
Interacting selectively and non-covalently with major histocompatibility complex class II molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
Interacting selectively and non-covalently with major histocompatibility complex class II molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.
Catalysis of the activation of the small ubiquitin-related modifier URM1, through the formation of an ATP-dependent high-energy thiolester bond.
Catalysis of the activation of the small ubiquitin-related modifier Hub1, through the formation of an ATP-dependent high-energy thiolester bond.
Catalysis of the transfer of URM1 from one protein to another via the reaction X-URM1 + Y --> Y-URM1 + X, where both X-URM1 and Y-URM1 are covalent linkages.
Catalysis of the transfer of ISG15 from one protein to another via the reaction X-ISG15 + Y --> Y-ISG15 + X, where both X-ISG15 and Y-ISG15 are covalent linkages.
A behavioral process whose outcome is a relatively long-lasting behavioral change whereby an organism modifies innate vocalizations to imitate sounds produced by others.
Catalysis of the reaction: (S)-2,3-epoxysqualene = lupeol. This reaction is the cyclization of (S)-2,3-epoxysqualene (2,3-oxidosqualene) to lupeol.
Catalysis of the reaction: (S)-2,3-epoxysqualene = beta-amyrin. This reaction is the cyclization and rearrangement of (S)-2,3-epoxysqualene (2,3-oxidosqualene) into beta-amyrin.
Interacting selectively and non-covalently with phosphate.
The action of a molecule that contributes to the structural integrity of a cuticle.
The periodic casting off and regeneration of an outer covering of cuticle, feathers, hair, horns, skin, etc.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of fatty acids, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of fatty acids, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of fatty acids, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of fatty acids, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils.
The specification of the characteristic structures of the mandibular segment following establishment of segment boundaries. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
Any process that activates or increases the frequency, rate or extent of movement of proteins from the cytoplasm into the nucleus.
Any process that activates or increases the frequency, rate or extent of movement of proteins from the cytoplasm into the nucleus.
Any process that activates or increases the frequency, rate or extent of movement of proteins from the cytoplasm into the nucleus.
Any process that activates or increases the frequency, rate or extent of movement of proteins from the cytoplasm into the nucleus.
Any process that activates or increases the frequency, rate or extent of movement of proteins from the cytoplasm into the nucleus.
Any process that activates or increases the frequency, rate or extent of movement of proteins from the cytoplasm into the nucleus.
Any process that activates or increases the frequency, rate or extent of movement of proteins from the cytoplasm into the nucleus.
Any process that activates or increases the frequency, rate or extent of movement of proteins from the cytoplasm into the nucleus.
Any process that stops, prevents, or reduces the frequency, rate or extent of the movement of proteins from the cytoplasm into the nucleus.
Any process that stops, prevents, or reduces the frequency, rate or extent of the movement of proteins from the cytoplasm into the nucleus.
Any process that stops, prevents, or reduces the frequency, rate or extent of the movement of proteins from the cytoplasm into the nucleus.
Any process that stops, prevents, or reduces the frequency, rate or extent of the movement of proteins from the cytoplasm into the nucleus.
Any process that stops, prevents, or reduces the frequency, rate or extent of the movement of proteins from the cytoplasm into the nucleus.
Any process that stops, prevents, or reduces the frequency, rate or extent of the movement of proteins from the cytoplasm into the nucleus.
Any process that stops, prevents, or reduces the frequency, rate or extent of the movement of proteins from the cytoplasm into the nucleus.
A decrease in the diameter of blood vessels, especially arteries, due to constriction of smooth muscle cells that line the vessels, and usually causing an increase in blood pressure.
An increase in the internal diameter of blood vessels, especially arterioles or capillaries, due to relaxation of smooth muscle cells that line the vessels, and usually resulting in a decrease in blood pressure.
An increase in the internal diameter of blood vessels, especially arterioles or capillaries, due to relaxation of smooth muscle cells that line the vessels, and usually resulting in a decrease in blood pressure.
Any process resulting in the inhibition or termination of the activity of protein kinase C.
Interacting selectively and non-covalently with bacteriochlorophyll, a form of chlorophyll found in photosynthetic bacteria, such as the purple and green bacteria. There are several types, designated a to g. Bacteriochlorophyll a and bacteriochlorophyll b are structurally similar to the chlorophyll a and chlorophyll b found in plants.
The chemical reactions and pathways involving any antibiotic that contains the condensed beta-lactamthiazolidine ring system. Penicillins are produced naturally during the growth of various microfungi of the genera Penicillium and Aspergillus.
The chemical reactions and pathways resulting in the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
The chemical reactions and pathways resulting in the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
The chemical reactions and pathways resulting in the breakdown of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
The chemical reactions and pathways resulting in the formation of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
The chemical reactions and pathways resulting in the formation of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
The chemical reactions and pathways resulting in the formation of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
The chemical reactions and pathways resulting in the formation of any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Any process that modulates the frequency, rate or extent of rapid eye movement (REM) sleep.
Any process that stops, prevents or reduces the duration or quality of sleep, a readily reversible state of reduced awareness and metabolic activity that occurs periodically in many animals.
Any process that stops, prevents or reduces the duration or quality of sleep, a readily reversible state of reduced awareness and metabolic activity that occurs periodically in many animals.
Any process that stops, prevents or reduces the duration or quality of sleep, a readily reversible state of reduced awareness and metabolic activity that occurs periodically in many animals.
Any process that stops, prevents or reduces the duration or quality of sleep, a readily reversible state of reduced awareness and metabolic activity that occurs periodically in many animals.
Any process that stops, prevents or reduces the duration or quality of sleep, a readily reversible state of reduced awareness and metabolic activity that occurs periodically in many animals.
Any process that stops, prevents or reduces the duration or quality of rapid eye movement (REM) sleep.
Any process that stops, prevents or reduces the duration or quality of rapid eye movement (REM) sleep.
Any process that stops, prevents or reduces the duration or quality of rapid eye movement (REM) sleep.
Any process that stops, prevents or reduces the duration or quality of rapid eye movement (REM) sleep.
Any process that stops, prevents or reduces the duration or quality of rapid eye movement (REM) sleep.
Any process that stops, prevents or reduces the duration or quality of non-rapid eye movement (NREM) sleep.
Any process that stops, prevents or reduces the duration or quality of non-rapid eye movement (NREM) sleep.
Any process that stops, prevents or reduces the duration or quality of non-rapid eye movement (NREM) sleep.
Any process that stops, prevents or reduces the duration or quality of non-rapid eye movement (NREM) sleep.
Any process that stops, prevents or reduces the duration or quality of non-rapid eye movement (NREM) sleep.
Interacting selectively and non-covalently with the hypocretin receptor.
Interacting selectively and non-covalently with the hypocretin receptor.
Interacting selectively and non-covalently with the hypocretin receptor.
Any process that modulates the frequency, rate or extent of addition of phosphate groups into a molecule.
Any process that stops, prevents or decreases the rate of addition of phosphate groups to a molecule.
Any process that stops, prevents or decreases the rate of addition of phosphate groups to a molecule.
Any process that stops, prevents or decreases the rate of addition of phosphate groups to a molecule.
Any process that stops, prevents or decreases the rate of addition of phosphate groups to a molecule.
Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to a molecule.
Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to a molecule.
Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to a molecule.
Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to a molecule.
Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to a molecule.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + heparan sulfate = UDP + (N-acetyl-D-glucosaminyl)-heparan sulfate.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + heparan sulfate = UDP + (N-acetyl-D-glucosaminyl)-heparan sulfate.
The action of a molecule that contributes to the structural integrity of a collagen and cuticulin-based cuticle. An example of this process is found in Caenorhabditis elegans.
The directed movement of a motile cell or organism in response to an external stimulus.
The directed movement of a motile cell or organism in response to light.
The directed movement of a motile cell or organism in response to light.
The directed movement of a motile cell or organism in response to light.
The directed movement of a motile cell or organism in response to light.
The directed movement of a motile cell or organism in response to gravity.
The directed movement of a motile cell or organism in response to gravity.
The directed movement of a motile cell or organism in response to gravity.
The directed movement of a motile cell or organism in response to gravity.
The directed movement of a motile cell or organism in response to gravity.
The directed movement of a motile cell or organism in response to gravity.
The directed movement of a motile cell or organism in response to gravity.
The directed movement of a motile cell or organism in response to gravity.
The directed movement of a motile cell or organism in response to the presence of an oxidizable substrate, for example, fructose.
The directed movement of a motile cell or organism in response to the presence of an alternative electron acceptor, for example, nitrate.
The chemical reactions and pathways resulting in the formation of a cuticle, the outer layer of some animals and plants, which acts to prevent water loss.
The chemical reactions and pathways resulting in the formation of a cuticle, the outer layer of some animals and plants, which acts to prevent water loss.
The chemical reactions and pathways resulting in the formation of a cuticle, the outer layer of some animals and plants, which acts to prevent water loss.
The chemical reactions and pathways resulting in the formation of a cuticle, the outer layer of some animals and plants, which acts to prevent water loss.
The chemical reactions and pathways resulting in the formation of a cuticle, the outer layer of some animals and plants, which acts to prevent water loss.
The synthesis and deposition of a chitin-based non-cellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. An example of this is found in Drosophila melanogaster.
The synthesis and deposition of a chitin-based non-cellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. An example of this is found in Drosophila melanogaster.
The synthesis and deposition of a chitin-based non-cellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. An example of this is found in Drosophila melanogaster.
The synthesis and deposition of a chitin-based non-cellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. An example of this is found in Drosophila melanogaster.
The synthesis and deposition of a chitin-based non-cellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. An example of this is found in Drosophila melanogaster.
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. An example of this process is found in Caenorhabditis elegans.
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. An example of this process is found in Caenorhabditis elegans.
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. An example of this process is found in Caenorhabditis elegans.
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. An example of this process is found in Caenorhabditis elegans.
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. An example of this process is found in Caenorhabditis elegans.
The chemical reactions and pathways involving keratan sulfate, a glycosaminoglycan with repeat units consisting of beta-1,4-linked D-galactopyranosyl-beta-(1,4)-N-acetyl-D-glucosamine 6-sulfate and with variable amounts of fucose, sialic acid and mannose units; keratan sulfate chains are covalently linked by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylose to peptidyl-threonine or serine residues.
The chemical reactions and pathways involving keratan sulfate, a glycosaminoglycan with repeat units consisting of beta-1,4-linked D-galactopyranosyl-beta-(1,4)-N-acetyl-D-glucosamine 6-sulfate and with variable amounts of fucose, sialic acid and mannose units; keratan sulfate chains are covalently linked by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylose to peptidyl-threonine or serine residues.
The chemical reactions and pathways involving keratan sulfate, a glycosaminoglycan with repeat units consisting of beta-1,4-linked D-galactopyranosyl-beta-(1,4)-N-acetyl-D-glucosamine 6-sulfate and with variable amounts of fucose, sialic acid and mannose units; keratan sulfate chains are covalently linked by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylose to peptidyl-threonine or serine residues.
The chemical reactions and pathways resulting in the breakdown of keratan sulfate, a glycosaminoglycan with repeat units consisting of beta-1,4-linked D-galactopyranosyl-beta-(1,4)-N-acetyl-D-glucosamine 6-sulfate and with variable amounts of fucose, sialic acid and mannose units; keratan sulfate chains are covalently linked by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylose to peptidyl-threonine or serine residues.
The chemical reactions and pathways resulting in the breakdown of keratan sulfate, a glycosaminoglycan with repeat units consisting of beta-1,4-linked D-galactopyranosyl-beta-(1,4)-N-acetyl-D-glucosamine 6-sulfate and with variable amounts of fucose, sialic acid and mannose units; keratan sulfate chains are covalently linked by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylose to peptidyl-threonine or serine residues.
The chemical reactions and pathways resulting in the breakdown of keratan sulfate, a glycosaminoglycan with repeat units consisting of beta-1,4-linked D-galactopyranosyl-beta-(1,4)-N-acetyl-D-glucosamine 6-sulfate and with variable amounts of fucose, sialic acid and mannose units; keratan sulfate chains are covalently linked by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylose to peptidyl-threonine or serine residues.
The chemical reactions and pathways resulting in the breakdown of keratan sulfate, a glycosaminoglycan with repeat units consisting of beta-1,4-linked D-galactopyranosyl-beta-(1,4)-N-acetyl-D-glucosamine 6-sulfate and with variable amounts of fucose, sialic acid and mannose units; keratan sulfate chains are covalently linked by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylose to peptidyl-threonine or serine residues.
The chemical reactions and pathways resulting in the breakdown of keratan sulfate, a glycosaminoglycan with repeat units consisting of beta-1,4-linked D-galactopyranosyl-beta-(1,4)-N-acetyl-D-glucosamine 6-sulfate and with variable amounts of fucose, sialic acid and mannose units; keratan sulfate chains are covalently linked by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylose to peptidyl-threonine or serine residues.
The chemical reactions and pathways involving cyanogenic glycosides, any glycoside containing a cyano group that is released as hydrocyanic acid on acid hydrolysis; such compounds occur in the kernels of various fruits.
The chemical reactions and pathways resulting in the breakdown of cyanogenic glycosides, any glycoside containing a cyano group that is released as hydrocyanic acid on acid hydrolysis; such compounds occur in the kernels of various fruits.
The chemical reactions and pathways resulting in the breakdown of cyanogenic glycosides, any glycoside containing a cyano group that is released as hydrocyanic acid on acid hydrolysis; such compounds occur in the kernels of various fruits.
The chemical reactions and pathways resulting in the breakdown of cyanogenic glycosides, any glycoside containing a cyano group that is released as hydrocyanic acid on acid hydrolysis; such compounds occur in the kernels of various fruits.
The chemical reactions and pathways resulting in the formation of indole glucosinolates. Glucosinolates are sulfur-containing compounds that have a common structure linked to an R group derived from tryptophan; indoles are biologically active substances based on 2,3-benzopyrrole, formed during the catabolism of tryptophan.
The chemical reactions and pathways resulting in the breakdown of indole glucosinolates, sulfur-containing compounds that have a common structure linked to an R group derived from tryptophan.
The chemical reactions and pathways resulting in the breakdown of indole glucosinolates, sulfur-containing compounds that have a common structure linked to an R group derived from tryptophan.
The chemical reactions and pathways resulting in the breakdown of indole glucosinolates, sulfur-containing compounds that have a common structure linked to an R group derived from tryptophan.
The orientation of free radical substrates in such a way that only a particular stereoisomer is synthesized by an enzyme. Best characterized as a function during lignan biosynthesis.
The chemical reactions and pathways resulting in the formation of GDP-L-fucose, a substance composed of L-fucose in glycosidic linkage with guanosine diphosphate.
The chemical reactions and pathways resulting in the formation of GDP-L-fucose, a substance composed of L-fucose in glycosidic linkage with guanosine diphosphate.
The chemical reactions and pathways resulting in the formation of GDP-L-fucose, a substance composed of L-fucose in glycosidic linkage with guanosine diphosphate.
The chemical reactions and pathways resulting in the formation of GDP-L-fucose, a substance composed of L-fucose in glycosidic linkage with guanosine diphosphate.
The chemical reactions and pathways resulting in the formation of GDP-L-fucose from GDP-D-mannose via GDP-4-dehydro-6-deoxy-D-mannose, requiring the functions of GDP-mannose 4,6-dehydratase (EC:4.2.1.47) and GDP-L-fucose synthase (EC:1.1.1.271).
The chemical reactions and pathways resulting in the formation of GDP-L-fucose from GDP-D-mannose via GDP-4-dehydro-6-deoxy-D-mannose, requiring the functions of GDP-mannose 4,6-dehydratase (EC:4.2.1.47) and GDP-L-fucose synthase (EC:1.1.1.271).
The chemical reactions and pathways resulting in the formation of GDP-L-fucose from GDP-D-mannose via GDP-4-dehydro-6-deoxy-D-mannose, requiring the functions of GDP-mannose 4,6-dehydratase (EC:4.2.1.47) and GDP-L-fucose synthase (EC:1.1.1.271).
The chemical reactions and pathways resulting in the formation of GDP-L-fucose from GDP-D-mannose via GDP-4-dehydro-6-deoxy-D-mannose, requiring the functions of GDP-mannose 4,6-dehydratase (EC:4.2.1.47) and GDP-L-fucose synthase (EC:1.1.1.271).
The chemical reactions and pathways resulting in the formation of GDP-L-fucose from GDP-D-mannose via GDP-4-dehydro-6-deoxy-D-mannose, requiring the functions of GDP-mannose 4,6-dehydratase (EC:4.2.1.47) and GDP-L-fucose synthase (EC:1.1.1.271).
The chemical reactions and pathways resulting in the formation of GDP-L-fucose from GDP-D-mannose via GDP-4-dehydro-6-deoxy-D-mannose, requiring the functions of GDP-mannose 4,6-dehydratase (EC:4.2.1.47) and GDP-L-fucose synthase (EC:1.1.1.271).
The formation of GDP-L-fucose from L-fucose, without de novo synthesis. L-fucose is phosphorylated by fucokinase and then converted by fucose-1-phosphate guanylyltransferase (EC:2.7.7.30).
The formation of GDP-L-fucose from L-fucose, without de novo synthesis. L-fucose is phosphorylated by fucokinase and then converted by fucose-1-phosphate guanylyltransferase (EC:2.7.7.30).
The chemical reactions and pathways resulting in the formation of fucose (6-deoxygalactose).
The chemical reactions and pathways resulting in the formation of fucose (6-deoxygalactose).
The chemical reactions and pathways resulting in the formation of fucose (6-deoxygalactose).
The chemical reactions and pathways resulting in the formation of fucose (6-deoxygalactose).
The chemical reactions and pathways involving L-fucose, 6-deoxy-L-galactose, a sugar that occurs in fucans, a class of polysaccharides in seaweeds, especially Fucus species, and in the cell wall matrix of higher plants.
The chemical reactions and pathways resulting in the breakdown of L-fucose (6-deoxy-Lgalactose).
The chemical reactions and pathways resulting in the breakdown of L-fucose (6-deoxy-Lgalactose).
The chemical reactions and pathways resulting in the breakdown of L-fucose (6-deoxy-Lgalactose).
Catalysis of the reaction: GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+. In the reverse reaction, a mixture of GDP-D-rhamnose and its C-4 epimer is formed.
Catalysis of the reaction: GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+. In the reverse reaction, a mixture of GDP-D-rhamnose and its C-4 epimer is formed.
Catalysis of the reaction: GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+. In the reverse reaction, a mixture of GDP-D-rhamnose and its C-4 epimer is formed.
Catalysis of the reaction: GDP-6-deoxy-D-mannose + NAD(P)+ = GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+. In the reverse reaction, a mixture of GDP-D-rhamnose and its C-4 epimer is formed.
The chemical reactions and pathways involving thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways involving thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways involving thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways involving thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways involving thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways involving thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways involving thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways involving thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways involving thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the breakdown of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the breakdown of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the breakdown of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the breakdown of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the breakdown of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the breakdown of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the breakdown of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the breakdown of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the breakdown of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the breakdown of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the breakdown of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways involving vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways involving vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways involving vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways involving vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways involving vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways involving vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways involving vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways involving vitamin E, tocopherol, which includes a series of eight structurally similar compounds. Alpha-tocopherol is the most active form in humans and is a powerful biological antioxidant.
The chemical reactions and pathways involving vitamin E, tocopherol, which includes a series of eight structurally similar compounds. Alpha-tocopherol is the most active form in humans and is a powerful biological antioxidant.
The chemical reactions and pathways involving vitamin E, tocopherol, which includes a series of eight structurally similar compounds. Alpha-tocopherol is the most active form in humans and is a powerful biological antioxidant.
The chemical reactions and pathways involving vitamin E, tocopherol, which includes a series of eight structurally similar compounds. Alpha-tocopherol is the most active form in humans and is a powerful biological antioxidant.
The chemical reactions and pathways involving vitamin E, tocopherol, which includes a series of eight structurally similar compounds. Alpha-tocopherol is the most active form in humans and is a powerful biological antioxidant.
The chemical reactions and pathways resulting in the breakdown of menaquinones, any of the quinone-derived compounds synthesized by intestinal bacteria. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones have vitamin K activity and are known as vitamin K2.
The chemical reactions and pathways resulting in the breakdown of menaquinones, any of the quinone-derived compounds synthesized by intestinal bacteria. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones have vitamin K activity and are known as vitamin K2.
The chemical reactions and pathways resulting in the breakdown of menaquinones, any of the quinone-derived compounds synthesized by intestinal bacteria. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones have vitamin K activity and are known as vitamin K2.
The chemical reactions and pathways resulting in the breakdown of menaquinones, any of the quinone-derived compounds synthesized by intestinal bacteria. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones have vitamin K activity and are known as vitamin K2.
The chemical reactions and pathways resulting in the breakdown of menaquinones, any of the quinone-derived compounds synthesized by intestinal bacteria. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones have vitamin K activity and are known as vitamin K2.
The chemical reactions and pathways resulting in the breakdown of menaquinones, any of the quinone-derived compounds synthesized by intestinal bacteria. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones have vitamin K activity and are known as vitamin K2.
The chemical reactions and pathways resulting in the breakdown of menaquinones, any of the quinone-derived compounds synthesized by intestinal bacteria. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones have vitamin K activity and are known as vitamin K2.
The chemical reactions and pathways resulting in the breakdown of menaquinones, any of the quinone-derived compounds synthesized by intestinal bacteria. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones have vitamin K activity and are known as vitamin K2.
The chemical reactions and pathways resulting in the breakdown of menaquinones, any of the quinone-derived compounds synthesized by intestinal bacteria. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones have vitamin K activity and are known as vitamin K2.
The chemical reactions and pathways resulting in the formation of any of a diverse group of vitamins that are soluble in organic solvents and relatively insoluble in water.
The chemical reactions and pathways resulting in the formation of any of a diverse group of vitamins that are soluble in organic solvents and relatively insoluble in water.
The chemical reactions and pathways resulting in the formation of any of a diverse group of vitamins that are soluble in organic solvents and relatively insoluble in water.
The chemical reactions and pathways resulting in the formation of any of a diverse group of vitamins that are soluble in organic solvents and relatively insoluble in water.
The chemical reactions and pathways resulting in the breakdown of any of a diverse group of vitamins that are soluble in organic solvents and relatively insoluble in water.
The chemical reactions and pathways resulting in the breakdown of any of a diverse group of vitamins that are soluble in organic solvents and relatively insoluble in water.
The chemical reactions and pathways resulting in the breakdown of any of a diverse group of vitamins that are soluble in organic solvents and relatively insoluble in water.
The chemical reactions and pathways resulting in the formation of any of a diverse group of vitamins that are soluble in water.
The chemical reactions and pathways resulting in the formation of any of a diverse group of vitamins that are soluble in water.
The chemical reactions and pathways resulting in the formation of any of a diverse group of vitamins that are soluble in water.
The chemical reactions and pathways resulting in the formation of any of a diverse group of vitamins that are soluble in water.
The chemical reactions and pathways resulting in the breakdown of any of a diverse group of vitamins that are soluble in water.
The chemical reactions and pathways resulting in the breakdown of any of a diverse group of vitamins that are soluble in water.
The chemical reactions and pathways resulting in the breakdown of any of a diverse group of vitamins that are soluble in water.
The chemical reactions and pathways resulting in the breakdown of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
The chemical reactions and pathways resulting in the breakdown of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
The chemical reactions and pathways resulting in the breakdown of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
The chemical reactions and pathways resulting in the breakdown of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
The chemical reactions and pathways resulting in the breakdown of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
The chemical reactions and pathways resulting in the breakdown of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid.
The chemical reactions and pathways resulting in the breakdown of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid.
The chemical reactions and pathways resulting in the breakdown of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid.
The chemical reactions and pathways resulting in the breakdown of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid.
The chemical reactions and pathways resulting in the breakdown of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid.
The chemical reactions and pathways resulting in the breakdown of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid.
The chemical reactions and pathways resulting in the breakdown of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid.
The chemical reactions and pathways resulting in the formation of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the formation of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the formation of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the formation of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the formation of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the formation of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the formation of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the formation of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the formation of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the formation of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the breakdown of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the breakdown of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the breakdown of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the breakdown of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the breakdown of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the breakdown of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the breakdown of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the breakdown of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The chemical reactions and pathways resulting in the breakdown of vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3).
The removal of one or more phosphate groups from thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The removal of one or more phosphate groups from thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
The chemical reactions and pathways resulting in the formation of any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals.
The chemical reactions and pathways resulting in the formation of any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals.
The chemical reactions and pathways resulting in the formation of any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals.
The chemical reactions and pathways resulting in the formation of any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals.
The chemical reactions and pathways resulting in the formation of any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals.
The chemical reactions and pathways resulting in the formation of any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the formation of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways involving any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals. Vitamin K substances share a methylated naphthoquinone ring structure and vary in the aliphatic side chains attached to the molecule.
The chemical reactions and pathways involving any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals. Vitamin K substances share a methylated naphthoquinone ring structure and vary in the aliphatic side chains attached to the molecule.
The chemical reactions and pathways involving any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals. Vitamin K substances share a methylated naphthoquinone ring structure and vary in the aliphatic side chains attached to the molecule.
The chemical reactions and pathways involving phylloquinone, a quinone-derived compound synthesized by green plants. Phylloquinone has vitamin K activity and is known as vitamin K1.
The chemical reactions and pathways involving phylloquinone, a quinone-derived compound synthesized by green plants. Phylloquinone has vitamin K activity and is known as vitamin K1.
The chemical reactions and pathways involving phylloquinone, a quinone-derived compound synthesized by green plants. Phylloquinone has vitamin K activity and is known as vitamin K1.
The chemical reactions and pathways involving phylloquinone, a quinone-derived compound synthesized by green plants. Phylloquinone has vitamin K activity and is known as vitamin K1.
The chemical reactions and pathways involving phylloquinone, a quinone-derived compound synthesized by green plants. Phylloquinone has vitamin K activity and is known as vitamin K1.
The chemical reactions and pathways involving phylloquinone, a quinone-derived compound synthesized by green plants. Phylloquinone has vitamin K activity and is known as vitamin K1.
The chemical reactions and pathways involving phylloquinone, a quinone-derived compound synthesized by green plants. Phylloquinone has vitamin K activity and is known as vitamin K1.
The chemical reactions and pathways involving phylloquinone, a quinone-derived compound synthesized by green plants. Phylloquinone has vitamin K activity and is known as vitamin K1.
The chemical reactions and pathways involving phylloquinone, a quinone-derived compound synthesized by green plants. Phylloquinone has vitamin K activity and is known as vitamin K1.
The chemical reactions and pathways resulting in the breakdown of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the breakdown of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the breakdown of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the breakdown of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the breakdown of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the breakdown of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the breakdown of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the breakdown of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the breakdown of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the breakdown of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the breakdown of phylloquinone, vitamin K1, a quinone-derived compound synthesized by green plants.
The chemical reactions and pathways resulting in the breakdown of any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals.
The chemical reactions and pathways resulting in the breakdown of any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals.
The chemical reactions and pathways resulting in the breakdown of any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals.
The chemical reactions and pathways resulting in the breakdown of any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals.
The chemical reactions and pathways resulting in the breakdown of any of the forms of vitamin K, quinone-derived vitamins which are involved in the synthesis of blood-clotting factors in mammals.
Interacting selectively and non-covalently with any chemokine receptor.
Catalysis of the formation of both isopentenyl pyrophosphate and dimethylallyl pyrophosphate from (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate.
Any process in which factors in the hemolymph (the invertebrate equivalent of vertebrate blood and lymph) precipitate into insoluble clots in order to prevent loss of body fluid, and at the same time prevent the movement of microbes. Hemolymph coagulation is also part of the invertebrate humoral immune response.
Discrete subnuclear bodies in the interchromatin nucleoplasmic space, often located adjacent to nuclear specks. 10-20 paraspeckles are typically found in human cell nuclei.
The outer membrane of a muscle cell, consisting of the plasma membrane, a covering basement membrane (about 100 nm thick and sometimes common to more than one fiber), and the associated loose network of collagen fibers.
A myosin complex containing a class III myosin heavy chain and associated light chains; myosin III is monomeric myosin that serves as a link between the cytoskeleton and the signaling complex involved in phototransduction, and differs from all other myosins in having an N-terminal kinase domain.
The process in which a relatively unspecialized cell acquires the characteristics 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 hemocyte precursor cell acquires the characteristics of the phagocytic blood-cell type, the plasmatocyte. Plasmatocytes are a class of arthropod hemocytes important in the cellular defense response.
A series of molecular signals mediated by the detection of gibberellic acid and dependent on the coupling of the alpha subunit of G proteins to the hormone receptors.
Catalysis of the introduction of an omega-3 double bond into the fatty acid hydrocarbon chain.
A series of molecular signals mediated by the detection of gibberellic acid and not dependent on the coupling of the alpha subunit of G proteins to the hormone receptors.
Any process that modulates the establishment or extent of a membrane potential, the electric potential existing across any membrane arising from charges in the membrane itself and from the charges present in the media on either side of the membrane.
Catalysis of the reaction: sphingosine 1-phosphate + H2O = sphingosine + phosphate.
Catalysis of the reaction: sphingosine 1-phosphate + H2O = sphingosine + phosphate.
Catalysis of the reaction: sphingosine 1-phosphate + H2O = sphingosine + phosphate.
The shedding of the old collagen and cuticulin-based cuticle fragments during the molting cycle. Examples of this process are found in invertebrates.
The chemical reactions and pathways resulting in the formation of phosphagen, any of a group of guanidine phosphates that occur in muscle and can be used to regenerate ATP from ADP during muscular contraction.
The chemical reactions and pathways resulting in the formation of phosphagen, any of a group of guanidine phosphates that occur in muscle and can be used to regenerate ATP from ADP during muscular contraction.
The chemical reactions and pathways resulting in the formation of phosphagen, any of a group of guanidine phosphates that occur in muscle and can be used to regenerate ATP from ADP during muscular contraction.
The chemical reactions and pathways resulting in the formation of phosphagen, any of a group of guanidine phosphates that occur in muscle and can be used to regenerate ATP from ADP during muscular contraction.
The chemical reactions and pathways resulting in the breakdown of phosphagen, any of a group of guanidine phosphates that occur in muscle and can be used to regenerate ATP from ADP during muscular contraction.
The chemical reactions and pathways resulting in the breakdown of phosphagen, any of a group of guanidine phosphates that occur in muscle and can be used to regenerate ATP from ADP during muscular contraction.
The chemical reactions and pathways resulting in the breakdown of phosphagen, any of a group of guanidine phosphates that occur in muscle and can be used to regenerate ATP from ADP during muscular contraction.
The chemical reactions and pathways resulting in the formation of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the formation of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the formation of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the formation of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the formation of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the formation of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the formation of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the formation of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the formation of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways resulting in the formation of compounds derived from amino acids, organic acids containing one or more amino substituents.
The chemical reactions and pathways involving ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidinecarboxylic acid), a tetrahydropyrimidine commonly synthesized by halophilic bacteria.
The chemical reactions and pathways resulting in the breakdown of ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidinecarboxylic acid), a tetrahydropyrimidine commonly synthesized by halophilic bacteria.
The chemical reactions and pathways resulting in the breakdown of ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidinecarboxylic acid), a tetrahydropyrimidine commonly synthesized by halophilic bacteria.
The chemical reactions and pathways resulting in the breakdown of ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidinecarboxylic acid), a tetrahydropyrimidine commonly synthesized by halophilic bacteria.
The chemical reactions and pathways occurring at the level of individual cells resulting in the formation of any of a group of naturally occurring, biologically active amines, such as norepinephrine, histamine, and serotonin, many of which act as neurotransmitters.
The chemical reactions and pathways occurring at the level of individual cells resulting in the formation of any of a group of naturally occurring, biologically active amines, such as norepinephrine, histamine, and serotonin, many of which act as neurotransmitters.
The chemical reactions and pathways occurring at the level of individual cells resulting in the formation of any of a group of naturally occurring, biologically active amines, such as norepinephrine, histamine, and serotonin, many of which act as neurotransmitters.
The chemical reactions and pathways occurring at the level of individual cells resulting in the formation of any of a group of naturally occurring, biologically active amines, such as norepinephrine, histamine, and serotonin, many of which act as neurotransmitters.
The chemical reactions and pathways occurring at the level of individual cells resulting in the breakdown of biogenic amines, any of a group of naturally occurring, biologically active amines, such as norepinephrine, histamine, and serotonin, many of which act as neurotransmitters.
The chemical reactions and pathways occurring at the level of individual cells resulting in the breakdown of biogenic amines, any of a group of naturally occurring, biologically active amines, such as norepinephrine, histamine, and serotonin, many of which act as neurotransmitters.
The chemical reactions and pathways occurring at the level of individual cells resulting in the breakdown of biogenic amines, any of a group of naturally occurring, biologically active amines, such as norepinephrine, histamine, and serotonin, many of which act as neurotransmitters.
The chemical reactions and pathways involving any of the compounds secreted by the thyroid gland, largely thyroxine and triiodothyronine.
The chemical reactions and pathways resulting in the breakdown of any of the compounds secreted by the thyroid gland, largely thyroxine and triiodothyronine.
The chemical reactions and pathways resulting in the breakdown of any of the compounds secreted by the thyroid gland, largely thyroxine and triiodothyronine.
The chemical reactions and pathways resulting in the breakdown of any of the compounds secreted by the thyroid gland, largely thyroxine and triiodothyronine.
An intranuclear focus at which aggregated proteins have been sequestered.
The component of the endoplasmic reticulum 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 the endoplasmic reticulum 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 assembly of cristae, the inwards folds of the inner mitochondrial membrane.
Catalysis of the reaction: S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine + feruloyl-CoA.
Catalysis of the reaction: S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine + feruloyl-CoA.
Catalysis of the reaction: S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine + feruloyl-CoA.
Catalysis of the reaction: S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine + feruloyl-CoA.
Catalysis of the reaction: ATP + CoA + pimelate = AMP + diphosphate + H(+) + pimelyl-CoA.
Catalysis of the reaction: ATP + CoA + pimelate = AMP + diphosphate + H(+) + pimelyl-CoA.
Catalysis of the reaction: ATP + CoA + pimelate = AMP + diphosphate + H(+) + pimelyl-CoA.
Catalysis of the reaction: ATP + CoA + pimelate = AMP + diphosphate + H(+) + pimelyl-CoA.
The chemical reactions and pathways resulting in the formation of taurine (2-aminoethanesulfonic acid), a sulphur-containing amino acid derivative important in the metabolism of fats.
The chemical reactions and pathways resulting in the formation of taurine (2-aminoethanesulfonic acid), a sulphur-containing amino acid derivative important in the metabolism of fats.
The chemical reactions and pathways resulting in the formation of taurine (2-aminoethanesulfonic acid), a sulphur-containing amino acid derivative important in the metabolism of fats.
The chemical reactions and pathways resulting in the formation of taurine (2-aminoethanesulfonic acid), a sulphur-containing amino acid derivative important in the metabolism of fats.
The chemical reactions and pathways resulting in the breakdown of carnitine (hydroxy-trimethyl aminobutyric acid), a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane.
The chemical reactions and pathways resulting in the breakdown of carnitine (hydroxy-trimethyl aminobutyric acid), a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane.
The chemical reactions and pathways resulting in the breakdown of carnitine (hydroxy-trimethyl aminobutyric acid), a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane.
The chemical reactions and pathways resulting in the breakdown of carnitine (hydroxy-trimethyl aminobutyric acid), a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane.
The chemical reactions and pathways resulting in the breakdown of carnitine (hydroxy-trimethyl aminobutyric acid), a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane.
The chemical reactions and pathways involving epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways involving epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways involving epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways involving norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways involving norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways involving norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways involving norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways involving norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the formation of dopamine, a catecholamine neurotransmitter and a metabolic precursor of noradrenaline and adrenaline.
The chemical reactions and pathways resulting in the formation of dopamine, a catecholamine neurotransmitter and a metabolic precursor of noradrenaline and adrenaline.
The chemical reactions and pathways resulting in the formation of dopamine, a catecholamine neurotransmitter and a metabolic precursor of noradrenaline and adrenaline.
The chemical reactions and pathways resulting in the formation of dopamine, a catecholamine neurotransmitter and a metabolic precursor of noradrenaline and adrenaline.
The chemical reactions and pathways involving dopamine, a catecholamine neurotransmitter and a metabolic precursor of noradrenaline and adrenaline.
The chemical reactions and pathways resulting in the formation of epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways resulting in the formation of epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways resulting in the formation of epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways resulting in the formation of epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways resulting in the formation of epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways resulting in the formation of epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways resulting in the breakdown of epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways resulting in the breakdown of epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways resulting in the breakdown of epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways resulting in the breakdown of epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways resulting in the breakdown of epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine.
The chemical reactions and pathways resulting in the breakdown of dopamine, a catecholamine neurotransmitter and a metabolic precursor of noradrenaline and adrenaline.
The chemical reactions and pathways resulting in the breakdown of dopamine, a catecholamine neurotransmitter and a metabolic precursor of noradrenaline and adrenaline.
The chemical reactions and pathways resulting in the breakdown of dopamine, a catecholamine neurotransmitter and a metabolic precursor of noradrenaline and adrenaline.
The chemical reactions and pathways resulting in the formation of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the formation of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the formation of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the formation of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the formation of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the formation of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the formation of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the formation of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the breakdown of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the breakdown of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the breakdown of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the breakdown of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the breakdown of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the breakdown of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the breakdown of norepinephrine, a hormone secreted by the adrenal medulla, and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts in the central nervous system. It is also the demethylated biosynthetic precursor of epinephrine.
The chemical reactions and pathways resulting in the formation of any of a group of physiologically important biogenic amines that possess a catechol (3,4-dihydroxyphenyl) nucleus and are derivatives of 3,4-dihydroxyphenylethylamine.
The chemical reactions and pathways resulting in the formation of any of a group of physiologically important biogenic amines that possess a catechol (3,4-dihydroxyphenyl) nucleus and are derivatives of 3,4-dihydroxyphenylethylamine.
The chemical reactions and pathways resulting in the formation of any of a group of physiologically important biogenic amines that possess a catechol (3,4-dihydroxyphenyl) nucleus and are derivatives of 3,4-dihydroxyphenylethylamine.
The chemical reactions and pathways resulting in the formation of any of a group of physiologically important biogenic amines that possess a catechol (3,4-dihydroxyphenyl) nucleus and are derivatives of 3,4-dihydroxyphenylethylamine.
The chemical reactions and pathways resulting in the breakdown of any of a group of physiologically important biogenic amines that possess a catechol (3,4-dihydroxyphenyl) nucleus and are derivatives of 3,4-dihydroxyphenylethylamine.
The chemical reactions and pathways resulting in the breakdown of any of a group of physiologically important biogenic amines that possess a catechol (3,4-dihydroxyphenyl) nucleus and are derivatives of 3,4-dihydroxyphenylethylamine.
The chemical reactions and pathways resulting in the breakdown of any of a group of physiologically important biogenic amines that possess a catechol (3,4-dihydroxyphenyl) nucleus and are derivatives of 3,4-dihydroxyphenylethylamine.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids and in the neurotransmitter acetylcholine.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids and in the neurotransmitter acetylcholine.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids and in the neurotransmitter acetylcholine.
The chemical reactions and pathways resulting in the formation of choline (2-hydroxyethyltrimethylammonium), an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids and in the neurotransmitter acetylcholine.
The chemical reactions and pathways resulting in the breakdown of choline (2-hydroxyethyltrimethylammonium), an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids and in the neurotransmitter acetylcholine.
The chemical reactions and pathways resulting in the breakdown of choline (2-hydroxyethyltrimethylammonium), an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids and in the neurotransmitter acetylcholine.
The chemical reactions and pathways resulting in the breakdown of choline (2-hydroxyethyltrimethylammonium), an amino alcohol that occurs widely in living organisms as a constituent of certain types of phospholipids and in the neurotransmitter acetylcholine.
The chemical reactions and pathways resulting in the formation of serotonin (5-hydroxytryptamine), a monoamine neurotransmitter occurring in the peripheral and central nervous systems, also having hormonal properties.
The chemical reactions and pathways resulting in the formation of serotonin (5-hydroxytryptamine), a monoamine neurotransmitter occurring in the peripheral and central nervous systems, also having hormonal properties.
The chemical reactions and pathways resulting in the formation of serotonin (5-hydroxytryptamine), a monoamine neurotransmitter occurring in the peripheral and central nervous systems, also having hormonal properties.
The chemical reactions and pathways resulting in the formation of serotonin (5-hydroxytryptamine), a monoamine neurotransmitter occurring in the peripheral and central nervous systems, also having hormonal properties.
The chemical reactions and pathways involving serotonin (5-hydroxytryptamine), a monoamine neurotransmitter occurring in the peripheral and central nervous systems, also having hormonal properties.
The chemical reactions and pathways resulting in the breakdown of serotonin (5-hydroxytryptamine), a monoamine neurotransmitter occurring in the peripheral and central nervous systems, also having hormonal properties.
The chemical reactions and pathways resulting in the breakdown of serotonin (5-hydroxytryptamine), a monoamine neurotransmitter occurring in the peripheral and central nervous systems, also having hormonal properties.
The chemical reactions and pathways resulting in the breakdown of serotonin (5-hydroxytryptamine), a monoamine neurotransmitter occurring in the peripheral and central nervous systems, also having hormonal properties.
The chemical reactions and pathways involving compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways involving compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways involving compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways involving compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways involving compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways involving compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways involving compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways involving compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways involving indole (2,3-benzopyrrole), the basis of many biologically active substances (e.g. serotonin, tryptophan).
The chemical reactions and pathways resulting in the formation of indole (2,3-benzopyrrole), the basis of many biologically active substances (e.g. serotonin, tryptophan).
The chemical reactions and pathways resulting in the formation of indole (2,3-benzopyrrole), the basis of many biologically active substances (e.g. serotonin, tryptophan).
The chemical reactions and pathways resulting in the formation of indole (2,3-benzopyrrole), the basis of many biologically active substances (e.g. serotonin, tryptophan).
The chemical reactions and pathways resulting in the formation of indole (2,3-benzopyrrole), the basis of many biologically active substances (e.g. serotonin, tryptophan).
The chemical reactions and pathways resulting in the breakdown of indole (2,3-benzopyrrole), the basis of many biologically active substances (e.g. serotonin, tryptophan).
The chemical reactions and pathways resulting in the breakdown of indole (2,3-benzopyrrole), the basis of many biologically active substances (e.g. serotonin, tryptophan).
The chemical reactions and pathways resulting in the breakdown of indole (2,3-benzopyrrole), the basis of many biologically active substances (e.g. serotonin, tryptophan).
The chemical reactions and pathways resulting in the formation of compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways resulting in the formation of compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways resulting in the formation of compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways resulting in the formation of compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways resulting in the formation of compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways resulting in the formation of compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways resulting in the breakdown of compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways resulting in the breakdown of compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways resulting in the breakdown of compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways resulting in the breakdown of compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways resulting in the breakdown of compounds that contain an indole (2,3-benzopyrrole) skeleton.
The chemical reactions and pathways resulting in the breakdown of indole-3-acetic acid, a compound which functions as a growth regulator in plants.
The chemical reactions and pathways resulting in the breakdown of indole-3-acetic acid, a compound which functions as a growth regulator in plants.
The chemical reactions and pathways resulting in the breakdown of indole-3-acetic acid, a compound which functions as a growth regulator in plants.
The chemical reactions and pathways resulting in the breakdown of indole-3-acetic acid, a compound which functions as a growth regulator in plants.
The chemical reactions and pathways resulting in the breakdown of indole-3-acetic acid, a compound which functions as a growth regulator in plants.
The chemical reactions and pathways resulting in the breakdown of indole-3-acetic acid, a compound which functions as a growth regulator in plants.
The chemical reactions and pathways resulting in the formation of melanins, pigments largely of animal origin. High molecular weight polymers of indole quinone, they are irregular polymeric structures and are divided into three groups: allomelanins in the plant kingdom and eumelanins and phaeomelanins in the animal kingdom.
The chemical reactions and pathways resulting in the formation of melanins, pigments largely of animal origin. High molecular weight polymers of indole quinone, they are irregular polymeric structures and are divided into three groups: allomelanins in the plant kingdom and eumelanins and phaeomelanins in the animal kingdom.
The chemical reactions and pathways resulting in the formation of melanins, pigments largely of animal origin. High molecular weight polymers of indole quinone, they are irregular polymeric structures and are divided into three groups: allomelanins in the plant kingdom and eumelanins and phaeomelanins in the animal kingdom.
The chemical reactions and pathways resulting in the formation of melanins, pigments largely of animal origin. High molecular weight polymers of indole quinone, they are irregular polymeric structures and are divided into three groups: allomelanins in the plant kingdom and eumelanins and phaeomelanins in the animal kingdom.
The chemical reactions and pathways involving ethanolamine (2-aminoethanol) and compounds derived from it.
The chemical reactions and pathways involving ethanolamine (2-aminoethanol) and compounds derived from it.
The chemical reactions and pathways involving ethanolamine (2-aminoethanol) and compounds derived from it.
The chemical reactions and pathways involving pigment, any general or particular coloring matter in living organisms, e.g. melanin.
The chemical reactions and pathways involving eye pigments, any general or particular coloring matter in living organisms, found or utilized in the eye.
The chemical reactions and pathways resulting in the breakdown of melatonin (N-acetyl-5-methoxytryptamine).
The chemical reactions and pathways resulting in the breakdown of melatonin (N-acetyl-5-methoxytryptamine).
The chemical reactions and pathways resulting in the breakdown of melatonin (N-acetyl-5-methoxytryptamine).
The chemical reactions and pathways resulting in the breakdown of melatonin (N-acetyl-5-methoxytryptamine).
The chemical reactions and pathways involving phenylethylamine, an amine with pharmacological properties similar to those of amphetamine, occurs naturally as a neurotransmitter in the brain, and is present in chocolate and oil of bitter almonds.
The chemical reactions and pathways resulting in the formation of phenylethylamine, an amine with pharmacological properties similar to those of amphetamine, occurs naturally as a neurotransmitter in the brain, and is present in chocolate and oil of bitter almonds.
The chemical reactions and pathways resulting in the formation of phenylethylamine, an amine with pharmacological properties similar to those of amphetamine, occurs naturally as a neurotransmitter in the brain, and is present in chocolate and oil of bitter almonds.
The chemical reactions and pathways resulting in the formation of phenylethylamine, an amine with pharmacological properties similar to those of amphetamine, occurs naturally as a neurotransmitter in the brain, and is present in chocolate and oil of bitter almonds.
The chemical reactions and pathways resulting in the formation of phenylethylamine, an amine with pharmacological properties similar to those of amphetamine, occurs naturally as a neurotransmitter in the brain, and is present in chocolate and oil of bitter almonds.
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.
The chemical reactions and pathways resulting in the formation of any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone.
The chemical reactions and pathways resulting in the formation of any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone.
The chemical reactions and pathways resulting in the formation of any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone.
The chemical reactions and pathways resulting in the formation of any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone.
The chemical reactions and pathways resulting in the breakdown of any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone.
The chemical reactions and pathways resulting in the breakdown of any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone.
The chemical reactions and pathways resulting in the breakdown of any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone.
The chemical reactions and pathways involving progesterone, a steroid hormone produced in the ovary which prepares and maintains the uterus for pregnancy. Also found in plants.
The chemical reactions and pathways resulting in the formation of arginine (2-amino-5-guanidinopentanoic acid) via the intermediate compound ornithine.
The chemical reactions and pathways resulting in the formation of arginine (2-amino-5-guanidinopentanoic acid) via the intermediate compound ornithine.
The chemical reactions and pathways resulting in the formation of arginine (2-amino-5-guanidinopentanoic acid) via the intermediate compound ornithine.
The chemical reactions and pathways resulting in the formation of any purine nucleoside, one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways resulting in the formation of any purine nucleoside, one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways resulting in the formation of any purine nucleoside, one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways resulting in the formation of any purine nucleoside, one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).
The chemical reactions and pathways resulting in the formation of deoxyguanosine, a nucleoside consisting of the base guanine and the sugar deoxyribose.
The chemical reactions and pathways resulting in the formation of deoxyguanosine, a nucleoside consisting of the base guanine and the sugar deoxyribose.
The chemical reactions and pathways resulting in the formation of deoxyguanosine, a nucleoside consisting of the base guanine and the sugar deoxyribose.
The chemical reactions and pathways resulting in the formation of deoxyguanosine, a nucleoside consisting of the base guanine and the sugar deoxyribose.
The chemical reactions and pathways involving deoxyguanosine, a nucleoside consisting of the base guanine and the sugar deoxyribose.
The chemical reactions and pathways resulting in the breakdown of any ribonucleoside, a nucleoside in which purine or pyrimidine base is linked to a ribose (beta-D-ribofuranose) molecule.
The chemical reactions and pathways resulting in the breakdown of any ribonucleoside, a nucleoside in which purine or pyrimidine base is linked to a ribose (beta-D-ribofuranose) molecule.
The chemical reactions and pathways resulting in the breakdown of any ribonucleoside, a nucleoside in which purine or pyrimidine base is linked to a ribose (beta-D-ribofuranose) molecule.
The chemical reactions and pathways resulting in the formation of any ribonucleoside, a nucleoside in which purine or pyrimidine base is linked to a ribose (beta-D-ribofuranose) molecule.
The chemical reactions and pathways resulting in the formation of any ribonucleoside, a nucleoside in which purine or pyrimidine base is linked to a ribose (beta-D-ribofuranose) molecule.
The chemical reactions and pathways resulting in the formation of any ribonucleoside, a nucleoside in which purine or pyrimidine base is linked to a ribose (beta-D-ribofuranose) molecule.
The chemical reactions and pathways resulting in the formation of any ribonucleoside, a nucleoside in which purine or pyrimidine base is linked to a ribose (beta-D-ribofuranose) molecule.
The chemical reactions and pathways resulting in the breakdown of ethylene (C2-H4, ethene), a simple hydrocarbon gas that can function in plants as a growth regulator.
The chemical reactions and pathways resulting in the breakdown of ethylene (C2-H4, ethene), a simple hydrocarbon gas that can function in plants as a growth regulator.
The chemical reactions and pathways resulting in the breakdown of ethylene (C2-H4, ethene), a simple hydrocarbon gas that can function in plants as a growth regulator.
The chemical reactions and pathways resulting in the breakdown of ethylene (C2-H4, ethene), a simple hydrocarbon gas that can function in plants as a growth regulator.
The chemical reactions and pathways resulting in the breakdown of ethylene (C2-H4, ethene), a simple hydrocarbon gas that can function in plants as a growth regulator.
The chemical reactions and pathways resulting in the breakdown of nopaline into other compounds, including proline.
The chemical reactions and pathways resulting in the breakdown of nopaline into other compounds, including proline.
The chemical reactions and pathways resulting in the breakdown of octopine into other compounds, including proline.
The chemical reactions and pathways resulting in the breakdown of octopine into other compounds, including proline.
Development of a photoreceptor, a cell that responds to incident electromagnetic radiation, particularly visible light.
Development of a photoreceptor, a cell that responds to incident electromagnetic radiation, particularly visible light.
Development of a photoreceptor, a sensory cell in the eye that reacts to the presence of light. They usually contain a pigment that undergoes a chemical change when light is absorbed, thus stimulating a nerve.
Development of photoreceptors, sensory cells that react to the presence of light, found in the ocellus.
Development of photoreceptors, sensory cells that react to the presence of light, found in the ocellus.
Compensating for the two-fold variation in X:autosome chromosome ratios between sexes by an inactivation of a proportion of genes on both of the X chromosomes of the XX sex, leading to a decrease, of half, of the levels of gene expression from these chromosomes. An example of this process is found in Caenorhabditis elegans.
The movement of a cell or organism in response to a stimulus in which the rate of movement depends on the intensity (rather than the direction) of the stimulus.
A response by a motile cell to a soluble chemical that involves an increase or decrease in speed (positive or negative orthokinesis) or of frequency of movement or a change in the frequency or magnitude of turning behavior (klinokinesis).
The movement of a cell or organism in response to a stimulus in which the speed or frequency of movement is increased or decreased.
The movement of a cell or organism in response to a stimulus in which the frequency or magnitude of turning behavior is altered.
Catalysis of the reduction of versicolorin A to sterigmatocystin.
A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells.
The process in which the anatomical structures of the ear are generated and organized. The ear is the sense organ in vertebrates that is specialized for the detection of sound, and the maintenance of balance. Includes the outer ear and middle ear, which collect and transmit sound waves; and the inner ear, which contains the organs of balance and (except in fish) hearing. Also includes the pinna, the visible part of the outer ear, present in some mammals.
The process in which the anatomical structures of the inner ear are generated and organized. The inner ear is the structure in vertebrates that contains the organs of balance and hearing. It consists of soft hollow sensory structures (the membranous labyrinth) containing fluid (endolymph) surrounded by fluid (perilymph) and encased in a bony cavity (the bony labyrinth). It consists of two chambers, the sacculus and utriculus, from which arise the cochlea and semicircular canals respectively.
The process in which the anatomical structures of the outer ear are generated and organized. The outer ear is the part of the ear external to the tympanum (eardrum). It consists of a tube (the external auditory meatus) that directs sound waves on to the tympanum, and may also include the external pinna, which extends beyond the skull.
The process in which the anatomical structures of the middle ear are generated and organized. The middle ear is the air-filled cavity within the skull of vertebrates that lies between the outer ear and the inner ear. It is linked to the pharynx (and therefore to outside air) via the Eustachian tube and in mammals contains the three ear ossicles, which transmit auditory vibrations from the outer ear (via the tympanum) to the inner ear (via the oval window).
The process whose specific outcome is the progression of a dentin-containing tooth over time, from its formation to the mature structure. A dentin-containing tooth is a hard, bony organ borne on the jaw or other bone of a vertebrate, and is composed mainly of dentin, a dense calcified substance, covered by a layer of enamel.
The process whose specific outcome is the progression of a dentin-containing tooth over time, from its formation to the mature structure. A dentin-containing tooth is a hard, bony organ borne on the jaw or other bone of a vertebrate, and is composed mainly of dentin, a dense calcified substance, covered by a layer of enamel.
The process whose specific outcome is the progression of a dentin-containing tooth over time, from its formation to the mature structure. A dentin-containing tooth is a hard, bony organ borne on the jaw or other bone of a vertebrate, and is composed mainly of dentin, a dense calcified substance, covered by a layer of enamel.
The process whose specific outcome is the progression of a dentin-containing tooth over time, from its formation to the mature structure. A dentin-containing tooth is a hard, bony organ borne on the jaw or other bone of a vertebrate, and is composed mainly of dentin, a dense calcified substance, covered by a layer of enamel.
The process whose specific outcome is the progression of a dentin-containing tooth over time, from its formation to the mature structure. A dentin-containing tooth is a hard, bony organ borne on the jaw or other bone of a vertebrate, and is composed mainly of dentin, a dense calcified substance, covered by a layer of enamel.
The process whose specific outcome is the progression of a tooth or teeth over time, from formation to the mature structure(s). A tooth is any hard bony, calcareous, or chitinous organ found in the mouth or pharynx of an animal and used in procuring or masticating food.
The process whose specific outcome is the progression of a tooth or teeth over time, from formation to the mature structure(s). A tooth is any hard bony, calcareous, or chitinous organ found in the mouth or pharynx of an animal and used in procuring or masticating food.
The process whose specific outcome is the progression of a tooth or teeth over time, from formation to the mature structure(s). A tooth is any hard bony, calcareous, or chitinous organ found in the mouth or pharynx of an animal and used in procuring or masticating food.
The process whose specific outcome is the progression of a tooth or teeth over time, from formation to the mature structure(s). A tooth is any hard bony, calcareous, or chitinous organ found in the mouth or pharynx of an animal and used in procuring or masticating food.
The process whose specific outcome is the progression of a tooth or teeth over time, from formation to the mature structure(s). A tooth is any hard bony, calcareous, or chitinous organ found in the mouth or pharynx of an animal and used in procuring or masticating food.
The process whose specific outcome is the progression of a tooth or teeth over time, from formation to the mature structure(s). A tooth is any hard bony, calcareous, or chitinous organ found in the mouth or pharynx of an animal and used in procuring or masticating food.
Any process that modulates the frequency, rate or extent of eye photoreceptor development.
Any process that activates or increases the frequency, rate or extent of eye photoreceptor development.
Any process that activates or increases the frequency, rate or extent of eye photoreceptor development.
Any process that activates or increases the frequency, rate or extent of eye photoreceptor development.
Any process that activates or increases the frequency, rate or extent of eye photoreceptor development.
Any process that activates or increases the frequency, rate or extent of eye photoreceptor development.
Any process that activates or increases the frequency, rate or extent of eye photoreceptor development.
Any process that stops, prevents, or reduces the frequency, rate or extent of eye photoreceptor development.
Any process that stops, prevents, or reduces the frequency, rate or extent of eye photoreceptor development.
Any process that stops, prevents, or reduces the frequency, rate or extent of eye photoreceptor development.
Any process that stops, prevents, or reduces the frequency, rate or extent of eye photoreceptor development.
Any process that stops, prevents, or reduces the frequency, rate or extent of eye photoreceptor development.
Any process that modulates the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that modulates the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that modulates the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that activates or increases the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that activates or increases the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that activates or increases the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that activates or increases the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that activates or increases the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that activates or increases the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that activates or increases the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that activates or increases the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of a tooth or teeth.
Any process that modulates the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages which are borne on the jaws, or on other bones in the walls of the mouth or pharynx of most vertebrates.
Any process that modulates the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages which are borne on the jaws, or on other bones in the walls of the mouth or pharynx of most vertebrates.
Any process that activates or increases the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages that are borne on the jaws, or on other bones in the walls of the mouth or pharynx of most vertebrates.
Any process that activates or increases the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages that are borne on the jaws, or on other bones in the walls of the mouth or pharynx of most vertebrates.
Any process that activates or increases the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages that are borne on the jaws, or on other bones in the walls of the mouth or pharynx of most vertebrates.
Any process that activates or increases the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages that are borne on the jaws, or on other bones in the walls of the mouth or pharynx of most vertebrates.
Any process that activates or increases the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages that are borne on the jaws, or on other bones in the walls of the mouth or pharynx of most vertebrates.
Any process that activates or increases the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages that are borne on the jaws, or on other bones in the walls of the mouth or pharynx of most vertebrates.
Any process that activates or increases the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages that are borne on the jaws, or on other bones in the walls of the mouth or pharynx of most vertebrates.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages which are borne on the jaws, or on other bones in the walls of the mouth or pharynx.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages which are borne on the jaws, or on other bones in the walls of the mouth or pharynx.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages which are borne on the jaws, or on other bones in the walls of the mouth or pharynx.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages which are borne on the jaws, or on other bones in the walls of the mouth or pharynx.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages which are borne on the jaws, or on other bones in the walls of the mouth or pharynx.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages which are borne on the jaws, or on other bones in the walls of the mouth or pharynx.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation and development of teeth, the hard, bony appendages which are borne on the jaws, or on other bones in the walls of the mouth or pharynx.
The process in which a relatively unspecialized cell acquires specialized features of a mechanoreceptor, a cell specialized to transduce mechanical stimuli and relay that information centrally in the nervous system.
The process in which a relatively unspecialized inner cell acquires specialized features of an auditory hair cell.
The process in which a relatively unspecialized inner cell acquires specialized features of an auditory hair cell.
The process in which a relatively unspecialized hemopoietic cell acquires specialized features of a gamma-delta T cell. A gamma-delta T cell is a T cell that expresses a gamma-delta T cell receptor complex.
The process in which a relatively unspecialized hemopoietic cell acquires specialized features of a gamma-delta T cell. A gamma-delta T cell is a T cell that expresses a gamma-delta T cell receptor complex.
The process in which a relatively unspecialized hemopoietic cell acquires specialized features of a gamma-delta T cell. A gamma-delta T cell is a T cell that expresses a gamma-delta T cell receptor complex.
The process in which a relatively unspecialized hemopoietic cell acquires specialized features of a gamma-delta T cell. A gamma-delta T cell is a T cell that expresses a gamma-delta T cell receptor complex.
The series of events in which a bacterial lipoprotein stimulus is received by a cell and converted into a molecular signal. Bacterial lipoproteins are lipoproteins characterized by the presence of conserved sequence motifs called pathogen-associated molecular patterns (PAMPs).
The series of events in which a bacterial lipoprotein stimulus is received by a cell and converted into a molecular signal. Bacterial lipoproteins are lipoproteins characterized by the presence of conserved sequence motifs called pathogen-associated molecular patterns (PAMPs).
The series of events in which a bacterial lipoprotein stimulus is received by a cell and converted into a molecular signal. Bacterial lipoproteins are lipoproteins characterized by the presence of conserved sequence motifs called pathogen-associated molecular patterns (PAMPs).
The series of events in which a bacterial lipoprotein stimulus is received by a cell and converted into a molecular signal. Bacterial lipoproteins are lipoproteins characterized by the presence of conserved sequence motifs called pathogen-associated molecular patterns (PAMPs).
The series of events in which a bacterial lipoprotein stimulus is received by a cell and converted into a molecular signal. Bacterial lipoproteins are lipoproteins characterized by the presence of conserved sequence motifs called pathogen-associated molecular patterns (PAMPs).
The series of events in which a triacylated bacterial lipoprotein stimulus is received by a cell and converted into a molecular signal. Triacylated bacterial lipoproteins are lipopeptides of bacterial origin containing a nonprotein moiety consisting of three acyl groups.
The series of events in which a triacylated bacterial lipoprotein stimulus is received by a cell and converted into a molecular signal. Triacylated bacterial lipoproteins are lipopeptides of bacterial origin containing a nonprotein moiety consisting of three acyl groups.
The series of events in which a triacylated bacterial lipoprotein stimulus is received by a cell and converted into a molecular signal. Triacylated bacterial lipoproteins are lipopeptides of bacterial origin containing a nonprotein moiety consisting of three acyl groups.
The series of events in which a diacylated bacterial lipopeptide stimulus is received by a cell and converted into a molecular signal. Diacylated bacterial lipoproteins are lipopeptides of bacterial origin containing a nonprotein moiety consisting of two acyl groups.
The series of events in which a diacylated bacterial lipopeptide stimulus is received by a cell and converted into a molecular signal. Diacylated bacterial lipoproteins are lipopeptides of bacterial origin containing a nonprotein moiety consisting of two acyl groups.
The series of events in which a diacylated bacterial lipopeptide stimulus is received by a cell and converted into a molecular signal. Diacylated bacterial lipoproteins are lipopeptides of bacterial origin containing a nonprotein moiety consisting of two acyl groups.
Interacting selectively and non-covalently with a lipopeptide containing a nonprotein moiety consisting of three acyl groups.
Interacting selectively and non-covalently with a lipopeptide containing a nonprotein moiety consisting of three acyl groups.
Interacting selectively and non-covalently with a lipopeptide containing a nonprotein moiety consisting of three acyl groups.
Interacting selectively and non-covalently with a lipopeptide containing a nonprotein moiety consisting of two acyl groups.
Interacting selectively and non-covalently with a lipopeptide containing a nonprotein moiety consisting of two acyl groups.
Interacting selectively and non-covalently with a lipopeptide containing a nonprotein moiety consisting of two acyl groups.
Catalysis of the hydrolysis of nonterminal peptide bonds in a polypeptide chain, occurring within a membrane.
The process of introducing a phosphate group to a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The process of introducing a phosphate group to a serine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine 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 introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of tumor necrosis factor, an inflammatory cytokine produced by macrophages/monocytes during acute inflammation and which is responsible for a diverse range of signaling events within cells, leading to necrosis or apoptosis.
The chemical reactions and pathways involving benzene, C6H6, a volatile, very inflammable liquid, contained in the naphtha produced by the destructive distillation of coal, from which it is separated by fractional distillation, or any of its derivatives.
The chemical reactions and pathways involving benzene, C6H6, a volatile, very inflammable liquid, contained in the naphtha produced by the destructive distillation of coal, from which it is separated by fractional distillation, or any of its derivatives.
The chemical reactions and pathways involving benzene, C6H6, a volatile, very inflammable liquid, contained in the naphtha produced by the destructive distillation of coal, from which it is separated by fractional distillation, or any of its derivatives.
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 detection of, or exposure to, an increase in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
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 detection of, or exposure to, an increase in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
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 detection of, or exposure to, a decrease in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
The chemical reactions and pathways resulting in the breakdown of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin; especially, the proteolytic cleavage of hemoglobin to yield free heme, peptides, and amino acids.
The chemical reactions and pathways resulting in the breakdown of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin; especially, the proteolytic cleavage of hemoglobin to yield free heme, peptides, and amino acids.
The chemical reactions and pathways resulting in the breakdown of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin; especially, the proteolytic cleavage of hemoglobin to yield free heme, peptides, and amino acids.
The chemical reactions and pathways resulting in the breakdown of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin; especially, the proteolytic cleavage of hemoglobin to yield free heme, peptides, and amino acids.
The chemical reactions and pathways resulting in the breakdown of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin; especially, the proteolytic cleavage of hemoglobin to yield free heme, peptides, and amino acids.
The chemical reactions and pathways resulting in the breakdown of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin; especially, the proteolytic cleavage of hemoglobin to yield free heme, peptides, and amino acids.
The chemical reactions and pathways resulting in the breakdown of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin; especially, the proteolytic cleavage of hemoglobin to yield free heme, peptides, and amino acids.
The chemical reactions and pathways resulting in the breakdown of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin; especially, the proteolytic cleavage of hemoglobin to yield free heme, peptides, and amino acids.
The chemical reactions and pathways resulting in the formation of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin.
The chemical reactions and pathways resulting in the formation of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin.
The chemical reactions and pathways resulting in the formation of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin.
The chemical reactions and pathways resulting in the formation of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin.
The chemical reactions and pathways resulting in the formation of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin.
The chemical reactions and pathways resulting in the formation of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin.
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 hydrogen peroxide (H2O2) stimulus.
The glycosylation of protein via peptidyl-arginine, omega-N-glycosyl-L-arginine.
The chemical reactions and pathways resulting in the formation of melibiose, the disaccharide 6-O-alpha-D-galactopyranosyl-D-glucose.
The chemical reactions and pathways resulting in the formation of melibiose, the disaccharide 6-O-alpha-D-galactopyranosyl-D-glucose.
The chemical reactions and pathways resulting in the formation of melibiose, the disaccharide 6-O-alpha-D-galactopyranosyl-D-glucose.
The chemical reactions and pathways resulting in the formation of melibiose, the disaccharide 6-O-alpha-D-galactopyranosyl-D-glucose.
The series of events leading to chemical and structural alterations of an existing cell wall that can result in loosening, increased extensibility or disassembly.
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a cell wall. Includes biosynthesis of constituent macromolecules, such as proteins and polysaccharides, and those macromolecular modifications that are involved in synthesis or assembly of the cellular component. A cell wall is the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
The series of events resulting in chemical or structural changes to existing cell walls and contribute to multidimensional cell growth.
The series of events resulting in chemical or structural changes to existing cell walls and contribute to multidimensional cell growth.
Any process that modulates the frequency, rate or extent of the light-dependent reaction of photosynthesis.
The stabilization of the photosystem II protein complex, resulting from the phosphorylation of its structural protein subunits, in a cell actively involved in photosynthesis.
The stabilization of the photosystem I protein complex, resulting from the phosphorylation of its structural protein subunits, in a cell actively involved in photosynthesis.
A developmental process, independent of morphogenetic (shape) change, that is required for a neuron to attain its fully functional state.
The process in which myelin sheaths are formed and maintained around neurons. Oligodendrocytes in the brain and spinal cord and Schwann cells in the peripheral nervous system wrap axons with compact layers of their plasma membrane. Adjacent myelin segments are separated by a non-myelinated stretch of axon called a node of Ranvier.
The enzymatic generation of superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species, by a cell in response to environmental stress, thereby mediating the activation of various stress-inducible signaling pathways.
A hexameric protein complex required for the initiation and regulation of DNA replication.
Modulates the activity of the enzyme eukaryotic elongation factor-2 kinase.
Binds to and increases the activity of the enzyme eukaryotic elongation factor-2 kinase.
The chemical reactions and pathways involving any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways involving any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways involving any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways involving any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways involving any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways involving any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the formation of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the formation of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the formation of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the formation of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the formation of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the formation of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the formation of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the formation of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the breakdown of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the breakdown of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the breakdown of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the breakdown of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the breakdown of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the breakdown of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
The chemical reactions and pathways resulting in the breakdown of any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid.
Catalysis of the reaction: (S)-2,3-epoxysqualene = alpha-amyrin. This reaction is a cyclization and rearrangement of (S)-2,3-epoxysqualene (2,3-oxidosqualene) into alpha-amyrin.
Interacting selectively and non-covalently with any hormone, naturally occurring substances secreted by specialized cells that affect the metabolism or behavior of other cells possessing functional receptors for the hormone.
A dimer consisting of an alpha and a beta-subunit that imports proteins with an NLS into the nucleus through a nuclear pore.
A complex which usually consists of three components, e.g. in Xenopus and yeast, the export receptor CRM1 (also known as exportin 1), the Ran protein and any RNA with a nuclear export sequence (NES). The complex acts to export RNA molecules with a NES from the nucleus through a nuclear pore.
A spherical, membrane-bounded organelle found in some anaerobic protozoa, which participates in ATP and molecular hydrogen formation.
A complex of three proteins, which in animals is approximately 150kDa and consists of the insulin-like growth factor (IGF), the insulin-like growth factor binding protein-3 (IGFBP-3), or -5 (IGFBP-5) and an acid-labile subunit (ALS). The complex plays a role in growth and development.
A complex of two proteins, which in animals is 50kDa and consists of the insulin-like growth factor (IGF) and one of the insulin-like growth factor binding protein-1 (IGFBP-1), -2 (IGFBP-2), -4 (IGFBP-4) and -6 (IGFBP-6). The complex plays a role in growth and development.
An immunoglobulin complex that is secreted into extracellular space and found in mucosal areas or other tissues or circulating in the blood or lymph. In its canonical form, a circulating immunoglobulin complex is composed of two identical heavy chains and two identical light chains, held together by disulfide bonds. Some forms of are polymers of the basic structure and contain additional components such as J-chain and the secretory component.
The chemical reactions and pathways involving retinol, one of the three compounds that makes up vitamin A.
The chemical reactions and pathways involving retinol, one of the three compounds that makes up vitamin A.
The chemical reactions and pathways involving retinol, one of the three compounds that makes up vitamin A.
The chemical reactions and pathways involving retinol, one of the three compounds that makes up vitamin A.
The chemical reactions and pathways involving retinol, one of the three compounds that makes up vitamin A.
The chemical reactions and pathways involving retinoic acid, one of the three components that makes up vitamin A.
The chemical reactions and pathways involving retinoic acid, one of the three components that makes up vitamin A.
The chemical reactions and pathways involving retinoic acid, one of the three components that makes up vitamin A.
The chemical reactions and pathways involving retinal, a compound that plays an important role in the visual process in most vertebrates. In the retina, retinal combines with opsins to form visual pigments. Retinal is one of the forms of vitamin A.
The chemical reactions and pathways involving retinal, a compound that plays an important role in the visual process in most vertebrates. In the retina, retinal combines with opsins to form visual pigments. Retinal is one of the forms of vitamin A.
The chemical reactions and pathways involving retinal, a compound that plays an important role in the visual process in most vertebrates. In the retina, retinal combines with opsins to form visual pigments. Retinal is one of the forms of vitamin A.
A protein complex that possesses DNA polymerase activity and is involved in template directed synthesis of DNA.
Catalysis of the reaction: a phospholipid + H2O = a lipid + phosphate.
Catalysis of the reaction: RPO-R' + H2O = RPOOH + R'H. This reaction is the hydrolysis of any phosphoric ester bond, any ester formed from orthophosphoric acid, O=P(OH)3.
Cytoplasmic organelles, spherical or oval in shape, that are bounded by a single membrane and contain oxidative enzymes, especially those utilizing hydrogen peroxide (H2O2).
A specialised tubular organelle, assembled in hexagonal bundles within an external membrane. Mannosomes are specific to molluscs and are thought to be involved in a general stress reaction.
Granule with a membranous, tubular internal structure, found primarily in mature neutrophil cells. Most are released into the extracellular fluid. Specific granules contain lactoferrin, lysozyme, vitamin B12 binding protein and elastase.
Primary lysosomal granule found in neutrophil granulocytes. Contains a wide range of hydrolytic enzymes and is released into the extracellular fluid.
Specialized secretory vesicle found in the cells of adrenal glands and various other organs, which is concerned with the synthesis, storage, metabolism, and secretion of epinephrine and norepinephrine.
The lipid bilayer surrounding a chromaffin granule, a specialized secretory vesicle found in the cells of adrenal glands and various other organs, which is concerned with the synthesis, storage, metabolism, and secretion of epinephrine and norepinephrine.
The enlarged, fluid filled nucleus of a primary oocyte, the development of which is suspended in prophase I of the first meiotic division between embryohood and sexual maturity.
Catalysis of the reaction: formyl-L-methionyl peptide + H2O = formate + methionyl peptide.
Catalysis of the reaction: formyl-L-methionyl peptide + H2O = formate + methionyl peptide.
Catalysis of the reaction: formyl-L-methionyl peptide + H2O = formate + methionyl peptide.
Cytoplasmic bead-like structures of animal cells, visible by electron microscope. Each granule is a functional unit with the biosynthesis and catabolism of glycogen being catalyzed by enzymes bound to the granule surface.
A membrane-bounded, cytoplasmic secretory granule found in enzyme-secreting cells and visible by light microscopy. Contain zymogen, an inactive enzyme precursor, often of a digestive enzyme.
The lipid bilayer surrounding a zymogen granule.
The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules.
The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules.
The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules.
The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules.
The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules.
The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules.
The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules.
Any biological process involved in the maintenance of an internal steady state.
Any biological process involved in the maintenance of an internal steady state.
Any biological process involved in the maintenance of an internal steady state.
Any biological process involved in the maintenance of an internal steady state.
Any biological process involved in the maintenance of an internal steady state.
Any biological process involved in the maintenance of an internal steady state.
Any biological process involved in the maintenance of an internal steady state.
Any biological process involved in the maintenance of an internal steady state.
Any biological process involved in the maintenance of an internal steady state.
Any process involved in the maintenance of an internal steady state of glucose within an organism or cell.
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 starvation stimulus, deprivation of nourishment.
Any process that results in a change in the behavior of an organism as a result of deprivation of nourishment.
The response of an organism to a perceived external threat.
The response of an organism to a perceived external threat.
The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
A membrane-bounded organelle, specialized for the storage and secretion of various substances (surfactant phospholipids, glycoproteins and acid phosphates) which are arranged in the form of tightly packed, concentric, membrane sheets or lamellae. Has some similar properties to, but is distinct from, a lysosome.
A membrane-bounded organelle, specialized for the storage and secretion of various substances (surfactant phospholipids, glycoproteins and acid phosphates) which are arranged in the form of tightly packed, concentric, membrane sheets or lamellae. Has some similar properties to, but is distinct from, a lysosome.
A membrane-bounded organelle, specialized for the storage and secretion of various substances (surfactant phospholipids, glycoproteins and acid phosphates) which are arranged in the form of tightly packed, concentric, membrane sheets or lamellae. Has some similar properties to, but is distinct from, a lysosome.
A membrane-bounded organelle, specialized for the storage and secretion of various substances (surfactant phospholipids, glycoproteins and acid phosphates) which are arranged in the form of tightly packed, concentric, membrane sheets or lamellae. Has some similar properties to, but is distinct from, a lysosome.
A protective, noncellular membrane that surrounds the eggs of various animals including insects and fish.
Portion of the cell formed during the process of bacterial sporulation that will ultimately become the core of the endospore. An endospore is a type of dormant cell that is resistant to adverse conditions.
A protective structure surrounding some fungi and bacteria, attached externally to the cell wall and composed primarily of polysaccharides. Capsules are highly organized structures that adhere strongly to cells and cannot be easily removed. Capsules play important roles in pathogenicity, preventing phagocytosis by other cells, adherance, and resistance to dessication.
A protective structure surrounding some fungi and bacteria, attached externally to the cell wall and composed primarily of polysaccharides. Capsules are highly organized structures that adhere strongly to cells and cannot be easily removed. Capsules play important roles in pathogenicity, preventing phagocytosis by other cells, adherance, and resistance to dessication.
Interacting selectively and non-covalently with a CD4, a receptor found on the surface of T cells, monocytes and macrophages.
Interacting selectively and non-covalently with a CD8, a receptor found on the surface of thymocytes and cytotoxic and suppressor T-lymphocytes.
A transmembrane protein complex composed of an MHC alpha chain and, in most cases, either an MHC class II beta chain or an invariant beta2-microglobin chain, and with or without a bound peptide, lipid, or polysaccharide antigen.
The chemical reactions and pathways involving paclitaxel, an alkaloid compound used as an anticancer treatment.
The chemical reactions and pathways involving paclitaxel, an alkaloid compound used as an anticancer treatment.
The chemical reactions and pathways involving paclitaxel, an alkaloid compound used as an anticancer treatment.
The chemical reactions and pathways resulting in the formation of paclitaxel, an alkaloid compound used as an anticancer treatment.
The chemical reactions and pathways resulting in the formation of paclitaxel, an alkaloid compound used as an anticancer treatment.
The chemical reactions and pathways resulting in the formation of paclitaxel, an alkaloid compound used as an anticancer treatment.
The chemical reactions and pathways resulting in the formation of paclitaxel, an alkaloid compound used as an anticancer treatment.
The chemical reactions and pathways resulting in the formation of paclitaxel, an alkaloid compound used as an anticancer treatment.
The chemical reactions and pathways resulting in the formation of paclitaxel, an alkaloid compound used as an anticancer treatment.
The chemical reactions and pathways involving poly-hydroxybutyrate (PHB), a polymer of beta-hydroxybutyrate and a common storage material of prokaryotic cells.
The chemical reactions and pathways involving poly-hydroxybutyrate (PHB), a polymer of beta-hydroxybutyrate and a common storage material of prokaryotic cells.
The chemical reactions and pathways involving poly-hydroxybutyrate (PHB), a polymer of beta-hydroxybutyrate and a common storage material of prokaryotic cells.
The chemical reactions and pathways resulting in the formation of poly-hydroxybutyrate (PHB), a polymer of beta-hydroxybutyrate and a common storage material of prokaryotic cells.
The chemical reactions and pathways resulting in the formation of poly-hydroxybutyrate (PHB), a polymer of beta-hydroxybutyrate and a common storage material of prokaryotic cells.
The chemical reactions and pathways resulting in the formation of poly-hydroxybutyrate (PHB), a polymer of beta-hydroxybutyrate and a common storage material of prokaryotic cells.
The chemical reactions and pathways resulting in the formation of poly-hydroxybutyrate (PHB), a polymer of beta-hydroxybutyrate and a common storage material of prokaryotic cells.
The chemical reactions and pathways resulting in the formation of poly-hydroxybutyrate (PHB), a polymer of beta-hydroxybutyrate and a common storage material of prokaryotic cells.
The chemical reactions and pathways resulting in the formation of poly-hydroxybutyrate (PHB), a polymer of beta-hydroxybutyrate and a common storage material of prokaryotic cells.
The chemical reactions and pathways involving poly(3-hydroxyalkanoates), polyesters of 3-hydroxyacids produced as intracellular granules by a large variety of bacteria.
The chemical reactions and pathways involving poly(3-hydroxyalkanoates), polyesters of 3-hydroxyacids produced as intracellular granules by a large variety of bacteria.
The chemical reactions and pathways involving poly(3-hydroxyalkanoates), polyesters of 3-hydroxyacids produced as intracellular granules by a large variety of bacteria.
The chemical reactions and pathways resulting in the formation of poly(3-hydroxyalkanoates), polyesters of 3-hydroxyacids produced as intracellular granules by a large variety of bacteria.
The chemical reactions and pathways resulting in the formation of poly(3-hydroxyalkanoates), polyesters of 3-hydroxyacids produced as intracellular granules by a large variety of bacteria.
The chemical reactions and pathways resulting in the formation of poly(3-hydroxyalkanoates), polyesters of 3-hydroxyacids produced as intracellular granules by a large variety of bacteria.
The chemical reactions and pathways resulting in the formation of poly(3-hydroxyalkanoates), polyesters of 3-hydroxyacids produced as intracellular granules by a large variety of bacteria.
The chemical reactions and pathways resulting in the formation of poly(3-hydroxyalkanoates), polyesters of 3-hydroxyacids produced as intracellular granules by a large variety of bacteria.
The chemical reactions and pathways resulting in the formation of poly(3-hydroxyalkanoates), polyesters of 3-hydroxyacids produced as intracellular granules by a large variety of bacteria.
The membrane surrounding the outer segment of a vertebrate photoreceptor.
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction is not directly coupled to any other reaction.
Enables the transfer of an ion from one side of a membrane to the other, driven by the reaction: ATP + H2O = ADP + phosphate.
A large lipoprotein particle (diameter 75-1200 nm) composed of a central core of triglycerides and cholesterol surrounded by a protein-phospholipid coating. The proteins include one molecule of apolipoprotein B-48 and may include a variety of apolipoproteins, including APOAs, APOCs and APOE. Chylomicrons are found in blood or lymph and carry lipids from the intestines into other body tissues.
The deposition of a plug of sperm or other gelatinous material into the opening of the vulva by a male at the termination of copulation. Probably acts to prevent subsequent matings by other males.
The deposition of a plug of sperm or other gelatinous material into the opening of the vulva by a male at the termination of copulation. Probably acts to prevent subsequent matings by other males.
The deposition of a plug of sperm or other gelatinous material into the opening of the vulva by a male at the termination of copulation. Probably acts to prevent subsequent matings by other males.
The deposition of a plug of sperm or other gelatinous material into the opening of the vulva by a male at the termination of copulation. Probably acts to prevent subsequent matings by other males.
Coarse, bluish-black staining cytoplasmic granules, bounded by a plasma membrane and found in mast cells and basophils. Contents include histamine, heparin, chondroitin sulfates, chymase and tryptase.
Any process that results in a change in the behavior of an organism as a result of deprivation of water.
Any process that results in a change in the behavior of an organism as a result of deprivation of water.
Any process that results in a change in the behavior of an organism as a result of deprivation of water.
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 water.
Any process involved in the maintenance of an internal steady state of cholesterol within an organism or cell.
Any process involved in the maintenance of an internal steady state of cholesterol within an organism or cell.
Any process involved in the maintenance of an internal steady state of cholesterol within an organism or cell.
Any process involved in the maintenance of an internal steady state of cholesterol within an organism or cell.
The cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair; one of the collection or mass of filaments growing from the skin of an animal, and forming a covering for a part of the head or for any part or the whole of the body.
Any process that modulates the frequency, rate or extent of the cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair.
Any process that activates or increases the frequency, rate or extent of the cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair.
Any process that activates or increases the frequency, rate or extent of the cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair.
Any process that activates or increases the frequency, rate or extent of the cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair.
Any process that activates or increases the frequency, rate or extent of the cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair.
Any process that activates or increases the frequency, rate or extent of the cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair.
Any process that stops, prevents, or reduces the frequency, rate or extent of the cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair.
Any process that stops, prevents, or reduces the frequency, rate or extent of the cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair.
Any process that stops, prevents, or reduces the frequency, rate or extent of the cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair.
Any process that stops, prevents, or reduces the frequency, rate or extent of the cyclical phases of growth (anagen), regression (catagen), quiescence (telogen), and shedding (exogen) in the life of a hair.
The regression phase of the hair cycle during which cell proliferation ceases, the hair follicle shortens, and an anchored club hair is produced.
The shedding phase of the hair cycle.
The resting phase of hair cycle.
The growth phase of the hair cycle. Lasts, for example, about 3 to 6 years for human scalp hair.
Any complex of actin, myosin, and accessory proteins.
Any complex of actin, myosin, and accessory proteins.
The myosin part of any complex of actin, myosin, and accessory proteins.
The actin part of any complex of actin, myosin, and accessory proteins.
The region of a chloroplast to which the DNA is confined.
The region of a mitochondrion to which the DNA is confined.
The region of a plastid to which the DNA is confined.
The region of a proplastid to which the DNA is confined.
A circular DNA molecule containing chloroplast encoded genes.
Underdeveloped thylakoids found in etioplasts, lacking competent photosynthetic membranes. Rapidly develop into mature thylakoids in the presence of light.
The membrane of prothylakoids, underdeveloped thylakoids found in etioplasts, lacking competent photosynthetic membranes.
The pigmented membrane of any thylakoid.
The peripheral segment of respiratory chain complex I located in the mitochondrion. Respiratory chain complex I is an enzyme of the respiratory chain, consisting of at least 34 polypeptide chains. The electrons of NADH enter the chain at this complex. The complete complex is L-shaped, with a horizontal arm lying in the membrane and a vertical arm that projects into the matrix.
The peripheral segment of respiratory chain complex I located in the mitochondrion. Respiratory chain complex I is an enzyme of the respiratory chain, consisting of at least 34 polypeptide chains. The electrons of NADH enter the chain at this complex. The complete complex is L-shaped, with a horizontal arm lying in the membrane and a vertical arm that projects into the matrix.
The mitochondrial membrane segment of respiratory chain complex I. Respiratory chain complex I is an enzyme of the respiratory chain, consisting of at least 34 polypeptide chains. The electrons of NADH enter the chain at this complex. The complete complex is L-shaped, with a horizontal arm lying in the membrane and a vertical arm that projects into the matrix.
Combining with ecdysis-triggering hormone to initiate a change in cell activity.
Combining with ecdysis-triggering hormone to initiate a change in cell activity.
The initiation of the activity of the inactive enzyme JUN kinase kinase kinase (JNKKK) activity.
The initiation of the activity of the inactive enzyme JUN kinase kinase kinase (JNKKK) activity.
Catalysis of the phosphorylation and activation of JUN kinase kinase kinases (JNKKKs).
Interacting selectively and non-covalently with the lateral surface of major histocompatibility complex class II molecules.
Interacting selectively and non-covalently with the antigen binding groove of major histocompatibility complex class II molecules.
Any process that mediates the adoption of a specific fate by a cell.
Any process that activates or enables a cell to adopt a specific fate.
Any process that activates or enables a cell to adopt a specific fate.
Any process that activates or enables a cell to adopt a specific fate.
Any process that activates or enables a cell to adopt a specific fate.
Any process that activates or enables a cell to adopt a specific fate.
Any process that modulates the frequency, rate or extent of mesoderm cell fate specification.
Any process that stops, prevents, or reduces the frequency, rate or extent of mesoderm cell fate specification.
Any process that stops, prevents, or reduces the frequency, rate or extent of mesoderm cell fate specification.
Any process that stops, prevents, or reduces the frequency, rate or extent of mesoderm cell fate specification.
Any process that stops, prevents, or reduces the frequency, rate or extent of mesoderm cell fate specification.
Any process that stops, prevents, or reduces the frequency, rate or extent of mesoderm cell fate specification.
Any process that mediates the specification of a cell into an endoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an endoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an endoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an endoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an endoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an endoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an endoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an endoderm cell.
Any process that mediates the specification of a cell into an ectoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an ectoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an ectoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an ectoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an ectoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an ectoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an ectoderm cell.
Any process that restricts, stops or prevents a cell from specifying into an ectoderm cell.
The process in which a cell becomes capable of differentiating autonomously into an auditory hair cell in an environment that is neutral with respect to the developmental pathway; upon specification, the cell fate can be reversed.
The process in which a cell becomes capable of differentiating autonomously into an auditory hair cell regardless of its environment; upon determination, the cell fate cannot be reversed.
Any process that mediates the specification of a cell into an auditory hair cell.
Any process that mediates the specification of a cell into an auditory hair cell.
The process in which a relatively unspecialized cell acquires the specialized features of a retinal cone cell.
The process in which a cell becomes capable of differentiating autonomously into a retinal cone cell regardless of its environment; upon determination, the cell fate cannot be reversed.
The process in which a cell becomes capable of differentiating autonomously into a retinal cone cell in an environment that is neutral with respect to the developmental pathway; upon specification, the cell fate can be reversed.
Any process that mediates the specification of a cell into a retinal cone cell.
The process in which a relatively unspecialized cell acquires the specialized features of a compound eye cone cell, a cone-shaped cell, that focuses light in a compound eye.
The process in which the cone cells of the compound eye, the lens-secreting cells in the ommatidia, adopt pathways of differentiation that lead to the establishment of their distinct cell type.
The process in which a cell becomes capable of differentiating autonomously into a compound eye cone cell in an environment that is neutral with respect to the developmental pathway; upon specification, the cell fate can be reversed.
The process in which a cell becomes capable of differentiating autonomously into a compound eye cone cell regardless of its environment; upon determination, the cell fate cannot be reversed.
Any process that mediates the specification of a cell into a compound eye cone cell.
Any process that restricts, stops or prevents a cell from specifying into a compound eye cone cell.
Any process that restricts, stops or prevents a cell from specifying into a compound eye cone cell.
Any process that restricts, stops or prevents a cell from specifying into a compound eye cone cell.
Any process that restricts, stops or prevents a cell from specifying into a compound eye cone cell.
Any process that restricts, stops or prevents a cell from specifying into a compound eye cone cell.
Any process that restricts, stops or prevents a cell from specifying into a compound eye cone cell.
The process in which a cell becomes committed to becoming a cardioblast. A cardioblast is a cardiac precursor cell. It is a cell that has been committed to a cardiac fate, but will undergo more cell division rather than terminally differentiating.
The process in which a cell becomes capable of differentiating autonomously into a cardioblast cell in an environment that is neutral with respect to the developmental pathway; upon specification, the cell fate can be reversed. A cardioblast is a cardiac precursor cell. It is a cell that has been committed to a cardiac fate, but will undergo more cell division rather than terminally differentiating.
Any process that mediates the specification of a cell into a cardioblast. A cardioblast is a cardiac precursor cell. It is a cell that has been committed to a cardiac fate, but will undergo more cell division rather than terminally differentiating.
The process in which a hemocyte precursor cell acquires the characteristics of a crystal cell, a class of cells that contain crystalline inclusions and are involved in the melanization of pathogenic material in the hemolymph.
Any process that modulates the frequency, rate or extent of crystal cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of crystal cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of crystal cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of crystal cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of crystal cell differentiation.
Any process that activates or increases the frequency, rate or extent of crystal cell differentiation.
Any process that activates or increases the frequency, rate or extent of crystal cell differentiation.
Any process that activates or increases the frequency, rate or extent of crystal cell differentiation.
Any process that activates or increases the frequency, rate or extent of crystal cell differentiation.
Any process that activates or increases the frequency, rate or extent of crystal cell differentiation.
The process in which a relatively unspecialized cell acquires specialized features of a muscle cell.
The process in which the cellular identity of muscle cells is acquired and determined.
The process in which a cell becomes capable of differentiating autonomously into a muscle cell in an environment that is neutral with respect to the developmental pathway; upon specification, the cell fate can be reversed.
The beginning of development of the breasts in the female.
The beginning of the menstrual cycle; the first menstrual cycle in an individual.
Cessation of menstruation, occurring in (e.g.) the human female usually around the age of 50.
The type of sexual cycle seen in females, often with physiologic changes in the endometrium that recur at regular intervals during the reproductive years.
The series of molecular signals mediated by follicle-stimulating hormone.
The series of molecular signals mediated by follicle-stimulating hormone.
The series of molecular signals mediated by follicle-stimulating hormone.
The series of molecular signals mediated by luteinizing hormone.
The regulated release of progesterone, a steroid hormone, by the corpus luteum of the ovary and by the placenta.
The regrowth of the endometrium and blood vessels in the uterus following menstruation, resulting from a rise in progesterone levels.
The cyclic, physiologic discharge through the vagina of blood and endometrial tissues from the nonpregnant uterus.
The sloughing of the endometrium and blood vessels during menstruation that results from a drop in progesterone levels.
The process in which a relatively unspecialized cell acquires specialized features of a photoreceptor cell found in the ocellus.
The process in which the developmental fate of a cell becomes restricted such that it will develop into an eye photoreceptor cell. A photoreceptor cell is a cell that responds to incident electromagnetic radiation. Different classes of photoreceptor have different spectral sensitivities and express different photosensitive pigments.
The process in which the developmental fate of a cell becomes restricted such that it will develop into photoreceptor cell in the ocellus. A photoreceptor cell is a cell that responds to incident electromagnetic radiation. Different classes of photoreceptor have different spectral sensitivities and express different photosensitive pigments.
A heterodimeric enzyme complex, usually composed of an alpha and beta chain. Functions in the TCA cycle, hydrolyzing succinyl-CoA into succinate and CoA, thereby forming ATP or GTP.
A process in which planktonically growing microorganisms grow at a liquid-air interface or on a solid substrate under the flow of a liquid and produce extracellular polymers that facilitate matrix formation, resulting in a change in the organisms' growth rate and gene transcription.
Female behaviors associated with the care and rearing of offspring.
Male behaviors associated with the care and rearing offspring.
The expulsion of seminal fluid, thick white fluid containing spermatozoa, from the male genital tract.
The aggregation, arrangement and bonding together of proteins on DNA or RNA to form the complex that mediates dosage compensation on one or more X chromosomes.
The aggregation, arrangement and bonding together of proteins on DNA to form the complex that mediates dosage compensation on both X chromosomes in the monogametic sex, ultimately resulting in a two-fold reduction in transcription from these chromosomes. An example of this process is found in Caenorhabditis elegans.
The lipid bilayer associated with a plasma membrane-derived chromatophore; surrounds chromatophores that form complete vesicles.
Discrete structures that partition the water-insoluble portion of the yolk of oocytes and ova, which may or may not be membrane enclosed.
Soluble complex of the mitochondrial intermembrane space composed of various combinations of small Tim proteins; acts as a protein transporter to guide proteins to the Tim22 complex for insertion into the mitochondrial inner membrane.
Protease complex of the mitochondrial inner membrane, consisting of at least two subunits, involved in processing of both nuclear- and mitochondrially-encoded proteins targeted to the intermembrane space.
A multi-subunit complex embedded in the mitochondrial inner membrane that mediates the inner membrane insertion of multi-transmembrane spanning proteins that contain internal targeting elements. In yeast cells, TIM22 is a 300-kDa complex, consisting of four membrane integral subunits, Tim22, Tim54, Tim18 and Sdh3, and a peripheral chaperone complex consisting of the small TIM proteins, Tim9-Tim10-Tim12.
A multi-subunit complex embedded in the mitochondrial inner membrane that mediates the inner membrane insertion of multi-transmembrane spanning proteins that contain internal targeting elements. In yeast cells, TIM22 is a 300-kDa complex, consisting of four membrane integral subunits, Tim22, Tim54, Tim18 and Sdh3, and a peripheral chaperone complex consisting of the small TIM proteins, Tim9-Tim10-Tim12.
A multi-subunit complex embedded in the mitochondrial inner membrane that mediates the inner membrane insertion of multi-transmembrane spanning proteins that contain internal targeting elements. In yeast cells, TIM22 is a 300-kDa complex, consisting of four membrane integral subunits, Tim22, Tim54, Tim18 and Sdh3, and a peripheral chaperone complex consisting of the small TIM proteins, Tim9-Tim10-Tim12.
The change in morphology and behavior of alpha-beta T cells resulting from exposure to a superantigen, a microbial antigen with an extremely potent activating effect on T cells that bear a specific variable region.
The change in morphology and behavior of alpha-beta T cells resulting from exposure to a superantigen, a microbial antigen with an extremely potent activating effect on T cells that bear a specific variable region.
The change in morphology and behavior of alpha-beta T cells resulting from exposure to a superantigen, a microbial antigen with an extremely potent activating effect on T cells that bear a specific variable region.
The chemical reactions and pathways involving thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways involving thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways involving thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways involving thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways involving thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways involving thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways involving thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways involving thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), and related compounds.
The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), and related compounds.
The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), and related compounds.
The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), and related compounds.
The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), and related compounds.
The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), and related compounds.
The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), and related compounds.
The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), and related compounds.
The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), and related compounds.
The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), and related compounds.
The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), and related compounds.
The chemical reactions and pathways resulting in the breakdown of thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways resulting in the breakdown of thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways resulting in the breakdown of thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways resulting in the breakdown of thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways resulting in the breakdown of thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways resulting in the breakdown of thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways resulting in the breakdown of thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways resulting in the breakdown of thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways resulting in the breakdown of thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways resulting in the breakdown of thiamine (vitamin B1), and compounds derived from it.
The chemical reactions and pathways involving a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways involving a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways involving a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways involving a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways involving a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the formation of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the formation of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the formation of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the formation of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the formation of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the formation of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the formation of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the formation of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the breakdown of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the breakdown of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the breakdown of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the breakdown of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the breakdown of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the breakdown of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
The chemical reactions and pathways resulting in the breakdown of a flavin, any derivative of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton, with a substituent on the 10 position.
A large protein complex, containing around 8-10 subunits in yeast, including Duo1p, Dam1p, Dad1p and Ask1p. The complex forms part of the kinetochore, associates with microtubules when the kinetochore attaches to the spindle, and plays a role in spindle attachment, chromosome segregation and spindle stability.
A large protein complex, containing around 8-10 subunits in yeast, including Duo1p, Dam1p, Dad1p and Ask1p. The complex forms part of the kinetochore, associates with microtubules when the kinetochore attaches to the spindle, and plays a role in spindle attachment, chromosome segregation and spindle stability.
A large protein complex, containing around 8-10 subunits in yeast, including Duo1p, Dam1p, Dad1p and Ask1p. The complex forms part of the kinetochore, associates with microtubules when the kinetochore attaches to the spindle, and plays a role in spindle attachment, chromosome segregation and spindle stability.
A large protein complex, containing around 8-10 subunits in yeast, including Duo1p, Dam1p, Dad1p and Ask1p. The complex forms part of the kinetochore, associates with microtubules when the kinetochore attaches to the spindle, and plays a role in spindle attachment, chromosome segregation and spindle stability.
A large protein complex, containing around 8-10 subunits in yeast, including Duo1p, Dam1p, Dad1p and Ask1p. The complex forms part of the kinetochore, associates with microtubules when the kinetochore attaches to the spindle, and plays a role in spindle attachment, chromosome segregation and spindle stability.
A large protein complex, containing around 8-10 subunits in yeast, including Duo1p, Dam1p, Dad1p and Ask1p. The complex forms part of the kinetochore, associates with microtubules when the kinetochore attaches to the spindle, and plays a role in spindle attachment, chromosome segregation and spindle stability.
A process that solubilizes fibrin in the bloodstream of a multicellular organism, chiefly by the proteolytic action of plasmin.
Interacting selectively and non-covalently with a PH domain (pleckstrin homology) of a protein, a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton.
The chemical reactions and pathways involving D-xylose, a naturally occurring plant polysaccharide.
The process, occurring in the embryo, by which the anatomical structures of the digit are generated and organized. A digit is one of the terminal divisions of an appendage, such as a finger or toe.
A specialized area of membrane of the axon terminal that faces the plasma membrane of the neuron or muscle fiber with which the axon terminal establishes a synaptic junction; many synaptic junctions exhibit structural presynaptic characteristics, such as conical, electron-dense internal protrusions, that distinguish it from the remainder of the axon plasma membrane.
A specialized area of membrane of the axon terminal that faces the plasma membrane of the neuron or muscle fiber with which the axon terminal establishes a synaptic junction; many synaptic junctions exhibit structural presynaptic characteristics, such as conical, electron-dense internal protrusions, that distinguish it from the remainder of the axon plasma membrane.
A membrane-bounded plant organelle found in the developing endosperm, contains storage proteins.
Catalysis of the reaction: ATP + NADH = ADP + 2 H(+) + NADPH.
Catalysis of the reaction: ATP + NADH = ADP + 2 H(+) + NADPH.
Catalysis of the reaction: ATP + NADH = ADP + 2 H(+) + NADPH.
Catalysis of the reaction: ATP + NADH = ADP + 2 H(+) + NADPH.
The chemical reactions and pathways resulting in the breakdown of a drug, a substance used in the diagnosis, treatment or prevention of a disease.
The chemical reactions and pathways resulting in the breakdown of a drug, a substance used in the diagnosis, treatment or prevention of a disease.
The chemical reactions and pathways resulting in the breakdown of a drug, a substance used in the diagnosis, treatment or prevention of a disease.
The chemical reactions and pathways resulting in the breakdown of a drug that has originated externally to the cell or organism.
The chemical reactions and pathways resulting in the breakdown of a drug that has originated externally to the cell or organism.
The chemical reactions and pathways resulting in the breakdown of a drug that has originated externally to the cell or organism.
The chemical reactions and pathways resulting in the breakdown of a drug that has originated internally within the cell or organism.
The chemical reactions and pathways resulting in the breakdown of a drug that has originated internally within the cell or organism.
The chemical reactions and pathways resulting in the breakdown of a drug that has originated internally within the cell or organism.
The chemical reactions and pathways resulting in the breakdown of an antibiotic that has originated externally to the cell or organism.
The chemical reactions and pathways resulting in the breakdown of an antibiotic that has originated externally to the cell or organism.
The chemical reactions and pathways resulting in the breakdown of an antibiotic that has originated externally to the cell or organism.
The chemical reactions and pathways resulting in the breakdown of an antibiotic that has originated internally within the cell or organism.
The chemical reactions and pathways resulting in the breakdown of an antibiotic that has originated internally within the cell or organism.
The chemical reactions and pathways resulting in the breakdown of an antibiotic that has originated internally within the cell or organism.
The chemical reactions and pathways involving hydrogen peroxide (H2O2), a potentially harmful byproduct of aerobic cellular respiration which can cause damage to DNA.
The chemical reactions and pathways involving hydrogen peroxide (H2O2), a potentially harmful byproduct of aerobic cellular respiration which can cause damage to DNA.
The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).
The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).
The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).
The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).
The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).
The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).
The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).
The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).
The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).
The cycle from wakefulness through an orderly succession of sleep states and stages that occurs on an approximately 24 hour rhythm.
The part of the circadian sleep/wake cycle where the organism is not asleep.
A stage in the circadian sleep cycle during which dreams occur and the body undergoes marked changes including rapid eye movement, loss of reflexes, and increased pulse rate and brain activity.
All sleep stages in the circadian sleep/wake cycle other than REM sleep. These stages are characterized by a slowing of brain waves and other physiological functions.
Any process that modulates the frequency, rate or extent of the circadian sleep/wake cycle.
Any process in which an organism enters and maintains a period of dormancy in which to pass the winter. It is characterized by narcosis and by sharp reduction in body temperature and metabolic activity and by a depression of vital signs.
Any process in which an organism enters and maintains a period of dormancy, similar to hibernation, but that occurs during the summer. It insulates against heat to prevent the harmful effects of the season.
Any process that modulates the frequency, rate or extent of a circadian rhythm. A circadian rhythm is a biological process in an organism that recurs with a regularity of approximately 24 hours.
Any process that activates or increases the frequency, rate or extent of a circadian rhythm behavior.
Any process that activates or increases the frequency, rate or extent of a circadian rhythm behavior.
Any process that activates or increases the frequency, rate or extent of a circadian rhythm behavior.
Any process that activates or increases the frequency, rate or extent of a circadian rhythm behavior.
Any process that activates or increases the frequency, rate or extent of a circadian rhythm behavior.
Any process that stops, prevents, or reduces the frequency, rate or extent of a circadian rhythm behavior.
Any process that stops, prevents, or reduces the frequency, rate or extent of a circadian rhythm behavior.
Any process that stops, prevents, or reduces the frequency, rate or extent of a circadian rhythm behavior.
Any process that stops, prevents, or reduces the frequency, rate or extent of a circadian rhythm behavior.
The specific behavior of an organism relating to the intake of food, any substance (usually solid) that can be metabolized by an organism to give energy and build tissue.
The specific behavior of an organism relating to the intake of liquids, especially water.
Extremely large, unmyelinated axon found in invertebrates. Has high conduction speeds and is usually involved in panic or escape responses.
The chemical reactions and pathways resulting in the breakdown of long-chain fatty acids, a fatty acid with a chain length between C13 and C22.
The chemical reactions and pathways resulting in the breakdown of long-chain fatty acids, a fatty acid with a chain length between C13 and C22.
The chemical reactions and pathways resulting in the breakdown of long-chain fatty acids, a fatty acid with a chain length between C13 and C22.
The chemical reactions and pathways resulting in the formation of long-chain fatty acids, any fatty acid with a chain length between C13 and C22.
The chemical reactions and pathways resulting in the formation of long-chain fatty acids, any fatty acid with a chain length between C13 and C22.
The chemical reactions and pathways resulting in the formation of long-chain fatty acids, any fatty acid with a chain length between C13 and C22.
The chemical reactions and pathways resulting in the formation of long-chain fatty acids, any fatty acid with a chain length between C13 and C22.
The chemical reactions and pathways resulting in the breakdown of a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways resulting in the breakdown of a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways resulting in the breakdown of a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways resulting in the breakdown of a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways resulting in the formation of a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways resulting in the formation of a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways resulting in the formation of a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways resulting in the formation of a fatty acid which has a chain length greater than C22.
The chemical reactions and pathways resulting in the formation of a fatty acid which has a chain length greater than C22.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving sulfur, the nonmetallic element sulfur or compounds that contain sulfur.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving sulfur, the nonmetallic element sulfur or compounds that contain sulfur.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving sulfur, the nonmetallic element sulfur or compounds that contain sulfur.
A cell or part of the cell that constitutes an early developmental stage of a spore, a small reproductive body that is highly resistant to desiccation and heat and is capable of growing into a new organism, produced especially by certain bacteria, fungi, algae, and nonflowering plants.
An immature spore undergoing development. The spore usually consists of nucleic acid, prospore membrane(s) that encase the nucleic acid, and ultimately a cell wall that covers the membrane(s). This type of spore is observed in ascospore-forming fungi.
An enzyme complex which in humans and yeast consists of at least five proteins; for example, the complex contains GAA1, GPI8, PIG-S, PIG-U, and PIG-T in human, and Gaa1p, Gab1p, Gpi8p, Gpi16p, and Gpi17p in yeast. Catalyzes the posttranslational attachment of the carboxyl-terminus of a precursor protein to a GPI-anchor.
The movement of nucleosomes along a DNA fragment.
Catalysis of the hydroxylation of an ecdysteroid at carbon position 22.
Catalysis of the hydroxylation of an ecdysteroid at carbon position 2.
The series of events required to receive a stimulus indicating DNA damage has occurred and convert it to a molecular signal.
The series of events required to receive a stimulus indicating DNA damage has occurred and convert it to a molecular signal.
A cascade of processes induced by the detection of DNA damage within a cell.
A cascade of processes induced by the detection of DNA damage within a cell.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage, and ends when the execution phase of apoptosis is triggered.
A cascade of processes initiated in response to the detection of DNA damage, and resulting in the induction of transcription.
The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP.
The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP in the plasma membrane.
The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP, as it occurs in the mitochondrial inner membrane or chloroplast thylakoid membrane.
The transfer of electrons through a series of electron donors and acceptors, generating energy that is ultimately used for synthesis of ATP, as it occurs in the mitochondrial inner membrane or chloroplast thylakoid membrane.
The transport of protons across a mitochondrial membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
The transport of protons across the plasma membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
The process in which the 3'-terminal CCA of a tRNA is removed and restored. This often happens to uncharged tRNA.
Cleavage of the 3'-end of the pre-tRNA as part of the process of generating the mature 3'-end of the tRNA; may involve endonucleolytic or exonucleolytic cleavage, or both.
Cleavage of the 3'-end of the pre-tRNA as part of the process of generating the mature 3'-end of the tRNA; may involve endonucleolytic or exonucleolytic cleavage, or both.
The process in which the 3' end of a pre-tRNA molecule is converted to that of a mature tRNA.
Catalysis of the endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Catalysis of the endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Catalysis of the endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Catalysis of the endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Catalysis of the endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Catalysis of the endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Catalysis of the endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Catalysis of the endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Any mechanism of immune avoidance that does not directly interfere with the host immune system; for example, some viruses enter a state of latency where their protein production is drastically downregulated, meaning that they are not detected by the host immune system. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any mechanism of immune avoidance that directly affects the host immune system, e.g. blocking any stage in host MHC class I and II presentation. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any mechanism of active immune avoidance which works by regulating the host complement system, e.g. by possessing complement receptors which mediate attachment to, then infection of, host macrophages, which are eventually destroyed. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any mechanism of active immune avoidance which works by regulating the host complement system, e.g. by possessing complement receptors which mediate attachment to, then infection of, host macrophages, which are eventually destroyed. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any mechanism of active immune avoidance which works by regulating host cytokine networks, e.g. by secreting proteins that mimic cytokine receptors that act to sequester host cytokines and inhibit action. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any mechanism of active immune avoidance which works by regulating host cytokine networks, e.g. by secreting proteins that mimic cytokine receptors that act to sequester host cytokines and inhibit action. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any mechanism of active immune avoidance which works by regulating the host's antigen processing or presentation pathways, e.g. by blocking any stage in MHC class II presentation. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any mechanism of active immune avoidance which works by regulating the host's antigen processing or presentation pathways, e.g. by blocking any stage in MHC class II presentation. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any mechanism of active immune avoidance which works by regulating the host's antigen processing or presentation pathways, e.g. by blocking any stage in MHC class II presentation. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any mechanism of active immune avoidance which works by regulating the host's antigen processing or presentation pathways, e.g. by blocking any stage in MHC class II presentation. The host is defined as the larger of the organisms involved in a symbiotic interaction.
A ribosome bound to mRNA that forms part of a polysome.
The cellular synthesis of messenger RNA (mRNA) from a DNA template by RNA polymerase II, originating at an RNA polymerase II promoter.
The cellular synthesis of messenger RNA (mRNA) from a DNA template by RNA polymerase II, originating at an RNA polymerase II promoter.
The synthesis of the large ribosomal RNA (rRNA) transcript which encodes several rRNAs, e.g. in mammals 28S, 18S and 5.8S, from a nuclear DNA template transcribed by RNA polymerase I.
The synthesis of the large ribosomal RNA (rRNA) transcript which encodes several rRNAs, e.g. in mammals 28S, 18S and 5.8S, from a nuclear DNA template transcribed by RNA polymerase I.
The synthesis of the large ribosomal RNA (rRNA) transcript which encodes several rRNAs, e.g. in mammals 28S, 18S and 5.8S, from a nuclear DNA template transcribed by RNA polymerase I.
The synthesis of 5S ribosomal RNA (rRNA), or an equivalent rRNA, from a DNA template by RNA polymerase III (Pol III), originating at a type 1 RNA polymerase III promoter.
The synthesis of 5S ribosomal RNA (rRNA), or an equivalent rRNA, from a DNA template by RNA polymerase III (Pol III), originating at a type 1 RNA polymerase III promoter.
The synthesis of ribosomal RNA (rRNA) from a mitochondrial DNA template.
The synthesis of RNA from a plastid DNA template, usually by a specific plastid RNA polymerase.
The synthesis of ribosomal RNA (rRNA) from a plastid DNA template, usually by a specific plastid RNA polymerase.
The synthesis of small nuclear RNA (snRNA) from a DNA template by RNA Polymerase II (Pol II), originating at a Pol II promoter.
The synthesis of small nuclear RNA (snRNA) from a DNA template by RNA Polymerase II (Pol II), originating at a Pol II promoter.
The synthesis of small nuclear RNA (snRNA) from a DNA template by RNA Polymerase III (Pol III), originating at a Pol III promoter.
The synthesis of small nuclear RNA (snRNA) from a DNA template by RNA Polymerase III (Pol III), originating at a Pol III promoter.
The synthesis of transfer RNA (tRNA) from a DNA template by RNA polymerase III (Pol III), originating at a Pol III promoter.
The synthesis of transfer RNA (tRNA) from a DNA template by RNA polymerase III (Pol III), originating at a Pol III promoter.
Catalysis of the reaction: S-adenosyl-L-methionine + histone H4 L-lysine (position 20) = S-adenosyl-L-homocysteine + histone H4 N6-methyl-L-lysine (position 20). This reaction is the addition of a methyl group onto lysine at position 20 of the histone H4 protein.
Catalysis of the reaction: S-adenosyl-L-methionine + histone H4 L-lysine (position 20) = S-adenosyl-L-homocysteine + histone H4 N6-methyl-L-lysine (position 20). This reaction is the addition of a methyl group onto lysine at position 20 of the histone H4 protein.
Catalysis of the reaction: S-adenosyl-L-methionine + histone H4 L-lysine (position 20) = S-adenosyl-L-homocysteine + histone H4 N6-methyl-L-lysine (position 20). This reaction is the addition of a methyl group onto lysine at position 20 of the histone H4 protein.
Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 4) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 4). This reaction is the addition of a methyl group onto lysine at position 4 of the histone H3 protein.
Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 4) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 4). This reaction is the addition of a methyl group onto lysine at position 4 of the histone H3 protein.
Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 4) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 4). This reaction is the addition of a methyl group onto lysine at position 4 of the histone H3 protein.
Interacting selectively and non-covalently with an identical protein to form a homodimer.
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
Interacting selectively and non-covalently with actinin, any member of a family of proteins that crosslink F-actin.
Interacting selectively and non-covalently with actinin, any member of a family of proteins that crosslink F-actin.
Interacting selectively and non-covalently with actinin, any member of a family of proteins that crosslink F-actin.
Interacting selectively and non-covalently with fucose, the pentose 6-deoxygalactose.
A membrane-enclosed sac that takes up most of the volume of a mature plant cell. Functions include storage, separation of toxic byproducts, and cell growth determination.
Interacting selectively and non-covalently with the vitamin D receptor, a nuclear receptor that mediates the action of vitamin D by binding DNA and controlling the transcription of hormone-sensitive genes.
Interacting selectively and non-covalently with the vitamin D receptor, a nuclear receptor that mediates the action of vitamin D by binding DNA and controlling the transcription of hormone-sensitive genes.
The chemical reactions and pathways involving pheromones, a substance that is secreted and released by an organism and detected by a second organism of the same or a closely related species, in which it causes a specific reaction, such as a definite behavioral reaction or a developmental process.
The chemical reactions and pathways resulting in the formation of pheromones, a substance that is secreted and released by an organism and detected by a second organism of the same or a closely related species, in which it causes a specific reaction, such as a definite behavioral reaction or a developmental process.
The chemical reactions and pathways resulting in the formation of pheromones, a substance that is secreted and released by an organism and detected by a second organism of the same or a closely related species, in which it causes a specific reaction, such as a definite behavioral reaction or a developmental process.
The chemical reactions and pathways resulting in the formation of pheromones, a substance that is secreted and released by an organism and detected by a second organism of the same or a closely related species, in which it causes a specific reaction, such as a definite behavioral reaction or a developmental process.
The chemical reactions and pathways resulting in the formation of pheromones, a substance that is secreted and released by an organism and detected by a second organism of the same or a closely related species, in which it causes a specific reaction, such as a definite behavioral reaction or a developmental process.
The chemical reactions and pathways resulting in the breakdown of pheromones, a substance that is secreted and released by an organism and detected by a second organism of the same or a closely related species, in which it causes a specific reaction, such as a definite behavioral reaction or a developmental process.
The chemical reactions and pathways resulting in the breakdown of pheromones, a substance that is secreted and released by an organism and detected by a second organism of the same or a closely related species, in which it causes a specific reaction, such as a definite behavioral reaction or a developmental process.
The chemical reactions and pathways resulting in the breakdown of pheromones, a substance that is secreted and released by an organism and detected by a second organism of the same or a closely related species, in which it causes a specific reaction, such as a definite behavioral reaction or a developmental process.
The chemical reactions and pathways resulting in the breakdown of pheromones, a substance that is secreted and released by an organism and detected by a second organism of the same or a closely related species, in which it causes a specific reaction, such as a definite behavioral reaction or a developmental process.
The chemical reactions and pathways resulting in the breakdown of pheromones, a substance that is secreted and released by an organism and detected by a second organism of the same or a closely related species, in which it causes a specific reaction, such as a definite behavioral reaction or a developmental process.
The chemical reactions and pathways involving any of the vitamin B6 compounds: pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate.
The chemical reactions and pathways involving 3-hydroxy-5-(hydroxymethyl)-2-methyl-4-pyridinecarboxaldehyde, one of the vitamin B6 compounds. Pyridoxal, pyridoxamine and pyridoxine are collectively known as vitamin B6, and are efficiently converted to the biologically active form of vitamin B6, pyridoxal phosphate.
The chemical reactions and pathways involving 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol, one of the vitamin B6 compounds. Pyridoxal, pyridoxamine and pyridoxine are collectively known as vitamin B6, and are efficiently converted to the biologically active form of vitamin B6, pyridoxal phosphate.
The chemical reactions and pathways resulting in the formation of any of the vitamin B6 compounds; pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate.
The chemical reactions and pathways resulting in the formation of any of the vitamin B6 compounds; pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate.
The chemical reactions and pathways resulting in the formation of any of the vitamin B6 compounds; pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate.
The chemical reactions and pathways resulting in the formation of any of the vitamin B6 compounds; pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate.
The chemical reactions and pathways resulting in the formation of any of the vitamin B6 compounds; pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate.
The chemical reactions and pathways resulting in the breakdown of any of the vitamin B6 compounds; pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate.
The chemical reactions and pathways resulting in the breakdown of any of the vitamin B6 compounds; pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate.
The chemical reactions and pathways resulting in the breakdown of any of the vitamin B6 compounds; pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate.
The chemical reactions and pathways resulting in the formation of 3-hydroxy-5-(hydroxymethyl)-2-methyl-4-pyridinecarboxaldehyde, one of the vitamin B6 compounds.
The chemical reactions and pathways resulting in the formation of 3-hydroxy-5-(hydroxymethyl)-2-methyl-4-pyridinecarboxaldehyde, one of the vitamin B6 compounds.
The chemical reactions and pathways resulting in the formation of 3-hydroxy-5-(hydroxymethyl)-2-methyl-4-pyridinecarboxaldehyde, one of the vitamin B6 compounds.
The chemical reactions and pathways resulting in the formation of 3-hydroxy-5-(hydroxymethyl)-2-methyl-4-pyridinecarboxaldehyde, one of the vitamin B6 compounds.
The chemical reactions and pathways involving pyridoxal phosphate, pyridoxal phosphorylated at the hydroxymethyl group of C-5, the active form of vitamin B6.
The chemical reactions and pathways involving pyridoxal phosphate, pyridoxal phosphorylated at the hydroxymethyl group of C-5, the active form of vitamin B6.
The chemical reactions and pathways involving 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 formation 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 formation 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 formation 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 formation 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 formation 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 formation of pyridoxal phosphate, pyridoxal phosphorylated at the hydroxymethyl group of C-5, the active form of vitamin B6.
A large, multisubunit complex which consists of the MHC class I-beta 2 microglobulin dimer, the transporter associated with antigen presentation (TAP), tapasin (an MHC-encoded membrane protein), the chaperone calreticulin and the thiol oxidoreductase ERp57. Functions in the assembly of peptides with newly synthesized MHC class I molecules.
A large, multisubunit complex which consists of the MHC class I-beta 2 microglobulin dimer, the transporter associated with antigen presentation (TAP), tapasin (an MHC-encoded membrane protein), the chaperone calreticulin and the thiol oxidoreductase ERp57. Functions in the assembly of peptides with newly synthesized MHC class I molecules.
A heterodimer composed of the subunits TAP1 and TAP2 (transporter associated with antigen presentation). Functions in the transport of antigenic peptides from the cytosol to the lumen of the endoplasmic reticulum.
Interacting selectively and non-covalently with the enzyme histone deacetylase.
Electron-dense granule occurring in blood platelets that stores and secretes adenosine nucleotides and serotonin. They contain a highly condensed core consisting of serotonin, histamine, calcium, magnesium, ATP, ADP, pyrophosphate and membrane lysosomal proteins.
Electron-dense granule occurring in blood platelets that stores and secretes adenosine nucleotides and serotonin. They contain a highly condensed core consisting of serotonin, histamine, calcium, magnesium, ATP, ADP, pyrophosphate and membrane lysosomal proteins.
Reactions triggered in response to the presence of a protozoan that act to protect the cell or organism.
Reactions triggered in response to the presence of a protozoan that act to protect the cell or organism.
Reactions triggered in response to the presence of a protozoan that act to protect the cell or organism.
Reactions triggered in response to the presence of a protozoan that act to protect the cell or organism.
Reactions triggered in response to the presence of a protozoan that act to protect the cell or organism.
Reactions triggered in response to the presence of a protozoan that act to protect the cell or organism.
Interacting selectively and non-covalently, in a non-covalent manner, with peptidoglycan, any of a class of glycoconjugates found in bacterial cell walls.
Interacting selectively and non-covalently with the RNA element BRE (Bruno response element).
The chemical reactions and pathways involving D-glucarate, the D-enantiomer of glucarate. D-glucarate is derived from either D-glucose or L-gulose.
The chemical reactions and pathways involving D-glucarate, the D-enantiomer of glucarate. D-glucarate is derived from either D-glucose or L-gulose.
The chemical reactions and pathways involving D-glucarate, the D-enantiomer of glucarate. D-glucarate is derived from either D-glucose or L-gulose.
The chemical reactions and pathways resulting in the formation of D-glucarate, the D-enantiomer of glucarate.
The chemical reactions and pathways resulting in the formation of D-glucarate, the D-enantiomer of glucarate.
The chemical reactions and pathways resulting in the formation of D-glucarate, the D-enantiomer of glucarate.
The chemical reactions and pathways resulting in the formation of D-glucarate, the D-enantiomer of glucarate.
The chemical reactions and pathways resulting in the formation of D-glucarate, the D-enantiomer of glucarate.
The chemical reactions and pathways resulting in the formation of D-glucarate, the D-enantiomer of glucarate.
The chemical reactions and pathways resulting in the breakdown of D-glucarate, the D-enantiomer of glucarate.
The chemical reactions and pathways resulting in the breakdown of D-glucarate, the D-enantiomer of glucarate.
The chemical reactions and pathways resulting in the breakdown of D-glucarate, the D-enantiomer of glucarate.
The chemical reactions and pathways resulting in the breakdown of D-glucarate, the D-enantiomer of glucarate.
The chemical reactions and pathways resulting in the breakdown of D-glucarate, the D-enantiomer of glucarate.
The chemical reactions and pathways involving D-glucuronate, the D-enantiomer of glucuronate.
The chemical reactions and pathways resulting in the breakdown of D-glucuronate, the D-enantiomer of glucuronate.
The chemical reactions and pathways resulting in the breakdown of D-glucuronate, the D-enantiomer of glucuronate.
The chemical reactions and pathways resulting in the breakdown of D-glucuronate, the D-enantiomer of glucuronate.
The chemical reactions and pathways resulting in the formation of D-glucuronate, the D-enantiomer of glucuronate.
The chemical reactions and pathways resulting in the formation of D-glucuronate, the D-enantiomer of glucuronate.
The chemical reactions and pathways resulting in the formation of D-glucuronate, the D-enantiomer of glucuronate.
The chemical reactions and pathways resulting in the formation of D-glucuronate, the D-enantiomer of glucuronate.
The chemical reactions and pathways resulting in the formation of D-xylose, a naturally occurring plant polysaccharide.
The chemical reactions and pathways resulting in the formation of D-xylose, a naturally occurring plant polysaccharide.
The chemical reactions and pathways resulting in the formation of D-xylose, a naturally occurring plant polysaccharide.
The chemical reactions and pathways resulting in the formation of D-xylose, a naturally occurring plant polysaccharide.
The chemical reactions and pathways resulting in the breakdown of D-xylose, a naturally occurring plant polysaccharide.
The chemical reactions and pathways resulting in the breakdown of D-xylose, a naturally occurring plant polysaccharide.
The chemical reactions and pathways resulting in the breakdown of D-xylose, a naturally occurring plant polysaccharide.
The chemical reactions and pathways involving glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways involving glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways involving glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the formation of glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the formation of glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the formation of glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the formation of glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the formation of glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the formation of glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the breakdown of glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the breakdown of glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the breakdown of glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the breakdown of glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the breakdown of glycol, a diol in which the two hydroxy groups are on different carbon atoms, usually but not necessarily adjacent.
The chemical reactions and pathways resulting in the formation of sorbose, the ketohexose xylo-2-hexulose. Sorbose is produced commercially by fermentation and is used as an intermediate in the manufacture of ascorbic acid.
The chemical reactions and pathways resulting in the formation of sorbose, the ketohexose xylo-2-hexulose. Sorbose is produced commercially by fermentation and is used as an intermediate in the manufacture of ascorbic acid.
The chemical reactions and pathways resulting in the formation of sorbose, the ketohexose xylo-2-hexulose. Sorbose is produced commercially by fermentation and is used as an intermediate in the manufacture of ascorbic acid.
The chemical reactions and pathways resulting in the formation of sorbose, the ketohexose xylo-2-hexulose. Sorbose is produced commercially by fermentation and is used as an intermediate in the manufacture of ascorbic acid.
The chemical reactions and pathways resulting in the breakdown of sorbose, the ketohexose xylo-2-hexulose. Sorbose is produced commercially by fermentation and is used as an intermediate in the manufacture of ascorbic acid.
The chemical reactions and pathways resulting in the breakdown of sorbose, the ketohexose xylo-2-hexulose. Sorbose is produced commercially by fermentation and is used as an intermediate in the manufacture of ascorbic acid.
The chemical reactions and pathways resulting in the breakdown of sorbose, the ketohexose xylo-2-hexulose. Sorbose is produced commercially by fermentation and is used as an intermediate in the manufacture of ascorbic acid.
The chemical reactions and pathways resulting in the formation of L-sorbose, the L-enantiomer of the ketohexose xylo-2-hexulose. L-sorbose is formed by bacterial oxidation of sorbitol.
The chemical reactions and pathways resulting in the formation of L-sorbose, the L-enantiomer of the ketohexose xylo-2-hexulose. L-sorbose is formed by bacterial oxidation of sorbitol.
The chemical reactions and pathways resulting in the formation of L-sorbose, the L-enantiomer of the ketohexose xylo-2-hexulose. L-sorbose is formed by bacterial oxidation of sorbitol.
The chemical reactions and pathways resulting in the formation of L-sorbose, the L-enantiomer of the ketohexose xylo-2-hexulose. L-sorbose is formed by bacterial oxidation of sorbitol.
The chemical reactions and pathways resulting in the breakdown of L-sorbose, the L-enantiomer of the ketohexose xylo-2-hexulose.
The chemical reactions and pathways resulting in the breakdown of L-sorbose, the L-enantiomer of the ketohexose xylo-2-hexulose.
The chemical reactions and pathways resulting in the breakdown of L-sorbose, the L-enantiomer of the ketohexose xylo-2-hexulose.
The chemical reactions and pathways involving L-alanine, the L-enantiomer of 2-aminopropanoic acid, i.e. (2S)-2-aminopropanoic acid.
The chemical reactions and pathways resulting in the formation of L-alanine, the L-enantiomer of 2-aminopropanoic acid, i.e. (2S)-2-aminopropanoic acid.
The chemical reactions and pathways resulting in the formation of L-alanine, the L-enantiomer of 2-aminopropanoic acid, i.e. (2S)-2-aminopropanoic acid.
The chemical reactions and pathways resulting in the formation of L-alanine, the L-enantiomer of 2-aminopropanoic acid, i.e. (2S)-2-aminopropanoic acid.
The chemical reactions and pathways resulting in the formation of L-alanine, the L-enantiomer of 2-aminopropanoic acid, i.e. (2S)-2-aminopropanoic acid.
The chemical reactions and pathways resulting in the breakdown of L-alanine, the L-enantiomer of 2-aminopropanoic acid, i.e. (2S)-2-aminopropanoic acid.
The chemical reactions and pathways resulting in the breakdown of L-alanine, the L-enantiomer of 2-aminopropanoic acid, i.e. (2S)-2-aminopropanoic acid.
The chemical reactions and pathways resulting in the breakdown of L-alanine, the L-enantiomer of 2-aminopropanoic acid, i.e. (2S)-2-aminopropanoic acid.
The chemical reactions and pathways involving eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways involving eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways involving eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways involving eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways involving eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the formation of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the formation of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the formation of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the formation of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the formation of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the formation of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the formation of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the formation of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the breakdown of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the breakdown of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the breakdown of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the breakdown of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the breakdown of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the breakdown of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways resulting in the breakdown of eugenol, a colorless, aromatic, liquid hydrocarbon (C10H12O2) found in clove oil.
The chemical reactions and pathways involving the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways resulting in the formation of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways resulting in the formation of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways resulting in the formation of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways resulting in the formation of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways resulting in the formation of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways resulting in the formation of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways resulting in the formation of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways resulting in the formation of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways resulting in the breakdown of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways resulting in the breakdown of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways resulting in the breakdown of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine).
The chemical reactions and pathways involving achromobactin, a citrate siderophore.
The chemical reactions and pathways resulting in the formation of achromobactin, a citrate siderophore.
The chemical reactions and pathways resulting in the formation of achromobactin, a citrate siderophore.
The chemical reactions and pathways resulting in the formation of achromobactin, a citrate siderophore.
The chemical reactions and pathways resulting in the formation of achromobactin, a citrate siderophore.
The chemical reactions and pathways resulting in the formation of achromobactin, a citrate siderophore.
The chemical reactions and pathways resulting in the formation of achromobactin, a citrate siderophore.
The chemical reactions and pathways resulting in the formation of achromobactin, a citrate siderophore.
The chemical reactions and pathways resulting in the formation of achromobactin, a citrate siderophore.
The chemical reactions and pathways resulting in the breakdown of achromobactin, a citrate siderophore.
The chemical reactions and pathways resulting in the breakdown of achromobactin, a citrate siderophore.
The chemical reactions and pathways resulting in the breakdown of achromobactin, a citrate siderophore.
The chemical reactions and pathways involving the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the formation of the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the formation of the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the formation of the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the formation of the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the formation of the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the formation of the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the formation of the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the formation of the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the breakdown of the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the breakdown of the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the breakdown of the siderochrome pyochelin (2-(2-o-hydroxyphenyl-2-thiazolin-4-yl)-3-methylthiazolidine-4-carboxylic acid).
The chemical reactions and pathways resulting in the formation of pyruvate, 2-oxopropanoate.
The chemical reactions and pathways resulting in the formation of pyruvate, 2-oxopropanoate.
The chemical reactions and pathways resulting in the formation of pyruvate, 2-oxopropanoate.
The chemical reactions and pathways resulting in the formation of pyruvate, 2-oxopropanoate.
The chemical reactions and pathways resulting in the breakdown of pyruvate, 2-oxopropanoate.
The chemical reactions and pathways resulting in the breakdown of pyruvate, 2-oxopropanoate.
The chemical reactions and pathways resulting in the breakdown of pyruvate, 2-oxopropanoate.
The chemical reactions and pathways involving antisense RNA, an RNA molecule complementary in sequence to another RNA or DNA molecule, which, by binding the latter, acts to inhibit its function and/or completion of synthesis.
The process in which aldarate is transported across a lipid bilayer, from one side of a membrane to the other.
The process in which D-glucarate, the D-enantiomer of glucarate, is transported across a lipid bilayer, from one side of a membrane to the other.
The process in which aldonate is transported across a lipid bilayer, from one side of a membrane to the other.
The process in which D-glucuronate, the D-enantiomer of glucuronate, is transported across a lipid bilayer, from one side of a membrane to the other.
The process in which D-galactonate, the D-enantiomer of galactonate, is transported across a lipid bilayer, from one side of a membrane to the other.
Enables the transfer of aldarate from one side of a membrane to the other.
Enables the transfer of D-glucarate, the D-enantiomer of glucarate, from one side of a membrane to the other.
Enables the transfer of aldonate from one side of a membrane to the other.
Enables the transfer of D-glucuronate, the D-enantiomer of glucuronate, from one side of a membrane to the other.
Enables the transfer of D-galactonate, the D-enantiomer of galactonate, from one side of a membrane to the other.
The process in which L-arabinose, the L-enantiomer of arabinose, is transported across a lipid bilayer, from one side of a membrane to the other.
The directed movement of cysteine 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 microcin, a class of glycine-rich, bactericidal peptides (antibiotics) produced by some enteric bacteria, 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 microcin B17, a bactericidal peptide (antibiotic) produced by some enteric bacteria, 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 an amide, any compound containing one, two, or three acyl groups attached to a nitrogen atom, 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 molybdenum (Mo) ions from one side of a membrane to the other.
The directed movement of 3-phenylpropionic 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 3-phenylpropionic 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 3-phenylpropionic acid 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 3-phenylpropionic acid from one side of a membrane to the other.
Enables the transfer of 3-phenylpropionic acid from one side of a membrane to the other.
Enables the transfer of 3-phenylpropionic acid from one side of a membrane to the other.
The directed movement of an antibiotic, a substance produced by or derived from certain fungi, bacteria, and other organisms, that can destroy or inhibit the growth of other microorganisms, 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 chloramphenicol, a broad-spectrum antibiotic that inhibits bacterial protein synthesis, 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 polymyxin, any of a group of related antibiotics produced by Bacillus polymyxa and active against most Gram-negative bacteria, 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 fosmidomycin, a phosphonic acid derivative with potent activity against Gram-negative organisms, 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 an antibiotic, a substance produced by or derived from certain fungi, bacteria, and other organisms, that can destroy or inhibit the growth of other microorganisms, from one side of a membrane to the other.
Enables the transfer of chloramphenicol, a broad-spectrum antibiotic that inhibits bacterial protein synthesis, from one side of a membrane to the other.
Enables the transfer of polymyxin, any of a group of related antibiotics produced by Bacillus polymyxa and active against most Gram-negative bacteria, from one side of a membrane to the other.
Enables the transfer of fosmidomycin, a phosphonic acid derivative with potent activity against Gram-negative organisms, from one side of a membrane to the other.
The process in which arabinan is transported across a lipid bilayer, from one side of a membrane to the other.
Enables the transfer of arabinose, a pentose monosaccharide that occurs in both D and L configurations, and as a polymer, from one side of a membrane to the other.
Enables the transfer of an arabinan, a polysaccharide composed of arabinose residues, from one side of a membrane to the other.
The process of linking a protein to peptidoglycan via a carboxy terminal threonine carboxyl group through a pentaglycyl peptide to the lysine or diaminopimelic acid of the peptidoglycan.
Catalysis of the reaction: N-acetyl(alpha-tubulin) + H2O = alpha-tubulin + acetate.
The chemical reactions and pathways resulting in the formation of 9-cis-retinoic acid, a metabolically active vitamin A derivative.
The chemical reactions and pathways resulting in the formation of 9-cis-retinoic acid, a metabolically active vitamin A derivative.
The chemical reactions and pathways resulting in the formation of 9-cis-retinoic acid, a metabolically active vitamin A derivative.
The chemical reactions and pathways resulting in the formation of 9-cis-retinoic acid, a metabolically active vitamin A derivative.
The chemical reactions and pathways involving 9-cis-retinoic acid, a metabolically active vitamin A derivative.
The directed movement of xanthine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Xanthine (2,6-dihydroxypurine) is a purine formed in the metabolic breakdown of guanine, but is not present in nucleic acids.
Enables the transfer of xanthine from one side of a membrane to the other. Xanthine (2,6-dihydroxypurine) is a purine formed in the metabolic breakdown of guanine, but is not present in nucleic acids.
The directed movement of a xenobiotic, a compound foreign to living organisms, 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 acridine (10-azaanthracene), a heterocyclic ring compound found in crude coal-tar anthracene, 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 xenobiotic, a compound foreign to living organisms, from one side of a membrane to the other.
Enables the directed movement of acridine (10-azaanthracene), a heterocyclic ring compound found in crude coal-tar anthracene from one side of a membrane to the other.
Enables the transfer of a colicin from one side of a membrane to the other. Colicins are a group of antibiotics produced by E. coli and related species that are encoded by a group of naturally occurring plasmids, e.g. Col E1.
Enables the transfer of group A colicins (colicins E1, E2, E3, A, K, and N) from one side of a membrane to the other.
The directed movement of a colicin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Colicins are a group of antibiotics produced by E. coli and related species that are encoded by a group of naturally occurring plasmids, e.g. Col E1.
The directed movement of group A colicins (colicins E1, E2, E3, A, K, and N) 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 an alkylphosphonate 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 an alkylphosphonate from one side of a membrane to the other.
The directed movement of an alkanesulfonate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Alkanesulfonates are organic esters or salts of sulfonic acid containing an aliphatic hydrocarbon radical.
The directed movement of benzoate, the anion of benzoic acid (benzenecarboxylic 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 3-hydroxyphenylpropionic 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 3-hydroxyphenylpropionic acid into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any series of molecular signals generated as a consequence of a glucocorticoid binding to its receptor.
Interacting selectively and non-covalently with one or more specific sites on a neuromedin U receptor.
Interacting selectively and non-covalently and stoichiometrically with neuropeptides, peptides with direct synaptic effects (peptide neurotransmitters) or indirect modulatory effects on the nervous system (peptide neuromodulators).
Interacting selectively and non-covalently and stoichiometrically with neuromedin U, a hypothalamic peptide involved in energy homeostasis and stress responses.
Enables the directed movement of benzoate, the anion of benzoic acid (benzenecarboxylic acid) from one side of a membrane to the other.
Enables the directed movement of 3-hydroxyphenylpropionic acid from one side of a membrane to the other.
Enables the directed movement of 3-hydroxyphenylpropionic acid from one side of a membrane to the other.
Enables the directed movement of 3-hydroxyphenylpropionic acid from one side of a membrane to the other.
The directed movement of a ferrichrome into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Ferrichromes are any of a group of growth-promoting Fe(III) chelates formed by various genera of microfungi. They are homodetic cyclic hexapeptides made up of a tripeptide of glycine (or other small neutral amino acids) and a tripeptide of an N'acyl-N4-hydroxy-L-ornithine.
Enables the directed movement of a ferrichrome from one side of a membrane to the other. Ferrichromes are any of a group of growth-promoting Fe(III) chelates formed by various genera of microfungi. They are homodetic cyclic hexapeptides made up of a tripeptide of glycine (or other small neutral amino acids) and a tripeptide of an N'acyl-N4-hydroxy-L-ornithine.
The directed movement of the siderochrome enterobactin, a cyclic trimer of 2, 3 dihydroxybenzoylserine 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 the siderochrome enterochelin, a cyclic trimer of 2, 3 dihydroxybenzoylserine from one side of a membrane to the other.
Enables the directed movement of the siderochrome enterochelin, a cyclic trimer of 2, 3 dihydroxybenzoylserine from one side of a membrane to the other.
The directed movement of the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine) 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 the siderophore chrysobactin (alpha-N-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine) from one side of a membrane to the other.
Enables the transfer of achromobactin, a citrate siderophore, from one side of a membrane to the other.
The directed movement of achromobactin, a citrate siderophore, 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 a tripeptide, a compound containing three amino acids linked together by peptide bonds, from one side of a membrane to the other.
The directed movement of a dipeptide, a combination of two amino acids by means of a peptide (-CO-NH-) link, 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 a tripeptide, a compound containing three amino acids linked together by peptide bonds, 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 the D-enantiomer of an amino 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 D-alanine, the D-enantiomer of 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 D-serine, the D-enantiomer of 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.
Enables the transfer of D-amino acids from one side of a membrane to the other. D-amino acids are the D-enantiomers of amino acids.
Enables the transfer of D-alanine from one side of a membrane to the other. D-alanine is the D-enantiomer of 2-aminopropanoic acid.
Enables the transfer of D-serine from one side of a membrane to the other. D-serine is the D-enantiomer of 2-amino-3-hydroxypropanoic acid.
Enables the transfer of D-serine from one side of a membrane to the other. D-serine is the D-enantiomer of 2-amino-3-hydroxypropanoic acid.
The directed movement of glucosides into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Glucosides are glycosides in which the sugar group is a glucose residue.
Enables the transfer of glucosides from one side of a membrane to the other. Glucosides are glycosides in which the sugar group is a glucose residue.
The directed movement of salicin (saligenin-beta-D-glucopyranoside), a glucoside of o-hydroxybenzylalcohol, 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 arbutin, a glycoside found in the bearberry and related plants which has been used to treat urinary-tract diseases, 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 salicin (saligenin-beta-D-glucopyranoside), a glucoside of o-hydroxybenzylalcohol, from one side of a membrane to the other.
Enables the transfer of arbutin, a glycoside found in the bearberry and related plants which has been used to treat urinary-tract diseases, from one side of a membrane to the other.
A pathway of aromatic compound degradation by ortho-cleavage; one branch converts protocatechuate, derived from phenolic compounds, to beta-ketoadipate, and the other branch converts catechol, generated from various aromatic hydrocarbons, amino aromatics, and lignin monomers, also to beta-ketoadipate. Two additional steps accomplish the conversion of beta-ketoadipate to tricarboxylic acid cycle intermediates.
The directed movement of any conjugated, water-soluble protein in which the nonprotein group consists of a lipid or lipids, 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 any conjugated, water-soluble protein in which the nonprotein group consists of a lipid or lipids, into, out of or within a cell, or between cells.
The directed movement of dextrin, any one, or the mixture, of the intermediate polysaccharides formed during the hydrolysis of starch, which are dextrorotatory, soluble in water, and precipitable in alcohol, 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 maltodextrin, any polysaccharide of glucose residues in beta-(1,4) linkage, 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 dextrin, any one, or the mixture, of the intermediate polysaccharides formed during the hydrolysis of starch, which are dextrorotatory, soluble in water, and precipitable in alcohol, from one side of a membrane to the other.
Enables the transfer of maltodextrin, any polysaccharide of glucose residues in beta-(1,4) linkage, from one side of a membrane to the other.
Enables the directed movement of alkanesulfonate from one side of a membrane to the other.
Enables the directed movement of alkanesulfonate from one side of a membrane to the other.
Enables the transfer of antimonite from one side of a membrane to the other, up its concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction and is driven by a chemiosmotic source of energy. Secondary active transporters include symporters and antiporters.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + antimonite(in) = ADP + phosphate + antimonite(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: H+(out) + acridine(in) = H+(in) + acridine(out).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: H+(out) + acridine(in) = H+(in) + acridine(out).
The chemical reactions and pathways resulting in the reduction of thioredoxin, a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase.
The chemical reactions and pathways resulting in the reduction of thioredoxin, a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase.
The chemical reactions and pathways resulting in the reduction of thioredoxin, a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase.
The chemical reactions and pathways resulting in the reduction of thioredoxin, a small disulfide-containing redox protein that serves as a general protein disulfide oxidoreductase.
The chemical reactions and pathways resulting in the formation of the biotin carboxyl carrier protein, a subunit of acetyl-coenzyme A carboxylase.
The chemical reactions and pathways resulting in the formation of the biotin carboxyl carrier protein, a subunit of acetyl-coenzyme A carboxylase.
The chemical reactions and pathways resulting in the formation of the biotin carboxyl carrier protein, a subunit of acetyl-coenzyme A carboxylase.
The chemical reactions and pathways resulting in the formation of the biotin carboxyl carrier protein, a subunit of acetyl-coenzyme A carboxylase.
The chemical reactions and pathways resulting in the formation of the biotin carboxyl carrier protein, a subunit of acetyl-coenzyme A carboxylase.
The chemical reactions and pathways resulting in the formation of the biotin carboxyl carrier protein, a subunit of acetyl-coenzyme A carboxylase.
The directed movement of homoserine, alpha-amino-gamma-hydroxybutyric acid, an intermediate in the biosynthesis of cystathionine, threonine and methionine, 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 lactone from one side of a membrane to the other. A lactone is a cyclic ester of a hydroxy carboxylic acid, containing a 1-oxacycloalkan-2-one structure, or an analogue having unsaturation or heteroatoms replacing one or more carbon atoms of the ring.
Enables the transfer of homoserine from one side of a membrane to the other. Homoserine is alpha-amino-gamma-hydroxybutyric acid, an intermediate in the biosynthesis of cystathionine, threonine and methionine.
Enables the transfer of lactone from one side of a membrane to the other. A lactone is a cyclic ester of a hydroxy carboxylic acid, containing a 1-oxacycloalkan-2-one structure, or an analogue having unsaturation or heteroatoms replacing one or more carbon atoms of the ring.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3) and (1->4) bonds.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3) and (1->4) bonds.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3) and (1->4) bonds.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3) and (1->4) bonds.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3) and (1->4) bonds.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3) and (1->4) bonds.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3) and (1->4) bonds.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3) and (1->4) bonds.
Catalysis of the hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3) and (1->4) bonds.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Catalysis of the hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Interacting selectively and non-covalently with the retinoic acid receptor, a ligand-regulated transcription factor belonging to the nuclear receptor superfamily.
Interacting selectively and non-covalently with any of the peroxisome proliferator activated receptors, alpha, beta or gamma.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it.
Upregulation of the activity of the enzyme ornithine decarboxylase.
Modulation of the activity of the enzyme ornithine decarboxylase.
Interacting selectively and non-covalently with one or more specific sites on an ion channel, 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.
The chemical reactions and pathways involving amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways involving amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways involving amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of amyloid precursor protein (APP), the precursor of amyloid-beta.
The chemical reactions and pathways resulting in the breakdown of amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways resulting in the breakdown of amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways resulting in the breakdown of amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways resulting in the breakdown of amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
The chemical reactions and pathways resulting in the breakdown of amyloid precursor protein (APP), the precursor of amyloid-beta, a glycoprotein associated with Alzheimer's disease.
Interacting selectively and non-covalently with X11-like protein, a neuron-specific adaptor protein.
A prolongation or process extending from a cell, e.g. a flagellum or axon.
A prolongation or process extending from a cell, e.g. a flagellum or axon.
A prolongation or process extending from a cell, e.g. a flagellum or axon.
Any process that modulates the frequency, rate or extent of the transport of proteins from the Golgi to the plasma membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of the transport of proteins from the Golgi to the plasma membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of the transport of proteins from the Golgi to the plasma membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of the transport of proteins from the Golgi to the plasma membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of the transport of proteins from the Golgi to the plasma membrane.
Any process that activates or increases the frequency, rate or extent of the transport of proteins from the Golgi to the plasma membrane.
Any process that activates or increases the frequency, rate or extent of the transport of proteins from the Golgi to the plasma membrane.
Any process that activates or increases the frequency, rate or extent of the transport of proteins from the Golgi to the plasma membrane.
Any process that activates or increases the frequency, rate or extent of the transport of proteins from the Golgi to the plasma membrane.
Any process that activates or increases the frequency, rate or extent of the transport of proteins from the Golgi to the plasma membrane.
Any process that modulates the frequency, rate or extent of transport of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein from the Golgi to the plasma membrane.
The directed movement of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein from the Golgi to the plasma membrane.
The directed movement of proteins from the Golgi to the plasma membrane in transport vesicles that move from the trans-Golgi network to the plasma membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of transport of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein from the Golgi to the plasma membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of transport of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein from the Golgi to the plasma membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of transport of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein from the Golgi to the plasma membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of transport of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein from the Golgi to the plasma membrane.
Any process that activates or increases the frequency, rate or extent of transport of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein from the Golgi to the plasma membrane.
Any process that activates or increases the frequency, rate or extent of transport of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein from the Golgi to the plasma membrane.
Any process that activates or increases the frequency, rate or extent of transport of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein from the Golgi to the plasma membrane.
Any process that activates or increases the frequency, rate or extent of transport of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein from the Golgi to the plasma membrane.
Any process that activates or increases the frequency, rate or extent of transport of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein from the Golgi to the plasma membrane.
The selective interaction of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein with specific molecules in the cytoplasm, thereby inhibiting its transport to the cell membrane.
The selective interaction of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein with specific molecules in the cytoplasm, thereby inhibiting its transport to the cell membrane.
The selective interaction of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein with specific molecules in the cytoplasm, thereby inhibiting its transport to the cell membrane.
The selective interaction of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein with specific molecules in the cytoplasm, thereby inhibiting its transport to the cell membrane.
The selective interaction of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein with specific molecules in the cytoplasm, thereby inhibiting its transport to the cell membrane.
The selective interaction of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein with specific molecules in the cytoplasm, thereby inhibiting its transport to the cell membrane.
The selective interaction of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein with specific molecules in the cytoplasm, thereby inhibiting its transport to the cell membrane.
The selective interaction of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein with specific molecules in the cytoplasm, thereby inhibiting its transport to the cell membrane.
The selective interaction of Cystic Fibrosis Transmembrane conductance Regulator (CFTR) protein with specific molecules in the cytoplasm, thereby inhibiting its transport to the cell membrane.
A series of molecular signals that leads to the upregulation of calcium-dependent phospholipase A2 activity in response to the signal.
A series of molecular signals that leads to the upregulation of calcium-dependent phospholipase A2 activity in response to the signal.
A series of molecular signals that leads to the upregulation of calcium-dependent phospholipase A2 activity in response to the signal.
Any process involved in sustaining the fidelity and copy number of rDNA repeats.
Any process involved in sustaining the fidelity and copy number of rDNA repeats.
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) using energy from the hydrolysis of ATP.
The process whose specific outcome is the progression of the embryo over time, from zygote formation through a stage including a notochord and neural tube until birth or egg hatching.
The process whose specific outcome is the progression of the camera-type eye over time, from its formation to the mature structure. The camera-type eye is an organ of sight that receives light through an aperture and focuses it through a lens, projecting it on a photoreceptor field.
The process whose specific outcome is the progression of the camera-type eye over time, from its formation to the mature structure. The camera-type eye is an organ of sight that receives light through an aperture and focuses it through a lens, projecting it on a photoreceptor field.
The process in which a monocyte acquires the specialized features of a dendritic cell, an immunocompetent cell of the lymphoid and hemopoietic systems and skin.
Any process that modulates the binding and fusion of a sperm to the oocyte plasma membrane.
Any process that stops or prevents the binding and fusion of a sperm to the oocyte plasma membrane.
Any process that stops or prevents the binding and fusion of a sperm to the oocyte plasma membrane.
Any process that stops or prevents the binding and fusion of a sperm to the oocyte plasma membrane.
Any process that stops or prevents the binding and fusion of a sperm to the oocyte plasma membrane.
Any process that stops or prevents the binding and fusion of a sperm to the oocyte plasma membrane.
Any process that stops or prevents the binding and fusion of a sperm to the oocyte plasma membrane.
Interacting selectively and non-covalently with the microtubule constituent protein alpha-tubulin.
Interacting selectively and non-covalently with the microtubule constituent protein gamma-tubulin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of the cytokine lymphotoxin A.