The chemical reactions and pathways resulting in the formation 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 involving glycosinolates, substituted thioglycosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the formation of glycosinolates, substituted thioglycosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the formation of glycosinolates, substituted thioglycosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the formation of glycosinolates, substituted thioglycosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the formation of glycosinolates, substituted thioglycosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the breakdown of glycosinolates, substituted thioglycosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the breakdown of glycosinolates, substituted thioglycosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the breakdown of glycosinolates, substituted thioglycosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways involving glucosinolates, substituted thioglucosides found in rapeseed products and related cruciferae. They are metabolized to a variety of toxic products which are most likely the cause of hepatocytic necrosis in animals and humans.
The chemical reactions and pathways resulting in the formation of glucosinolates, substituted thioglucosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the formation of glucosinolates, substituted thioglucosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the formation of glucosinolates, substituted thioglucosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the formation of glucosinolates, substituted thioglucosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the breakdown of glucosinolates, substituted thioglucosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the breakdown of glucosinolates, substituted thioglucosides found in rapeseed products and related cruciferae.
The chemical reactions and pathways resulting in the breakdown of glucosinolates, substituted thioglucosides found in rapeseed products and related cruciferae.
Combining with the Fc region of an immunoglobulin protein and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with the Fc region of an immunoglobulin protein and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with high affinity with an immunoglobulin of the IgE isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with high affinity with an immunoglobulin of the IgE isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with high affinity with an immunoglobulin of an IgG isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with high affinity with an immunoglobulin of an IgG isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with low affinity with an immunoglobulin of the IgE isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with low affinity with an immunoglobulin of the IgE isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with low affinity with an immunoglobulin of an IgG isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with low affinity with an immunoglobulin of an IgG isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with an immunoglobulin of an IgA isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with an immunoglobulin of the IgE isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with an immunoglobulin of an IgG isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
The proteasome core subcomplex that constitutes the two outer rings of the proteasome core complex. An example of this component is found in Mus musculus.
The proteasome core subcomplex that constitutes the two inner rings of the proteasome core complex. An example of this component is found in Mus musculus.
Catalysis of the transfer of FAT10 from one protein to another via the reaction X-FAT10 + Y --> Y-FAT10 + X, where both X-FAT10 and Y-FAT10 are covalent linkages.
Catalysis of the covalent attachment of the ubiquitin-like protein Atg8 to substrate molecules; phosphatidylethanolamine is a known substrate.
Catalysis of the covalent attachment of the ubiquitin-like protein Atg8 to substrate molecules; phosphatidylethanolamine is a known substrate.
Catalysis of the covalent attachment of the ubiquitin-like protein Atg8 to substrate molecules; phosphatidylethanolamine is a known substrate.
Catalysis of the transfer of ATG12 from one protein to another via the reaction X-ATG12 + Y --> Y-ATG12 + X, where both X-ATG12 and Y-ATG12 are covalent linkages.
Catalysis of the transfer of ATG12 from one protein to another via the reaction X-ATG12 + Y --> Y-ATG12 + X, where both X-ATG12 and Y-ATG12 are covalent linkages.
Catalysis of the transfer of ATG12 from one protein to another via the reaction X-ATG12 + Y --> Y-ATG12 + X, where both X-ATG12 and Y-ATG12 are covalent linkages.
Catalysis of the transfer of ATG12 from one protein to another via the reaction X-ATG12 + Y --> Y-ATG12 + X, where both X-ATG12 and Y-ATG12 are covalent linkages.
Catalysis of the activation of the small ubiquitin-related modifier APG12, through the formation of an ATP-dependent high-energy thiolester bond.
Catalysis of the activation of the small ubiquitin-related modifier APG8, through the formation of an ATP-dependent high-energy thiolester bond.
Catalysis of the activation of the small ubiquitin-related modifier APG8, through the formation of an ATP-dependent high-energy thiolester bond.
Catalysis of the activation of the small ubiquitin-related modifier FAT10, through the formation of an ATP-dependent high-energy thiolester bond.
Catalysis of the initiation of the NEDD8 (RUB1) conjugation cascade.
Catalysis of the initiation of the NEDD8 (RUB1) conjugation cascade.
Catalysis of the activation of the small ubiquitin-related modifier ISG15, through the formation of an ATP-dependent high-energy thiolester bond.
Catalysis of the hydrolysis of peptide or isopeptide bonds within small proteins such as ubiquitin or ubiquitin-like proteins (e.g. APG8, ISG15, NEDD8, SUMO), or between the small protein and a larger protein to which it has been conjugated.
Catalysis of the hydrolysis of peptide or isopeptide bonds within small proteins such as ubiquitin or ubiquitin-like proteins (e.g. APG8, ISG15, NEDD8, SUMO), or between the small protein and a larger protein to which it has been conjugated.
Catalysis of the hydrolysis of peptide or isopeptide bonds within small proteins such as ubiquitin or ubiquitin-like proteins (e.g. APG8, ISG15, NEDD8, SUMO), or between the small protein and a larger protein to which it has been conjugated.
Catalysis of the hydrolysis of NEDD8, a small ubiquitin-related modifier, from previously neddylated substrates.
Catalysis of the hydrolysis of ISG15, a small ubiquitin-related modifier, from previously modified substrates.
Catalysis of the hydrolysis of APG8, a small ubiquitin-related modifier.
Catalysis of the hydrolysis of APG8, a small ubiquitin-related modifier.
Catalysis of the transfer of a ubiquitin-like from one protein to another via the reaction X-ULP + Y --> Y-ULP + X, where both X-ULP and Y-ULP are covalent linkages. ULP represents a ubiquitin-like protein.
Catalysis of the transfer of a ubiquitin-like from one protein to another via the reaction X-ULP + Y --> Y-ULP + X, where both X-ULP and Y-ULP are covalent linkages. ULP represents a ubiquitin-like protein.
Catalysis of the transfer of a ubiquitin-like from one protein to another via the reaction X-ULP + Y --> Y-ULP + X, where both X-ULP and Y-ULP are covalent linkages. ULP represents a ubiquitin-like protein.
Catalysis of the transfer of a ubiquitin-like from one protein to another via the reaction X-ULP + Y --> Y-ULP + X, where both X-ULP and Y-ULP are covalent linkages. ULP represents a ubiquitin-like protein.
Catalysis of the transfer of a ubiquitin-like from one protein to another via the reaction X-ULP + Y --> Y-ULP + X, where both X-ULP and Y-ULP are covalent linkages. ULP represents a ubiquitin-like protein.
Catalysis of the transfer of a ubiquitin-like from one protein to another via the reaction X-ULP + Y --> Y-ULP + X, where both X-ULP and Y-ULP are covalent linkages. ULP represents a ubiquitin-like protein.
Catalysis of the transfer of a ubiquitin-like from one protein to another via the reaction X-ULP + Y --> Y-ULP + X, where both X-ULP and Y-ULP are covalent linkages. ULP represents a ubiquitin-like protein.
Catalysis of the transfer of a ubiquitin-like from one protein to another via the reaction X-ULP + Y --> Y-ULP + X, where both X-ULP and Y-ULP are covalent linkages. ULP represents a ubiquitin-like protein.
Catalysis of the transfer of a ubiquitin-like from one protein to another via the reaction X-ULP + Y --> Y-ULP + X, where both X-ULP and Y-ULP are covalent linkages. ULP represents a ubiquitin-like protein.
Catalysis of the transfer of NEDD8 from one protein to another via the reaction X-NEDD8 + Y --> Y-NEDD8 + X, where both X-NEDD8 and Y-NEDD8 are covalent linkages.
Catalysis of the transfer of NEDD8 from one protein to another via the reaction X-NEDD8 + Y --> Y-NEDD8 + X, where both X-NEDD8 and Y-NEDD8 are covalent linkages.
Catalysis of the transfer of NEDD8 from one protein to another via the reaction X-NEDD8 + Y --> Y-NEDD8 + X, where both X-NEDD8 and Y-NEDD8 are covalent linkages.
Catalysis of the transfer of NEDD8 from one protein to another via the reaction X-NEDD8 + Y --> Y-NEDD8 + X, where both X-NEDD8 and Y-NEDD8 are covalent linkages.
Catalysis of the transfer of NEDD8 from one protein to another via the reaction X-NEDD8 + Y --> Y-NEDD8 + X, where both X-NEDD8 and Y-NEDD8 are covalent linkages.
Catalysis of the transfer of NEDD8 from one protein to another via the reaction X-NEDD8 + Y --> Y-NEDD8 + X, where both X-NEDD8 and Y-NEDD8 are covalent linkages.
Catalysis of the transfer of SUMO from one protein to another via the reaction X-SUMO + Y --> Y-SUMO + X, where both X-SUMO and Y-SUMO are covalent linkages.
Catalysis of the transfer of SUMO from one protein to another via the reaction X-SUMO + Y --> Y-SUMO + X, where both X-SUMO and Y-SUMO are covalent linkages.
Catalysis of the transfer of SUMO from one protein to another via the reaction X-SUMO + Y --> Y-SUMO + X, where both X-SUMO and Y-SUMO are covalent linkages.
Catalysis of the transfer of SUMO from one protein to another via the reaction X-SUMO + Y --> Y-SUMO + X, where both X-SUMO and Y-SUMO are covalent linkages.
Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: acetyl-CoA + (alpha-tubulin) L-lysine = CoA + (alpha-tubulin) N6-acetyl-L-lysine.
Catalysis of the reaction: acetyl-CoA + (alpha-tubulin) L-lysine = CoA + (alpha-tubulin) N6-acetyl-L-lysine.
Catalysis of the reaction: acetyl-CoA + (alpha-tubulin) L-lysine = CoA + (alpha-tubulin) N6-acetyl-L-lysine.
Catalysis of the reaction: acetyl-CoA + (alpha-tubulin) L-lysine = CoA + (alpha-tubulin) N6-acetyl-L-lysine.
Catalysis of the reaction: acetyl-CoA + (alpha-tubulin) L-lysine = CoA + (alpha-tubulin) N6-acetyl-L-lysine.
Catalysis of the reaction: acetyl-CoA + (alpha-tubulin) L-lysine = CoA + (alpha-tubulin) N6-acetyl-L-lysine.
Catalysis of the reaction: acetyl-CoA + (alpha-tubulin) L-lysine = CoA + (alpha-tubulin) N6-acetyl-L-lysine.
Catalysis of the reaction: acetyl-CoA + (alpha-tubulin) L-lysine = CoA + (alpha-tubulin) N6-acetyl-L-lysine.
The formation of a cross-link between peptide chains mediated by a chondroitin 4-sulfate glycosaminoglycan that originates from a typical O-glycosidic link to serine of one chain; the other chain is esterified, via the alpha-carbon of its C-terminal Asp, to C-6 of an internal N-acetylgalactosamine of the glycosaminoglycan chain.
The cyclization of asparagine to yield an L-aspartimide (otherwise known as alpha-aminosuccinimide) residue at the C-terminus of an excised intein during protein splicing.
The cyclization of glutamine to yield an L-glutamimide residue at the C-terminus of an excised intein during protein splicing.
The carboxylation of peptidyl-aspartic acid to form peptidyl-L-beta-carboxyaspartic acid.
The chemical reactions and pathways resulting in the formation of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.
The chemical reactions and pathways resulting in the formation of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.
The chemical reactions and pathways resulting in the formation of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.
The chemical reactions and pathways resulting in the formation of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.
Catalysis of the reaction: 2 R-H + 2 bromide + hydrogen peroxide = 2 R-Br + 2 H2O. Enzymes with this activity often accept other halide ions as substrates, including chloride and iodide.
Catalysis of the reaction: N-acyl-L-aspartate + H2O = a fatty acid anion + L-aspartate.
Catalysis of the reaction: N-acyl-L-aspartate + H2O = a fatty acid anion + L-aspartate.
Catalysis of the reaction: N-acyl-L-aspartate + H2O = a fatty acid anion + L-aspartate.
Catalysis of the reaction: N-acyl-L-aspartate + H2O = a fatty acid anion + L-aspartate.
Catalysis of the reaction: N-acyl-L-aspartate + H2O = a fatty acid anion + L-aspartate.
Interacting selectively and non-covalently with polyamines, organic compounds containing two or more amino groups.
Interacting selectively and non-covalently with spermidine, N-(3-aminopropyl)-1,4-diaminobutane.
Interacting selectively and non-covalently with putrescine, 1,4-diaminobutane, the polyamine formed by decarboxylation of ornithine and the metabolic precursor of spermidine and spermine.
Interacting selectively and non-covalently with cocaine (2-beta-carbomethoxy-3-beta-benzoxytropane), an alkaloid obtained from dried leaves of the South American shrub Erythroxylon coca or by chemical synthesis.
A multisubunit complex composed of two copies of a restriction (R) subunit, two copies of a methylation (M) subunit, and one copy of a specificity (S) subunit. This complex recognizes specific short DNA sequences (through the S subunit), and binds to them. If the recognition site is hemimethylated, the complex acts as a methyltransferase which modifies the recognition site, using S-adenosylmethionine as the methyl donor. Only the M and S subunits are required for this reaction. If the complex binds to an unmethylated recognition site, then the complex translocates the DNA bidirectionally in an ATP-dependent manner. When the translocation is stalled by impact with another complex or unusual DNA structure, the enzyme functions as an endonuclease and cleavage of the DNA will occur, hundreds or thousands of base pairs away from the recognition site. These DNA restriction systems are used by bacteria to defend against phage and other foreign DNA that may enter a cell.
A heterodimeric enzyme complex composed of two subunits, Res and Mod, that functions as an endonuclease and cleaves DNA. Cleavage will only occur when there are two un-methylated copies of a specific recognition site in an inverse orientation on the DNA. Cleavage occurs at a specific distance away from one of the recognition sites. The Mod subunit can act alone as a methyltansferase. DNA restriction systems such as this are used by bacteria to defend against phage and other foreign DNA that may enter a cell.
A protein complex that in its canonical form is composed of two identical immunoglobulin heavy chains and two identical immunoglobulin light chains, held together by disulfide bonds and sometimes complexed with additional proteins. An immunoglobulin complex may be embedded in the plasma membrane or present in the extracellular space, in mucosal areas or other tissues, or circulating in the blood or lymph.
An immunoglobulin complex that is present in the plasma membrane of B cells and that in its canonical form is composed of two identical immunoglobulin heavy chains and two identical immunoglobulin light chains and a signaling subunit, a heterodimer of the Ig-alpha and Ig-beta proteins.
An immunoglobulin complex that is present in the plasma membrane of B cells and that in its canonical form is composed of two identical immunoglobulin heavy chains and two identical immunoglobulin light chains and a signaling subunit, a heterodimer of the Ig-alpha and Ig-beta proteins.
An immunoglobulin complex that is present in the plasma membrane of B cells and that in its canonical form is composed of two identical immunoglobulin heavy chains and two identical immunoglobulin light chains and a signaling subunit, a heterodimer of the Ig-alpha and Ig-beta proteins.
An immunoglobulin complex that is present in the plasma membrane of B cells and that in its canonical form is composed of two identical immunoglobulin heavy chains and two identical immunoglobulin light chains and a signaling subunit, a heterodimer of the Ig-alpha and Ig-beta proteins.
An immunoglobulin complex that is present in the plasma membrane of B cells and that in its canonical form is composed of two identical immunoglobulin heavy chains and two identical immunoglobulin light chains and a signaling subunit, a heterodimer of the Ig-alpha and Ig-beta proteins.
An immunoglobulin complex that is present in the plasma membrane of B cells and that in its canonical form is composed of two identical immunoglobulin heavy chains and two identical immunoglobulin light chains and a signaling subunit, a heterodimer of the Ig-alpha and Ig-beta proteins.
An immunoglobulin complex that is present in the plasma membrane of B cells and that in its canonical form is composed of two identical immunoglobulin heavy chains and two identical immunoglobulin light chains and a signaling subunit, a heterodimer of the Ig-alpha and Ig-beta proteins.
An immunoglobulin complex that is present in the plasma membrane of B cells and that in its canonical form is composed of two identical immunoglobulin heavy chains and two identical immunoglobulin light chains and a signaling subunit, a heterodimer of the Ig-alpha and Ig-beta proteins.
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P1 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content; they contain fewer peroxisomal proteins than the other subforms.
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P2 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content; they are the least dense of the subforms observed.
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P3 peroxisomes are formed by fusion of P1 and P2 peroxisomes, and are distinguished from the other subforms on the bases of buoyant density and protein content.
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P4 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content.
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P5 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content.
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P6 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content, and are equivalent to mature peroxisomes.
Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of oxygen (O2).
The process by which an organism or tissue maintains a population of stem cells of a single type.  This can be achieved by a number of mechanisms: stem cell asymmetric division maintains stem cell numbers; stem cell symmetric division increases them; maintenance of a stem cell niche maintains the conditions for commitment to the stem cell fate for some types of stem cell; stem cells may arise de novo from other cell types.
Stops, prevents or reduces the activity of aspartic-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; the optimum reaction pH is below 5 due to an aspartic residue involved in the catalytic process.
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 cadmium (Cd) 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 cadmium (Cd) 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 chromate 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 mercury 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 mercury 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 mercury ion stimulus.
Stops, prevents or reduces the activity of the enzyme phospholipase A2.
Interacting selectively and non-covalently with any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
Interacting selectively and non-covalently with retinol, vitamin A1, 2,6,6-trimethyl-1-(9'-hydroxy-3',7'-dimethylnona-1',3',5',7'-tetraenyl)cyclohex-1-ene, one of the three components that makes up vitamin A. Retinol is an intermediate in the vision cycle and it also plays a role in growth and differentiation.
Interacting selectively and non-covalently with retinol, vitamin A1, 2,6,6-trimethyl-1-(9'-hydroxy-3',7'-dimethylnona-1',3',5',7'-tetraenyl)cyclohex-1-ene, one of the three components that makes up vitamin A. Retinol is an intermediate in the vision cycle and it also plays a role in growth and differentiation.
Interacting selectively and non-covalently with a vitamin, 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.
Interacting selectively and non-covalently with ribosomal RNA.
Stops, prevents, or reduces the activity of a calcium channel.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a neurotransmitter.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a neurotransmitter.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a neurotransmitter.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a neurotransmitter.
Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of a neurotransmitter.
The chemical reactions and pathways involving L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.
The chemical reactions and pathways involving L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.
The chemical reactions and pathways involving L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.
The chemical reactions and pathways involving L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.
The chemical reactions and pathways involving L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.
The chemical reactions and pathways resulting in the formation of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the formation of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the formation of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the formation of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the formation of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the formation of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the formation of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the formation of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the breakdown of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the breakdown of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the breakdown of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the breakdown of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the breakdown of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the breakdown of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the breakdown of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases.
The chemical reactions and pathways involving 5-methylcytosine, a methylated base of DNA.
The chemical reactions and pathways involving cytosine, 4-amino-2-hydroxypyrimidine, a pyrimidine derivative that is one of the five main bases found in nucleic acids; it occurs widely in cytidine derivatives.
The chemical reactions and pathways involving thymine, 5-methyluracil, one of the two major pyrimidine bases present (as thymidine) in DNA but not found in RNA other than (as ribothymidine) in transfer RNA, where it is a minor base.
The chemical reactions and pathways involving uracil, 2,4-dioxopyrimidine, one of the pyrimidine bases occurring in RNA, but not in DNA.
Interacting selectively and non-covalently with an immunoglobulin of an IgA isotype.
Interacting selectively and non-covalently with an immunoglobulin of the IgE isotype.
Interacting selectively and non-covalently with an immunoglobulin of an IgG isotype.
Interacting selectively and non-covalently with an immunoglobulin.
The inner, i.e. lumen-facing, lipid bilayer of an organelle envelope; usually highly selective to most ions and metabolites.
The external membrane of Gram-negative bacteria or certain organelles such as mitochondria and chloroplasts; freely permeable to most ions and metabolites.
Stops, prevents, or reduces the activity of a chloride channel.
Stops, prevents, or reduces the activity of a potassium channel.
Stops, prevents, or reduces the activity of a sodium channel.
The chemical reactions and pathways resulting in the formation of streptomycin, a commonly used antibiotic in cell culture media; it acts only on prokaryotes and blocks transition from initiation complex to chain elongating ribosome.
The chemical reactions and pathways resulting in the formation of streptomycin, a commonly used antibiotic in cell culture media; it acts only on prokaryotes and blocks transition from initiation complex to chain elongating ribosome.
The chemical reactions and pathways resulting in the formation of streptomycin, a commonly used antibiotic in cell culture media; it acts only on prokaryotes and blocks transition from initiation complex to chain elongating ribosome.
The chemical reactions and pathways resulting in the formation of streptomycin, a commonly used antibiotic in cell culture media; it acts only on prokaryotes and blocks transition from initiation complex to chain elongating ribosome.
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 tellurium 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 tellurium ion stimulus.
Catalysis of the reaction: 1,8-diazacyclotetradecane-2,9-dione + H(2)O = N-(6-aminohexanoyl)-6-aminohexanoate.
Catalysis of the reaction: N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate.
Catalysis of the reaction: N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate.
The chemical reactions and pathways resulting in the breakdown of 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 resulting in the breakdown of 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 resulting in the breakdown of 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 resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.
The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.
The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.
The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.
The chemical reactions and pathways resulting in the formation of lysine by the aminoadipic pathway.
The chemical reactions and pathways resulting in the formation of lysine by the aminoadipic pathway.
The chemical reactions and pathways resulting in the formation of lysine by the aminoadipic pathway.
The chemical reactions and pathways resulting in the formation of lysine by the aminoadipic pathway.
The chemical reactions and pathways resulting in the formation of lysine by the aminoadipic pathway.
The chemical reactions and pathways resulting in the formation of lysine by the aminoadipic pathway.
The chemical reactions and pathways resulting in the formation of lysine by the aminoadipic pathway.
The formation of peptidyl-thyronine from peptidyl-tyrosine in thyroglobulin by phenyl transfer coupled with the formation of peptidyl-dehydroalanine.
The formation of peptidyl-thyronine from peptidyl-tyrosine in thyroglobulin by phenyl transfer coupled with the formation of peptidyl-dehydroalanine.
The formation of peptidyl-thyronine from peptidyl-tyrosine in thyroglobulin by phenyl transfer coupled with the formation of peptidyl-dehydroalanine.
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 bacteriocin stimulus. A bacteriocin is a protein substance released by certain bacteria that kills but does not lyse closely related strains of bacteria. Specific bacteriocins attach to specific receptors on cell walls and induce specific metabolic block, e.g. cessation of nucleic acid or protein synthesis of oxidative phosphorylation.
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 streptomycin stimulus. Streptomycin is a commonly used antibiotic in cell culture media which acts only on prokaryotes and blocks transition from initiation complex to chain elongating ribosome.
The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex.
The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex.
The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex.
The process in which an antigen-presenting cell expresses antigen (peptide or lipid) of endogenous origin on its cell surface in association with an MHC protein complex.
The process in which an antigen-presenting cell expresses antigen (peptide or lipid) of exogenous origin on its cell surface in association with an MHC protein complex.
The process in which an antigen-presenting cell expresses a peptide antigen of endogenous 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 endogenous 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 endogenous 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 endogenous 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 endogenous 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 II protein complex. The peptide antigen is typically, but not always, processed from a whole protein.
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 II protein complex. The peptide antigen is typically, but not always, processed from a whole protein.
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 II protein complex. The peptide antigen is typically, but not always, processed from a whole protein.
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 II protein complex. The peptide antigen is typically, but not always, processed from a whole protein.
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 II protein complex. The peptide antigen is typically, but not always, processed from a whole protein.
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 II protein complex. The peptide antigen is typically, but not always, processed from a whole protein.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
Modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.
The chemical reactions and pathways involving pteridine, pyrazino(2,3-dipyrimidine), the parent structure of pterins and the pteroyl group.
Interacting selectively and non-covalently and stoichiometrically with kinesin, a member of a superfamily of microtubule-based motor proteins that perform force-generating tasks such as organelle transport and chromosome segregation.
The activity of linking kinesins, cytoplasmic proteins responsible for moving vesicles and organelles towards the distal end of microtubules, to mitochondria.
The directed movement of mitochondria along microtubules in nerve cell axons.
The component of a plasma 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 plasma 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 plasma 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 plasma membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
Interacting selectively and non-covalently with a kinase, any enzyme that catalyzes the transfer of a phosphate group.
Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
Interacting selectively and non-covalently with any phosphatase.
Interacting selectively and non-covalently with any protein phosphatase.
Interacting selectively and non-covalently with a specific domain of a protein.
Interacting selectively and non-covalently with a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse.
Interacting selectively and non-covalently with a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse.
Interacting selectively and non-covalently with a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse.
Interacting selectively and non-covalently with a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse.
Interacting selectively and non-covalently with a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse.
Interacting selectively and non-covalently with a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse.
Interacting selectively and non-covalently with a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse.
Interacting selectively and non-covalently with a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse.
A cyclin-dependent kinase activating kinase complex capable of activating cyclin-dependent kinases by threonine phosphorylation, thus regulating cell cycle progression. consists of a kinase, cyclin and optional assembly factors, in human CDK7, CCNH and MNAT1. CAK activity is itself regulated throughout the cell cycle by T-loop phosphorylation of its kinase component (CDK7 in human). Phosphorylation of serine residues during mitosis inactivates the enzyme. Also capable of CAK phosphorylating the carboxyl-terminal domain (CTD) of RNA polymerase II and other transcription activating proteins, as part of the general transcription factor TFIIH.
A cyclin-dependent kinase activating kinase complex capable of activating cyclin-dependent kinases by threonine phosphorylation, thus regulating cell cycle progression. consists of a kinase, cyclin and optional assembly factors, in human CDK7, CCNH and MNAT1. CAK activity is itself regulated throughout the cell cycle by T-loop phosphorylation of its kinase component (CDK7 in human). Phosphorylation of serine residues during mitosis inactivates the enzyme. Also capable of CAK phosphorylating the carboxyl-terminal domain (CTD) of RNA polymerase II and other transcription activating proteins, as part of the general transcription factor TFIIH.
Cyclin-dependent protein kinase (CDK) complex found in the nucleus.
Modification of the activity of the enzyme [pyruvate dehydrogenase (lipoamide)] phosphatase.
A mitochondrial complex of a regulatory and catalytic subunit that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. An example of this component is found in Mus musculus.
The action of a molecule that contributes to the structural integrity of the myelin sheath of a nerve.
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein; increases the activity of a cyclin-dependent protein kinase (CDK).
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein; increases the activity of a cyclin-dependent protein kinase (CDK).
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein; increases the activity of a cyclin-dependent protein kinase (CDK).
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein; increases the activity of a cyclin-dependent protein kinase (CDK).
Modulation of the activity of the enzyme cyclin-dependent protein kinase activating kinase.
The accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development.
The accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development.
The accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development.
The accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development.
The accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development.
The accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development.
The accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development.
The accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development.
The racemization of peptidyl-alanine.
The dehydration of peptidyl-serine, followed by hydrogenation to produce peptidyl-D-alanine.
The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N'(omega)-dimethyl-L-arginine.
The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N(omega)-dimethyl-L-arginine.
The chemical reactions and pathways resulting in the formation of internal peptidyl-1-thioglycine, which has an internal C=S bond, instead of an internal C=O bond, in the peptide.
The chemical reactions and pathways resulting in the formation of internal peptidyl-1-thioglycine, which has an internal C=S bond, instead of an internal C=O bond, in the peptide.
The chemical reactions and pathways resulting in the formation of internal peptidyl-1-thioglycine, which has an internal C=S bond, instead of an internal C=O bond, in the peptide.
The chemical reactions and pathways resulting in the formation of carboxy-terminal peptidyl-1-thioglycine, which has a carboxy-terminal thiocarboxy-C(=O)-SH bond.
The chemical reactions and pathways resulting in the formation of carboxy-terminal peptidyl-1-thioglycine, which has a carboxy-terminal thiocarboxy-C(=O)-SH bond.
The chemical reactions and pathways resulting in the formation of carboxy-terminal peptidyl-1-thioglycine, which has a carboxy-terminal thiocarboxy-C(=O)-SH bond.
The covalent linking of a chromophore to a protein via peptidyl-cysteines.
The covalent linking of the alpha-1-microglobulin chromophore to the protein; the structure of the chromophore is not known. It is probably heterogeneous and involving two cysteines in thioether bonds.
The oxidation of peptidyl-tryptophan to form tryptophan-6,7-dione, otherwise known as tryptophyl quinone, which is further modified by cross-linking to either tryptophan or cysteine.
The cross-linking of a cysteine residue to tryptophyl quinone to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone, a cofactor found at the active site of amine dehydrogenase.
The cross-linking of a cysteine residue to an aspartic acid residue to form 3-(S-L-cysteinyl)-L-aspartic acid.
The cross-linking of a cysteine residue to a glutamic acid residue to form 4-(S-L-cysteinyl)-L-glutamic acid.
The modification of peptidyl-aspartic acid to form peptidyl-cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester, typical of the barley lipid transfer protein 1.
The modification of peptidyl-aspartic acid to form peptidyl-cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester, typical of the barley lipid transfer protein 1.
The modification of peptidyl-aspartic acid to form peptidyl-cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester, typical of the barley lipid transfer protein 1.
The modification of peptidyl-lysine to form N6-3,4-didehydroretinylidene-L-lysine.
Any intracellular signal transduction in which the signal is passed on within the cell via a second messenger; a small molecule or ion that can be quickly generated or released from intracellular stores, and can diffuse within the cell. Second-messenger signaling includes production or release of the second messenger, and effectors downstream of the second messenger that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via a second messenger; a small molecule or ion that can be quickly generated or released from intracellular stores, and can diffuse within the cell. Second-messenger signaling includes production or release of the second messenger, and effectors downstream of the second messenger that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via a second messenger; a small molecule or ion that can be quickly generated or released from intracellular stores, and can diffuse within the cell. Second-messenger signaling includes production or release of the second messenger, and effectors downstream of the second messenger that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via a second messenger; a small molecule or ion that can be quickly generated or released from intracellular stores, and can diffuse within the cell. Second-messenger signaling includes production or release of the second messenger, and effectors downstream of the second messenger that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via a second messenger; a small molecule or ion that can be quickly generated or released from intracellular stores, and can diffuse within the cell. Second-messenger signaling includes production or release of the second messenger, and effectors downstream of the second messenger that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via a second messenger; a small molecule or ion that can be quickly generated or released from intracellular stores, and can diffuse within the cell. Second-messenger signaling includes production or release of the second messenger, and effectors downstream of the second messenger that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic AMP (cAMP). Includes production of cAMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via cyclic GMP (cGMP). Includes production of cGMP, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via a cyclic nucleotide. Includes production or release of the cyclic nucleotide, and downstream effectors that further transmit the signal within the cell.
Any intracellular signal transduction in which the signal is passed on within the cell via an inositol phosphate. Includes production of the inositol phosphate, and downstream effectors that further transmit the signal within the cell. Inositol phosphates are a group of mono- to poly-phosphorylated inositols, and include inositol monophosphate (IP), inositol trisphosphate (IP3), inositol pentakisphosphate (IP5) and inositol hexaphosphate (IP6).
A series of molecular signals in which a cell uses an inositol-containing lipid to convert a signal into a response. Inositol lipids include the phosphoinositides (phosphatidylinositol and its phosphorylated derivatives), ceramides containing inositol, and inositol glycolipids.
A series of molecular signals in which a cell uses an inositol-containing lipid to convert a signal into a response. Inositol lipids include the phosphoinositides (phosphatidylinositol and its phosphorylated derivatives), ceramides containing inositol, and inositol glycolipids.
A series of molecular signals in which a cell uses an inositol-containing lipid to convert a signal into a response. Inositol lipids include the phosphoinositides (phosphatidylinositol and its phosphorylated derivatives), ceramides containing inositol, and inositol glycolipids.
The autocatalytic formation of isopeptide bonds by ligation of peptidyl-lysine and peptidyl-asparagine residues; known to occur in the capsid of some bacteriophage, such as HK97, where it is thought to provide a mechanism for stabilizing the capsid.
The formation of isopeptide bonds by ligation of peptidyl-lysine and peptidyl-asparagine residues; occurs in mammals in proteins as yet unidentified by a mechanism probably analogous to that of transglutaminase reactions.
The modification of peptidyl-cysteine to form peptidyl-S-palmitoleyl-L-cysteine specifically.
The modification of peptidyl-cysteine to form peptidyl-S-palmitoleyl-L-cysteine specifically.
The modification of peptidyl-cysteine to form peptidyl-S-palmitoleyl-L-cysteine specifically.
Covalent attachment of the ubiquitin-like protein NEDD8 (RUB1) to another protein.
Covalent attachment of the ubiquitin-like protein NEDD8 (RUB1) to another protein.
Catalysis of the activation of the proteolytically processed small ubiquitin-related modifier SUMO, through the formation of an ATP-dependent high-energy thiolester bond.
Catalysis of the activation of the proteolytically processed small ubiquitin-related modifier SUMO, through the formation of an ATP-dependent high-energy thiolester bond.
Catalysis of the activation of the proteolytically processed small ubiquitin-related modifier SUMO, through the formation of an ATP-dependent high-energy thiolester bond.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by covalent attachment of the ubiquitin-like protein SMT3 to the target protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by covalent attachment of the ubiquitin-like protein SMT3 to the target protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by covalent attachment of the ubiquitin-like protein SMT3 to the target protein.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by covalent attachment of the ubiquitin-like protein SMT3 to the target protein.
The covalent addition to a protein of Smt3, a ubiquitin-like protein.
The covalent addition to a protein of Smt3, a ubiquitin-like protein.
A reproduction process that creates a new organism by combining the genetic material of two gametes, which may come from two organisms or from a single organism, in the case of self-fertilizing hermaphrodites, e.g. C. elegans, or self-fertilization in plants. It occurs both in eukaryotes and prokaryotes: in multicellular eukaryotic organisms, an individual is created anew; in prokaryotes, the initial cell has additional or transformed genetic material. In a process called genetic recombination, genetic material (DNA) originating from two gametes join up so that homologous sequences are aligned with each other, and this is followed by exchange of genetic information. After the new recombinant chromosome is formed, it is passed on to progeny.
The biological process in which new individuals are produced by either a single cell or a group of cells, in the absence of any sexual process.
Interacting selectively and non-covalently with a cytokine, 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.
Interacting selectively and non-covalently with a cytokine, 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.
Interacting selectively and non-covalently with a cytokine, 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.
Interacting selectively and non-covalently with a chemokine. Chemokines are 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.
Interacting selectively and non-covalently with a C-C chemokine; C-C chemokines do not have an amino acid between the first two cysteines of the characteristic four-cysteine motif.
Interacting selectively and non-covalently with a C-X-C chemokine; C-X-C chemokines have a single amino acid between the first two cysteines of the characteristic four cysteine motif.
Interacting selectively and non-covalently with interleukin-8.
Interacting selectively and non-covalently with a C-X3-C chemokine; C-X3-C chemokines have three amino acids between the first two cysteines of the characteristic four-cysteine motif.
Interacting selectively and non-covalently with an interferon, a protein produced by the immune systems of many animals in response to a challenge by a foreign agent.
Interacting selectively and non-covalently with a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families.
Interacting selectively and non-covalently with a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families.
Interacting selectively and non-covalently with a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families.
Interacting selectively and non-covalently with a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families.
Interacting selectively and non-covalently with a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families.
Interacting selectively and non-covalently with a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families.
Interacting selectively and non-covalently with a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families.
Interacting selectively and non-covalently with a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families.
Interacting selectively and non-covalently with a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families.
Interacting selectively and non-covalently with a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families.
Interacting selectively and non-covalently with interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
Interacting selectively and non-covalently with interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
Interacting selectively and non-covalently with interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
Interacting selectively and non-covalently with interleukin-1.
Interacting selectively and non-covalently with interleukin-10.
Interacting selectively and non-covalently with interleukin-11.
Interacting selectively and non-covalently with interleukin-12.
Interacting selectively and non-covalently with interleukin-13.
Interacting selectively and non-covalently with interleukin-14.
Interacting selectively and non-covalently with any member of the interleukin-17 family of cytokines.
Interacting selectively and non-covalently with interleukin-2.
Interacting selectively and non-covalently with interleukin-21.
Interacting selectively and non-covalently with interleukin-3.
Interacting selectively and non-covalently with interleukin-4.
Interacting selectively and non-covalently with interleukin-5.
Interacting selectively and non-covalently with interleukin-6.
Interacting selectively and non-covalently with interleukin-7.
Interacting selectively and non-covalently with interleukin-9.
The replication of damaged DNA by synthesis across a lesion in the template strand; a specialized DNA polymerase or replication complex inserts a defined nucleotide across from the lesion which allows DNA synthesis to continue beyond the lesion. This process can be mutagenic depending on the damaged nucleotide and the inserted nucleotide.
The covalent alteration of an amino acid charged on a tRNA before it is incorporated into a protein, as in N-formylmethionine, selenocysteine or pyrrolysine.
The covalent alteration of an amino acid charged on a tRNA before it is incorporated into a protein, as in N-formylmethionine, selenocysteine or pyrrolysine.
The covalent alteration of an amino acid charged on a tRNA before it is incorporated into a protein, as in N-formylmethionine, selenocysteine or pyrrolysine.
The covalent alteration of an amino acid charged on a tRNA before it is incorporated into a protein, as in N-formylmethionine, selenocysteine or pyrrolysine.
The covalent alteration of an amino acid charged on a tRNA before it is incorporated into a protein, as in N-formylmethionine, selenocysteine or pyrrolysine.
The covalent alteration of an amino acid charged on a tRNA before it is incorporated into a protein, as in N-formylmethionine, selenocysteine or pyrrolysine.
The covalent alteration of an amino acid charged on a tRNA before it is incorporated into a protein, as in N-formylmethionine, selenocysteine or pyrrolysine.
The covalent alteration of an amino acid charged on a tRNA before it is incorporated into a protein, as in N-formylmethionine, selenocysteine or pyrrolysine.
The chemical reactions and pathways resulting in the breakdown of pteridine, pyrazino(2,3-dipyrimidine), the parent structure of pterins and the pteroyl group.
The chemical reactions and pathways resulting in the breakdown of pteridine, pyrazino(2,3-dipyrimidine), the parent structure of pterins and the pteroyl group.
The chemical reactions and pathways resulting in the breakdown of pteridine, pyrazino(2,3-dipyrimidine), the parent structure of pterins and the pteroyl group.
The assembly of a septate junction, an intercellular junction found in invertebrate epithelia that is characterized by a ladder like appearance in electron micrographs and thought to provide structural strength and to provide a barrier to diffusion of solutes through the intercellular space.
Interacting selectively and non-covalently with diacylglycerol, a diester of glycerol and two fatty acids.
The plasma membrane surrounding a host cell.
Membrane-bounded vacuole within a host cell in which a symbiont organism resides. The vacuole membrane is derived from both the host and symbiont.
Membrane-bounded vacuole within a host cell in which a symbiont organism resides. The vacuole membrane is derived from both the host and symbiont.
Membrane-bounded vacuole within a host cell in which a symbiont organism resides. The vacuole membrane is derived from both the host and symbiont.
Membrane-bounded vacuole within a host cell in which a symbiont organism resides. The vacuole membrane is derived from both the host and symbiont.
Membrane-bounded vacuole within a host cell in which a symbiont organism resides. The vacuole membrane is derived from both the host and symbiont.
The space between a symbiont plasma membrane and the symbiont-containing vacuole membrane.
The space between a symbiont plasma membrane and the symbiont-containing vacuole membrane.
The lipid bilayer surrounding a symbiont-containing vacuole, derived from both the host and symbiont.
Tubular network of extensions from the symbiont-containing vacuole membrane that protrude into the host cytoplasm.
Tubular network of extensions from the symbiont-containing vacuole membrane that protrude into the host cytoplasm.
Tubular network of extensions from the symbiont-containing vacuole membrane that protrude into the host cytoplasm.
A group of cytoskeletal structures and associated membrane-bounded organelles found at the anterior end of adult obligate intracellular protozoan parasites in the phylum Apicomplexa. The apical complex is involved in attachment to and penetration of the host cell, and in parasite proliferation.
A large, club-shaped secretory organelle that forms part of the apical complex of an apicomplexan parasite, and consists of a bulbous body and a narrow electron-dense neck that extends through the conoid at the apical tip of the parasite. The rhoptry necks serve as ducts through which the contents of the rhoptries are secreted after attachment to the host has been completed and at the commencement of invasion. Rhoptry proteins function in the biogenesis and host organellar association of the parasitophorous vacuole.
A large, club-shaped secretory organelle that forms part of the apical complex of an apicomplexan parasite, and consists of a bulbous body and a narrow electron-dense neck that extends through the conoid at the apical tip of the parasite. The rhoptry necks serve as ducts through which the contents of the rhoptries are secreted after attachment to the host has been completed and at the commencement of invasion. Rhoptry proteins function in the biogenesis and host organellar association of the parasitophorous vacuole.
A small, elongated secretory organelle that forms part of the apical complex, located along the main axis of an apicomplexan parasite cell within the extreme apical region and at the periphery under the inner membrane complex. Of the specialized secretory compartments identified in apicomplexans, micronemes discharge their contents first, during initial contact of the parasite's apical pole with the host cell surface. Micronemal proteins function during parasite attachment and penetration into the target cell.
A spiral cytoskeletal structure located at the apical end of the apical complex in some apicomplexan parasites. Fibers form a left-handed spiral, and are comprised of tubulin protofilaments organized in a ribbon-like structure that differs from the conventional tubular structure characteristic of microtubules.
The plastid organelle found in apicomplexans.
Any process, either active or passive, by which an organism avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process in which a symbiont organism modulates the frequency, rate or extent of erythrocyte aggregation in its host organism, e.g. the binding of parasite-infected erythrocytes to uninfected erythrocytes.
Cell division by multiple fission in which nuclei and other organelles in the parent cell divide repeatedly and move to the cell periphery before internal membranes develop around them, producing a large number of daughter cells simultaneously.
A membrane-bounded organelle found in organisms from the order Kinetoplastida that houses the enzymes of glycolysis.
Invagination of the plasma membrane from which a cilium (also called flagellum) protrudes.
Invagination of the plasma membrane from which a cilium (also called flagellum) protrudes.
Invagination of the plasma membrane from which a cilium (also called flagellum) protrudes.
That part of the plasma membrane found in the ciliary pocket (also called flagellar pocket).
That part of the plasma membrane found in the ciliary pocket (also called flagellar pocket).
That part of the plasma membrane found in the ciliary pocket (also called flagellar pocket).
Vacuole within a parasite used for digestion of the host cell cytoplasm. An example of this component is found in the Apicomplexa.
Vacuole within a parasite used for digestion of the host cell cytoplasm. An example of this component is found in the Apicomplexa.
The modification of a host cell into an immortal cell line as a consequence of infection. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The modification of a host cell into an immortal cell line as a consequence of infection. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The modification of a host cell into an immortal cell line as a consequence of infection. The host is defined as the larger of the organisms involved in a symbiotic interaction.
An electron-dense acidic membrane-bounded organelle which contains a matrix of pyrophosphate and polyphosphates with bound calcium and other cations.
An electron-dense acidic membrane-bounded organelle which contains a matrix of pyrophosphate and polyphosphates with bound calcium and other cations.
An electron-dense acidic membrane-bounded organelle which contains a matrix of pyrophosphate and polyphosphates with bound calcium and other cations.
A sub-structure within the large single mitochondrion of kinetoplastid parasites and which is closely associated with the flagellar pocket and basal body of the flagellum.
Singlet microtubule that lie underneath the inner membrane pellicle complex and emanate from the basal ring of the conoid.
Electron-dense organelle with a granular internal matrix found throughout the merozoite life cycle stage of apicomplexan parasites; contains proteins destined to be secreted into the parasitophorous vacuole following parasite invasion of a host cell.
The chemical reactions and pathways involving hemoglobin, including its uptake and utilization.
The chemical reactions and pathways involving hemoglobin, including its uptake and utilization.
The chemical reactions and pathways involving hemoglobin, including its uptake and utilization.
The directed movement into a tissue or a cell or organelle of externally available hemoglobin by receptor-mediated endocytosis.
The directed movement into a tissue or a cell or organelle of externally available hemoglobin by receptor-mediated endocytosis.
Protrusion that develops in the plasma membrane of a parasitized erythrocyte. An example of this component is found in Plasmodium species.
An electron dense ring at the most anterior position of the apical complex, from which the conoid fibers originate; formed during an invasive life cycle stage of an apicomplexan parasite.
An electron dense ring at the most anterior position of the apical complex, from which the conoid fibers originate; formed during an invasive life cycle stage of an apicomplexan parasite.
An electron dense ring at the most posterior position of the apical complex, from which the subpellicular microtubules originate; formed during an invasive life cycle stage of an apicomplexan parasite.
An electron dense ring at the most posterior position of the apical complex, from which the subpellicular microtubules originate; formed during an invasive life cycle stage of an apicomplexan parasite.
An electron dense ring at the most posterior position of the apical complex, from which the subpellicular microtubules originate; formed during an invasive life cycle stage of an apicomplexan parasite.
Any process involved in the biological strategy of changing antigenic determinants on the surface that are exposed to another organism's immune system.
Any process involved in the biological strategy of changing antigenic determinants on the surface that are exposed to another organism's immune system.
The adherence of symbiont-infected erythrocytes to microvascular endothelium via symbiont proteins embedded in the membrane of the erythrocyte.
The adherence of symbiont-infected erythrocytes to microvascular endothelium via symbiont proteins embedded in the membrane of the erythrocyte.
The adherence of symbiont-infected erythrocytes to microvascular endothelium via symbiont proteins embedded in the membrane of the erythrocyte.
The adherence of symbiont-infected erythrocytes to microvascular endothelium via symbiont proteins embedded in the membrane of the erythrocyte.
A disk-like structure that appears at the periphery of a red blood cell infected by an apicomplexan parasite, characterized by a translucent lumen and an electron-dense coat of variable thickness; often appears to be tethered to the host cell membrane by fibrous connections with the erythrocyte cytoskeleton.
Interacting selectively and non-covalently with heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.
A mechanically stable cytoskeletal structure associated with the cytoplasmic face of the pellicle and surrounding the microtubule-based cytoskeleton.
The structure enclosing certain parasite cells such as certain apicomplexa and Euglenozoa; consists of the cell membrane with its associated infrastructure of microtubules, microfilaments and other organelles.
The formation of the prechordal plate. The prechordal plate is a thickening of the endoderm at the cranial end of the primitive streak formed by the involution of Spemann's organizer cells. The prechordal plate and the notochord induce the formation of the neural plate from the overlying ectodermal cells.
The process in which the lateral borders of the neural plate begin to migrate upwards to form the neural folds, caused by the proliferation of the underlying mesoderm.
The morphogenesis of the neural fold elevations that results in the movement of the tips of the elevations towards each other in order to fuse.
The formation of the median and lateral hinge points in the neural folds. These are created by apical constriction and basal expansion of the underlying neural cells. The median hinge point extends for the entire length of the neural tube, and the lateral hinge points do not form in the spinal cord region of the neural tube.
The process of folding the neuroepithelium around the medial hinge point to create the neural elevations, and around the lateral hinge points to produce convergence of the folds.
The joining together of the neural folds of the rostral opening of the neural tube. The anterior neuropore appears before the process of neural tube closure is complete.
The joining together of the neural folds of the caudal opening of the neural tube. The posterior neuropore appears before the process of neural tube closure is complete.
The formation of a ventral region of glial cells in the neural tube that provides inductive signals for the specification of neuronal cell types. The floor plate is evident at the ventral midline by the neural fold stage.
The formation of a single row of glia at the dorsal midline of the developing neural tube. This region provides inductive signals for the specification of neuronal cell types and of the specification of neural crest cells. The cells comprising the roof plate are the precursors to radial glial cells.
The process whose specific outcome is the progression of the spinal cord over time, from its formation to the mature structure. The spinal cord primarily conducts sensory and motor nerve impulses between the brain and the peripheral nervous tissues.
The regionalization process that regulates the coordinated growth and establishes the non-random spatial arrangement of the spinal cord.
The process that regulates the coordinated growth and differentiation that establishes the non-random anterior-posterior spatial arrangement of the spinal cord.
The process that regulates the coordinated growth and differentiation that establishes the non-random anterior-posterior spatial arrangement of the spinal cord.
The process that regulates the coordinated growth and differentiation that establishes the non-random dorsal-ventral spatial arrangement of the spinal cord.
The process that regulates the coordinated growth and differentiation that establishes the non-random dorsal-ventral spatial arrangement of the spinal cord.
The process in which neuroepithelial cells in the neural tube acquire specialized structural and/or functional features of ventral spinal cord interneurons. Ventral spinal cord interneurons are cells located in the ventral portion of the spinal cord that transmit signals between sensory and motor neurons and are required for reflexive responses. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which relatively unspecialized cells acquire specialized structural and/or functional features that characterize the cells of the spinal cord. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process whose specific outcome is the progression of the dorsal region of the spinal cord over time, from its formation to the mature structure. The dorsal region of the mature spinal cord contains neurons that process and relay sensory input.
The process whose specific outcome is the progression of the ventral region of the spinal cord over time, from its formation to the mature structure. The neurons of the ventral region of the mature spinal cord participate in motor output.
The process in which a cell becomes capable of differentiating autonomously into a commissural neuron in an environment that is neutral with respect to the developmental pathway.
The process in which a cell becomes capable of differentiating autonomously into an association neuron in an environment that is neutral with respect to the developmental pathway.
The process in which a cell becomes capable of differentiating autonomously into a motor neuron in an environment that is neutral with respect to the developmental pathway.
The process in which a cell becomes capable of differentiating autonomously into a ventral spinal cord interneuron in an environment that is neutral with respect to the developmental pathway.
The process in which neuroepithelial cells in the ventral neural tube acquire specialized structural and/or functional features of motor neurons. Motor neurons innervate an effector (muscle or glandular) tissue and are responsible for transmission of motor impulses from the brain to the periphery. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which neuroepithelial cells in the neural tube acquire specialized structural and/or functional features of somatic motor neurons. Somatic motor neurons innervate skeletal muscle targets and are responsible for transmission of motor impulses from the brain to the periphery. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which neuroepithelial cells in the neural tube acquire specialized structural and/or functional features of visceral motor neurons. Visceral motor neurons innervate glandular targets and are responsible for transmission of motor impulses from the brain to the periphery. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which differentiating motor neurons in the neural tube acquire the specialized structural and/or functional features of lateral motor column neurons. Lateral motor column neurons are generated only on limb levels and send axons into the limb mesenchyme. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which differentiating motor neurons in the neural tube acquire the specialized structural and/or functional features of medial motor column neurons. Medial motor column neurons are generated at all rostrocaudal levels and send axons to the axial muscles (medial group) and to the body wall muscles (lateral group). Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which neuroepithelial cells in the neural tube acquire specialized structural and/or functional features of association neurons. Association neurons are cells located in the dorsal portion of the spinal cord that integrate sensory input. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which neuroepithelial cells in the ventral neural tube acquire specialized structural and/or functional features of commissural neurons. Commissural neurons in both vertebrates and invertebrates transfer information from one side of their bodies to the other through the midline. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which neuroepithelial cells in the neural tube acquire specialized structural and/or functional features of oligodendrocytes. Oligodendrocytes are non-neuronal cells. The primary function of oligodendrocytes is the myelination of nerve axons in the central nervous system. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which a cell becomes capable of differentiating autonomously into an oligodendrocyte in an environment that is neutral with respect to the developmental pathway.
The process in which neuroepithelial cells in the ventral neural tube acquire specialized structural and/or functional features of radial glial cells. Radial cell precursors differentiate into both neuronal cell types and mature radial glial cells. Mature radial glial cells regulate the axon growth and pathfinding processes that occur during white matter patterning of the developing spinal cord. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The regionalization process that regulates the coordinated growth that establishes the non-random spatial arrangement of the neural tube.
The process in which relatively unspecialized cells acquire specialized structural and/or functional features that characterize the mature cells of the hindbrain. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The multiplication or reproduction of cells, resulting in the expansion of a cell population in the hindbrain.
The orderly movement of a cell that will reside in the hindbrain.
The process whose specific outcome is the progression of the diencephalon over time, from its formation to the mature structure. The diencephalon is the paired caudal parts of the prosencephalon from which the thalamus, hypothalamus, epithalamus and subthalamus are derived; these regions regulate autonomic, visceral and endocrine function, and process information directed to the cerebral cortex.
The process whose specific outcome is the progression of the telencephalon over time, from its formation to the mature structure. The telencephalon is the paired anteriolateral division of the prosencephalon plus the lamina terminalis from which the olfactory lobes, cerebral cortex, and subcortical nuclei are derived.
The progression of the epithalamus over time from its initial formation until its mature state. The epithalamus is the small dorsomedial area of the thalamus including the habenular nuclei and associated fiber bundles, the pineal body, and the epithelial roof of the third ventricle.
The process whose specific outcome is the progression of the subthalamus over time, from its formation to the mature structure. The subthalamus is the anterior part of the diencephalon that lies between the thalamus, hypothalamus, and tegmentum of the mesencephalon, including subthalamic nucleus, zona incerta, the fields of Forel, and the nucleus of ansa lenticularis.
The process in which the anatomical structures of the corpus callosum are generated and organized. The corpus callosum is a thick bundle of nerve fibers comprising a commissural plate connecting the two cerebral hemispheres. It consists of contralateral axon projections that provides communications between the right and left cerebral hemispheres.
The process whose specific outcome is the progression of the ammon gyrus over time, from its formation to the mature structure. The ammon gyrus, often subdivided into the CA1 and CA3 regions, is one of the two interlocking gyri of the hippocampus that is rich in large pyramidal neurons.
The process whose specific outcome is the progression of the ammon gyrus over time, from its formation to the mature structure. The ammon gyrus, often subdivided into the CA1 and CA3 regions, is one of the two interlocking gyri of the hippocampus that is rich in large pyramidal neurons.
The process whose specific outcome is the progression of the dentate gyrus over time, from its formation to the mature structure. The dentate gyrus is one of two interlocking gyri of the hippocampus. It contains granule cells, which project to the pyramidal cells and interneurons of the CA3 region of the ammon gyrus.
The process whose specific outcome is the progression of the pallium over time, from its formation to the mature structure. The pallium is the roof region of the telencephalon.
The process whose specific outcome is the progression of the subpallium over time, from its formation to the mature structure. The subpallium is the base region of the telencephalon.
The process whose specific outcome is the progression of the cranial nerves over time, from its formation to the mature structure. The cranial nerves are composed of twelve pairs of nerves that emanate from the nervous tissue of the hindbrain. These nerves are sensory, motor, or mixed in nature, and provide the motor and general sensory innervation of the head, neck and viscera. They mediate vision, hearing, olfaction and taste and carry the parasympathetic innervation of the autonomic ganglia that control visceral functions.
The process whose specific outcome is the progression of the rhombomere over time, from its formation to the mature structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates.
The regionalization process that gives rise to the midbrain-hindbrain boundary. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The regionalization process that gives rise to the midbrain-hindbrain boundary. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The regionalization process that gives rise to the midbrain-hindbrain boundary. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The regionalization process that gives rise to the midbrain-hindbrain boundary. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The regionalization process that gives rise to the midbrain-hindbrain boundary. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The regionalization process that gives rise to the midbrain-hindbrain boundary. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The process whose specific outcome is the progression of the pons over time, from its formation to the mature structure. The pons lies above the medulla and next to the cerebellum. The pons conveys information about movement from the cerebral hemisphere to the cerebellum.
The process whose specific outcome is the progression of the cerebellum over time, from its formation to the mature structure. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. In mice, the cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.
The process whose specific outcome is the progression of the medulla oblongata over time, from its formation to the mature structure. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
The process whose specific outcome is the progression of the medulla oblongata over time, from its formation to the mature structure. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
The process in which the anatomical structure of the central nervous system is generated and organized. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain and spinal cord. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
The process that contributes to the act of creating the structural organization of the midbrain-hindbrain boundary structure. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The process that contributes to the act of creating the structural organization of the midbrain-hindbrain boundary structure. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The process that contributes to the act of creating the structural organization of the midbrain-hindbrain boundary structure. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The process whose specific outcome is the progression of the olfactory nerve over time, from its formation to the mature structure. The olfactory nerve is a collection of sensory nerve rootlets that extend down from the olfactory bulb to the olfactory mucosa of the upper parts of the nasal cavity. This nerve conducts odor information to the brainstem.
The process whose specific outcome is the progression of the olfactory nerve over time, from its formation to the mature structure. The olfactory nerve is a collection of sensory nerve rootlets that extend down from the olfactory bulb to the olfactory mucosa of the upper parts of the nasal cavity. This nerve conducts odor information to the brainstem.
The process whose specific outcome is the progression of the olfactory nerve over time, from its formation to the mature structure. The olfactory nerve is a collection of sensory nerve rootlets that extend down from the olfactory bulb to the olfactory mucosa of the upper parts of the nasal cavity. This nerve conducts odor information to the brainstem.
The process whose specific outcome is the progression of the optic nerve over time, from its formation to the mature structure. The sensory optic nerve originates from the bipolar cells of the retina and conducts visual information to the brainstem. The optic nerve exits the back of the eye in the orbit, enters the optic canal, and enters the central nervous system at the optic chiasm (crossing) where the nerve fibers become the optic tract just prior to entering the hindbrain.
The process whose specific outcome is the progression of the optic nerve over time, from its formation to the mature structure. The sensory optic nerve originates from the bipolar cells of the retina and conducts visual information to the brainstem. The optic nerve exits the back of the eye in the orbit, enters the optic canal, and enters the central nervous system at the optic chiasm (crossing) where the nerve fibers become the optic tract just prior to entering the hindbrain.
The process whose specific outcome is the progression of the optic nerve over time, from its formation to the mature structure. The sensory optic nerve originates from the bipolar cells of the retina and conducts visual information to the brainstem. The optic nerve exits the back of the eye in the orbit, enters the optic canal, and enters the central nervous system at the optic chiasm (crossing) where the nerve fibers become the optic tract just prior to entering the hindbrain.
The process in which the anatomical structure of the midbrain-hindbrain boundary is generated and organized. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The process in which the anatomical structure of the midbrain-hindbrain boundary is generated and organized. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The process that gives rise to the central nervous system. This process pertains to the initial formation of a structure from unspecified parts. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain, spinal cord and spinal nerves. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
The process whose specific outcome is the progression of the oculomotor nerve over time, from its formation to the mature structure. This motor nerve innervates all extraocular muscles except the superior oblique and the lateral rectus muscles. The superior division supplies the levator palpebrae superioris and superior rectus muscles. The inferior division supplies the medial rectus, inferior rectus and inferior oblique muscles. This nerve also innervates the striated muscles of the eyelid. Pupillary constriction and lens movement are mediated by this nerve for near vision. In the orbit the inferior division sends branches that enter the ciliary ganglion where they form functional contacts (synapses) with the ganglion cells. The ganglion cells send nerve fibers into the back of the eye where they travel to ultimately innervate the ciliary muscle and the constrictor pupillae muscle.
The process whose specific outcome is the progression of the oculomotor nerve over time, from its formation to the mature structure. This motor nerve innervates all extraocular muscles except the superior oblique and the lateral rectus muscles. The superior division supplies the levator palpebrae superioris and superior rectus muscles. The inferior division supplies the medial rectus, inferior rectus and inferior oblique muscles. This nerve also innervates the striated muscles of the eyelid. Pupillary constriction and lens movement are mediated by this nerve for near vision. In the orbit the inferior division sends branches that enter the ciliary ganglion where they form functional contacts (synapses) with the ganglion cells. The ganglion cells send nerve fibers into the back of the eye where they travel to ultimately innervate the ciliary muscle and the constrictor pupillae muscle.
The process whose specific outcome is the progression of the oculomotor nerve over time, from its formation to the mature structure. This motor nerve innervates all extraocular muscles except the superior oblique and the lateral rectus muscles. The superior division supplies the levator palpebrae superioris and superior rectus muscles. The inferior division supplies the medial rectus, inferior rectus and inferior oblique muscles. This nerve also innervates the striated muscles of the eyelid. Pupillary constriction and lens movement are mediated by this nerve for near vision. In the orbit the inferior division sends branches that enter the ciliary ganglion where they form functional contacts (synapses) with the ganglion cells. The ganglion cells send nerve fibers into the back of the eye where they travel to ultimately innervate the ciliary muscle and the constrictor pupillae muscle.
The process whose specific outcome is the progression of the trochlear nerve over time, from its formation to the mature structure. The trochlear nerve is a motor nerve and is the only cranial nerve to exit the brain dorsally. The trochlear nerve innervates the superior oblique muscle.
The process whose specific outcome is the progression of the trochlear nerve over time, from its formation to the mature structure. The trochlear nerve is a motor nerve and is the only cranial nerve to exit the brain dorsally. The trochlear nerve innervates the superior oblique muscle.
The process whose specific outcome is the progression of the trochlear nerve over time, from its formation to the mature structure. The trochlear nerve is a motor nerve and is the only cranial nerve to exit the brain dorsally. The trochlear nerve innervates the superior oblique muscle.
The process whose specific outcome is the progression of the trigeminal nerve over time, from its formation to the mature structure. The trigeminal nerve is composed of three large branches. They are the ophthalmic (V1, sensory), maxillary (V2, sensory) and mandibular (V3, motor and sensory) branches. The sensory ophthalmic branch travels through the superior orbital fissure and passes through the orbit to reach the skin of the forehead and top of the head. The maxillary nerve contains sensory branches that reach the pterygopalatine fossa via the inferior orbital fissure (face, cheek and upper teeth) and pterygopalatine canal (soft and hard palate, nasal cavity and pharynx). The motor part of the mandibular branch is distributed to the muscles of mastication, the mylohyoid muscle and the anterior belly of the digastric. The mandibular nerve also innervates the tensor veli palatini and tensor tympani muscles. The sensory part of the mandibular nerve is composed of branches that carry general sensory information from the mucous membranes of the mouth and cheek, anterior two-thirds of the tongue, lower teeth, skin of the lower jaw, side of the head and scalp and meninges of the anterior and middle cranial fossae.
The process whose specific outcome is the progression of the trigeminal nerve over time, from its formation to the mature structure. The trigeminal nerve is composed of three large branches. They are the ophthalmic (V1, sensory), maxillary (V2, sensory) and mandibular (V3, motor and sensory) branches. The sensory ophthalmic branch travels through the superior orbital fissure and passes through the orbit to reach the skin of the forehead and top of the head. The maxillary nerve contains sensory branches that reach the pterygopalatine fossa via the inferior orbital fissure (face, cheek and upper teeth) and pterygopalatine canal (soft and hard palate, nasal cavity and pharynx). The motor part of the mandibular branch is distributed to the muscles of mastication, the mylohyoid muscle and the anterior belly of the digastric. The mandibular nerve also innervates the tensor veli palatini and tensor tympani muscles. The sensory part of the mandibular nerve is composed of branches that carry general sensory information from the mucous membranes of the mouth and cheek, anterior two-thirds of the tongue, lower teeth, skin of the lower jaw, side of the head and scalp and meninges of the anterior and middle cranial fossae.
The process whose specific outcome is the progression of the trigeminal nerve over time, from its formation to the mature structure. The trigeminal nerve is composed of three large branches. They are the ophthalmic (V1, sensory), maxillary (V2, sensory) and mandibular (V3, motor and sensory) branches. The sensory ophthalmic branch travels through the superior orbital fissure and passes through the orbit to reach the skin of the forehead and top of the head. The maxillary nerve contains sensory branches that reach the pterygopalatine fossa via the inferior orbital fissure (face, cheek and upper teeth) and pterygopalatine canal (soft and hard palate, nasal cavity and pharynx). The motor part of the mandibular branch is distributed to the muscles of mastication, the mylohyoid muscle and the anterior belly of the digastric. The mandibular nerve also innervates the tensor veli palatini and tensor tympani muscles. The sensory part of the mandibular nerve is composed of branches that carry general sensory information from the mucous membranes of the mouth and cheek, anterior two-thirds of the tongue, lower teeth, skin of the lower jaw, side of the head and scalp and meninges of the anterior and middle cranial fossae.
The process whose specific outcome is the progression of the abducens nerve over time, from its formation to the mature structure. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
The process whose specific outcome is the progression of the abducens nerve over time, from its formation to the mature structure. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
The process whose specific outcome is the progression of the abducens nerve over time, from its formation to the mature structure. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
The process whose specific outcome is the progression of the facial nerve over time, from its formation to the mature structure. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial opthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives off nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
The process whose specific outcome is the progression of the facial nerve over time, from its formation to the mature structure. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial opthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives off nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
The process whose specific outcome is the progression of the facial nerve over time, from its formation to the mature structure. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial opthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives off nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
The process whose specific outcome is the progression of the vestibulocochlear nerve over time, from its formation to the mature structure. This sensory nerve innervates the membranous labyrinth of the inner ear. The vestibular branch innervates the vestibular apparatus that senses head position changes relative to gravity. The auditory branch innervates the cochlear duct, which is connected to the three bony ossicles which transduce sound waves into fluid movement in the cochlea.
The process whose specific outcome is the progression of the vestibulocochlear nerve over time, from its formation to the mature structure. This sensory nerve innervates the membranous labyrinth of the inner ear. The vestibular branch innervates the vestibular apparatus that senses head position changes relative to gravity. The auditory branch innervates the cochlear duct, which is connected to the three bony ossicles which transduce sound waves into fluid movement in the cochlea.
The process whose specific outcome is the progression of the vestibulocochlear nerve over time, from its formation to the mature structure. This sensory nerve innervates the membranous labyrinth of the inner ear. The vestibular branch innervates the vestibular apparatus that senses head position changes relative to gravity. The auditory branch innervates the cochlear duct, which is connected to the three bony ossicles which transduce sound waves into fluid movement in the cochlea.
The process whose specific outcome is the progression of the vestibulocochlear nerve over time, from its formation to the mature structure. This sensory nerve innervates the membranous labyrinth of the inner ear. The vestibular branch innervates the vestibular apparatus that senses head position changes relative to gravity. The auditory branch innervates the cochlear duct, which is connected to the three bony ossicles which transduce sound waves into fluid movement in the cochlea.
Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
The process whose specific outcome is the progression of the vagus nerve over time, from its formation to the mature structure. This nerve is primarily sensory but also has visceromotor components. It originates in the brain stem and controls many autonomic functions of the heart, lungs, stomach, pharynx, larynx, trachea, esophagus and other gastrointestinal tract components. It controls some motor functions such as speech. The sensory branches mediate sensation from the pharynx, larynx, thorax and abdomen; it also innervates taste buds in the epiglottis.
The process whose specific outcome is the progression of the vagus nerve over time, from its formation to the mature structure. This nerve is primarily sensory but also has visceromotor components. It originates in the brain stem and controls many autonomic functions of the heart, lungs, stomach, pharynx, larynx, trachea, esophagus and other gastrointestinal tract components. It controls some motor functions such as speech. The sensory branches mediate sensation from the pharynx, larynx, thorax and abdomen; it also innervates taste buds in the epiglottis.
The process whose specific outcome is the progression of the vagus nerve over time, from its formation to the mature structure. This nerve is primarily sensory but also has visceromotor components. It originates in the brain stem and controls many autonomic functions of the heart, lungs, stomach, pharynx, larynx, trachea, esophagus and other gastrointestinal tract components. It controls some motor functions such as speech. The sensory branches mediate sensation from the pharynx, larynx, thorax and abdomen; it also innervates taste buds in the epiglottis.
The process whose specific outcome is the progression of the accessory nerve over time, from its formation to the mature structure. In mice, the spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
The process whose specific outcome is the progression of the accessory nerve over time, from its formation to the mature structure. In mice, the spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
The process whose specific outcome is the progression of the accessory nerve over time, from its formation to the mature structure. In mice, the spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
The process whose specific outcome is the progression of the accessory nerve over time, from its formation to the mature structure. In mice, the spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
The process whose specific outcome is the progression of the hypoglossal nerve over time, from its formation to the mature structure. This motor nerve innervates all the intrinsic and all but one of the extrinsic muscles of the tongue.
The process whose specific outcome is the progression of the hypoglossal nerve over time, from its formation to the mature structure. This motor nerve innervates all the intrinsic and all but one of the extrinsic muscles of the tongue.
The process whose specific outcome is the progression of the hypoglossal nerve over time, from its formation to the mature structure. This motor nerve innervates all the intrinsic and all but one of the extrinsic muscles of the tongue.
The process whose specific outcome is the progression of rhombomere 1 over time, from its formation to the mature structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process whose specific outcome is the progression of rhombomere 2 over time, from its formation to the mature structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process whose specific outcome is the progression of rhombomere 3 over time, from its formation to the mature structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process whose specific outcome is the progression of rhombomere 4 over time, from its formation to the mature structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process whose specific outcome is the progression of rhombomere 5 over time, from its formation to the mature structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process whose specific outcome is the progression of rhombomere 6 over time, from its formation to the mature structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process whose specific outcome is the progression of rhombomere 7 over time, from its formation to the mature structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process whose specific outcome is the progression of rhombomere 8 over time, from its formation to the mature structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process in which the anatomical structure of the hindbrain is generated and organized. The hindbrain is the region consisting of the medulla, pons and cerebellum. Areas of the hindbrain control motor and autonomic functions.
The process that gives rise to the hindbrain. This process pertains to the initial formation of a structure from unspecified parts. The hindbrain is the region consisting of the medulla, pons and cerebellum. Areas of the hindbrain control motor and autonomic functions.
The process that contributes to the act of creating the structural organization of the hindbrain. This process pertains to the physical shaping of a rudimentary structure. The hindbrain is the region consisting of the medulla, pons and cerebellum. Areas of the hindbrain control motor and autonomic functions.
A developmental process, independent of morphogenetic (shape) change, that is required for the hindbrain to attain its fully functional state. The hindbrain is the region consisting of the medulla, pons and cerebellum. Areas of the hindbrain control motor and autonomic functions.
The process in which the anatomical structure of the medulla oblongata is generated and organized. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
The process in which the anatomical structure of the medulla oblongata is generated and organized. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
The process that gives rise to the medulla oblongata. This process pertains to the initial formation of a structure from unspecified parts. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
The process that gives rise to the medulla oblongata. This process pertains to the initial formation of a structure from unspecified parts. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
The process that gives rise to the medulla oblongata. This process pertains to the initial formation of a structure from unspecified parts. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
The process that gives rise to the medulla oblongata. This process pertains to the initial formation of a structure from unspecified parts. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
The process that contributes to the act of creating the structural organization of the medulla oblongata. This process pertains to the physical shaping of a rudimentary structure. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
The process that contributes to the act of creating the structural organization of the medulla oblongata. This process pertains to the physical shaping of a rudimentary structure. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
The process that contributes to the act of creating the structural organization of the medulla oblongata. This process pertains to the physical shaping of a rudimentary structure. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
A developmental process, independent of morphogenetic (shape) change, that is required for the medulla oblongata to attain its fully functional state. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
A developmental process, independent of morphogenetic (shape) change, that is required for the medulla oblongata to attain its fully functional state. The medulla oblongata lies directly above the spinal cord and controls vital autonomic functions such as digestion, breathing and the control of heart rate.
The process in which the anatomical structure of the pons is generated and organized. The pons lies above the medulla and next to the cerebellum. The pons conveys information about movement from the cerebral hemisphere to the cerebellum.
The process that gives rise to the pons. This process pertains to the initial formation of a structure from unspecified parts. The pons lies above the medulla and next to the cerebellum. The pons conveys information about movement from the cerebral hemisphere to the cerebellum.
The process that contributes to the act of creating the structural organization of the pons. This process pertains to the physical shaping of a rudimentary structure. The pons lies above the medulla and next to the cerebellum. The pons conveys information about movement from the cerebral hemisphere to the cerebellum.
A developmental process, independent of morphogenetic (shape) change, that is required for the pons to attain its fully functional state. The pons lies above the medulla and next to the cerebellum. The pons conveys information about movement from the cerebral hemisphere to the cerebellum.
The process in which the anatomical structure of the cerebellum is generated and organized. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. The cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.
The process that gives rise to the cerebellum. This process pertains to the initial formation of a structure from unspecified parts. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. The cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.
The process that contributes to the act of creating the structural organization of the cerebellum. This process pertains to the physical shaping of a rudimentary structure. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. The cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.
A developmental process, independent of morphogenetic (shape) change, that is required for the cerebellum to attain its fully functional state. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. The cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.
The process whose specific outcome is the progression of the brain ventricular system over time, from its formation to the mature structure. The brain ventricular system consists of four communicating cavities within the brain that are continuous with the central canal of the spinal cord. These cavities include two lateral ventricles, the third ventricle and the fourth ventricle. Cerebrospinal fluid fills the ventricles and is produced by the choroid plexus.
The process whose specific outcome is the progression of the fourth ventricle over time, from its formation to the mature structure. The fourth ventricle is an irregularly shaped cavity in the rhombencephalon, between the medulla oblongata, the pons, and the isthmus in front, and the cerebellum behind. It is continuous with the central canal of the cord below and with the cerebral aqueduct above, and through its lateral and median apertures it communicates with the subarachnoid space.
The process in which the anatomical structure of the rhombomere is generated and organized. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates.
The process that gives rise to the rhombomere. This process pertains to the initial formation of a structure from unspecified parts. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates.
The process that contributes to the act of creating the structural organization of the rhombomere structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates.
The process that contributes to the act of creating the structural organization of the central nervous system structure. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain, spinal cord and spinal nerves. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
The process in which the anatomical structure of the abducens nerve is generated and organized. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
The process that gives rise to the abducens nerve. This process pertains to the initial formation of a structure from unspecified parts. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
The process that gives rise to the abducens nerve. This process pertains to the initial formation of a structure from unspecified parts. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
The process that contributes to the act of creating the structural organization of the abducens nerve. This process pertains to the physical shaping of a rudimentary structure. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
The process that contributes to the act of creating the structural organization of the abducens nerve. This process pertains to the physical shaping of a rudimentary structure. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
A developmental process, independent of morphogenetic (shape) change, that is required for the abducens nerve to attain its fully functional state. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
The process in which the anatomical structure of the cranial nerves are generated and organized. The cranial nerves are composed of twelve pairs of nerves that emanate from the nervous tissue of the hindbrain. These nerves are sensory, motor, or mixed in nature, and provide the motor and general sensory innervation of the head, neck and viscera. They mediate vision, hearing, olfaction and taste and carry the parasympathetic innervation of the autonomic ganglia that control visceral functions.
The process that gives rise to the cranial nerves. This process pertains to the initial formation of a structure from unspecified parts. The cranial nerves are composed of twelve pairs of nerves that emanate from the nervous tissue of the hindbrain. These nerves are sensory, motor, or mixed in nature, and provide the motor and general sensory innervation of the head, neck and viscera. They mediate vision, hearing, olfaction and taste and carry the parasympathetic innervation of the autonomic ganglia that control visceral functions.
The process that contributes to the act of creating the structural organization of the cranial nerves. This process pertains to the physical shaping of a rudimentary structure. The cranial nerves are composed of twelve pairs of nerves that emanate from the nervous tissue of the hindbrain. These nerves are sensory, motor, or mixed in nature, and provide the motor and general sensory innervation of the head, neck and viscera. They mediate vision, hearing, olfaction and taste and carry the parasympathetic innervation of the autonomic ganglia that control visceral functions.
A developmental process, independent of morphogenetic (shape) change, that is required for a cranial nerve to attain its fully functional state. The cranial nerves are composed of twelve pairs of nerves that emanate from the nervous tissue of the hindbrain. These nerves are sensory, motor, or mixed in nature, and provide the motor and general sensory innervation of the head, neck and viscera. They mediate vision, hearing, olfaction and taste and carry the parasympathetic innervation of the autonomic ganglia that control visceral functions.
A developmental process, independent of morphogenetic (shape) change, that is required for the accessory nerve to attain its fully functional state. The spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
A developmental process, independent of morphogenetic (shape) change, that is required for the accessory nerve to attain its fully functional state. The spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
The process in which the anatomical structure of the accessory nerve is generated and organized. The spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
The process that gives rise to the accessory nerve. This process pertains to the initial formation of a structure from unspecified parts. The spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
The process that gives rise to the accessory nerve. This process pertains to the initial formation of a structure from unspecified parts. The spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
The process that contributes to the act of creating the structural organization of the accessory nerve This process pertains to the physical shaping of a rudimentary structure. The spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
The process that contributes to the act of creating the structural organization of the accessory nerve This process pertains to the physical shaping of a rudimentary structure. The spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
The process in which the anatomical structure of the facial nerve is generated and organized. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial opthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives of nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
The process that gives rise to the facial nerve. This process pertains to the initial formation of a structure from unspecified parts. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial opthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives of nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
The process that gives rise to the facial nerve. This process pertains to the initial formation of a structure from unspecified parts. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial opthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives of nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
The process that contributes to the act of creating the structural organization of the facial nerve. This process pertains to the physical shaping of a rudimentary structure. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial opthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives of nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
The process that contributes to the act of creating the structural organization of the facial nerve. This process pertains to the physical shaping of a rudimentary structure. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial opthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives of nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
A developmental process, independent of morphogenetic (shape) change, that is required for the facial nerve to attain its fully functional state. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial opthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives of nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
A developmental process, independent of morphogenetic (shape) change, that is required for the glossopharyngeal nerve to attain its fully functional state. Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
The process in which the anatomical structure of the glossopharyngeal nerve is generated and organized. Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
The process that gives rise to the glossopharyngeal nerve. This process pertains to the initial formation of a structure from unspecified parts. Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
The process that gives rise to the glossopharyngeal nerve. This process pertains to the initial formation of a structure from unspecified parts. Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
The process that contributes to the act of creating the structural organization of the glossopharyngeal nerve. This process pertains to the physical shaping of a rudimentary structure. Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
The process that contributes to the act of creating the structural organization of the glossopharyngeal nerve. This process pertains to the physical shaping of a rudimentary structure. Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
The process in which the anatomical structure of the hypoglossal nerve is generated and organized. This motor nerve innervates all the intrinsic and all but one of the extrinsic muscles of the tongue.
A developmental process, independent of morphogenetic (shape) change, that is required for the hypoglossal nerve to attain its fully functional state. This motor nerve innervates all the intrinsic and all but one of the extrinsic muscles of the tongue.
The process that gives rise to the hypoglossal nerve. This process pertains to the initial formation of a structure from unspecified parts. This motor nerve innervates all the intrinsic and all but one of the extrinsic muscles of the tongue.
The process that gives rise to the hypoglossal nerve. This process pertains to the initial formation of a structure from unspecified parts. This motor nerve innervates all the intrinsic and all but one of the extrinsic muscles of the tongue.
The process that contributes to the act of creating the structural organization of the hypoglossal nerve. This process pertains to the physical shaping of a rudimentary structure. This motor nerve innervates all the intrinsic and all but one of the extrinsic muscles of the tongue.
The process that contributes to the act of creating the structural organization of the hypoglossal nerve. This process pertains to the physical shaping of a rudimentary structure. This motor nerve innervates all the intrinsic and all but one of the extrinsic muscles of the tongue.
The process in which the anatomical structure of the oculomotor nerve is generated and organized. This motor nerve innervates all extraocular muscles except the superior oblique and the lateral rectus muscles. The superior division supplies the levator palpebrae superioris and superior rectus muscles. The inferior division supplies the medial rectus, inferior rectus and inferior oblique muscles. This nerve also innervates the striated muscles of the eyelid. Pupillary constriction and lens movement are mediated by this nerve for near vision. In the orbit the inferior division sends branches that enter the ciliary ganglion where they form functional contacts (synapses) with the ganglion cells. The ganglion cells send nerve fibers into the back of the eye where they travel to ultimately innervate the ciliary muscle and the constrictor pupillae muscle.
The process that gives rise to the oculomotor nerve. This process pertains to the initial formation of a structure from unspecified parts. This motor nerve innervates all extraocular muscles except the superior oblique and the lateral rectus muscles. The superior division supplies the levator palpebrae superioris and superior rectus muscles. The inferior division supplies the medial rectus, inferior rectus and inferior oblique muscles. This nerve also innervates the striated muscles of the eyelid. Pupillary constriction and lens movement are mediated by this nerve for near vision. In the orbit the inferior division sends branches that enter the ciliary ganglion where they form functional contacts (synapses) with the ganglion cells. The ganglion cells send nerve fibers into the back of the eye where they travel to ultimately innervate the ciliary muscle and the constrictor pupillae muscle.
The process that gives rise to the oculomotor nerve. This process pertains to the initial formation of a structure from unspecified parts. This motor nerve innervates all extraocular muscles except the superior oblique and the lateral rectus muscles. The superior division supplies the levator palpebrae superioris and superior rectus muscles. The inferior division supplies the medial rectus, inferior rectus and inferior oblique muscles. This nerve also innervates the striated muscles of the eyelid. Pupillary constriction and lens movement are mediated by this nerve for near vision. In the orbit the inferior division sends branches that enter the ciliary ganglion where they form functional contacts (synapses) with the ganglion cells. The ganglion cells send nerve fibers into the back of the eye where they travel to ultimately innervate the ciliary muscle and the constrictor pupillae muscle.
The process that contributes to the act of creating the structural organization of the oculomotor nerve. This process pertains to the physical shaping of a rudimentary structure. This motor nerve innervates all extraocular muscles except the superior oblique and the lateral rectus muscles. The superior division supplies the levator palpebrae superioris and superior rectus muscles. The inferior division supplies the medial rectus, inferior rectus and inferior oblique muscles. This nerve also innervates the striated muscles of the eyelid. Pupillary constriction and lens movement are mediated by this nerve for near vision. In the orbit the inferior division sends branches that enter the ciliary ganglion where they form functional contacts (synapses) with the ganglion cells. The ganglion cells send nerve fibers into the back of the eye where they travel to ultimately innervate the ciliary muscle and the constrictor pupillae muscle.
The process that contributes to the act of creating the structural organization of the oculomotor nerve. This process pertains to the physical shaping of a rudimentary structure. This motor nerve innervates all extraocular muscles except the superior oblique and the lateral rectus muscles. The superior division supplies the levator palpebrae superioris and superior rectus muscles. The inferior division supplies the medial rectus, inferior rectus and inferior oblique muscles. This nerve also innervates the striated muscles of the eyelid. Pupillary constriction and lens movement are mediated by this nerve for near vision. In the orbit the inferior division sends branches that enter the ciliary ganglion where they form functional contacts (synapses) with the ganglion cells. The ganglion cells send nerve fibers into the back of the eye where they travel to ultimately innervate the ciliary muscle and the constrictor pupillae muscle.
A developmental process, independent of morphogenetic (shape) change, that is required for the oculomotor nerve to attain its fully functional state. This motor nerve innervates all extraocular muscles except the superior oblique and the lateral rectus muscles. The superior division supplies the levator palpebrae superioris and superior rectus muscles. The inferior division supplies the medial rectus, inferior rectus and inferior oblique muscles. This nerve also innervates the striated muscles of the eyelid. Pupillary constriction and lens movement are mediated by this nerve for near vision. In the orbit the inferior division sends branches that enter the ciliary ganglion where they form functional contacts (synapses) with the ganglion cells. The ganglion cells send nerve fibers into the back of the eye where they travel to ultimately innervate the ciliary muscle and the constrictor pupillae muscle.
A developmental process, independent of morphogenetic (shape) change, that is required for the central nervous system to attain its fully functional state. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain and spinal cord. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
The process in which the anatomical structure of the olfactory nerve is generated and organized. The olfactory nerve is a collection of sensory nerve rootlets that extend down from the olfactory bulb to the olfactory mucosa of the upper parts of the nasal cavity. This nerve conducts odor information to the brainstem.
The process that gives rise to the olfactory nerve. This process pertains to the initial formation of a structure from unspecified parts. The olfactory nerve is a collection of sensory nerve rootlets that extend down from the olfactory bulb to the olfactory mucosa of the upper parts of the nasal cavity. This nerve conducts odor information to the brainstem.
The process that gives rise to the olfactory nerve. This process pertains to the initial formation of a structure from unspecified parts. The olfactory nerve is a collection of sensory nerve rootlets that extend down from the olfactory bulb to the olfactory mucosa of the upper parts of the nasal cavity. This nerve conducts odor information to the brainstem.
The process that contributes to the act of creating the structural organization of the oculomotor nerve. This process pertains to the physical shaping of a rudimentary structure. The olfactory nerve is a collection of sensory nerve rootlets that extend down from the olfactory bulb to the olfactory mucosa of the upper parts of the nasal cavity. This nerve conducts odor information to the brainstem.
The process that contributes to the act of creating the structural organization of the oculomotor nerve. This process pertains to the physical shaping of a rudimentary structure. The olfactory nerve is a collection of sensory nerve rootlets that extend down from the olfactory bulb to the olfactory mucosa of the upper parts of the nasal cavity. This nerve conducts odor information to the brainstem.
A developmental process, independent of morphogenetic (shape) change, that is required for the olfactory nerve to attain its fully functional state. The olfactory nerve is a collection of sensory nerve rootlets that extend down from the olfactory bulb to the olfactory mucosa of the upper parts of the nasal cavity. This nerve conducts odor information to the brainstem.
The process in which the anatomical structure of the optic nerve is generated and organized. The sensory optic nerve originates from the bipolar cells of the retina and conducts visual information to the brainstem. The optic nerve exits the back of the eye in the orbit, enters the optic canal, and enters the central nervous system at the optic chiasm (crossing) where the nerve fibers become the optic tract just prior to entering the hindbrain.
A developmental process, independent of morphogenetic (shape) change, that is required for the optic nerve to attain its fully functional state. The sensory optic nerve originates from the bipolar cells of the retina and conducts visual information to the brainstem. The optic nerve exits the back of the eye in the orbit, enters the optic canal, and enters the central nervous system at the optic chiasm (crossing) where the nerve fibers become the optic tract just prior to entering the hindbrain.
The process that contributes to the act of creating the structural organization of the optic nerve. This process pertains to the physical shaping of a rudimentary structure. The sensory optic nerve originates from the bipolar cells of the retina and conducts visual information to the brainstem. The optic nerve exits the back of the eye in the orbit, enters the optic canal, and enters the central nervous system at the optic chiasm (crossing) where the nerve fibers become the optic tract just prior to entering the hindbrain.
The process that contributes to the act of creating the structural organization of the optic nerve. This process pertains to the physical shaping of a rudimentary structure. The sensory optic nerve originates from the bipolar cells of the retina and conducts visual information to the brainstem. The optic nerve exits the back of the eye in the orbit, enters the optic canal, and enters the central nervous system at the optic chiasm (crossing) where the nerve fibers become the optic tract just prior to entering the hindbrain.
The process that gives rise to the optic nerve. This process pertains to the initial formation of a structure from unspecified parts. The sensory optic nerve originates from the bipolar cells of the retina and conducts visual information to the brainstem. The optic nerve exits the back of the eye in the orbit, enters the optic canal, and enters the central nervous system at the optic chiasm (crossing) where the nerve fibers become the optic tract just prior to entering the hindbrain.
The process that gives rise to the optic nerve. This process pertains to the initial formation of a structure from unspecified parts. The sensory optic nerve originates from the bipolar cells of the retina and conducts visual information to the brainstem. The optic nerve exits the back of the eye in the orbit, enters the optic canal, and enters the central nervous system at the optic chiasm (crossing) where the nerve fibers become the optic tract just prior to entering the hindbrain.
A developmental process, independent of morphogenetic (shape) change, that is required for the trigeminal nerve to attain its fully functional state. The trigeminal nerve is composed of three large branches. They are the ophthalmic (V1, sensory), maxillary (V2, sensory) and mandibular (V3, motor and sensory) branches. The sensory ophthalmic branch travels through the superior orbital fissure and passes through the orbit to reach the skin of the forehead and top of the head. The maxillary nerve contains sensory branches that reach the pterygopalatine fossa via the inferior orbital fissure (face, cheek and upper teeth) and pterygopalatine canal (soft and hard palate, nasal cavity and pharynx). The motor part of the mandibular branch is distributed to the muscles of mastication, the mylohyoid muscle and the anterior belly of the digastric. The mandibular nerve also innervates the tensor veli palatini and tensor tympani muscles. The sensory part of the mandibular nerve is composed of branches that carry general sensory information from the mucous membranes of the mouth and cheek, anterior two-thirds of the tongue, lower teeth, skin of the lower jaw, side of the head and scalp and meninges of the anterior and middle cranial fossae.
The process in which the anatomical structure of the trigeminal nerve is generated and organized. The trigeminal nerve is composed of three large branches. They are the ophthalmic (V1, sensory), maxillary (V2, sensory) and mandibular (V3, motor and sensory) branches. The sensory ophthalmic branch travels through the superior orbital fissure and passes through the orbit to reach the skin of the forehead and top of the head. The maxillary nerve contains sensory branches that reach the pterygopalatine fossa via the inferior orbital fissure (face, cheek and upper teeth) and pterygopalatine canal (soft and hard palate, nasal cavity and pharynx). The motor part of the mandibular branch is distributed to the muscles of mastication, the mylohyoid muscle and the anterior belly of the digastric. The mandibular nerve also innervates the tensor veli palatini and tensor tympani muscles. The sensory part of the mandibular nerve is composed of branches that carry general sensory information from the mucous membranes of the mouth and cheek, anterior two-thirds of the tongue, lower teeth, skin of the lower jaw, side of the head and scalp and meninges of the anterior and middle cranial fossae.
The process that contributes to the act of creating the structural organization of the oculomotor nerve. This process pertains to the physical shaping of a rudimentary structure. The trigeminal nerve is composed of three large branches. They are the ophthalmic (V1, sensory), maxillary (V2, sensory) and mandibular (V3, motor and sensory) branches. The sensory ophthalmic branch travels through the superior orbital fissure and passes through the orbit to reach the skin of the forehead and top of the head. The maxillary nerve contains sensory branches that reach the pterygopalatine fossa via the inferior orbital fissure (face, cheek and upper teeth) and pterygopalatine canal (soft and hard palate, nasal cavity and pharynx). The motor part of the mandibular branch is distributed to the muscles of mastication, the mylohyoid muscle and the anterior belly of the digastric. The mandibular nerve also innervates the tensor veli palatini and tensor tympani muscles. The sensory part of the mandibular nerve is composed of branches that carry general sensory information from the mucous membranes of the mouth and cheek, anterior two-thirds of the tongue, lower teeth, skin of the lower jaw, side of the head and scalp and meninges of the anterior and middle cranial fossae.
The process that contributes to the act of creating the structural organization of the oculomotor nerve. This process pertains to the physical shaping of a rudimentary structure. The trigeminal nerve is composed of three large branches. They are the ophthalmic (V1, sensory), maxillary (V2, sensory) and mandibular (V3, motor and sensory) branches. The sensory ophthalmic branch travels through the superior orbital fissure and passes through the orbit to reach the skin of the forehead and top of the head. The maxillary nerve contains sensory branches that reach the pterygopalatine fossa via the inferior orbital fissure (face, cheek and upper teeth) and pterygopalatine canal (soft and hard palate, nasal cavity and pharynx). The motor part of the mandibular branch is distributed to the muscles of mastication, the mylohyoid muscle and the anterior belly of the digastric. The mandibular nerve also innervates the tensor veli palatini and tensor tympani muscles. The sensory part of the mandibular nerve is composed of branches that carry general sensory information from the mucous membranes of the mouth and cheek, anterior two-thirds of the tongue, lower teeth, skin of the lower jaw, side of the head and scalp and meninges of the anterior and middle cranial fossae.
The process that gives rise to the trigeminal nerve. This process pertains to the initial formation of a structure from unspecified parts. The trigeminal nerve is composed of three large branches. They are the ophthalmic (V1, sensory), maxillary (V2, sensory) and mandibular (V3, motor and sensory) branches. The sensory ophthalmic branch travels through the superior orbital fissure and passes through the orbit to reach the skin of the forehead and top of the head. The maxillary nerve contains sensory branches that reach the pterygopalatine fossa via the inferior orbital fissure (face, cheek and upper teeth) and pterygopalatine canal (soft and hard palate, nasal cavity and pharynx). The motor part of the mandibular branch is distributed to the muscles of mastication, the mylohyoid muscle and the anterior belly of the digastric. The mandibular nerve also innervates the tensor veli palatini and tensor tympani muscles. The sensory part of the mandibular nerve is composed of branches that carry general sensory information from the mucous membranes of the mouth and cheek, anterior two-thirds of the tongue, lower teeth, skin of the lower jaw, side of the head and scalp and meninges of the anterior and middle cranial fossae.
The process that gives rise to the trigeminal nerve. This process pertains to the initial formation of a structure from unspecified parts. The trigeminal nerve is composed of three large branches. They are the ophthalmic (V1, sensory), maxillary (V2, sensory) and mandibular (V3, motor and sensory) branches. The sensory ophthalmic branch travels through the superior orbital fissure and passes through the orbit to reach the skin of the forehead and top of the head. The maxillary nerve contains sensory branches that reach the pterygopalatine fossa via the inferior orbital fissure (face, cheek and upper teeth) and pterygopalatine canal (soft and hard palate, nasal cavity and pharynx). The motor part of the mandibular branch is distributed to the muscles of mastication, the mylohyoid muscle and the anterior belly of the digastric. The mandibular nerve also innervates the tensor veli palatini and tensor tympani muscles. The sensory part of the mandibular nerve is composed of branches that carry general sensory information from the mucous membranes of the mouth and cheek, anterior two-thirds of the tongue, lower teeth, skin of the lower jaw, side of the head and scalp and meninges of the anterior and middle cranial fossae.
The process in which the anatomical structure of the trochlear nerve is generated and organized. The trochlear nerve is a motor nerve and is the only cranial nerve to exit the brain dorsally. The trochlear nerve innervates the superior oblique muscle.
A developmental process, independent of morphogenetic (shape) change, that is required for the trochlear nerve to attain its fully functional state. The trochlear nerve is a motor nerve and is the only cranial nerve to exit the brain dorsally. The trochlear nerve innervates the superior oblique muscle.
The process that contributes to the act of creating the structural organization of the trochlear nerve. This process pertains to the physical shaping of a rudimentary structure. The trochlear nerve is a motor nerve and is the only cranial nerve to exit the brain dorsally. The trochlear nerve innervates the superior oblique muscle.
The process that contributes to the act of creating the structural organization of the trochlear nerve. This process pertains to the physical shaping of a rudimentary structure. The trochlear nerve is a motor nerve and is the only cranial nerve to exit the brain dorsally. The trochlear nerve innervates the superior oblique muscle.
The process that gives rise to the trochlear nerve. This process pertains to the initial formation of a structure from unspecified parts. The trochlear nerve is a motor nerve and is the only cranial nerve to exit the brain dorsally. The trochlear nerve innervates the superior oblique muscle.
The process that gives rise to the trochlear nerve. This process pertains to the initial formation of a structure from unspecified parts. The trochlear nerve is a motor nerve and is the only cranial nerve to exit the brain dorsally. The trochlear nerve innervates the superior oblique muscle.
A developmental process, independent of morphogenetic (shape) change, that is required for the vagus nerve to attain its fully functional state. This nerve is primarily sensory but also has visceromotor components. It originates in the brain stem and controls many autonomic functions of the heart, lungs, stomach, pharynx, larynx, trachea, esophagus and other gastrointestinal tract components. It controls some motor functions such as speech. The sensory branches mediate sensation from the pharynx, larynx, thorax and abdomen; it also innervates taste buds in the epiglottis.
The process in which the anatomical structure of the vagus nerve is generated and organized. This nerve is primarily sensory but also has visceromotor components. It originates in the brain stem and controls many autonomic functions of the heart, lungs, stomach, pharynx, larynx, trachea, esophagus and other gastrointestinal tract components. It controls some motor functions such as speech. The sensory branches mediate sensation from the pharynx, larynx, thorax and abdomen; it also innervates taste buds in the epiglottis.
The process that contributes to the act of creating the structural organization of the vagus nerve. This process pertains to the physical shaping of a rudimentary structure. This nerve is primarily sensory but also has visceromotor components. It originates in the brain stem and controls many autonomic functions of the heart, lungs, stomach, pharynx, larynx, trachea, esophagus and other gastrointestinal tract components. It controls some motor functions such as speech. The sensory branches mediate sensation from the pharynx, larynx, thorax and abdomen; it also innervates taste buds in the epiglottis.
The process that contributes to the act of creating the structural organization of the vagus nerve. This process pertains to the physical shaping of a rudimentary structure. This nerve is primarily sensory but also has visceromotor components. It originates in the brain stem and controls many autonomic functions of the heart, lungs, stomach, pharynx, larynx, trachea, esophagus and other gastrointestinal tract components. It controls some motor functions such as speech. The sensory branches mediate sensation from the pharynx, larynx, thorax and abdomen; it also innervates taste buds in the epiglottis.
The process that gives rise to the vagus nerve. This process pertains to the initial formation of a structure from unspecified parts. This nerve is primarily sensory but also has visceromotor components. It originates in the brain stem and controls many autonomic functions of the heart, lungs, stomach, pharynx, larynx, trachea, esophagus and other gastrointestinal tract components. It controls some motor functions such as speech. The sensory branches mediate sensation from the pharynx, larynx, thorax and abdomen; it also innervates taste buds in the epiglottis.
The process that gives rise to the vagus nerve. This process pertains to the initial formation of a structure from unspecified parts. This nerve is primarily sensory but also has visceromotor components. It originates in the brain stem and controls many autonomic functions of the heart, lungs, stomach, pharynx, larynx, trachea, esophagus and other gastrointestinal tract components. It controls some motor functions such as speech. The sensory branches mediate sensation from the pharynx, larynx, thorax and abdomen; it also innervates taste buds in the epiglottis.
A developmental process, independent of morphogenetic (shape) change, that is required for the vestibulocochlear nerve to attain its fully functional state. This sensory nerve innervates the membranous labyrinth of the inner ear. The vestibular branch innervates the vestibular apparatus that senses head position changes relative to gravity. The auditory branch innervates the cochlear duct, which is connected to the three bony ossicles which transduce sound waves into fluid movement in the cochlea.
A developmental process, independent of morphogenetic (shape) change, that is required for the vestibulocochlear nerve to attain its fully functional state. This sensory nerve innervates the membranous labyrinth of the inner ear. The vestibular branch innervates the vestibular apparatus that senses head position changes relative to gravity. The auditory branch innervates the cochlear duct, which is connected to the three bony ossicles which transduce sound waves into fluid movement in the cochlea.
The process in which the anatomical structure of the vestibulocochlear nerve is generated and organized. This sensory nerve innervates the membranous labyrinth of the inner ear. The vestibular branch innervates the vestibular apparatus that senses head position changes relative to gravity. The auditory branch innervates the cochlear duct, which is connected to the three bony ossicles which transduce sound waves into fluid movement in the cochlea.
The process that contributes to the act of creating the structural organization of the vestibulocochlear nerve. This process pertains to the physical shaping of a rudimentary structure. This sensory nerve innervates the membranous labyrinth of the inner ear. The vestibular branch innervates the vestibular apparatus that senses head position changes relative to gravity. The auditory branch innervates the cochlear duct, which is connected to the three bony ossicles which transduce sound waves into fluid movement in the cochlea.
The process that contributes to the act of creating the structural organization of the vestibulocochlear nerve. This process pertains to the physical shaping of a rudimentary structure. This sensory nerve innervates the membranous labyrinth of the inner ear. The vestibular branch innervates the vestibular apparatus that senses head position changes relative to gravity. The auditory branch innervates the cochlear duct, which is connected to the three bony ossicles which transduce sound waves into fluid movement in the cochlea.
The process that gives rise to the vestibulocochlear nerve. This process pertains to the initial formation of a structure from unspecified parts. This sensory nerve innervates the membranous labyrinth of the inner ear. The vestibular branch innervates the vestibular apparatus that senses head position changes relative to gravity. The auditory branch innervates the cochlear duct, which is connected to the three bony ossicles which transduce sound waves into fluid movement in the cochlea.
The process in which the anatomical structure of rhombomere 1 is generated and organized. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that gives rise to rhombomere 1. This process pertains to the initial formation of a structure from unspecified parts. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process that contributes to creating the structural organization of rhombomere 1. This process pertains to the physical shaping of a rudimentary structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that gives rise to a rhombomere boundary. This process pertains to the initial formation of a boundary delimiting a rhombomere. Rhombomeres are transverse segments of the developing rhombencephalon that are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process in which the anatomical structure of rhombomere 2 is generated and organized. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that contributes to creating the structural organization of rhombomere 2. This process pertains to the physical shaping of a rudimentary structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that gives rise to rhombomere 2. This process pertains to the initial formation of a structure from unspecified parts. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process in which the anatomical structure of rhombomere 3 is generated and organized. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that contributes to creating the structural organization of rhombomere 3. This process pertains to the physical shaping of a rudimentary structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that gives rise to rhombomere 3. This process pertains to the initial formation of a structure from unspecified parts. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process in which the anatomical structure of rhombomere 4 is generated and organized. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that contributes to creating the structural organization of rhombomere 4. This process pertains to the physical shaping of a rudimentary structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that gives rise to rhombomere 4. This process pertains to the initial formation of a structure from unspecified parts. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process in which the anatomical structures of rhombomere 5 are generated and organized. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that contributes to creating the structural organization of rhombomere 5. This process pertains to the physical shaping of a rudimentary structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that gives rise to rhombomere 5. This process pertains to the initial formation of a structure from unspecified parts. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process in which the anatomical structure of rhombomere 6 is generated and organized. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that contributes to creating the structural organization of rhombomere 6. This process pertains to the physical shaping of a rudimentary structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that gives rise to rhombomere 6. This process pertains to the initial formation of a structure from unspecified parts. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process whose specific outcome is the progression of the lateral ventricles over time, from the formation to the mature structure. The two lateral ventricles are a cavity in each of the cerebral hemispheres derived from the cavity of the embryonic neural tube. They are separated from each other by the septum pellucidum, and each communicates with the third ventricle by the foramen of Monro, through which also the choroid plexuses of the lateral ventricles become continuous with that of the third ventricle.
The process in which the anatomical structure of rhombomere 7 is generated and organized. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that contributes to creating the structural organization of rhombomere 7. This process pertains to the physical shaping of a rudimentary structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that gives rise to rhombomere 7. This process pertains to the initial formation of a structure from unspecified parts. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process in which the anatomical structure of rhombomere 8 is generated and organized. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process whose specific outcome is the progression of a nerve over time, from its formation to the mature structure.
The process that contributes to creating the structural organization of rhombomere 8. This process pertains to the physical shaping of a rudimentary structure. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in an anterior to posterior order.
The process that gives rise to rhombomere 8. This process pertains to the initial formation of a structure from unspecified parts. Rhombomeres are transverse segments of the developing rhombencephalon. Rhombomeres are lineage restricted, express different genes from one another, and adopt different developmental fates. Rhombomeres are numbered in anterior to posterior order.
The process whose specific outcome is the progression of the third ventricle over time, from its formation to the mature structure. The third ventricle is the narrow cleft inferior to the corpus callosum, within the diencephalon, between the paired thalami. Its floor is formed by the hypothalamus, its anterior wall by the lamina terminalis, and its roof by ependyma, and it communicates with the fourth ventricle by the cerebral aqueduct, and with the lateral ventricles by the interventricular foramina.
The process whose specific outcome is the progression of the cerebellar molecular layer nerve over time, from its formation to the mature structure. The molecular layer is the outermost layer of the cerebellar cortex. It contains the parallel fibers of the granule cells, interneurons such as stellate and basket cells, and the dendrites of the underlying Purkinje cells.
The process whose specific outcome is the progression of the cerebellar Purkinje cell layer over time, from its formation to the mature structure. The Purkinje cell layer lies just underneath the molecular layer of the cerebellar cortex. It contains the neuronal cell bodies of the Purkinje cells that are arranged side by side in a single layer. Candelabrum interneurons are vertically oriented between the Purkinje cells. Purkinje neurons are inhibitory and provide the output of the cerebellar cortex through axons that project into the white matter. Extensive dendritic trees from the Purkinje cells extend upward in a single plane into the molecular layer where they synapse with parallel fibers of granule cells.
The process whose specific outcome is the progression of the cerebellar granule layer over time, from its formation to the mature structure. The granular layer is the innermost layer of the cerebellar cortex. This layer contains densely packed small neurons, mostly granule cells. Some Golgi cells are found at the outer border. Granule neurons send parallel fibers to the upper molecular layer, where they synapse with Purkinje cell dendrites. Mossy fibers from the pontine nuclei in the white matter synapse with granule cell axons, Golgi cell axons and unipolar brush interneuron axons at cerebellar glomeruli in the granule cell layer.
A developmental process, independent of morphogenetic (shape) change, that is required for a nerve to attain its fully functional state.
The process in which the anatomical structure of the cerebellar granular layer is generated and organized. The granular layer is the innermost layer of the cerebellar cortex. This layer contains densely packed small neurons, mostly granule cells. Some Golgi cells are found at the outer border. Granule neurons send parallel fibers to the upper molecular layer, where they synapse with Purkinje cell dendrites. Mossy fibers from the pontine nuclei in the white matter synapse with granule cell axons, Golgi cell axons and unipolar brush interneuron axons at cerebellar glomeruli in the granule cell layer.
The process that gives rise to the cerebellar granule layer. This process pertains to the initial formation of a structure from unspecified parts. The granular layer is the innermost layer of the cerebellar cortex. This layer contains densely packed small neurons, mostly granule cells. Some Golgi cells are found at the outer border. Granule neurons send parallel fibers to the upper molecular layer, where they synapse with Purkinje cell dendrites. Mossy fibers from the pontine nuclei in the white matter synapse with granule cell axons, Golgi cell axons and unipolar brush interneuron axons at cerebellar glomeruli in the granule cell layer.
The process that contributes to the act of creating the structural organization of the cerebellar granule layer. This process pertains to the physical shaping of a rudimentary structure. The granular layer is the innermost layer of the cerebellar cortex. This layer contains densely packed small neurons, mostly granule cells. Some Golgi cells are found at the outer border. Granule neurons send parallel fibers to the upper molecular layer, where they synapse with Purkinje cell dendrites. Mossy fibers from the pontine nuclei in the white matter synapse with granule cell axons, Golgi cell axons and unipolar brush interneuron axons at cerebellar glomeruli in the granule cell layer.
A developmental process, independent of morphogenetic (shape) change, that is required for the cerebellar granular layer to attain its fully functional state. The granular layer is the innermost layer of the cerebellar cortex. This layer contains densely packed small neurons, mostly granule cells. Some Golgi cells are found at the outer border. Granule neurons send parallel fibers to the upper molecular layer, where they synapse with Purkinje cell dendrites. Mossy fibers from the pontine nuclei in the white matter synapse with granule cell axons, Golgi cell axons and unipolar brush interneuron axons at cerebellar glomeruli in the granule cell layer.
The process in which the anatomical structure of the cerebellar molecular layer is generated and organized. The molecular layer is the outermost layer of the cerebellar cortex. It contains the parallel fibers of the granule cells, interneurons such as stellate and basket cells, and the dendrites of the underlying Purkinje cells.
The process that gives rise to the cerebellar molecular layer. This process pertains to the initial formation of a structure from unspecified parts. The molecular layer is the outermost layer of the cerebellar cortex. It contains the parallel fibers of the granule cells, interneurons such as stellate and basket cells, and the dendrites of the underlying Purkinje cells.
The process that contributes to the act of creating the structural organization of the cerebellar molecular layer. This process pertains to the physical shaping of a rudimentary structure. The molecular layer is the outermost layer of the cerebellar cortex. It contains the parallel fibers of the granule cells, interneurons such as stellate and basket cells, and the dendrites of the underlying Purkinje cells.
A developmental process, independent of morphogenetic (shape) change, that is required for the cerebellar molecular layer to attain its fully functional state. The molecular layer is the outermost layer of the cerebellar cortex. It contains the parallel fibers of the granule cells, interneurons such as stellate and basket cells, and the dendrites of the underlying Purkinje cells.
A developmental process, independent of morphogenetic (shape) change, that is required for the cerebellar Purkinje cell layer to attain its fully functional state. The Purkinje cell layer lies just underneath the molecular layer of the cerebellar cortex. It contains the neuronal cell bodies of the Purkinje cells that are arranged side by side in a single layer. Candelabrum interneurons are vertically oriented between the Purkinje cells. Purkinje neurons are inhibitory and provide the output of the cerebellar cortex through axons that project into the white matter. Extensive dendritic trees from the Purkinje cells extend upward in a single plane into the molecular layer where they synapse with parallel fibers of granule cells.
The process in which the anatomical structure of the cerebellar Purkinje cell layer is generated and organized. The Purkinje cell layer lies just underneath the molecular layer of the cerebellar cortex. It contains the neuronal cell bodies of the Purkinje cells that are arranged side by side in a single layer. Candelabrum interneurons are vertically oriented between the Purkinje cells. Purkinje neurons are inhibitory and provide the output of the cerebellar cortex through axons that project into the white matter. Extensive dendritic trees from the Purkinje cells extend upward in a single plane into the molecular layer where they synapse with parallel fibers of granule cells.
The process that contributes to the act of creating the structural organization of the cerebellar Purkinje cell layer. This process pertains to the physical shaping of a rudimentary structure. The Purkinje cell layer lies just underneath the molecular layer of the cerebellar cortex. It contains the neuronal cell bodies of the Purkinje cells that are arranged side by side in a single layer. Candelabrum interneurons are vertically oriented between the Purkinje cells. Purkinje neurons are inhibitory and provide the output of the cerebellar cortex through axons that project into the white matter. Extensive dendritic trees from the Purkinje cells extend upward in a single plane into the molecular layer where they synapse with parallel fibers of granule cells.
The process that gives rise to the cerebellar Purkinje cell layer. This process pertains to the initial formation of a structure from unspecified parts. The Purkinje cell layer lies just underneath the molecular layer of the cerebellar cortex. It contains the neuronal cell bodies of the Purkinje cells that are arranged side by side in a single layer. Candelabrum interneurons are vertically oriented between the Purkinje cells. Purkinje neurons are inhibitory and provide the output of the cerebellar cortex through axons that project into the white matter. Extensive dendritic trees from the Purkinje cells extend upward in a single plane into the molecular layer where they synapse with parallel fibers of granule cells.
The process whose specific outcome is the progression of the cerebellar cortex over time, from its formation to the mature structure. The cerebellar cortex is a thin mantle of gray matter that covers the surface of each cerebral hemisphere. It has a characteristic morphology with convolutions (gyri) and crevices (sulci) that have specific functions. Six layers of nerve cells and the nerve pathways that connect them comprise the cerebellar cortex. Together, these regions are responsible for the processes of conscious thought, perception, emotion and memory as well as advanced motor function.
The process in which the anatomical structure of the cranial nerves are generated and organized. The cerebellar cortex is a thin mantle of gray matter that covers the surface of each cerebral hemisphere. It has a characteristic morphology with convolutions (gyri) and crevices (sulci) that have specific functions. Six layers of nerve cells and the nerve pathways that connect them comprise the cerebellar cortex. Together, these regions are responsible for the processes of conscious thought, perception, emotion and memory as well as advanced motor function.
The process that gives rise to the cerebellar cortex. This process pertains to the initial formation of a structure from unspecified parts. The cerebellar cortex is a thin mantle of gray matter that covers the surface of each cerebral hemisphere. It has a characteristic morphology with convolutions (gyri) and crevices (sulci) that have specific functions. Six layers of nerve cells and the nerve pathways that connect them comprise the cerebellar cortex. Together, these regions are responsible for the processes of conscious thought, perception, emotion and memory as well as advanced motor function.
The process that contributes to the act of creating the structural organization of the cerebellar cortex. This process pertains to the physical shaping of a rudimentary structure. The cerebellar cortex is a thin mantle of gray matter that covers the surface of each cerebral hemisphere. It has a characteristic morphology with convolutions (gyri) and crevices (sulci) that have specific functions. Six layers of nerve cells and the nerve pathways that connect them comprise the cerebellar cortex. Together, these regions are responsible for the processes of conscious thought, perception, emotion and memory as well as advanced motor function.
A developmental process, independent of morphogenetic (shape) change, that is required for the cerebellar cortex to attain its fully functional state. The cerebellar cortex is a thin mantle of gray matter that covers the surface of each cerebral hemisphere. It has a characteristic morphology with convolutions (gyri) and crevices (sulci) that have specific functions. Six layers of nerve cells and the nerve pathways that connect them comprise the cerebellar cortex. Together, these regions are responsible for the processes of conscious thought, perception, emotion and memory as well as advanced motor function.
A developmental process, independent of morphogenetic (shape) change, that is required for an anatomical structure, cell or cellular component to attain its fully functional state.
The process in which neuroblasts acquire specialized structural and/or functional features that characterize the mature cerebellar Golgi cell. Differentiation includes the processes involved in commitment of a neuroblast to a Golgi cell fate. A cerebellar Golgi cell is an inhibitory GABAergic interneuron found in the cerebellar cortex.
The process in which neuroblasts acquire specialized structural and/or functional features that characterize the mature cerebellar Purkinje cell. Differentiation includes the processes involved in commitment of a neuroblast to a Purkinje cell fate. A Purkinje cell is an inhibitory GABAergic neuron found in the cerebellar cortex that projects to the deep cerebellar nuclei and brain stem.
The process whose specific outcome is the progression of the locus ceruleus over time, from its formation to the mature structure. The locus ceruleus is a dense cluster of neurons within the dorsorostral pons. This nucleus is the major location of neurons that release norepinephrine throughout the brain, and is responsible for physiological responses to stress and panic.
The process whose specific outcome is the progression of the locus ceruleus over time, from its formation to the mature structure. The locus ceruleus is a dense cluster of neurons within the dorsorostral pons. This nucleus is the major location of neurons that release norepinephrine throughout the brain, and is responsible for physiological responses to stress and panic.
The process in which the anatomical structure of the locus ceruleus is generated and organized. In mice, the locus ceruleus is a dense cluster of neurons within the dorsorostral pons. This nucleus is the major location of neurons that release norepinephrine throughout the brain, and is responsible for physiological responses to stress and panic.
The process that gives rise to the locus ceruleus. This process pertains to the initial formation of a structure from unspecified parts. In mice, the locus ceruleus is a dense cluster of neurons within the dorsorostral pons. This nucleus is the major location of neurons that release norepinephrine throughout the brain, and is responsible for physiological responses to stress and panic.
A developmental process, independent of morphogenetic (shape) change, that is required for the locus ceruleus to attain its fully functional state. The locus ceruleus is a dense cluster of neurons within the dorsorostral pons. This nucleus is the major location of neurons that release norepinephrine throughout the brain, and is responsible for physiological responses to stress and panic.
The process in which neuroblasts acquire specialized structural and/or functional features that characterize the mature cerebellar granule cell. Differentiation includes the processes involved in commitment of a neuroblast to a granule cell fate. A granule cell is a glutamatergic interneuron found in the cerebellar cortex.
The process in which neuroblasts acquire specialized structural and/or functional features that characterize the mature Lugaro cell. Differentiation includes the processes involved in commitment of a neuroblast to a Lugaro cell fate. A Lugaro cell is an inhibitory GABAergic interneuron found in the cerebellar cortex.
The process in which neuroblasts acquire specialized structural and/or functional features that characterize the mature cerebellar basket cell. Differentiation includes the processes involved in commitment of a neuroblast to a cerebellar basket cell fate. A cerebellar basket cell is an inhibitory GABAergic interneuron found in the cerebellar cortex.
The process in which neuroblasts acquire specialized structural and/or functional features that characterize the mature cerebellar stellate cell. Differentiation includes the processes involved in commitment of a neuroblast to a cerebellar stellate cell fate. A cerebellar stellate cell is an inhibitory GABAergic interneuron found in the cerebellar cortex.
The process in which neuroblasts acquire specialized structural and/or functional features that characterize the mature unipolar brush cell in the cerebellum. Differentiation includes the processes involved in commitment of a neuroblast to a unipolar brush cell fate. A unipolar brush cell is a glutamatergic interneuron found in the cerebellar cortex.
The process in which neuroblasts acquire specialized structural and/or functional features that characterize the mature candelabrum cell. Differentiation includes the processes involved in commitment of a neuroblast to a candelabrum cell fate. A candelabrum cell is an inhibitory GABAergic interneuron found in the cerebellar cortex.
The process whose specific outcome is the progression of the inferior olivary nucleus over time, from its formation to the mature structure. The inferior olivary nucleus is a capsule-shaped structure in the ventral medulla located just lateral and dorsal to the medullary pyramids. Neurons in the inferior olivary nucleus are the source of climbing fiber input to the cerebellar cortex; these neurons have been implicated in various functions, such as learning and timing of movements.
The process in which the anatomical structure of the inferior olivary nucleus is generated and organized. The inferior olivary nucleus is a capsule-shaped structure in the ventral medulla located just lateral and dorsal to the medullary pyramids. Neurons in the inferior olivary nucleus are the source of climbing fiber input to the cerebellar cortex; these neurons have been implicated in various functions, such as learning and timing of movements.
The process that gives rise to the inferior olivary nucleus. This process pertains to the initial formation of a structure from unspecified parts. The inferior olivary nucleus is a capsule-shaped structure in the ventral medulla located just lateral and dorsal to the medullary pyramids. Neurons in the inferior olivary nucleus are the source of climbing fiber input to the cerebellar cortex; these neurons have been implicated in various functions, such as learning and timing of movements.
The process that gives rise to the inferior olivary nucleus. This process pertains to the initial formation of a structure from unspecified parts. The inferior olivary nucleus is a capsule-shaped structure in the ventral medulla located just lateral and dorsal to the medullary pyramids. Neurons in the inferior olivary nucleus are the source of climbing fiber input to the cerebellar cortex; these neurons have been implicated in various functions, such as learning and timing of movements.
The process that contributes to the act of creating the structural organization of the inferior olivary nucleus structure. The inferior olivary nucleus is a capsule-shaped structure in the ventral medulla located just lateral and dorsal to the medullary pyramids. Neurons in the inferior olivary nucleus are the source of climbing fiber input to the cerebellar cortex; these neurons have been implicated in various functions, such as learning and timing of movements.
The process that contributes to the act of creating the structural organization of the inferior olivary nucleus structure. The inferior olivary nucleus is a capsule-shaped structure in the ventral medulla located just lateral and dorsal to the medullary pyramids. Neurons in the inferior olivary nucleus are the source of climbing fiber input to the cerebellar cortex; these neurons have been implicated in various functions, such as learning and timing of movements.
A developmental process, independent of morphogenetic (shape) change, that is required for the inferior olivary nucleus to attain its fully functional state. The inferior olivary nucleus is a capsule-shaped structure in the ventral medulla located just lateral and dorsal to the medullary pyramids. Neurons in the inferior olivary nucleus are the source of climbing fiber input to the cerebellar cortex; these neurons have been implicated in various functions, such as learning and timing of movements.
The process whose specific outcome is the progression of the superior olivary nucleus over time, from its formation to the mature structure. In mice, the superior olivary nucleus is a small cylindrical mass on the dorsal surface of the lateral part of the trapezoid body of the pons, and it is situated immediately above the inferior olivary nucleus. It receives projections from the cochlear nucleus and thus is involved in the perception of sound.
The process in which the anatomical structure of the superior olivary nucleus is generated and organized. In mice, the superior olivary nucleus is a small cylindrical mass on the dorsal surface of the lateral part of the trapezoid body of the pons, and it is situated immediately above the inferior olivary nucleus. It receives projections from the cochlear nucleus and thus is involved in the perception of sound.
The process that gives rise to the superior olivary nucleus. This process pertains to the initial formation of a structure from unspecified parts. In mice, the superior olivary nucleus is a small cylindrical mass on the dorsal surface of the lateral part of the trapezoid body of the pons, and it is situated immediately above the inferior olivary nucleus. It receives projections from the cochlear nucleus and thus is involved in the perception of sound.
The process that contributes to the act of creating the structural organization of the superior olivary nucleus structure. In mice, the superior olivary nucleus is a small cylindrical mass on the dorsal surface of the lateral part of the trapezoid body of the pons, and it is situated immediately above the inferior olivary nucleus. It receives projections from the cochlear nucleus and thus is involved in the perception of sound.
A developmental process, independent of morphogenetic (shape) change, that is required for the superior olivary nucleus to attain its fully functional state. The superior olivary nucleus is a small cylindrical mass on the dorsal surface of the lateral part of the trapezoid body of the pons, and it is situated immediately above the inferior olivary nucleus. It receives projections from the cochlear nucleus and thus is involved in the perception of sound.
The process whose specific outcome is the progression of the medullary reticular formation over time, from its formation to the mature structure. The medullary reticular formation is a series of brain nuclei located in the medulla oblongata.
The process whose specific outcome is the progression of the inferior raphe nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the inferior raphe nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the superior raphe nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the superior raphe nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the lateral reticular nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the intermediate reticular formation over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the inferior reticular formation over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the superior reticular formation over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the trigeminal sensory nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the trigeminal motor nucleus over time, from its formation to the mature structure.
A developmental process, independent of morphogenetic (shape) change, that is required for the midbrain-hindbrain boundary to attain its fully functional state. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
A developmental process, independent of morphogenetic (shape) change, that is required for the midbrain-hindbrain boundary to attain its fully functional state. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The process whose specific outcome is the progression of the dentate nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the globose nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the emboliform nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the fastigial nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the mesencephalic trigeminal nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the pontine nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the spinal trigeminal nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the abducens nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the hypoglossal nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the dorsal motor nucleus of the vagus nerve over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the nucleus ambiguus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the solitary nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the cochlear nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the dorsal cochlear nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the ventral cochlear nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the vestibular nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of a salivary nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the inferior salivary nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the superior salivary nucleus over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the facial nucleus over time, from its formation to the mature structure.
The process in which neuroblasts acquire specialized structural and/or functional features that characterize the mature eurydendroid cell. Differentiation includes the processes involved in commitment of a neuroblast to a eurydendroid cell fate. A eurydendroid cell is an efferent neuron found in the cerebellar cortex of teleosts.
The progression of the striatum over time from its initial formation until its mature state. The striatum is a region of the forebrain consisting of the caudate nucleus, putamen and fundus striati.
The progression of the striatum over time from its initial formation until its mature state. The striatum is a region of the forebrain consisting of the caudate nucleus, putamen and fundus striati.
The progression of the caudate nucleus over time from its initial formation until its mature state. The caudate nucleus is the C-shaped structures of the striatum containing input neurons involved with control of voluntary movement in the brain.
The progression of the putamen over time from its initial formation until its mature state. The putamen is the lens-shaped basal ganglion involved with control of voluntary movement in the brain.
The progression of the globus pallidus over time from its initial formation until its mature state. The globus pallidus is one of the basal ganglia involved with control of voluntary movement in the brain.
The progression of the limbic system over time from its initial formation until its mature state. The limbic system is a collection of structures in the brain involved in emotion, motivation and emotional aspects of memory.
The progression of the substantia nigra over time from its initial formation until its mature state. The substantia nigra is the layer of gray substance that separates the posterior parts of the cerebral peduncles (tegmentum mesencephali) from the anterior parts; it normally includes a posterior compact part with many pigmented cells (pars compacta) and an anterior reticular part whose cells contain little pigment (pars reticularis).
The progression of the subthalamic nucleus over time from its initial formation until its mature state. The subthalamic nucleus is the lens-shaped nucleus located in the ventral part of the subthalamus on the inner aspect of the internal capsule that is concerned with the integration of somatic motor function.
The progression of the amygdala over time from its initial formation until its mature state. The amygdala is an almond-shaped set of neurons in the medial temporal lobe of the brain that play a key role in processing emotions such as fear and pleasure.
The progression of the cingulate gyrus over time from its initial formation until its mature state. The cingulate gyrus is a ridge in the cerebral cortex located dorsal to the corpus callosum.
The progression of the hippocampus over time from its initial formation until its mature state.
The progression of the mammillary body over time from its initial formation until its mature state. The mammillary body is a protrusion at the posterior end of the hypothalamus that contains hypothalamic nuclei.
The progression of the nucleus accumbens over time from its initial formation until its mature state. The nucleus accumbens is a collection of pleomorphic cells in the caudal part of the anterior horn of the lateral ventricle, in the region of the olfactory tubercle, lying between the head of the caudate nucleus and the anterior perforated substance. It is part of the ventral striatum, a composite structure considered part of the basal ganglia.
The progression of the nucleus accumbens over time from its initial formation until its mature state. The nucleus accumbens is a collection of pleomorphic cells in the caudal part of the anterior horn of the lateral ventricle, in the region of the olfactory tubercle, lying between the head of the caudate nucleus and the anterior perforated substance. It is part of the ventral striatum, a composite structure considered part of the basal ganglia.
The progression of the orbitofrontal cortex over time from its initial formation until its mature state. The orbitofrontal cortex is a cerebral cortex region located in the frontal lobe.
The progression of the parahippocampal gyrus over time from its initial formation until its mature state. The parahippocampal gyrus is a ridge in the cerebral cortex.
The progression of the lateral geniculate nucleus over time from its initial formation until its mature state. The lateral geniculate nucleus is the primary processor of visual information received from the retina.
The progression of the olfactory bulb over time from its initial formation until its mature state. The olfactory bulb coordinates neuronal signaling involved in the perception of smell. It receives input from the sensory neurons and outputs to the olfactory cortex.
The process in which a relatively unspecialized cell acquires specialized features of a medium spiny neuron residing in the striatum.
The process in which a relatively unspecialized cell acquires specialized features of a medium spiny neuron residing in the striatum.
The series of molecular signals initiated by binding of a ligand to a retinoic acid receptor in a precursor cell in the ventral spinal cord that contributes to the commitment of the precursor cell to an interneuron fate.
The series of molecular signals initiated by binding of a ligand to the transmembrane receptor smoothened in a precursor cell in the ventral spinal cord that contributes to the commitment of the precursor cell to an interneuron fate.
The series of molecular signals initiated by binding of a ligand to the transmembrane receptor smoothened in a precursor cell in the ventral spinal cord that contributes to the commitment of the precursor cell to an interneuron fate.
The series of molecular signals initiated by binding of a ligand to the transmembrane receptor smoothened in a precursor cell in the ventral spinal cord that contributes to the commitment of the precursor cell to an interneuron fate.
The series of molecular signals initiated by binding of a ligand to the transmembrane receptor smoothened in a precursor cell in the spinal cord that contributes to the process of a precursor cell becoming capable of differentiating autonomously into a motor neuron in an environment that is neutral with respect to the developmental pathway.
The series of molecular signals initiated by binding of a ligand to the transmembrane receptor smoothened in a precursor cell in the spinal cord that contributes to the process of a precursor cell becoming capable of differentiating autonomously into a motor neuron in an environment that is neutral with respect to the developmental pathway.
The series of molecular signals initiated by binding of a ligand to the transmembrane receptor smoothened in a precursor cell in the spinal cord that contributes to the process of a precursor cell becoming capable of differentiating autonomously into a motor neuron in an environment that is neutral with respect to the developmental pathway.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, which contributes to its commitment to an association neuron fate.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, which contributes to its commitment to an association neuron fate.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, which contributes to its commitment to an association neuron fate.
The process in which a cell becomes capable of differentiating autonomously into an oligodendrocyte in an environment that is neutral with respect to the developmental pathway. Upon specification, the cell fate can be reversed.
The process in which the developmental fate of a cell becomes restricted such that it will develop into an oligodendrocyte.
The process in which a cell becomes capable of differentiating autonomously into a glial 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 the developmental fate of a cell becomes restricted such that it will develop into a glial cell.
The process aimed at the progression of a glial cell over time, from initial commitment of the cell to a specific fate, to the fully functional differentiated cell.
The process whose specific outcome is the progression of a preganglionic parasympathetic fiber over time, from its formation to the mature structure. A preganglionic parasympathetic fiber is a cholinergic axonal fiber projecting from the CNS to a parasympathetic ganglion.
The process whose specific outcome is the progression of the postganglionic portion of the parasympathetic fiber over time, from its formation to the mature structure. The parasympathetic fiber is one of the two divisions of the vertebrate autonomic nervous system. Parasympathetic nerves emerge cranially as pre ganglionic fibers from oculomotor, facial, glossopharyngeal and vagus and from the sacral region of the spinal cord. Most neurons are cholinergic and responses are mediated by muscarinic receptors. The parasympathetic system innervates, for example: salivary glands, thoracic and abdominal viscera, bladder and genitalia.
The process in which a branchiomotor neuron growth cone is directed to a specific target site. Branchiomotor neurons are located in the hindbrain and innervate branchial arch-derived muscles that control jaw movements, facial expression, the larynx, and the pharynx.
The process in which a branchiomotor neuron growth cone is directed to a specific target site. Branchiomotor neurons are located in the hindbrain and innervate branchial arch-derived muscles that control jaw movements, facial expression, the larynx, and the pharynx.
The process in which a branchiomotor neuron growth cone is directed to a specific target site. Branchiomotor neurons are located in the hindbrain and innervate branchial arch-derived muscles that control jaw movements, facial expression, the larynx, and the pharynx.
The process in which a branchiomotor neuron growth cone in the neural tube is directed to a specific target site in the neural tube. Branchiomotor neurons are located in the hindbrain and innervate branchial arch-derived muscles that control jaw movements, facial expression, the larynx, and the pharynx.
The process in which a branchiomotor neuron growth cone in the neural tube is directed to a specific target site in the neural tube in response to a repulsive chemical cue. Branchiomotor neurons are located in the hindbrain and innervate branchial arch-derived muscles that control jaw movements, facial expression, the larynx, and the pharynx.
The process in which a branchiomotor neuron growth cone in the neural tube is directed to a specific target site in the neural tube in response to an attractive chemical cue. Branchiomotor neurons are located in the hindbrain and innervate branchial arch-derived muscles that control jaw movements, facial expression, the larynx, and the pharynx.
The process in which a branchiomotor neuron growth cone in the branchial arch mesenchyme is directed to a specific target site in the branchial arch mesenchyme. Branchiomotor neurons are located in the hindbrain and innervate branchial arch-derived muscles that control jaw movements, facial expression, the larynx, and the pharynx.
The process in which a branchiomotor neuron growth cone in the branchial arch mesenchyme is directed to a specific target site in the branchial arch mesenchyme in response to a repulsive chemical cue. Branchiomotor neurons are located in the hindbrain and innervate branchial arch-derived muscles that control jaw movements, facial expression, the larynx, and the pharynx.
The process in which a branchiomotor neuron growth cone in the branchial arch mesenchyme is directed to a specific target site in the branchial arch mesenchyme in response to an attractive chemical cue. Branchiomotor neurons are located in the hindbrain and innervate branchial arch-derived muscles that control jaw movements, facial expression, the larynx, and the pharynx.
The process in which a branchiomotor neuron growth cone is directed to a specific target site in response to an attractive chemical signal. Branchiomotor neurons are located in the hindbrain and innervate branchial arch-derived muscles that control jaw movements, facial expression, the larynx, and the pharynx.
The process in which a branchiomotor neuron growth cone is directed to a specific target site in response to a repulsive chemical cue. Branchiomotor neurons are located in the hindbrain and innervate branchial arch-derived muscles that control jaw movements, facial expression, the larynx, and the pharynx.
The process in which the thalamus changes over time, from its initial formation to its mature state.
The orderly movement of cells from one site to another in the cerebral cortex.
The regionalization process that results in the creation of areas within the cerebral cortex that will direct the behavior of cell migration and differentiation as the cortex develops.
The regionalization process that results in the creation of areas within the cerebral cortex that will direct the behavior of cell migration and differentiation as the cortex develops.
The regionalization process that results in the creation of areas within the cerebral cortex that will direct the behavior of cell migration and differentiation as the cortex develops.
The creation of specific areas of progenitor domains along the anterior-posterior axis of the developing forebrain.
The formation of specific regional progenitor domains along the dorsal-ventral axis in the developing forebrain.
The formation of specific regional progenitor domains along the dorsal-ventral axis in the developing forebrain.
The migration of cells in the developing cerebral cortex in which cells move from the ventricular and/or subventricular zone toward the surface of the brain.
The migration of cells in the cerebral cortex in which cells move orthogonally to the direction of radial migration and do not use radial glial cell processes as substrates for migration.
The radial migration of neuronal or glial precursor cells along radial glial cells during the development of the cerebral cortex.
The radial migration of cells from the ventricular zone that is independent of radial glial cells. Cells extend processes that terminate at the pial surface and follow the processes as they migrate.
The extension of a long process to the pial surface as a cell leaves the ventricular zone.
The process that results in the loss of attachments of a cell in the ventricular zone.
The process that results in the loss of attachments of a cell in the ventricular zone.
The process that results in the loss of attachments of a cell in the ventricular zone.
The process that results in the loss of attachments of a cell in the ventricular zone.
The movement of a cell body from the ventricular zone to the pial surface with a concomitant shortening of the process that extends to the pial surface.
The initial stages of cell motility involved in the glial-mediated movement of cells in the developing cerebral cortex.
The interaction of soluble factors and receptors that result in the movement of cells in the primitive cerebral cortex.
The process that results in the fluctuations in intracellular calcium that are responsible for the initiation of movement as a component of the process of cerebral cortex glial-mediated radial migration.
Signaling between members of the neurotrophin family and their receptors that result in the start of cell motility as a component of the process of cerebral cortex glial-mediated radial migration.
Signaling by neurotransmitters and their receptors that results in the initiation of movement of cells as a component of the process of glial-mediated radial migration.
Signaling between growth factors and their receptors that results in the start of cell movement, where this process is involved in glial-mediated radial migration in the cerebral cortex.
Signaling between growth factors and their receptors that results in the start of cell movement, where this process is involved in glial-mediated radial migration in the cerebral cortex.
The changes in adhesion between neuronal cells and glial cells as a component of the process of cerebral cortex glial-mediated radial cell migration.
The interaction between two cells that modulates the association of a neuronal cell and a glial cell involved in glial-mediated radial cell migration in the cerebral cortex.
The movement of a cell along the process of a radial glial cell involved in cerebral cortex glial-mediated radial migration.
The movement of a cell along the process of a radial glial cell involved in cerebral cortex glial-mediated radial migration.
Rearrangements of the microtubule cytoskeleton that contribute to the movement of cells along radial glial cells as a component of the process of cerebral cortex glial-mediated radial migration.
The rearrangements of the microtubule cytoskeleton that result in the extension of a leading process, where this process is involved in the movement of cells along radial glial cells.
The microtubule-mediated movement of the nucleus that is required for the movement of cells along radial glial fibers as a component of the process of cerebral cortex glial-mediated radial cell migration.
The microtubule-mediated movement of the nucleus that is required for the movement of cells along radial glial fibers as a component of the process of cerebral cortex glial-mediated radial cell migration.
The changes in the actin cytoskeleton that are necessary for the movement of cells along radial glial cells as a component of the process of cerebral cortex glial-mediated radial cell migration.
The detachment of cells from radial glial fibers at the appropriate time when they cease to migrate and form distinct layer in the cerebral cortex.
The process that leads to the deposition of extracellular matrix signals in the marginal zone of the developing cerebral cortex. This extracellular matrix controls the movement of migrating cells. In mammals, the matrix is modified by Cajal-Retzius cells.
The process that leads to the deposition of extracellular matrix signals in the marginal zone of the developing cerebral cortex. This extracellular matrix controls the movement of migrating cells. In mammals, the matrix is modified by Cajal-Retzius cells.
The process that results in the release of migrating cells from their interaction with radial glial cells as a component of the process of cerebral cortex glial-mediated radial cell migration.
The process that results in the release of migrating cells from their interaction with radial glial cells as a component of the process of cerebral cortex glial-mediated radial cell migration.
The process that results in the release of migrating cells from their interaction with radial glial cells as a component of the process of cerebral cortex glial-mediated radial cell migration.
The process that results in the release of migrating cells from their interaction with radial glial cells as a component of the process of cerebral cortex glial-mediated radial cell migration.
The intracellular signaling pathway that results in the cessation of cell movement involved in lamination of the cerebral cortex.
The intracellular signaling pathway that results in the cessation of cell movement involved in lamination of the cerebral cortex.
The intracellular signaling pathway that results in the cessation of cell movement involved in lamination of the cerebral cortex.
The intracellular signaling pathway that results in the cessation of cell movement involved in lamination of the cerebral cortex.
The intracellular signaling pathway that results in the cessation of cell movement involved in lamination of the cerebral cortex.
The intracellular signaling pathway that results in the cessation of cell movement involved in lamination of the cerebral cortex.
The process in which neurons interact with each other to promote migration along a tangential plane.
The movement of cerebral cortex neuronal precursors tangentially through the cortex using interaction of the migrating cells with axons of other neurons.
The process where neuronal precursors migrate tangentially in the cerebral cortex, primarily guided through physical cell-cell interactions.
The process where neuronal precursors migrate tangentially in the telencephalon, primarily guided by interactions that do not require cell-cell contact.
The migration of olfactory bulb interneuron precursors in the cerebral cortex that occurs after birth.
The directional movement of a gonadotrophin-releasing hormone producing neuron from the nasal placode to the hypothalamus.
The directional movement of a gonadotrophin-releasing hormone producing neuron from the nasal placode to the hypothalamus.
The directed movement of oligodendrocytes from the subpallium to the cerebral cortex during forebrain development.
The directed movement of interneurons from the subpallium to the cortex during forebrain development.
The directed movement of individual interneuron precursors during the embryonic development of the olfactory bulb.
The attachment of cells to one another to form groups of cells involved in cerebral cortex tangential migration.
The interaction of a cell and the extracellular matrix involved in the directed tangential movement of cells mediated by cell-cell interactions in the developing cerebral cortex.
The creation and reception of signals that guide olfactory bulb interneuron precursors down concentration gradients towards the olfactory bulb.
The creation and reception of signals that result in the migration of interneuron precursors up a concentration gradient towards the olfactory bulb.
The creation and reception of signals that repel olfactory bulb interneurons from the subventricular zone as a component process in tangential migration.
The signaling that results in the stimulation of cell movement in the rostral migratory stream.
The creation and reception of signals that result in the directional movement of interneuron precursors from the subpallium to the cortex.
The process in which migrating interneurons interact with an external substratum as a component of migration from the subpallium to the cortex.
The creation and reception of signals that control the direction of migration of interneurons as a component of the process of migration from the subpallium to the cortex.
The creation and reception of signals that result in the movement of interneurons toward the signal, where this process is involved in migration from the subpallium to the cortex.
The creation and reception of signals that result in the movement of interneurons away from the signal during migration from the subpallium to the cortex.
The directional movement of tangentially migrating interneurons that are not guided by attaching to extracellular substrates.
The establishment and response to guidance cues that distribute interneurons to different cerebral cortex structures.
The response of migrating interneurons to neurotransmitters that alter electrical activity in cells in calcium dependent manner.
The creation of greater cell numbers in the forebrain due to cell division of progenitor cells.
The proliferation of neuroblasts in the ventricular zone of the cerebral cortex. The neuronal progenitors of these cells will migrate radially.
The division of neuroblasts in the subpallium area of the forebrain. The interneuron precursors that these cells give rise to include GABAergic interneurons and will migrate tangentially.
The division of neuroblasts in the subventricular zone of the forebrain. The interneuron precursors that these cells give rise to include adult olfactory bulb interneurons and migrate tangentially.
The division of glioblasts in the subpallium. These cells will give rise to oligodendrocytes.
The division of glioblasts in the subpallium. These cells will give rise to oligodendrocytes.
The division of neuroblasts in the dorsal region of the lateral ganglionic eminence. These cells give rise to embryonic interneuron precursors that will migrate tangentially to the olfactory bulb.
The migration of pyramidal a neuron precursor from the ventricular zone to the correct layer of the cerebral cortex.
The migration of GABAergic interneuron precursors from the subpallium to the cerebral cortex.
The progression of the hypothalamus region of the forebrain, from its initial formation to its mature state.
The directed movement of a cell into the hypothalamus region of the forebrain.
The movement of a hypothalamic neuronal precursor tangentially through the forebrain using an interaction of the migrating cells with axons of other neurons.
The process in which a neuroblast acquires the specialized structural and functional features of a GABAergic inhibitory neuron in the basal ganglia. Differentiation includes the processes involved in commitment of a neuroblast to a GABAergic neuron.
The process in which a neuroblast or one of its progeny commits to a pyramidal neuron fate, migrates from the ventricular zone to the appropriate layer in the cortex and develops into a mature neuron.
The progression of a pyramidal neuron from its initial formation to its mature state.
The process in which neuroepithelial cells of the neural tube give rise to radial glial cells, specialized bipotential progenitors cells of the forebrain. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which neuroepithelial cells in the neural tube acquire specialized structural and/or functional features of neurons. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which neuroepithelial cells in the neural tube acquire specialized structural and/or functional features of basal progenitor cells, neuroblasts that lose their contacts with the ventricular surface. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which neuroepithelial cells in the neural tube acquire specialized structural and/or functional features of basal progenitor cells, neuroblasts that lose their contacts with the ventricular surface. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The process in which neuroepithelial cells in the neural tube acquire specialized structural and/or functional features of basal progenitor cells, neuroblasts that lose their contacts with the ventricular surface. Differentiation includes the processes involved in commitment of a cell to a specific fate.
The mitotic division of a basal progenitor giving rise to two neurons.
The process in which a neuroblast acquires specialized structural and/or functional features of a Cajal-Retzius cell, one of a transient population of pioneering neurons in the cerebral cortex. These cells are slender bipolar cells of the developing marginal zone. One feature of these cells in mammals is that they express the Reelin gene.
The regionalization process resulting in the creation of areas within the forebrain that will direct the behavior of cell migration in differentiation as the forebrain develops.
The process in which nerve cells are generated in the forebrain. This includes the production of neuroblasts from and their differentiation into neurons.
The division of a neuroblast located in the forebrain. Neuroblast division gives rise to at least another neuroblast.
The series of molecular signals initiated by binding of Wnt protein to a receptor on the surface of the target cell that contributes to the self renewal of neuroblasts in the forebrain.
The series of molecular signals initiated by binding of Wnt protein to a receptor on the surface of the target cell that contributes to the self renewal of neuroblasts in the forebrain.
The series of molecular signals initiated by binding of Wnt protein to a receptor on the surface of the target cell that contributes to the self renewal of neuroblasts in the forebrain.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands that contributes to the self renewal of neuroblasts in the forebrain.
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 the self renewal of neuroblasts in the forebrain.
The process in which the developmental fate of a cell becomes restricted such that it will develop into a neuron that resides in the forebrain.
The process in which the developmental fate of a cell becomes restricted such that it will develop into an astrocyte that resides in the forebrain.
The process in which a relatively unspecialized cell acquires specialized features of a neuron that will reside in the forebrain.
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 the commitment of a neuroblast to a neuronal fate. The neuron will reside in the forebrain.
The series of molecular signals initiated by binding of Wnt protein to a receptor on the surface of the target cell that contributes to the commitment of a neuroblast to aneuronal fate. The neuron will reside in the forebrain.
The series of molecular signals initiated by binding of Wnt protein to a receptor on the surface of the target cell that contributes to the commitment of a neuroblast to aneuronal fate. The neuron will reside in the forebrain.
The series of molecular signals initiated by binding of Wnt protein to a receptor on the surface of the target cell that contributes to the commitment of a neuroblast to aneuronal fate. The neuron will reside in the forebrain.
Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter that contributes to the commitment of a neuroblast to a neuronal fate. The neuron will reside in the forebrain.
The process in which the cell cycle is halted during one of the normal phases (G1, S, G2, M) in a cell that has been committed to become a neuron that will reside in the forebrain.
The process whose specific outcome is the progression of a neuron that resides in the forebrain, from its initial commitment to its fate, to the fully functional differentiated cell.
The orderly movement of a cell from one site to another at least one of which is located in the forebrain.
The process in which a relatively unspecialized cell acquires specialized features of a neuron located in the hypothalamus. These neurons release gonadotrophin-releasing hormone as a neural transmitter.
The process in which the developmental fate of a cell becomes restricted such that it will develop into a hypothalamus neuron that releases gonadotrophin-releasing hormone.
The process whose specific outcome is the progression of a hypothalamus gonadotrophin-releasing hormone neuron over time, from initial commitment of its fate, to the fully functional differentiated cell.
The process in which a neuroblast acquires specialized features of an interneuron residing in the olfactory bulb.
The process in which the developmental fate of a neuroblast becomes restricted such that it will develop into an interneuron residing in the olfactory bulb.
The process whose specific outcome is the progression of an interneuron residing in the olfactory bulb, from its initial commitment, to the fully functional differentiated cell.
The process in which a relatively unspecialized cell acquires specialized features of a GABAergic interneuron residing in the cerebral cortex.
The process in which the developmental fate of a neuroblast becomes restricted such that it will develop into a GABAergic interneuron residing in the cerebral cortex.
The process whose specific outcome is the progression of a cerebral cortex GABAergic interneuron over time, from initial commitment to its fate, to the fully functional differentiated cell.
The process in which a relatively unspecialized cell acquires specialized features of a neuron residing in the cerebral cortex.
The process in which a relatively unspecialized cell acquires the specialized features of an astrocyte residing in the forebrain. An astrocyte is the most abundant type of glial cell. Astrocytes provide support for neurons and regulate the environment in which they function.
The process aimed at the progression of an astrocyte that resides in the forebrain, from initial commitment of the cell to its fate, to the fully functional differentiated cell. An astrocyte is the most abundant type of glial cell. Astrocytes provide support for neurons and regulate the environment in which they function.
The initial commitment of cells whereby the developmental fate of a cell becomes restricted such that it will develop into some type of neuron in the forebrain.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands that contributes to the commitment of a neuroblast to a neuronal fate. The neuron will reside in the forebrain.
The commitment of neuroblast to become a basal progenitor cell. Basal progenitor cells are neuronal precursor cells that are committed to becoming neurons.
The commitment of neuroepithelial cell to become a neuron that will reside in the forebrain.
The commitment of neuronal precursor cells to become specialized types of neurons in the forebrain.
The process in which the neural tube is divided into specific regions along the rostrocaudal axis.
The process in which the neural tube is regionalized in the dorsoventral axis.
The process in which the neural tube is regionalized in the dorsoventral axis.
The process whose specific outcome is the creation of the forebrain-midbrain boundary.
The process whose specific outcome is the formation of the hindbrain-spinal cord boundary.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands that results in the spatial identity of regions along the anterior-posterior axis of the spinal cord.
The series of molecular signals generated as a consequence of a retinoic acid receptor binding to one of its physiological ligands that results in the spatial identity of regions along the anterior-posterior axis of the spinal cord.
Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter that results in the spatial identity of regions along the anterior-posterior axis of the spinal cord.
The series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened that results in the spatial identity of regions along the dorsal-ventral axis of the spinal cord.
The series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened that results in the spatial identity of regions along the dorsal-ventral axis of the spinal cord.
The series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened that results in the spatial identity of regions along the dorsal-ventral axis of the spinal cord.
The chemical reactions and pathways involving the synthesis and degradation of retionic acid that results in the spatial identity of regions along the anterior-posterior axis of the spinal cord.
Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter that results the commitment of a cell to become a motor neuron in the ventral spinal cord.
Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter that results in the commitment of a cell to become an interneuron in the ventral spinal cord.
Any process that stops, prevents, or reduces the frequency, rate or extent of smoothened signaling that is involved in the patterns of cell differentiation in the ventral spinal cord.
Any process that stops, prevents, or reduces the frequency, rate or extent of smoothened signaling that is involved in the patterns of cell differentiation in the ventral spinal cord.
Any process that stops, prevents, or reduces the frequency, rate or extent of smoothened signaling that is involved in the patterns of cell differentiation in the ventral spinal cord.
Any process that stops, prevents, or reduces the frequency, rate or extent of smoothened signaling that is involved in the patterns of cell differentiation in the ventral spinal cord.
Any process that stops, prevents, or reduces the frequency, rate or extent of smoothened signaling that is involved in the patterns of cell differentiation in the ventral spinal cord.
Any process that stops, prevents, or reduces the frequency, rate or extent of smoothened signaling that is involved in the patterns of cell differentiation in the ventral spinal cord.
Any process that stops, prevents, or reduces the frequency, rate or extent of smoothened signaling that is involved in the patterns of cell differentiation in the ventral spinal cord.
The process whose specific outcome is the progression of the neural tube over time, from its formation to the mature structure. The mature structure of the neural tube exists when the tube has been segmented into the forebrain, midbrain, hindbrain and spinal cord regions. In addition neural crest has budded away from the epithelium.
Short range signaling between cells of the paraxial mesoderm and motor neuron precursors in the spinal cord that specifies the fate of the motor column neuron precursors along the anterior-posterior axis.
The commitment of unspecified motor neurons to specific motor neuron cell along the anterior-posterior axis of the spinal cord and their capacity to differentiate into specific motor neurons.
Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter that contributes to the commitment of spinal cord motor neurons to specific motor neuron types along the anterior-posterior axis.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, which contributes to the spatial identity of regions along the dorsal-ventral axis of the spinal cord.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, which contributes to the spatial identity of regions along the dorsal-ventral axis of the spinal cord.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, which contributes to the spatial identity of regions along the dorsal-ventral axis of the spinal cord.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, which contributes to the spatial identity of regions along the dorsal-ventral axis of the spinal cord.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, which contributes to the spatial identity of regions along the dorsal-ventral axis of the spinal cord.
Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter that contributes to the commitment of neuronal precursors to association neurons in the dorsal spinal cord.
The process that modulates the frequency, rate or extent of cell proliferation in the dorsal spinal cord.
The series of molecular signals initiated by binding of Wnt protein to a receptor on the surface of a cell in the dorsal spinal cord that affects the rate of its division.
The series of molecular signals initiated by binding of Wnt protein to a receptor on the surface of a cell in the dorsal spinal cord that affects the rate of its division.
The series of molecular signals initiated by binding of Wnt protein to a receptor on the surface of a cell in the dorsal spinal cord that affects the rate of its division.
The multiplication or reproduction of cells, resulting in the expansion of a cell population in the hindbrain region that is adjacent to the ventricular cavity.
The multiplication or reproduction of neuroblasts resulting in the expansion of a cell population in the external granule layer of the hindbrain. The external granule layer is the layer that originates from the rostral half of the rhombic lip in the first rhombomere.
The multiplication or reproduction of neuroblasts that will give rise to Purkinje cells. A Purkinje cell is an inhibitory GABAergic neuron found in the cerebellar cortex that projects to the deep cerebellar nuclei and brain stem.
The multiplication or reproduction of neuroblasts that will give rise to Golgi cells. A Golgi cell is an inhibitory GABAergic interneuron found in the cerebellar cortex.
The multiplication or reproduction of neuroblasts that will give rise to deep nuclear neurons.
The multiplication or reproduction of neuroblasts that will give rise to basket cells. A cerebellar basket cell is an inhibitory GABAergic interneuron found in the cerebellar cortex.
The multiplication or reproduction of neuroblasts that will give rise to stellate cells. A cerebellar stellate cell is an inhibitory GABAergic interneuron found in the cerebellar cortex.
The multiplication or reproduction of neuroblasts that will give rise to granule cells. A granule cell is a glutamatergic interneuron found in the cerebellar cortex.
The multiplication or reproduction of neuroblasts that will give rise to neurons of the lateral pontine nucleus and the locus ceruleus.
The radially directed movement of a cell along radial glial cells in the hindbrain. Radial migration refers to a directed movement from the internal ventricular area to the outer surface of the hindbrain.
The inward migration of postmitotic granule cells along a radial glial cell from the external granule layer to the internal granule cell layer.
The migration of a cell in the hindbrain in which cells move orthogonal to the direction of radial migration.
The early migration of granule cell precursors in which cells move orthogonal to the direction of radial migration and ultimately cover the superficial zone of the cerebellar primordium.
The process that modulates the frequency, rate or extent of granule cell precursor proliferation.
The process that mediates the transfer of information from Purkinje cells to granule cell precursors resulting in an increase in rate of granule cell precursor cell proliferation.
The series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened in cerebellar granule cells that contributes to the regulation of proliferation of the cells.
The series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened in cerebellar granule cells that contributes to the regulation of proliferation of the cells.
The series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened in cerebellar granule cells that contributes to the regulation of proliferation of the cells.
The process that mediates the transfer of information from the extracellular matrix to granule cell precursors resulting in a decrease in rate of granule cell precursor cell proliferation.
The process that activates or increases the rate or extent of granule cell precursor proliferation.
The process that activates or increases the rate or extent of granule cell precursor proliferation.
The process that activates or increases the rate or extent of granule cell precursor proliferation.
The process that activates or increases the rate or extent of granule cell precursor proliferation.
The process that activates or increases the rate or extent of granule cell precursor proliferation.
The process that stops, prevents or reduces the rate or extent of granule cell precursor proliferation.
The process that stops, prevents or reduces the rate or extent of granule cell precursor proliferation.
The process that stops, prevents or reduces the rate or extent of granule cell precursor proliferation.
The process that stops, prevents or reduces the rate or extent of granule cell precursor proliferation.
The migration of postmitotic a Purkinje cell along radial glial cells from the ventricular zone to the Purkinje cell layer.
The formation of scaffolds from a radial glial cell. The scaffolds are used as a substrate for the radial migration of cells.
The formation of scaffolds from a radial glial cell. The scaffolds are used as a substrate for the radial migration of cells.
The changes in adhesion between a neuronal cell and a glial cell as a component of the process of hindbrain glial-mediated radial cell migration.
The process that increases the extent of granule cell motility using intracellular calcium signaling mechanisms during radial migration.
The process that increases the extent of granule cell motility using intracellular calcium signaling mechanisms during radial migration.
The process that increases the extent of granule cell motility using intracellular calcium signaling mechanisms during radial migration.
The process that increases the extent of granule cell motility using intracellular calcium signaling mechanisms during radial migration.
The process that increases the extent of granule cell motility using intracellular calcium signaling mechanisms during radial migration.
The process that increases the extent of granule cell motility using intracellular calcium signaling mechanisms during radial migration.
The directed movement of a deep nuclear neuron from the ventricular zone to the deep hindbrain nuclei.
The directed movement of a deep nuclear neuron from their ventrolateral origin to a rostrodorsal region of the cerebellar plate.
The directed movement of a deep nuclear neuron from the rostrodorsal region of the cerebellar plate to their final more ventral position.
The early migration of a precerebellar neuronal precursor in which a cell move from the rhombic lip, orthogonal to the direction of radial migration and ultimately reside in the brainstem.
The creation and reception of signals that repel a precerebellar neuron as a component of the process of tangential migration.
The creation and reception of signals that guide a precerebellar neuron towards their signals, where this process is involved in tangential migration.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body towards target cells in a different central nervous system region.
The process in which a relatively unspecialized cell acquires specialized features of a neuron whose cell body resides in the central nervous system.
The process whose specific outcome is the progression of a neuron whose cell body is located in the central nervous system, from initial commitment of the cell to a neuronal fate, to the fully functional differentiated neuron.
Generation of a long process from a neuron whose cell body resides in the central nervous system. The process carries efferent (outgoing) action potentials from the cell body towards target cells.
Generation of a long process that carries efferent (outgoing) action potentials from the cell body towards target cells from a neuron located in the central nervous system whose axons remain within a single brain region.
Generation of a long process of a pyramidal cell, that carries efferent (outgoing) action potentials from the cell body in cerebral cortex layer V towards target cells in the gray matter of the spinal cord. This axonal process is a member of those that make up the corticospinal tract.
Generation of a long process of a pyramidal cell, that carries efferent (outgoing) action potentials from the cell body in cerebral cortex layer V towards target cells in the gray matter of the spinal cord. This axonal process is a member of those that make up the corticospinal tract.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in the dorsal root ganglion towards target cells in the medulla. This axonal process is a member of those that make up the gracilis tract, a group of axons that are from neurons involved in proprioception from the lower trunk and lower limb.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in the dorsal root ganglion towards target cells in the medulla. This axonal process is a member of those that make up the cuneatus tract, a group of axons that are from neurons involved in proprioception from the upper trunk and upper limb.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in one half of the cerebral cortex towards target cells in the contralateral half. This axonal process is a member of those that make up the anterior commissure, a small midline fiber tract that lies at the anterior end of the corpus callosum.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in the midbrain towards target cells in the diencephalon.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in the vestibular nucleus of the pons towards target cells in the spinal cord.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in the spinal cord towards target cells in the thalamus. This axonal process is a member of those that make up the spinothalamic tract, one of the major routes of nociceptive signaling.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in the red nucleus of the midbrain towards target cells in the spinal cord.
The process in which the anatomical structures of the spinal cord ventral commissure are generated and organized.
The process in which the migration of an axon growth cone of a neuron that is part of the corticospinal tract is directed from the cerebral cortex layer V to the spinal cord dorsal funiculus in response to a combination of attractive and repulsive cues.
The process in which the migration of an axon growth cone of a pyramidal cell that is part of the corticospinal tract is directed from its cell body in layer V through the cerebral cortex in response to a combination of attractive and repulsive cues.
The process in which the migration of an axon growth cone of a pyramidal cell that is part of the corticospinal tract is directed after exiting the cerebral cortex through the internal capsule in response to a combination of attractive and repulsive cues.
The process in which the migration of an axon growth cone of a pyramidal cell that is part of the corticospinal tract is directed after exiting the internal capsule through the cerebral peduncle in response to a combination of attractive and repulsive cues.
The process in which the migration of an axon growth cone of a pyramidal cell that is part of the corticospinal tract is directed after exiting the cerebral peduncle through the basilar pons in response to a combination of attractive and repulsive cues.
The process in which the migration of an axon growth cone of a pyramidal cell that is part of the corticospinal tract is directed after exiting the basilar pons through the medullary pyramid in response to a combination of attractive and repulsive cues.
The process in which the migration of an axon growth cone of a pyramidal cell that is part of the corticospinal tract is directed after decussation through the spinal cord in response to a combination of attractive and repulsive cues.
The process in which the migration of an axon growth cone of a pyramidal cell that is part of the corticospinal tract is directed to cross the midline to the contralateral side.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in spinal cord towards target cells in the thalamus. This axonal process is a member of those that make up the trigeminothalamic tract, one of the major routes of nociceptive and temperature signaling from the face.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in the pons towards target cells in the spinal cord.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in the medulla towards target cells in the spinal cord.
Generation of a long process of a CNS neuron, that carries efferent (outgoing) action potentials from the cell body in the superior colliculus of the midbrain towards target cells in the ventral spinal cord.
The regionalization process that creates areas within the forebrain that will direct the behavior of cell migration in differentiation as the telencephalon develops.
The differentiation of cells that will contribute to the structure and function of the hypothalamus.
The orderly movement of cells from one site to another in the subpallium.
The migration of cells in the developing subpallium in which cells move from the ventricular and/or subventricular zone toward the surface of the brain.
The progression of the pineal gland over time from its initial formation until its mature state. The pineal gland is an endocrine gland that secretes melatonin and is involved in circadian rhythms.
The progression of the pituitary gland over time from its initial formation until its mature state. The pituitary gland is an endocrine gland that secretes hormones that regulate many other glands.
The progression of the adenohypophysis over time from its initial formation until its mature state. The adenohypophysis is the anterior part of the pituitary. It secretes a variety of hormones and its function is regulated by the hypothalamus.
The progression of the adenohypophysis over time from its initial formation until its mature state. The adenohypophysis is the anterior part of the pituitary. It secretes a variety of hormones and its function is regulated by the hypothalamus.
The progression of the adenohypophysis over time from its initial formation until its mature state. The adenohypophysis is the anterior part of the pituitary. It secretes a variety of hormones and its function is regulated by the hypothalamus.
The progression of the neurohypophysis over time from its initial formation until its mature state. The neurohypophysis is the part of the pituitary gland that secretes hormones involved in blood pressure regulation.
The progression of the neurohypophysis over time from its initial formation until its mature state. The neurohypophysis is the part of the pituitary gland that secretes hormones involved in blood pressure regulation.
The progression of the neurohypophysis over time from its initial formation until its mature state. The neurohypophysis is the part of the pituitary gland that secretes hormones involved in blood pressure regulation.
The progression of the habenula over time from its initial formation until its mature state. The habenula is the group of nuclei that makes up the stalk of the pineal gland.
The progression of the cerebral cortex over time from its initial formation until its mature state. The cerebral cortex is the outer layered region of the telencephalon.
The progression of the cerebral cortex over time from its initial formation until its mature state. The cerebral cortex is the outer layered region of the telencephalon.
The progression of the olfactory lobe over time from its initial formation until its mature state. The olfactory lobe is the area of the brain that process the neural inputs for the sense of smell.
The progression of the olfactory cortex over time from its initial formation until its mature state. The olfactory cortex is involved in the perception of smell. It receives input from the olfactory bulb and is responsible for the identification of odors.
The formation of the flat, thickened layer of ectodermal cells known as the neural plate. The underlying dorsal mesoderm signals the ectodermal cells above it to elongate into columnar neural plate cells. The neural plate subsequently develops into the neural tube, which gives rise to the central nervous system.
The process of apical-basal elongation of individual ectodermal cells during the formation of the neural placode.
The process of expansion of cell numbers in the neural plate due to cell division of progenitor cells preferentially in the rostrocaudal direction, resulting in the elongation of the tissue.
The process in which closure points are established at multiple points and along the neural rostrocaudal axis.
The process in which the neural folds are fused extending from the initial closure points.
The process of joining together the neural folds at either end of the neural tube.
The process in which the anterior-most portion of the neural axis is formed by closure of the anterior neuropore.
The pattern specification process in which the axes of the nervous system are established.
The process that regulates the coordinated growth and differentiation that establishes the non-random mediolateral spatial arrangement of the neural plate.
The process that regulates the coordinated growth and differentiation that establishes the non-random anterior-posterior spatial arrangement of the neural plate.
The close range interaction of the anterior neural ridge to the caudal region of the neural plate that specifies the forebrain fate.
Any process that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate.
Any process that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate.
Any process that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate.
Any process that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate.
Any process that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate.
Any process that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate.
Any process that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate, initiated by binding of Wnt protein to a receptor on the surface of the target cell.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate, initiated by binding of Wnt protein to a receptor on the surface of the target cell.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate, initiated by binding of Wnt protein to a receptor on the surface of the target cell.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate, initiated by binding of Wnt protein to a receptor on the surface of the target cell.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate, initiated by binding of Wnt protein to a receptor on the surface of the target cell.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate, initiated by binding of Wnt protein to a receptor on the surface of the target cell.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate, initiated by binding of Wnt protein to a receptor on the surface of the target cell.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which a cell adopts an anterior neural cell fate, initiated by binding of Wnt protein to a receptor on the surface of the target cell.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which cell adopts an anterior neural cell fate, generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which cell adopts an anterior neural cell fate, generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which cell adopts an anterior neural cell fate, generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which cell adopts an anterior neural cell fate, generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which cell adopts an anterior neural cell fate, generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands.
The series of molecular signals that stops, prevents or reduces the frequency or rate at which cell adopts an anterior neural cell fate, generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands.
A developmental process occurring after the brain has been specified along the neural axis that is required for the midbrain-hindbrain boundary to attain its fully functional state. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
A developmental process occurring before the brain has been specified along the neural axis that is required for the midbrain-hindbrain boundary to attain its fully functional state. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
The formation of the narrow stripe of cells that lies between the prospective dorsal and ventral thalami. This boundary contains signals that pattern the prethalamic and thalamic territories of the future mid-diencephalon.
The formation of the narrow stripe of cells that lies between the prospective dorsal and ventral thalami. This boundary contains signals that pattern the prethalamic and thalamic territories of the future mid-diencephalon.
The process of directed cell movement in the neural plate resulting in tissue elongation via intercalation of adjacent cells in an epithelial sheet at the midline, leading to narrowing and lengthening of the neural plate.
Generation of cells within the nervous system.
Generation of cells within the nervous system.
The differentiation of endothelial cells from progenitor cells during blood vessel development, and the de novo formation of blood vessels and tubes in the central nervous system. The capillary endothelial cells in the brain are specialized to form the blood-brain barrier.
The process in which neuronal axons and dendrites become coated with a segmented lipid-rich sheath (myelin) to enable faster and more energetically efficient conduction of electrical impulses. The sheath is formed by the cell membranes of oligodendrocytes in the central nervous system. Adjacent myelin segments are separated by a non-myelinated stretch of axon called a node of Ranvier.
The process in which neuronal axons and dendrites become coated with a segmented lipid-rich sheath (myelin) to enable faster and more energetically efficient conduction of electrical impulses. The sheath is formed by the cell membranes of Schwann cells in the peripheral nervous system. Adjacent myelin segments are separated by a non-myelinated stretch of axon called a node of Ranvier.
The multiplication or reproduction of subpallium cells in the forebrain, resulting in the expansion of a cell population.
The multiplication or reproduction of pallium cells in the forebrain, resulting in the expansion of the cell population.
The division of a radial glial cell in the pallium. A radial glial cell is a precursor cell that gives rise to neurons and astrocytes.
The division of a glioblast in the pallium. A glioblast is a dividing precursor cell that gives rise to glial cells.
The division of neuroblasts in the pallium. Neuroblasts are precursor cells that give rise to neurons.
The multiplication or reproduction of lateral ganglionic eminence cells, resulting in the expansion of the cell population.
The multiplication or reproduction of dorsal lateral ganglionic eminence cells, resulting in the expansion of the cell population.
The multiplication or reproduction of medial ganglionic eminence cells, resulting in the expansion of a cell population.
The multiplication or reproduction of caudal ganglionic eminence cells, resulting in the expansion of a cell population.
The multiplication or reproduction of septal cells, resulting in the expansion of a cell population.
The process in which the developmental fate of a cell becomes restricted such that it will develop into a radial glial cell in the forebrain.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, which contributes to the commitment of a neuroblast to a neuronal fate. The neuron will reside in the forebrain.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, which contributes to the commitment of a neuroblast to a neuronal fate. The neuron will reside in the forebrain.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, which contributes to the commitment of a neuroblast to a neuronal fate. The neuron will reside in the forebrain.
Any series of molecular signals initiated by the binding of leukemia inhibitory factor to a receptor on the surface of the target cell, that contributes to the commitment of a neuroblast to a neuronal fate. The neuron will reside in the forebrain.
The series of molecular signals generated as a consequence of a epidermal growth factor receptor binding to one of its physiological ligands that contributes to the commitment of a neuroblast to a neuronal fate. The neuron will reside in the forebrain.
The movement of the nucleus of the ventricular zone cell between the apical and the basal zone surfaces. Mitosis occurs when the nucleus is near the apical surface, that is, the lumen of the ventricle.
The migration of cells in the telencephalon from the subventricular zone to the olfactory bulb in which cells move orthogonally to the direction of radial migration and do not use radial glial cell processes as substrates for migration.
The orderly movement of a cell from one site to another at least one of which is located in the telencephalon.
The orderly movement of glial cells through the telencephalon.
The orderly movement of an astrocyte cell through the telencephalon.
The multiplication or reproduction of telencephalon oligodendrocyte cells, resulting in the expansion of a cell population.
The orderly movement of microglial cells through the telencephalon.
The multiplication or reproduction of rhombomere cells, resulting in the expansion of the cell population.
The movement of a cell within a rhombomere. This process is known to occur as an early step in the generation of anatomical structure from a rhombomere.
The process in which a relatively unspecialized cell acquires specialized features of a rhombomere cell.
The process whose specific outcome is the progression of the metencephalon over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the corpus callosum over time, from its formation to the mature structure. The corpus callosum is a thick bundle of nerve fibers comprising a commissural plate connecting the two cerebral hemispheres. It consists of contralateral axon projections that provide communication between the right and left cerebral hemispheres.
Any process that modulates the frequency, rate or extent of rhodopsin-mediated signaling.
The negative regulation of a signal transduction pathway in response to a stimulus upon prolonged exposure to that stimulus.
The negative regulation of a signal transduction pathway in response to a stimulus upon prolonged exposure to that stimulus.
The cellular process that ensures successive accurate and complete genome replication and chromosome segregation.
One of the distinct periods or stages into which the cell cycle is divided. Each phase is characterized by the occurrence of specific biochemical and morphological events.
A multicellular organismal process involved in the periodic casting off and regeneration of an outer covering of cuticle, feathers, hair, horns, skin.
A multicellular organismal process involved in 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.
The initial attachment of a membrane or protein to a target membrane. Docking requires only that the proteins come close enough to interact and adhere.
Any process that modulates the frequency, rate or extent of attachment of a cell to another cell.
Any process that stops, prevents or reduces the rate or extent of cell adhesion to another cell.
Any process that stops, prevents or reduces the rate or extent of cell adhesion to another cell.
Any process that stops, prevents or reduces the rate or extent of cell adhesion to another cell.
Any process that stops, prevents or reduces the rate or extent of cell adhesion to another cell.
Any process that activates or increases the rate or extent of cell adhesion to another cell.
Any process that activates or increases the rate or extent of cell adhesion to another cell.
Any process that activates or increases the rate or extent of cell adhesion to another cell.
Any process that activates or increases the rate or extent of cell adhesion to another cell.
Any process that activates or increases the rate or extent of cell adhesion to another cell.
A behavioral process involved in the cycle from wakefulness through an orderly succession of sleep states and stages that occurs on an approximately 24 hour rhythm.
A cellular process that results in the breakdown of a cellular component.
A cellular process that results in the breakdown of a cellular component.
A cellular process that results in the breakdown of a cellular component.
A process, occurring at the cellular level, that is involved in the reproductive function of a multicellular organism.
A process, occurring at the cellular level, that is involved in the reproductive function of a single-celled organism.
A biological process that directly contributes to the process of producing new individuals by one or two organisms. The new individuals inherit some proportion of their genetic material from the parent or parents.
A biological process that directly contributes to the process of producing new individuals by one or two organisms. The new individuals inherit some proportion of their genetic material from the parent or parents.
The process whose specific outcome is the progression of a chaeta over time, from its formation to the mature structure. A chaeta is a sensory multicellular cuticular outgrowth of a specifically differentiated cell.
The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that results in the attainment of the full functional capacity of a protein.
A physical, chemical, or biochemical process carried out by living organisms to break down ingested nutrients into components that may be easily absorbed and directed into metabolism.
The progression of physiological phases, occurring in the endometrium during the menstrual cycle that recur at regular intervals during the reproductive years. The menstrual cycle is an ovulation cycle where the endometrium is shed if pregnancy does not occur.
A process involved in the sexual cycle seen in females, often with physiologic changes in the endometrium that recur at regular intervals during the reproductive years.
A process involved in the sexual cycle seen in females, often with physiologic changes in the endometrium that recur at regular intervals during the reproductive years.
Any process that modulates the frequency, rate or extent of anatomical structure morphogenesis.
Any process that modulates the frequency, rate or extent of cell morphogenesis. Cell morphogenesis is the developmental process in which the shape of a cell is generated and organized.
Any process that modulates the frequency, rate or extent of cell morphogenesis. Cell morphogenesis is the developmental process in which the shape of a cell is generated and organized.
Any process that modulates the frequency, rate or extent of cell morphogenesis. Cell morphogenesis is the developmental process in which the shape of a cell is generated and organized.
A reproductive process that is a step in the formation and maturation of an ovum or female gamete from a primordial female germ cell.
The specification and formation of the polarity of a cell along its proximal/distal axis.
The attachment of a multicellular organism to a substrate or other organism.
The attachment of a multicellular organism to a surface or material.
The attachment of a cell or organism to a substrate, another cell, or other organism. Biological adhesion includes intracellular attachment between membrane regions.
A developmental process in which dormancy (sometimes called a dormant state) is induced, maintained or broken. Dormancy is a suspension of most physiological activity and growth that can be reactivated.
A developmental process in which dormancy (sometimes called a dormant state) is induced, maintained or broken. Dormancy is a suspension of most physiological activity and growth that can be reactivated.
The process in which the anatomical structures of a gland are generated and organized.
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a complex containing RNA and proteins. Includes the biosynthesis of the constituent RNA and protein molecules, and those macromolecular modifications that are involved in synthesis or assembly of the ribonucleoprotein complex.
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a complex containing RNA and proteins. Includes the biosynthesis of the constituent RNA and protein molecules, and those macromolecular modifications that are involved in synthesis or assembly of the ribonucleoprotein complex.
The initial attachment of a membrane to a target membrane, mediated by proteins protruding from the two membranes. Docking requires only that the membranes come close enough for the proteins to interact and adhere.
The initial attachment of a protein to a target membrane, mediated by a proteins protruding from the target membrane. Docking requires only that the proteins come close enough to interact and adhere.
The DNA metabolic process in which a DNA strand is synthesized by adding nucleotides to the 3' end of an existing DNA stand.
A process that results in the breakdown of the extracellular matrix.
The aggregation, arrangement and bonding together of proteins and RNA molecules to form a ribonucleoprotein complex.
The aggregation, arrangement and bonding together of proteins and RNA molecules to form a ribonucleoprotein complex.
The aggregation, arrangement and bonding together of proteins and RNA molecules to form a ribonucleoprotein complex.
The process in which a relatively unspecialized cell acquires specialized features of a generative cell. The generative cell gives rise to the sperm cells in the male gametophyte.
The process in which a relatively unspecialized cell acquires specialized features of a vegetative cell. The vegetative cell is gives rise to the pollen tube.
The process whose specific outcome is the progression of the root system over time, from its formation to the mature structure.
A homohexameric complex that recognizes and unfolds core proteasome substrate proteins, and translocates them to the core complex in an ATP dependent manner.
A protein complex, that caps one or both ends of the proteasome core complex and regulates entry into, or exit from, the proteasome core complex.
A ribosome located in the cytosol.
A ribosome located in the cytosol.
A ribosome located in the cytosol.
A ribosome located in the cytosol.
A ribosome located in the cytosol.
The large subunit of a ribosome contained within a chloroplast.
The large subunit of a ribosome contained within a chloroplast.
The small subunit of a ribosome contained within a chloroplast.
The small subunit of a ribosome contained within a chloroplast.
Enables the transfer of a single solute from one side of a membrane to the other by a mechanism involving conformational change, either by facilitated diffusion or in a membrane potential dependent process if the solute is charged.
Enables the transfer of a single solute from one side of a membrane to the other by a mechanism involving conformational change, either by facilitated diffusion or in a membrane potential dependent process if the solute is charged.
Enables the transfer of a single solute from one side of a membrane to the other by a mechanism involving conformational change, either by facilitated diffusion or in a membrane potential dependent process if the solute is charged.
Enables the transfer of a single solute from one side of a membrane to the other by a mechanism involving conformational change, either by facilitated diffusion or in a membrane potential dependent process if the solute is charged.
Enables the transfer of a specific substance or related group of substances from one side of a membrane to the other, up the solute's concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction.
Enables the transfer of a specific substance or related group of substances from one side of a membrane to the other, up the solute's concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction.
Enables the transfer of a specific substance or related group of substances from one side of a membrane to the other, up the solute's concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction.
Enables the transfer of a specific substance or related group of substances from one side of a membrane to the other, up the solute's concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction.
Small molecule produced by bacteria that carries an ion across the membrane by enclosing the ion and travelling with the ion across the membrane. It does not form a fully open pore across the membrane.
Enables the active transport of a solute across a membrane by a mechanism involving conformational change, where energy for active transport is derived from membrane potential if the solute is charged.
Catalysis of the active transport of a sodium ion across a membrane by a mechanism involving conformational change, where energy for active transport is derived from membrane potential if the solute is charged.
Catalysis of the active transport of a potassium ion across a membrane by a mechanism involving conformational change, where energy for active transport is derived from membrane potential if the solute is charged.
Catalysis of the active transport of a potassium ion across a membrane by a mechanism whereby two or more species are transported in opposite directions in a tightly coupled process not directly linked to a form of energy other than chemiosmotic energy.
Enables the transmembrane transfer of an ion by a channel that opens when a specific neurotransmitter has been bound by the channel complex or one of its constituent parts.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cu2+ = ADP + phosphate + Cu2+, directly driving the transport of the copper ions across a membrane.
Enables the transmembrane transfer of a solute by a channel that opens in response to phosphorylation of one of its constituent parts.
Enables the transport of a solute across a membrane via a large pore, un-gated channel. Examples include gap junctions, which transport substances from one cell to another; and porins which transport substances in and out of bacteria, mitochondria and chloroplasts.
Enables the transport of a solute across a membrane via a large pore, un-gated channel. Examples include gap junctions, which transport substances from one cell to another; and porins which transport substances in and out of bacteria, mitochondria and chloroplasts.
Enables the transport of a solute across a membrane via a narrow pore channel that opens in response to a particular stimulus.
Enables the transmembrane transfer of a solute by a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of a solute by a channel that opens when a specific ligand has been bound by the channel complex or one of its constituent parts.
Enables the transmembrane transfer of a solute by a channel that opens when a specific neurotransmitter has been bound by the channel complex or one of its constituent parts.
Enables the transmembrane transfer of a solute by a channel that opens when a specific neurotransmitter has been bound by the channel complex or one of its constituent parts.
Enables the transmembrane transfer of a solute by a channel that opens in response to a specific stimulus.
Enables the energy-independent facilitated diffusion, mediated by passage of a specific solute through a transmembrane aqueous pore or channel. Stereospecificity is not exhibited but this transport may be specific for a particular molecular species or class of molecules.
Enables the transmembrane transfer of a solute by a channel that opens in response to a specific ion stimulus.
Enables the transport of a solute across a membrane via a narrow pore channel that is open even in an unstimulated or 'resting' state.
Enables the transport of a potassium ion across a membrane via a narrow pore channel that is open even in an unstimulated or 'resting' state.
Enables the transport of a solute across a membrane via a narrow pore channel that may be gated or ungated.
Enables the transmembrane transfer of a cation by a voltage-gated channel. A cation is a positively charged ion. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Selectively enables the transmembrane transfer of a cation by a channel that opens upon binding acetylcholine.
Selectively enables the transmembrane transfer of a cation by a channel that opens upon binding acetylcholine.
Selectively enables the transmembrane transfer of a cation by a channel that opens upon binding acetylcholine.
Selectively enables the transmembrane transfer of a cation by a channel that opens upon binding acetylcholine.
Selectively enables the transmembrane transfer of a cation by a channel that opens upon binding acetylcholine.
Selectively enables the transmembrane transfer of a cation by a channel that opens upon binding acetylcholine.
Selectively enables the transmembrane transfer of a cation by a channel that opens upon binding acetylcholine.
Selectively enables the transmembrane transfer of a cation by a channel that opens upon binding acetylcholine.
Enables the transmembrane transfer of a calcium ion by a channel that opens when glutamate has been bound by the channel complex or one of its constituent parts.
Enables the transmembrane transfer of a cation by a channel that opens when serotonin has been bound by the channel complex or one of its constituent parts.
Enables the transmembrane transfer of a cation by a channel that opens when serotonin has been bound by the channel complex or one of its constituent parts.
Enables the transmembrane transfer of a cation by a channel that opens when serotonin has been bound by the channel complex or one of its constituent parts.
Enables the transmembrane transfer of a cation by a channel that opens when serotonin has been bound by the channel complex or one of its constituent parts.
Enables the transmembrane transfer of a chloride ion by a channel that opens when GABA has been bound by the channel complex or one of its constituent parts.
Enables the transmembrane transfer of a chloride ion by a channel that opens when glycine has been bound by the channel complex or one of its constituent parts.
Enables the transfer of an ion from one side of a membrane to the other up the solute's concentration gradient. This is carried out by binding the solute and undergoing a series of conformational changes. Transport works equally well in either direction.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + glucose(out) = protein histidine + glucose phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + sorbitol(out) = protein histidine + sorbitol phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Enables the transfer of alanine from one side of a membrane to the other. Alanine is 2-aminopropanoic acid.
Enables the transmembrane transfer of a solute by a channel that opens in response to dephosphorylation of one of its constituent parts.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + lactose(out) = protein histidine + lactose phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + mannose(out) = protein histidine + mannose phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + sorbose(out) = protein histidine + sorbose phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + mannitol(out) = protein histidine + mannitol phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + maltose(out) = protein histidine + maltose phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + cellobiose(out) = protein histidine + cellobiose phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + galactitol(out) = protein histidine + galactitol phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + galactosamine(out) = protein histidine + galactosamine phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + fructose(out) = protein histidine + fructose phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + sucrose(out) = protein histidine + sucrose phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + trehalose(out) = protein histidine + trehalose phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + N-acetylglucosamine(out) = protein histidine + N-acetylglucosamine phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + N-acetylgalactosamine(out) = protein histidine + N-acetylgalactosamine phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein N-phosphohistidine + beta-glucoside(out) = protein histidine + beta-glucoside phosphate(in). This differs from primary and secondary active transport in that the solute is modified during transport.
Enables the transfer of a zinc ion or zinc ions from the inside of the cell to the outside of the cell across a membrane.
Enables the transfer of a macromolecule from one side of a membrane to the other.
Enables the transfer of a bacteriocin from one side of a membrane to the other.
Enables transport of a solute across a membrane. This kind of transporter interacts much more weakly with the solute than the carrier does. It is an aqueous pore that extends across the membrane. It may change from closed to open and back. It transports faster than a carrier. It is always passive.
Enables the transfer of serine from one side of a membrane to the other. Serine is 2-amino-3-hydroxypropanoic acid.
Enables the transfer of inorganic cations from one side of a membrane to the other. Inorganic cations are atoms or small molecules with a positive charge that do not contain carbon in covalent linkage.
Enables the transfer of inorganic cations from one side of a membrane to the other. Inorganic cations are atoms or small molecules with a positive charge that do not contain carbon in covalent linkage.
Catalysis of the low-affinity transfer of L-tryptophan from one side of a membrane to the other. Tryptophan is 2-amino-3-(1H-indol-3-yl)propanoic acid. In low-affinity transport the transporter is able to bind the solute only if it is present at very high concentrations.
Catalysis of the low-affinity transfer of L-tryptophan from one side of a membrane to the other. Tryptophan is 2-amino-3-(1H-indol-3-yl)propanoic acid. In low-affinity transport the transporter is able to bind the solute only if it is present at very high concentrations.
Enables the transmembrane transfer of potassium by a channel with a unit conductance of 20 to 85 picoSiemens that opens in response to stimulus by internal calcium ions. Intermediate conductance calcium-activated potassium channels are more sensitive to calcium than are large conductance calcium-activated potassium channels. Transport by a channel involves catalysis of facilitated diffusion of a solute (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel, without evidence for a carrier-mediated mechanism.
Enables the transmembrane transfer of potassium by a channel with a unit conductance of 20 to 85 picoSiemens that opens in response to stimulus by internal calcium ions. Intermediate conductance calcium-activated potassium channels are more sensitive to calcium than are large conductance calcium-activated potassium channels. Transport by a channel involves catalysis of facilitated diffusion of a solute (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel, without evidence for a carrier-mediated mechanism.
Enables the transmembrane transfer of potassium by a channel with a unit conductance of 20 to 85 picoSiemens that opens in response to stimulus by internal calcium ions. Intermediate conductance calcium-activated potassium channels are more sensitive to calcium than are large conductance calcium-activated potassium channels. Transport by a channel involves catalysis of facilitated diffusion of a solute (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel, without evidence for a carrier-mediated mechanism.
Enables the transfer of a peptide 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 proton movement.
Any process that modulates the frequency, rate or extent of transmembrane transporter activity.
Migration of the nuclei of the two-nucleate embryo sac to opposite poles of the cell.
Migration of the nuclei of the two-nucleate embryo sac to opposite poles of the cell.
Migration of the nuclei of the two-nucleate embryo sac to opposite poles of the cell.
Migration of the nuclei of the two-nucleate embryo sac to opposite poles of the cell.
Migration of the nuclei of the two-nucleate embryo sac to opposite poles of the cell.
Migration of one of the four nuclei at each pole of the eight-nucleate embryo sac, to the center of the cell.
Migration of one of the four nuclei at each pole of the eight-nucleate embryo sac, to the center of the cell.
Migration of one of the four nuclei at each pole of the eight-nucleate embryo sac, to the center of the cell.
Migration of one of the four nuclei at each pole of the eight-nucleate embryo sac, to the center of the cell.
Migration of one of the four nuclei at each pole of the eight-nucleate embryo sac, to the center of the cell.
Migration of one of the four nuclei at each pole of the eight-nucleate embryo sac, to the center of the cell.
Migration of one of the four nuclei at each pole of the eight-nucleate embryo sac, to the center of the cell.
Any process that activates or increases the frequency, rate or extent of the dopamine receptor protein signaling pathway. A dopamine receptor signaling pathway is the series of molecular signals generated as a consequence of a dopamine receptor binding to one of its physiological ligands.
Combining with a neurotransmitter and transmitting the signal to initiate a change in cell 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 an amino acid stimulus. An amino acid is a carboxylic acids containing one or more amino groups.
A protein complex that contains a disulfide-linked heterodimer of T cell receptor (TCR) chains, which are members of the immunoglobulin superfamily, and mediates antigen recognition, ultimately resulting in T cell activation. The TCR heterodimer is associated with the CD3 complex, which consists of the nonpolymorphic polypeptides gamma, delta, epsilon, zeta, and, in some cases, eta (an RNA splice variant of zeta) or Fc epsilon chains.
A protein complex that contains a disulfide-linked heterodimer of T cell receptor (TCR) chains, which are members of the immunoglobulin superfamily, and mediates antigen recognition, ultimately resulting in T cell activation. The TCR heterodimer is associated with the CD3 complex, which consists of the nonpolymorphic polypeptides gamma, delta, epsilon, zeta, and, in some cases, eta (an RNA splice variant of zeta) or Fc epsilon chains.
A protein complex that contains a disulfide-linked heterodimer of T cell receptor (TCR) chains, which are members of the immunoglobulin superfamily, and mediates antigen recognition, ultimately resulting in T cell activation. The TCR heterodimer is associated with the CD3 complex, which consists of the nonpolymorphic polypeptides gamma, delta, epsilon, zeta, and, in some cases, eta (an RNA splice variant of zeta) or Fc epsilon chains.
A protein complex that contains a disulfide-linked heterodimer of T cell receptor (TCR) chains, which are members of the immunoglobulin superfamily, and mediates antigen recognition, ultimately resulting in T cell activation. The TCR heterodimer is associated with the CD3 complex, which consists of the nonpolymorphic polypeptides gamma, delta, epsilon, zeta, and, in some cases, eta (an RNA splice variant of zeta) or Fc epsilon chains.
A protein complex that contains a disulfide-linked heterodimer of T cell receptor (TCR) chains, which are members of the immunoglobulin superfamily, and mediates antigen recognition, ultimately resulting in T cell activation. The TCR heterodimer is associated with the CD3 complex, which consists of the nonpolymorphic polypeptides gamma, delta, epsilon, zeta, and, in some cases, eta (an RNA splice variant of zeta) or Fc epsilon chains.
Interacting selectively and non-covalently with a T cell receptor, the antigen-recognizing receptor on the surface of T cells.
Interacting selectively and non-covalently with a T cell receptor, the antigen-recognizing receptor on the surface of T cells.
Interacting selectively and non-covalently with a T cell receptor, the antigen-recognizing receptor on the surface of T cells.
Interacting selectively and non-covalently with a T cell receptor, the antigen-recognizing receptor on the surface of T cells.
A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell.
A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell.
A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell.
A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell.
A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell.
A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell.
A series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell.
The activity of a gene product that interacts with a receptor to effect a change in the activity of the receptor. Ligands may be produced by the same, or different, cell that expresses the receptor. Ligands may diffuse extracellularly from their point of origin to the receiving cell, or remain attached to an adjacent cell surface (e.g. Notch ligands).
The activity of a gene product that interacts with a receptor to effect a change in the activity of the receptor. Ligands may be produced by the same, or different, cell that expresses the receptor. Ligands may diffuse extracellularly from their point of origin to the receiving cell, or remain attached to an adjacent cell surface (e.g. Notch ligands).
The activity of a gene product that interacts with a receptor to effect a change in the activity of the receptor. Ligands may be produced by the same, or different, cell that expresses the receptor. Ligands may diffuse extracellularly from their point of origin to the receiving cell, or remain attached to an adjacent cell surface (e.g. Notch ligands).
The activity of a gene product that interacts with a receptor to effect a change in the activity of the receptor. Ligands may be produced by the same, or different, cell that expresses the receptor. Ligands may diffuse extracellularly from their point of origin to the receiving cell, or remain attached to an adjacent cell surface (e.g. Notch ligands).
Any process that modulates the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that modulates the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that modulates the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that modulates the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that modulates the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that modulates the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that modulates the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
Any process that activates or increases the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
A process in which the transfer of one or more phosphate groups to a substrate transmits a signal to the phosphorylated substrate.
A process in which the transfer of one or more phosphate groups to a substrate transmits a signal to the phosphorylated substrate.
A process in which the transfer of one or more phosphate groups by a kinase to a residue in the same kinase molecule transmits a signal. For example, ligand-binding can induce autophosphorylation of the activated receptor, creating binding sites for intracellular signaling molecules.
A process in which the transfer of one or more phosphate groups by a kinase to a residue in the same kinase molecule transmits a signal. For example, ligand-binding can induce autophosphorylation of the activated receptor, creating binding sites for intracellular signaling molecules.
A process in which the transfer of one or more phosphate groups by a kinase to a residue in the same kinase molecule transmits a signal. For example, ligand-binding can induce autophosphorylation of the activated receptor, creating binding sites for intracellular signaling molecules.
A process in which the transfer of one or more phosphate groups by a kinase to a residue in a different protein molecule transmits a signal.
A process in which the transfer of one or more phosphate groups by a kinase to a residue in a different protein molecule transmits a signal.
Any process that modulates the frequency, rate or extent of gene expression as a consequence of a process in which a signal is released and/or conveyed from one location to another.
The signaling process in which signal transduction is brought to an end rather than being reversibly modulated.
The signaling process in which T cell signal transduction is brought to an end rather than being reversibly modulated.
Interacting selectively and non-covalently with the major histocompatibility complex.
Interacting selectively and non-covalently with the class I major histocompatibility complex.
Interacting selectively and non-covalently with the class Ib major histocompatibility complex.
Interacting selectively and non-covalently with the class II major histocompatibility complex.
Interacting selectively and non-covalently with major histocompatibility complex class I molecules via the antigen binding groove.
Interacting selectively and non-covalently with major histocompatibility complex class I molecules via the lateral surface.
Interacting selectively and non-covalently with major histocompatibility complex class Ib molecules.
Interacting selectively and non-covalently with major histocompatibility complex class Ib molecules via the antigen binding groove.
Interacting selectively and non-covalently with major histocompatibility complex class Ib molecules via the lateral surface.
A series of molecular signals initiated by the binding of the cell surface receptor CD40 to one of its physiological ligands, and ending with regulation of a downstream cellular process, e.g. transcription.
The transfer of information from one cell to another, where the signal travels from the signal-producing cell to the receiving cell by passive diffusion or bulk flow in intercellular fluid. The signaling cell and the receiving cell are usually in the vicinity of each other.
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 indicating the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).
The entirety of a process in which information is transmitted within a biological system. This process begins with an active signal and ends when a cellular response has been triggered.
The entirety of a process in which information is transmitted within a biological system. This process begins with an active signal and ends when a cellular response has been triggered.
The entirety of a process in which information is transmitted within a biological system. This process begins with an active signal and ends when a cellular response has been triggered.
The entirety of a process in which information is transmitted within a biological system. This process begins with an active signal and ends when a cellular response has been triggered.
The entirety of a process in which information is transmitted within a biological system. This process begins with an active signal and ends when a cellular response has been triggered.
The entirety of a process in which information is transmitted within a biological system. This process begins with an active signal and ends when a cellular response has been triggered.
The entirety of a process in which information is transmitted within a biological system. This process begins with an active signal and ends when a cellular response has been triggered.
The process in which an activated neuronal cell receptor conveys information down a signaling pathway, resulting in a change in the function or state of a cell. This process may be intracellular or intercellular.
A process where induction of a conformational change in a molecule transmits a signal to that molecule.
A process where induction of a conformational change in a molecule transmits a signal to that molecule.
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 chemical stimulus.
Combining with a bioactive lipid 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 bioactive lipid is a lipid for which changes in lipid levels result in functional consequences in a variety of cellular processes.
Any process that modulates the frequency, rate or extent of a signaling process.
Any process that modulates the frequency, rate or extent of a signaling process.
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 mechanical stimulus.
Any process that activates, maintains or increases the frequency, rate or extent of a signaling process.
Any process that activates, maintains or increases the frequency, rate or extent of a signaling process.
Any process that stops, prevents, or reduces the frequency, rate or extent of a signaling process.
Any process that stops, prevents, or reduces the frequency, rate or extent of a signaling process.
The regulation of a signal transduction pathway in response to a stimulus upon prolonged exposure to that stimulus.
The positive regulation of a signal transduction pathway in response to a stimulus upon prolonged exposure to that stimulus.
The directed movement of endocytosed material through the cell and its exocytosis from the plasma membrane at the opposite side.
Any process involved in the maintenance of an internal steady state of anions at the level of a cell.
Any process involved in the maintenance of an internal steady state of cations at the level of a cell.
Any process involved in the maintenance of an internal steady state of monovalent inorganic cations at the level of a cell.
Any process involved in the maintenance of an internal steady state of divalent cations at the level of a cell.
Any process involved in the maintenance of an internal steady state of trivalent cations at the level of a cell.
Any process involved in the maintenance of an internal steady state of potassium ions at the level of a cell.
A large complex that acts as a tethering factor involved in transporting vesicles from the ER through the Golgi to the plasma membrane. A TRAPP (transport protein particle) complex has a core set of proteins which are joined by specific subunits depending on the cellular component where a given TRAPP complex is active.
A large complex that acts as a tethering factor involved in transporting vesicles from the ER through the Golgi to the plasma membrane. A TRAPP (transport protein particle) complex has a core set of proteins which are joined by specific subunits depending on the cellular component where a given TRAPP complex is active.
A large complex that acts as a tethering factor involved in transporting vesicles from the ER through the Golgi to the plasma membrane. A TRAPP (transport protein particle) complex has a core set of proteins which are joined by specific subunits depending on the cellular component where a given TRAPP complex is active.
A large complex that acts as a tethering factor involved in transporting vesicles from the ER through the Golgi to the plasma membrane. A TRAPP (transport protein particle) complex has a core set of proteins which are joined by specific subunits depending on the cellular component where a given TRAPP complex is active.
The maintenance of established anisotropic intracellular organization or cell growth patterns.
The maintenance of established anisotropic intracellular organization or cell growth patterns.
The evolutionarily conserved CCR4-NOT complex is involved in several aspects of mRNA metabolism, including repression and activation of mRNA initiation, control of mRNA elongation, and the deadenylation and subsequent degradation of mRNA. In Saccharomyces the CCR4-NOT complex comprises a core complex of 9 proteins (Ccr4p, Caf1p, Caf40p, Caf130p, Not1p, Not2p, Not3p, Not4p, and Not5p), Caf4p, Caf16p, and several less well characterized proteins.
The core of the CCR4-NOT complex. In Saccharomyces the CCR4-NOT core complex comprises Ccr4p, Caf1p, Caf40p, Caf130p, Not1p, Not2p, Not3p, Not4p, and Not5p.
The contractile element of skeletal and cardiac muscle; a long, highly organized bundle of actin, myosin, and other proteins that contracts by a sliding filament mechanism.
The contractile element of skeletal and cardiac muscle; a long, highly organized bundle of actin, myosin, and other proteins that contracts by a sliding filament mechanism.
The repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs.
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.
A constituent of the extracellular matrix that enables the matrix to resist longitudinal stress.
A constituent of the extracellular matrix that enables the matrix to resist compressive forces; often a proteoglycan.
Interacting selectively and non-covalently with a component of the extracellular matrix.
Interacting selectively and non-covalently with a component of the extracellular matrix.
Any process involved in the maintenance of an internal steady state of manganese ions at the level of a cell.
A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments.
Any cellular process that depends upon or alters the actin cytoskeleton, that part of the cytoskeleton comprising actin filaments and their associated proteins.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a prolongation or process extending from a cell, e.g. a flagellum or axon.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a prolongation or process extending from a cell, e.g. a flagellum or axon.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a prolongation or process extending from a cell, e.g. a flagellum or axon.
Formation of a prolongation or process extending from a cell, e.g. a flagellum or axon.
Formation of a prolongation or process extending from a cell, e.g. a flagellum or axon.
Formation of a lamellipodium, a thin sheetlike extension of the surface of a migrating cell.
Formation of a lamellipodium, a thin sheetlike extension of the surface of a migrating cell.
Formation of a lamellipodium, a thin sheetlike extension of the surface of a migrating cell.
Formation of a microvillus, a thin cylindrical membrane-covered projection on the surface of a cell.
Assembly of the parallel bundle of actin filaments at the core of a microvillus.
Formation of a microspike, a dynamic, actin-rich projection extending from the surface of a migrating animal cell.
Formation of a microspike, a dynamic, actin-rich projection extending from the surface of a migrating animal cell.
Formation of a microspike, a dynamic, actin-rich projection extending from the surface of a migrating animal cell.
The cell cycle process in which rearrangement of the spatial distribution of actin filaments and associated proteins occurs.
The cell cycle process in which rearrangement of the spatial distribution of actin filaments and associated proteins occurs.
Assembly of actin filament bundles in which the filaments are loosely packed (approximately 30-60 nm apart) and arranged with opposing polarities; the loose packing allows myosin (usually myosin-II) to enter the bundle.
The severing of actin filaments into numerous short fragments, usually mediated by actin severing proteins.
Assembly of actin filament bundles in which the filaments are tightly packed (approximately 10-20 nm apart) and oriented with the same polarity.
Covalent modification of an actin molecule.
The sliding of actin thin filaments and myosin thick filaments past each other in muscle contraction. This involves a process of interaction of myosin located on a thick filament with actin located on a thin filament. During this process ATP is split and forces are generated.
Movement of a vesicle along an actin filament, mediated by motor proteins.
A cellular component that forms a specialized region of connection between two or more cells or between a cell and the extracellular matrix. At a cell junction, anchoring proteins extend through the plasma membrane to link cytoskeletal proteins in one cell to cytoskeletal proteins in neighboring cells or to proteins in the extracellular matrix.
A cell junction that forms a connection between a cell and the extracellular matrix.
A cell-substrate junction (attachment structure) found in epithelial cells that links intermediate filaments to extracellular matrices via transmembrane complexes. In vertebrates, hemidesmosomes mediate contact between the basal side of epithelial cells and the basal lamina. In C. elegans, hemidesmosomes connect epithelial cells to distinct extracellular matrices on both the apical and basal cell surfaces.
A cell-substrate junction (attachment structure) found in epithelial cells that links intermediate filaments to extracellular matrices via transmembrane complexes. In vertebrates, hemidesmosomes mediate contact between the basal side of epithelial cells and the basal lamina. In C. elegans, hemidesmosomes connect epithelial cells to distinct extracellular matrices on both the apical and basal cell surfaces.
A cell-substrate junction (attachment structure) found in epithelial cells that links intermediate filaments to extracellular matrices via transmembrane complexes. In vertebrates, hemidesmosomes mediate contact between the basal side of epithelial cells and the basal lamina. In C. elegans, hemidesmosomes connect epithelial cells to distinct extracellular matrices on both the apical and basal cell surfaces.
A cell-substrate junction (attachment structure) found in epithelial cells that links intermediate filaments to extracellular matrices via transmembrane complexes. In vertebrates, hemidesmosomes mediate contact between the basal side of epithelial cells and the basal lamina. In C. elegans, hemidesmosomes connect epithelial cells to distinct extracellular matrices on both the apical and basal cell surfaces.
A cell-cell junction in which: on the cytoplasmic surface of each interacting plasma membrane is a dense plaque composed of a mixture of intracellular anchor proteins; a bundle of keratin intermediate filaments is attached to the surface of each plaque; transmembrane adhesion proteins of the cadherin family bind to the plaques and interact through their extracellular domains to hold the adjacent membranes together by a Ca2+-dependent mechanism.
A cell-cell junction in which: on the cytoplasmic surface of each interacting plasma membrane is a dense plaque composed of a mixture of intracellular anchor proteins; a bundle of keratin intermediate filaments is attached to the surface of each plaque; transmembrane adhesion proteins of the cadherin family bind to the plaques and interact through their extracellular domains to hold the adjacent membranes together by a Ca2+-dependent mechanism.
Catalysis of the reaction: R-CH2-NH2 + H2O + acceptor = R-CHO + NH3 + reduced acceptor.
Catalysis of the reaction: R-CH2-NH2 + H2O + acceptor = R-CHO + NH3 + reduced acceptor.
Catalysis of the reaction: R-CH2-NH2 + H2O + acceptor = R-CHO + NH3 + reduced acceptor.
Catalysis of the reaction: R-CH2-NH2 + H2O + acceptor = R-CHO + NH3 + reduced acceptor.
Catalysis of the reaction: R-CH2-NH2 + H2O + acceptor = R-CHO + NH3 + reduced acceptor.
Catalysis of the reaction: R-CH2-NH2 + H2O + acceptor = R-CHO + NH3 + reduced acceptor.
Catalysis of the reaction: H(2)O + arCH(2)NH(2) + 2 azurin = 2 reduced azurin + ArCHO + NH(3). The symbol arCH(2)NH(2) represents an aralkylamine and ArCHO is an aryl aldehyde.
Catalysis of the reaction: H(2)O + arCH(2)NH(2) + 2 azurin = 2 reduced azurin + ArCHO + NH(3). The symbol arCH(2)NH(2) represents an aralkylamine and ArCHO is an aryl aldehyde.
Catalysis of the reaction: H(2)O + arCH(2)NH(2) + 2 azurin = 2 reduced azurin + ArCHO + NH(3). The symbol arCH(2)NH(2) represents an aralkylamine and ArCHO is an aryl aldehyde.
Catalysis of the reaction: H(2)O + arCH(2)NH(2) + 2 azurin = 2 reduced azurin + ArCHO + NH(3). The symbol arCH(2)NH(2) represents an aralkylamine and ArCHO is an aryl aldehyde.
Catalysis of the reaction: H(2)O + arCH(2)NH(2) + 2 azurin = 2 reduced azurin + ArCHO + NH(3). The symbol arCH(2)NH(2) represents an aralkylamine and ArCHO is an aryl aldehyde.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Catalysis of the reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+.
Any of the inward folds of the mitochondrial inner membrane. Their number, extent, and shape differ in mitochondria from different tissues and organisms. They appear to be devices for increasing the surface area of the mitochondrial inner membrane, where the enzymes of electron transport and oxidative phosphorylation are found. Their shape can vary with the respiratory state of the mitochondria.
Any of the inward folds of the mitochondrial inner membrane. Their number, extent, and shape differ in mitochondria from different tissues and organisms. They appear to be devices for increasing the surface area of the mitochondrial inner membrane, where the enzymes of electron transport and oxidative phosphorylation are found. Their shape can vary with the respiratory state of the mitochondria.
Any of the heteromeric enzymes, located in the mitochondrion, that act in the tricarboxylic acid (TCA) cycle.
The killing by a virus of a cell in its host organism by means of the rupture of cell membranes and the loss of cytoplasm.
The killing by a virus of a cell in its host organism by means of the rupture of cell membranes and the loss of cytoplasm.
The killing by a virus of a cell in its host organism by means of the rupture of cell membranes and the loss of cytoplasm.
The killing by a virus of a cell in its host organism by means of the rupture of cell membranes and the loss of cytoplasm.
The killing by a virus of a cell in its host organism by means of the rupture of cell membranes and the loss of cytoplasm.
The killing by a virus of a cell in its host organism by means of the rupture of cell membranes and the loss of cytoplasm.
The formation of mature insulin by proteolysis of the precursor preproinsulin. The signal sequence is first cleaved from preproinsulin to form proinsulin; proinsulin is then cleaved to release the C peptide, leaving the A and B chains of mature insulin linked by disulfide bridges.
Any process that modulates the frequency, rate or extent of the cell cycle process in which a cell progresses from metaphase to anaphase during mitosis, triggered by the activation of the anaphase promoting complex by Cdc20/Sleepy homolog which results in the degradation of Securin.
The regulated release of a peptide hormone from a cell.
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.
A protein-pigment complex that may be closely or peripherally associated to photosynthetic reaction centers that participate in harvesting and transferring radiant energy to the reaction center.
A plasma membrane protein-pigment complex that may be closely or peripherally associated to photosynthetic reaction centers that participate in harvesting and transferring radiant energy to the reaction center. Examples of this complex are found in bacterial species.
Light harvesting complex associated with the reaction complex of photosynthetic purple bacteria.
Bacteriochlorophyll a binding complex that is peripherally associated to the bacterial reaction center.
Protein complex that surrounds and transfers excitation energy directly to the bacterial reaction center; binds bacteriochlorophyll a and has a single absorption band between 870 and 890 nm.
Protein complex that surrounds and transfers excitation energy directly to the bacterial reaction center; binds bacteriochlorophyll a and has a single absorption band between 870 and 890 nm.
Protein-pigment complex that absorbs light at 800 and 820 nm; is peripherally associated to the bacterial reaction center; transfers excitation energy to the B875 antenna complex.
Protein-pigment complex that absorbs light at 800 and 820 nm; is peripherally associated to the bacterial reaction center; transfers excitation energy to the B875 antenna complex.
Protein-pigment complex that absorbs light at 800 and 850 nm; is peripherally associated to the bacterial reaction center; transfers excitation energy to the B875 antenna complex.
Protein-pigment complex that absorbs light at 800 and 850 nm; is peripherally associated to the bacterial reaction center; transfers excitation energy to the B875 antenna complex.
A pigment protein complex that forms part of the photosystem I associated light-harvesting complex I; contains two proteins (usually about 24 and 21.5 kDa); has a fluorescence maximum between 680 and 690 nm.
A pigment protein complex that forms part of the photosystem I associated light-harvesting complex I; contains two proteins (usually about 20 kDa); has a fluorescence maximum of 730 nm.
A pigment protein complex that forms part of the photosystem II associated light-harvesting complex II; contains two proteins (usually about 28 and 27 kDa), and may contain a third; peripherally located relative to other LHC polypeptides.
Any of the granules, approximately 32 nm x 48 nm and consisting of highly aggregated phycobiliproteins, that are attached in arrays to the external face of a thylakoid membrane in algae of the phyla Cyanophyta and Rhodophyta, where they function as light-harvesting devices in photosynthesis. Excitation energy in the phycobilisome flows in the sequence: phycoerythrin, phycocyanin, allophycocyanin before passing to the antenna chlorophyll of photosystem II.
The process of restoring a protein to its original state after damage by such things as oxidation or spontaneous decomposition of residues.
Photosystem located in the chloroplast that functions as a light-dependent plastocyanin-ferredoxin oxidoreductase, transferring electrons from plastocyanin to ferredoxin. An example of this is found in Arabidopsis thaliana.
A protein complex located in the plasma membrane-derived thylakoid. The photosystem functions as a light-dependent plastocyanin-ferredoxin oxidoreductase, transferring electrons from plastocyanin to ferredoxin. Examples of this complex are found in bacterial species.
An integral chloroplast membrane complex containing the P680 reaction center. In the light, PSII functions as a water-plastoquinone oxidoreductase, transferring electrons from water to plastoquinone.
A protein complex, located in the membrane-derived thylakoid, containing the P680 reaction center. In the light, PSII functions as a water-plastoquinone oxidoreductase, transferring electrons from water to plastoquinone.
The process whose specific outcome is the progression of the myeloid and lymphoid derived organ/tissue systems of the blood and other parts of the body over time, from formation to the mature structure. The site of hemopoiesis is variable during development, but occurs primarily in bone marrow or kidney in many adult vertebrates.
The process whose specific outcome is the progression of the myeloid and lymphoid derived organ/tissue systems of the blood and other parts of the body over time, from formation to the mature structure. The site of hemopoiesis is variable during development, but occurs primarily in bone marrow or kidney in many adult vertebrates.
The process whose specific outcome is the progression of the myeloid and lymphoid derived organ/tissue systems of the blood and other parts of the body over time, from formation to the mature structure. The site of hemopoiesis is variable during development, but occurs primarily in bone marrow or kidney in many adult vertebrates.
The process whose specific outcome is the progression of the myeloid and lymphoid derived organ/tissue systems of the blood and other parts of the body over time, from formation to the mature structure. The site of hemopoiesis is variable during development, but occurs primarily in bone marrow or kidney in many adult vertebrates.
The process in which a relatively unspecialized precursor cell acquires specialized features of a lymphocyte. A lymphocyte is a leukocyte commonly found in the blood and lymph that has the characteristics of a large nucleus, a neutral staining cytoplasm, and prominent heterochromatin.
The process in which a relatively unspecialized precursor cell acquires specialized features of a lymphocyte. A lymphocyte is a leukocyte commonly found in the blood and lymph that has the characteristics of a large nucleus, a neutral staining cytoplasm, and prominent heterochromatin.
The process in which a relatively unspecialized precursor cell acquires specialized features of a lymphocyte. A lymphocyte is a leukocyte commonly found in the blood and lymph that has the characteristics of a large nucleus, a neutral staining cytoplasm, and prominent heterochromatin.
The process in which a relatively unspecialized precursor cell acquires specialized features of a lymphocyte. A lymphocyte is a leukocyte commonly found in the blood and lymph that has the characteristics of a large nucleus, a neutral staining cytoplasm, and prominent heterochromatin.
The process in which a relatively unspecialized myeloid precursor cell acquires the specialized features of any cell of the myeloid leukocyte, megakaryocyte, thrombocyte, or erythrocyte lineages.
Any process that modulates the frequency, rate or extent of endocytosis.
The change in morphology and behavior of a natural killer cell in response to a cytokine, chemokine, cellular ligand, or soluble factor.
The regulated release of vasopressin from secretory granules into the blood.
Any process involved in the maintenance of an internal steady state of water within an organism or cell.
Any process involved in the maintenance of an internal steady state of water within an organism or cell.
Any process involved in the maintenance of an internal steady state of water within an organism or cell.
Combining with an MHC class I protein complex to initiate a change in cellular activity. Class I here refers to classical class I molecules.
Combining with an MHC class I protein complex to initiate a change in cellular activity. Class I here refers to classical class I molecules.
Combining with an MHC class I protein complex to initiate a change in cellular activity. Class I here refers to classical class I molecules.
Combining with a MHC class I molecule of the HLA-A subclass to mediate signaling that inhibits activation of a lymphocyte.
Combining with a MHC class I molecule of the HLA-A subclass to mediate signaling that activates a lymphocyte.
Combining with a MHC class I molecule of the HLA-B subclass to mediate signaling that inhibits activation of a lymphocyte.
Combining with a MHC class I molecule of the HLA-C subclass to mediate signaling that inhibits activation of a lymphocyte.
Any process that modulates the frequency, rate or extent of the activity of the Wnt signal transduction pathway.
Any process that modulates the frequency, rate or extent of the activity of the Wnt signal transduction pathway.
Any process that modulates the frequency, rate or extent of the activity of the Wnt signal transduction pathway.
Any process that modulates the frequency, rate or extent of the activity of the Wnt signal transduction pathway.
Any process that modulates the frequency, rate or extent of the activity of the Wnt signal transduction pathway.
Any process that modulates the frequency, rate or extent of the activity of the Wnt signal transduction pathway.
A viscous, carbohydrate rich layer at the outermost periphery of a cell.
A slime layer is an easily removed, diffuse, unorganized layer of extracellular material that surrounds a cell. Specifically this consists mostly of exopolysaccharides, glycoproteins, and glycolipids.
A crystalline protein layer surrounding some bacteria.
A growth factor that binds selectively and non-covalently to glial cell-derived neurotrophic factor receptors.
A growth factor that binds selectively and non-covalently to glial cell-derived neurotrophic factor receptors.
Any of several different proteinaceous coats that can associate with membranes. Membrane coats include those formed by clathrin plus an adaptor complex, the COPI and COPII complexes, and possibly others. They are found associated with membranes on many vesicles as well as other membrane features such as pits and perhaps tubules.
A membrane coat found on coated pits and some coated vesicles; consists of polymerized clathrin triskelions, each comprising three clathrin heavy chains and three clathrin light chains, linked to the membrane via one of the AP adaptor complexes.
A membrane coat found on coated pits and some coated vesicles; consists of polymerized clathrin triskelions, each comprising three clathrin heavy chains and three clathrin light chains, linked to the membrane via one of the AP adaptor complexes.
A membrane coat found on a coated vesicle.
A heterotetrameric AP-type membrane coat adaptor complex that consists of beta3, delta, mu3 and sigma3 subunits and is found associated with endosomal membranes. AP-3 does not appear to associate with clathrin in all organisms. 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).
An AP-type membrane coat adaptor complex that consists of beta4, epsilon, mu4 and sigma4 subunits and is found associated with membranes in the trans-Golgi network; it is not clear whether AP-4 forms clathrin coats in vivo.
A clathrin coat found on a vesicle.
One of two multimeric complexes that forms a membrane vesicle coat. COPII is best characterized in S. cerevisiae, where the subunits are called Sar1p, Sec13p, Sec31p, Sec23p, and Sec24p. Vesicles with COPII coats are found associated with endoplasmic reticulum (ER) membranes at steady state.
A clathrin coat found on an endocytic vesicle.
A clathrin coat found on a synaptic vesicle.
A clathrin coat found on a vesicle of the trans-Golgi network.
A membrane coat adaptor complex that links clathrin to a membrane.
The coat found on coated pits and the coated vesicles derived from coated pits; comprises clathrin and the AP-2 adaptor complex.
Small membrane-bounded organelle formed by pinching off of a coated region of membrane. Some coats are made of clathrin, whereas others are made from other proteins.
A vesicle with a coat formed of clathrin connected to the membrane via one of the clathrin adaptor complexes.
A vesicle that mediates transport between the trans-Golgi network and other parts of the cell.
A vesicle that mediates transport between the trans-Golgi network and other parts of the cell.
A vesicle that mediates transport of cargo within the Golgi complex (for example, between cisternae of the Golgi stack).
A vesicle that mediates transport of cargo within the Golgi complex (for example, between cisternae of the Golgi stack).
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl,1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-(N-acetyl-beta-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R. Only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues act as acceptors.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl,1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-(N-acetyl-beta-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R. Only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues act as acceptors.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl,1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-(N-acetyl-beta-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R. Only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues act as acceptors.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl,1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-(N-acetyl-beta-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R. Only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues act as acceptors.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl,1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-(N-acetyl-beta-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R. Only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues act as acceptors.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl,1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-(N-acetyl-beta-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R. Only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues act as acceptors.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl,1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-(N-acetyl-beta-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R. Only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues act as acceptors.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl,1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-(N-acetyl-beta-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R. Only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues act as acceptors.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl,1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-(N-acetyl-beta-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R. Only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues act as acceptors.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl,1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,2-(N-acetyl-beta-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R. Only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues act as acceptors.
Interacting selectively and non-covalently with manganese (Mn) ions.
The chemical reactions and pathways resulting in the formation of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
The chemical reactions and pathways resulting in the formation of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
The chemical reactions and pathways resulting in the formation of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
The chemical reactions and pathways resulting in the formation of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
The chemical reactions and pathways resulting in the breakdown of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
The chemical reactions and pathways resulting in the breakdown of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
The chemical reactions and pathways resulting in the breakdown of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
The import of proteins across the outer and inner mitochondrial membranes into the matrix. Unfolded proteins enter the mitochondrial matrix with a chaperone protein; the information required to target the precursor protein from the cytosol to the mitochondrial matrix is contained within its N-terminal matrix-targeting sequence. Translocation of precursors to the matrix occurs at the rare sites where the outer and inner membranes are close together.
The import of proteins across the outer and inner mitochondrial membranes into the matrix. Unfolded proteins enter the mitochondrial matrix with a chaperone protein; the information required to target the precursor protein from the cytosol to the mitochondrial matrix is contained within its N-terminal matrix-targeting sequence. Translocation of precursors to the matrix occurs at the rare sites where the outer and inner membranes are close together.
The import of proteins across the outer and inner mitochondrial membranes into the matrix. Unfolded proteins enter the mitochondrial matrix with a chaperone protein; the information required to target the precursor protein from the cytosol to the mitochondrial matrix is contained within its N-terminal matrix-targeting sequence. Translocation of precursors to the matrix occurs at the rare sites where the outer and inner membranes are close together.
Interacting selectively and non-covalently with molybdenum (Mo) ions.
The chemical reactions and pathways resulting in the formation of a bacteriocin, any of a heterogeneous group of polypeptide antibiotics that are secreted by certain bacterial strains and are able to kill cells of other susceptible (frequently related) strains after adsorption at specific receptors on the cell surface. They include the colicins, and their mechanisms of action vary.
The chemical reactions and pathways resulting in the formation of a bacteriocin, any of a heterogeneous group of polypeptide antibiotics that are secreted by certain bacterial strains and are able to kill cells of other susceptible (frequently related) strains after adsorption at specific receptors on the cell surface. They include the colicins, and their mechanisms of action vary.
The chemical reactions and pathways resulting in the formation of a bacteriocin, any of a heterogeneous group of polypeptide antibiotics that are secreted by certain bacterial strains and are able to kill cells of other susceptible (frequently related) strains after adsorption at specific receptors on the cell surface. They include the colicins, and their mechanisms of action vary.
The chemical reactions and pathways resulting in the formation of a bacteriocin, any of a heterogeneous group of polypeptide antibiotics that are secreted by certain bacterial strains and are able to kill cells of other susceptible (frequently related) strains after adsorption at specific receptors on the cell surface. They include the colicins, and their mechanisms of action vary.
A process that mediates resistance to a bacteriocin: any of a heterogeneous group of polypeptide antibiotics that are secreted by certain bacterial strains and are able to kill cells of other susceptible (frequently related) strains after adsorption at specific receptors on the cell surface. They include the colicins, and their mechanisms of action vary.
The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state.
Any process that modulates the frequency, rate or extent of attachment of a cell to another cell or to the extracellular matrix.
The regulated release of pancreatic juice by the exocrine pancreas into the upper part of the intestine. Pancreatic juice is slightly alkaline and contains numerous enzymes and inactive enzyme precursors including alpha-amylase, chymotrypsinogen, lipase, procarboxypeptidase, proelastase, prophospholipase A2, ribonuclease, and trypsinogen. Its high concentration of bicarbonate ions helps to neutralize the acid from the stomach.
Catalysis of the transfer of a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate.
Catalysis of the transfer of a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate.
Catalysis of the transfer of a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate.
Catalysis of the transfer of a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate.
Catalysis of the transfer of a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate.
Catalysis of the transfer of a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate.
Catalysis of the transfer of a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate.
Catalysis of the transfer of a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate.
Functions to provide a physical support for the assembly of a multiprotein receptor signaling complex.
Functions to provide a physical support for the assembly of a multiprotein receptor signaling complex.
Functions as a physical support bridging the N-methyl-D-aspartate receptor-PSD-95-GKAP complex and the mGluR-Homer complex, which are involved in receptor signaling in synapses.
Functions as a physical support bridging the N-methyl-D-aspartate receptor-PSD-95-GKAP complex and the mGluR-Homer complex, which are involved in receptor signaling in synapses.
Any process that modulates the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
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 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 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 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 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 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 protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
Structural change in proteins which destroys the native, active configuration without rupture of peptide bonds.
Interacting selectively and non-covalently with a PDZ domain of a protein, a domain found in diverse signaling proteins.
Interacting selectively and non-covalently with a PDZ domain of a protein, a domain found in diverse signaling proteins.
The chemical reactions and pathways resulting in the formation of proteoglycans, any glycoprotein in which the carbohydrate units are glycosaminoglycans.
The chemical reactions and pathways resulting in the formation of proteoglycans, any glycoprotein in which the carbohydrate units are glycosaminoglycans.
The chemical reactions and pathways resulting in the formation of proteoglycans, any glycoprotein in which the carbohydrate units are glycosaminoglycans.
The chemical reactions and pathways resulting in the formation of proteoglycans, any glycoprotein in which the carbohydrate units are glycosaminoglycans.
The chemical reactions and pathways resulting in the breakdown of proteoglycans, any glycoprotein in which the carbohydrate units are glycosaminoglycans.
The chemical reactions and pathways resulting in the breakdown of proteoglycans, any glycoprotein in which the carbohydrate units are glycosaminoglycans.
The chemical reactions and pathways resulting in the breakdown of proteoglycans, any glycoprotein in which the carbohydrate units are glycosaminoglycans.
A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug.
Interacting selectively and non-covalently with a low-density lipoprotein particle, a lipoprotein particle that is rich in cholesterol esters and low in triglycerides, is typically composed of APOB100 and APOE, and has a density of 1.02-1.06 g/ml and a diameter of between 20-25 nm.
Interacting selectively and non-covalently with pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
Enables the transmembrane transfer of a proton by a voltage-gated channel. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Enables the transmembrane transfer of a proton by a voltage-gated channel. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Interacting selectively and non-covalently with troponin C, the calcium-binding subunit of the troponin complex.
The component of the Golgi membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
The component of the Golgi membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
Any process that modulates the frequency, rate or extent of initiation of DNA-dependent DNA replication; the process in which DNA becomes competent to replicate. In eukaryotes, replication competence is established in early G1 and lost during the ensuing S phase.
Any process that modulates the frequency, rate or extent of initiation of DNA-dependent DNA replication; the process in which DNA becomes competent to replicate. In eukaryotes, replication competence is established in early G1 and lost during the ensuing S phase.
Any process that modulates the frequency, rate or extent of initiation of DNA-dependent DNA replication; the process in which DNA becomes competent to replicate. In eukaryotes, replication competence is established in early G1 and lost during the ensuing S phase.
Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that activates or increases the frequency, rate or extent of Wnt signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the Wnt signaling pathway.
The process in which a relatively unspecialized cell acquires specialized features of a neuron.
The process in which a precursor cell type acquires the specialized features of a B cell. A B cell is a lymphocyte of B lineage with the phenotype CD19-positive and capable of B cell mediated immunity.
The process in which a precursor cell type acquires the specialized features of a B cell. A B cell is a lymphocyte of B lineage with the phenotype CD19-positive and capable of B cell mediated immunity.
The process in which a precursor cell type acquires the specialized features of a B cell. A B cell is a lymphocyte of B lineage with the phenotype CD19-positive and capable of B cell mediated immunity.
The process in which a precursor cell type acquires the specialized features of a B cell. A B cell is a lymphocyte of B lineage with the phenotype CD19-positive and capable of B cell mediated immunity.
The process in which a precursor cell type acquires the specialized features of a B cell. A B cell is a lymphocyte of B lineage with the phenotype CD19-positive and capable of B cell mediated immunity.
Enables the transfer of nitric oxide, nitrogen monoxide, from one side of a membrane to the other.
The directed movement of nitric oxide, nitrogen monoxide, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The chemical reactions and pathways involving melatonin (N-acetyl-5-methoxytryptamine).
The chemical reactions and pathways resulting in the formation of melatonin (N-acetyl-5-methoxytryptamine).
The chemical reactions and pathways resulting in the formation of melatonin (N-acetyl-5-methoxytryptamine).
The chemical reactions and pathways resulting in the formation of melatonin (N-acetyl-5-methoxytryptamine).
The chemical reactions and pathways resulting in the formation of melatonin (N-acetyl-5-methoxytryptamine).
Any process that modulates the frequency, rate or extent of blood coagulation.
Any process that activates or increases the frequency, rate or extent of blood coagulation.
Any process that activates or increases the frequency, rate or extent of blood coagulation.
Any process that activates or increases the frequency, rate or extent of blood coagulation.
Any process that activates or increases the frequency, rate or extent of blood coagulation.
Any process that activates or increases the frequency, rate or extent of blood coagulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of blood coagulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of blood coagulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of blood coagulation.
Any process that stops, prevents, or reduces the frequency, rate or extent of blood coagulation.
Catalysis of the reaction: formamide = H(2)O + hydrogen cyanide.
Catalysis of the reaction: formamide = H(2)O + hydrogen cyanide.
Catalysis of the reaction: formamide = H(2)O + hydrogen cyanide.
Functions as a lubricant for an extracellular matrix, such as a mucous membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix.
Any process that determines the size and arrangement of collagen fibrils within an extracellular matrix.
Any process that determines the size and arrangement of collagen fibrils within an extracellular matrix.
The chemical reactions and pathways resulting in the breakdown of proteoglycan containing heparan sulfate, any member of a group of glycosaminoglycans that have repeat units consisting of alternating alpha-(1->4) linked hexuronic acid and glucosamine residues, the former being a mixture of sulfated and nonsulfated D-glucuronic and L-iduronic acids, and the latter being either sulfated or acetylated on its amino group as well as sulfated on one of its hydroxyl groups.
The chemical reactions and pathways resulting in the breakdown of proteoglycan containing heparan sulfate, any member of a group of glycosaminoglycans that have repeat units consisting of alternating alpha-(1->4) linked hexuronic acid and glucosamine residues, the former being a mixture of sulfated and nonsulfated D-glucuronic and L-iduronic acids, and the latter being either sulfated or acetylated on its amino group as well as sulfated on one of its hydroxyl groups.
The chemical reactions and pathways resulting in the breakdown of proteoglycan containing heparan sulfate, any member of a group of glycosaminoglycans that have repeat units consisting of alternating alpha-(1->4) linked hexuronic acid and glucosamine residues, the former being a mixture of sulfated and nonsulfated D-glucuronic and L-iduronic acids, and the latter being either sulfated or acetylated on its amino group as well as sulfated on one of its hydroxyl groups.
The chemical reactions and pathways resulting in the breakdown of proteoglycan containing heparan sulfate, any member of a group of glycosaminoglycans that have repeat units consisting of alternating alpha-(1->4) linked hexuronic acid and glucosamine residues, the former being a mixture of sulfated and nonsulfated D-glucuronic and L-iduronic acids, and the latter being either sulfated or acetylated on its amino group as well as sulfated on one of its hydroxyl groups.
The chemical reactions and pathways resulting in the breakdown of proteoglycan containing heparan sulfate, any member of a group of glycosaminoglycans that have repeat units consisting of alternating alpha-(1->4) linked hexuronic acid and glucosamine residues, the former being a mixture of sulfated and nonsulfated D-glucuronic and L-iduronic acids, and the latter being either sulfated or acetylated on its amino group as well as sulfated on one of its hydroxyl groups.
The chemical reactions and pathways resulting in the breakdown of proteoglycan containing heparan sulfate, any member of a group of glycosaminoglycans that have repeat units consisting of alternating alpha-(1->4) linked hexuronic acid and glucosamine residues, the former being a mixture of sulfated and nonsulfated D-glucuronic and L-iduronic acids, and the latter being either sulfated or acetylated on its amino group as well as sulfated on one of its hydroxyl groups.
The chemical reactions and pathways involving any proteoglycan containing heparan sulfate, any member of a group of glycosaminoglycans that have repeat units consisting of alternating alpha-(1->4)-linked hexuronic acid and glucosamine residues, the former being a mixture of sulfated and nonsulfated D-glucuronic and L-iduronic acids, and the latter being either sulfated or acetylated on its amino group as well as sulfated on one of its hydroxyl groups.
The chemical reactions and pathways involving any proteoglycan containing heparan sulfate, any member of a group of glycosaminoglycans that have repeat units consisting of alternating alpha-(1->4)-linked hexuronic acid and glucosamine residues, the former being a mixture of sulfated and nonsulfated D-glucuronic and L-iduronic acids, and the latter being either sulfated or acetylated on its amino group as well as sulfated on one of its hydroxyl groups.
The chemical reactions and pathways involving any proteoglycan containing heparan sulfate, any member of a group of glycosaminoglycans that have repeat units consisting of alternating alpha-(1->4)-linked hexuronic acid and glucosamine residues, the former being a mixture of sulfated and nonsulfated D-glucuronic and L-iduronic acids, and the latter being either sulfated or acetylated on its amino group as well as sulfated on one of its hydroxyl groups.
The chemical reactions and pathways involving any proteoglycan containing heparan sulfate, any member of a group of glycosaminoglycans that have repeat units consisting of alternating alpha-(1->4)-linked hexuronic acid and glucosamine residues, the former being a mixture of sulfated and nonsulfated D-glucuronic and L-iduronic acids, and the latter being either sulfated or acetylated on its amino group as well as sulfated on one of its hydroxyl groups.
The chemical reactions and pathways involving heparin, any member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells. They are similar to heparan sulfates but are of somewhat higher average Mr (6000-20000) and contain fewer N-acetyl groups and more N-sulfate and O-sulfate groups; they may be attached in the same manner to protein, forming proteoglycans. They consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways involving heparin, any member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells. They are similar to heparan sulfates but are of somewhat higher average Mr (6000-20000) and contain fewer N-acetyl groups and more N-sulfate and O-sulfate groups; they may be attached in the same manner to protein, forming proteoglycans. They consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways involving glycosaminoglycans, any one of a group of polysaccharides that contain amino sugars. Formerly known as mucopolysaccharides, they include hyaluronic acid and chondroitin, which provide lubrication in joints and form part of the matrix of cartilage. The three-dimensional structure of these molecules enables them to trap water, which forms a gel and gives glycosaminoglycans their elastic properties.
The chemical reactions and pathways involving chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate. They usually occur linked to a protein to form proteoglycans. Two subgroups exist, one in which the sulfate is on the 4-position (chondroitin sulfate A) and the second in which it is in the 6-position (chondroitin sulfate C). They often are polydisperse and often differ in the degree of sulfation from tissue to tissue. The chains of repeating disaccharide are covalently linked to the side chains of serine residues in the polypeptide backbone of a protein by a glycosidic attachment through the trisaccharide unit galactosyl-galactosyl-xylosyl. Chondroitin sulfate B is more usually known as dermatan sulfate.
The chemical reactions and pathways involving chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate. They usually occur linked to a protein to form proteoglycans. Two subgroups exist, one in which the sulfate is on the 4-position (chondroitin sulfate A) and the second in which it is in the 6-position (chondroitin sulfate C). They often are polydisperse and often differ in the degree of sulfation from tissue to tissue. The chains of repeating disaccharide are covalently linked to the side chains of serine residues in the polypeptide backbone of a protein by a glycosidic attachment through the trisaccharide unit galactosyl-galactosyl-xylosyl. Chondroitin sulfate B is more usually known as dermatan sulfate.
The chemical reactions and pathways involving chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate. They usually occur linked to a protein to form proteoglycans. Two subgroups exist, one in which the sulfate is on the 4-position (chondroitin sulfate A) and the second in which it is in the 6-position (chondroitin sulfate C). They often are polydisperse and often differ in the degree of sulfation from tissue to tissue. The chains of repeating disaccharide are covalently linked to the side chains of serine residues in the polypeptide backbone of a protein by a glycosidic attachment through the trisaccharide unit galactosyl-galactosyl-xylosyl. Chondroitin sulfate B is more usually known as dermatan sulfate.
The chemical reactions and pathways involving dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units. They are important components of ground substance or intercellular cement of skin and some connective tissues.
The chemical reactions and pathways involving dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units. They are important components of ground substance or intercellular cement of skin and some connective tissues.
The chemical reactions and pathways involving dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units. They are important components of ground substance or intercellular cement of skin and some connective tissues.
The chemical reactions and pathways involving dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units. They are important components of ground substance or intercellular cement of skin and some connective tissues.
The chemical reactions and pathways involving dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units. They are important components of ground substance or intercellular cement of skin and some connective tissues.
The chemical reactions and pathways resulting in the formation of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
The chemical reactions and pathways resulting in the formation of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
The chemical reactions and pathways resulting in the formation of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
The chemical reactions and pathways resulting in the formation of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
The chemical reactions and pathways resulting in the formation of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
The chemical reactions and pathways resulting in the formation of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
The chemical reactions and pathways resulting in the breakdown of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
The chemical reactions and pathways resulting in the breakdown of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
The chemical reactions and pathways resulting in the breakdown of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
The chemical reactions and pathways resulting in the breakdown of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
The chemical reactions and pathways resulting in the breakdown of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
The chemical reactions and pathways resulting in the formation of dermatan sulfate, any glycosaminoglycan with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the formation of dermatan sulfate, any glycosaminoglycan with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the formation of dermatan sulfate, any glycosaminoglycan with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the formation of dermatan sulfate, any glycosaminoglycan with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the formation of dermatan sulfate, any glycosaminoglycan with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the formation of dermatan sulfate, any glycosaminoglycan with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the formation of dermatan sulfate, any glycosaminoglycan with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the formation of dermatan sulfate, any glycosaminoglycan with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the breakdown of dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the breakdown of dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the breakdown of dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the breakdown of dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the breakdown of dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the breakdown of dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the breakdown of dermatan sulfate, any of a group of glycosaminoglycans with repeats consisting of beta-(1,4)-linked L-iduronyl-beta-(1,3)-N-acetyl-D-galactosamine 4-sulfate units.
The chemical reactions and pathways resulting in the formation of heparin, any member of a group of glycosaminoglycans of average Mr (6000-20000), consisting predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways resulting in the formation of heparin, any member of a group of glycosaminoglycans of average Mr (6000-20000), consisting predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways resulting in the formation of heparin, any member of a group of glycosaminoglycans of average Mr (6000-20000), consisting predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways resulting in the formation of heparin, any member of a group of glycosaminoglycans of average Mr (6000-20000), consisting predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways resulting in the formation of heparin, any member of a group of glycosaminoglycans of average Mr (6000-20000), consisting predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways resulting in the breakdown of heparin, any member of a group of glycosaminoglycans of average Mr (6000-20000), consisting predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways resulting in the breakdown of heparin, any member of a group of glycosaminoglycans of average Mr (6000-20000), consisting predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways resulting in the breakdown of heparin, any member of a group of glycosaminoglycans of average Mr (6000-20000), consisting predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways resulting in the breakdown of heparin, any member of a group of glycosaminoglycans of average Mr (6000-20000), consisting predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
The chemical reactions and pathways involving hyaluronan, the naturally occurring anionic form of hyaluronic acid, any member of a group of glycosaminoglycans, the repeat units of which consist of beta-1,4 linked D-glucuronyl-beta-(1,3)-N-acetyl-D-glucosamine.
The chemical reactions and pathways resulting in the formation of hyaluronan, the naturally occurring anionic form of hyaluronic acid, any member of a group of glycosaminoglycans, the repeat units of which consist of beta-1,4 linked D-glucuronyl-beta-(1,3)-N-acetyl-D-glucosamine.
The chemical reactions and pathways resulting in the formation of hyaluronan, the naturally occurring anionic form of hyaluronic acid, any member of a group of glycosaminoglycans, the repeat units of which consist of beta-1,4 linked D-glucuronyl-beta-(1,3)-N-acetyl-D-glucosamine.
The chemical reactions and pathways resulting in the formation of hyaluronan, the naturally occurring anionic form of hyaluronic acid, any member of a group of glycosaminoglycans, the repeat units of which consist of beta-1,4 linked D-glucuronyl-beta-(1,3)-N-acetyl-D-glucosamine.
The chemical reactions and pathways resulting in the formation of hyaluronan, the naturally occurring anionic form of hyaluronic acid, any member of a group of glycosaminoglycans, the repeat units of which consist of beta-1,4 linked D-glucuronyl-beta-(1,3)-N-acetyl-D-glucosamine.
The chemical reactions and pathways resulting in the breakdown of hyaluronan, the naturally occurring anionic form of hyaluronic acid, any member of a group of glycosaminoglycans, the repeat units of which consist of beta-1,4 linked D-glucuronyl-beta-(1,3)-N-acetyl-D-glucosamine.
The chemical reactions and pathways resulting in the breakdown of hyaluronan, the naturally occurring anionic form of hyaluronic acid, any member of a group of glycosaminoglycans, the repeat units of which consist of beta-1,4 linked D-glucuronyl-beta-(1,3)-N-acetyl-D-glucosamine.
The chemical reactions and pathways resulting in the breakdown of hyaluronan, the naturally occurring anionic form of hyaluronic acid, any member of a group of glycosaminoglycans, the repeat units of which consist of beta-1,4 linked D-glucuronyl-beta-(1,3)-N-acetyl-D-glucosamine.
Interacting selectively and non-covalently with semaphorin receptors.
Interacting selectively and non-covalently with semaphorin receptors.
Interacting selectively and non-covalently with semaphorin receptors.
The process in which a relatively unspecialized cell acquires specialized features of a keratinocyte.
The process in which a precursor cell type acquires characteristics of a more mature T-cell. A T cell is a type of lymphocyte whose definin characteristic is the expression of a T cell receptor complex.
The process in which a precursor cell type acquires characteristics of a more mature T-cell. A T cell is a type of lymphocyte whose definin characteristic is the expression of a T cell receptor complex.
The process in which a precursor cell type acquires characteristics of a more mature T-cell. A T cell is a type of lymphocyte whose definin characteristic is the expression of a T cell receptor complex.
The process in which a precursor cell type acquires characteristics of a more mature T-cell. A T cell is a type of lymphocyte whose definin characteristic is the expression of a T cell receptor complex.
The process in which a precursor cell type acquires characteristics of a more mature T-cell. A T cell is a type of lymphocyte whose definin characteristic is the expression of a T cell receptor complex.
The process in which a precursor cell type acquires characteristics of a more mature T-cell. A T cell is a type of lymphocyte whose definin characteristic is the expression of a T cell receptor complex.
The process in which a myeloid precursor cell acquires specializes features of an erythrocyte.
The process in which a myeloid precursor cell acquires specializes features of an erythrocyte.
The process in which a myeloid precursor cell acquires specializes features of an erythrocyte.
The process in which a myeloid precursor cell acquires specializes features of an erythrocyte.
The process in which a myeloid precursor cell acquires specializes features of a megakaryocyte.
The process in which platelets bud from long processes extended by megakaryocytes.
The process in which a relatively unspecialized myeloid precursor cell acquires specialized features of a basophil cell.
The process in which a relatively unspecialized myeloid precursor cell acquires the specializes features of an eosinophil.
The process in which a relatively unspecialized myeloid precursor cell acquires the specializes features of an eosinophil.
The process in which a relatively unspecialized myeloid precursor cell acquires the specializes features of an eosinophil.
The process in which a relatively unspecialized myeloid precursor cell acquires the specializes features of an eosinophil.
The process in which a myeloid precursor cell acquires the specialized features of a neutrophil.
The process in which a myeloid precursor cell acquires the specialized features of a neutrophil.
The process in which a myeloid precursor cell acquires the specialized features of a neutrophil.
The process in which a relatively unspecialized myeloid precursor cell acquires the specialized features of a monocyte.
The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage.
Combining with an apolipoprotein to initiate a change in cell activity.
Combining with a very-low-density lipoprotein particle and delivering the very-low-density lipoprotein into the cell via endocytosis.
Combining with a very-low-density lipoprotein particle and delivering the very-low-density lipoprotein into the cell via endocytosis.
Combining with a very-low-density lipoprotein particle and delivering the very-low-density lipoprotein into the cell via endocytosis.
Combining with a lipoprotein particle and delivering the lipoprotein particle into the cell via endocytosis. A lipoprotein particle, also known as a lipoprotein, is a clathrate complex consisting of a lipid enwrapped in a protein host without covalent binding in such a way that the complex has a hydrophilic outer surface consisting of all the protein and the polar ends of any phospholipids.
Combining with a lipoprotein particle and delivering the lipoprotein particle into the cell via endocytosis. A lipoprotein particle, also known as a lipoprotein, is a clathrate complex consisting of a lipid enwrapped in a protein host without covalent binding in such a way that the complex has a hydrophilic outer surface consisting of all the protein and the polar ends of any phospholipids.
Transcription factor complex that binds to the insulin control element (ICE), a DNA sequence element found within the 5'-flanking region of the insulin gene, and activates ICE-mediated transcription.
Catalyzes transport of all four deoxy (d) NDPs, and, less efficiently, the corresponding dNTPs, in exchange for dNDPs, ADP, or ATP.
Binds to and modulates the activity of an enzyme.
Binds to and modulates the activity of an enzyme.
Binds to and modulates the activity of an enzyme.
Binds to and modulates the activity of an enzyme.
Modulates the activity of nitric oxide synthase.
The specification of female sex of an individual organism.
The specification of male sex of an individual organism.
Formation of myofibrils, the repeating units of striated muscle.
The aggregation, arrangement and bonding together of proteins to form the actin-based thin filaments of myofibrils in skeletal muscle.
The aggregation, arrangement and bonding together of proteins to form the myosin-based thick filaments of myofibrils in skeletal muscle.
The process in which peroxisomes are delivered to the vacuole and degraded in response to changing nutrient conditions.
The process in which peroxisomes are delivered to the vacuole and degraded in response to changing nutrient conditions.
The chemical reactions and pathways involving cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
The chemical reactions and pathways involving cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
The chemical reactions and pathways resulting in the formation of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
The chemical reactions and pathways resulting in the formation of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
The chemical reactions and pathways resulting in the formation of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
The chemical reactions and pathways resulting in the formation of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
The chemical reactions and pathways resulting in the formation of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
The chemical reactions and pathways resulting in the breakdown of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
The chemical reactions and pathways resulting in the breakdown of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
The chemical reactions and pathways resulting in the breakdown of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
The chemical reactions and pathways resulting in the breakdown of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation.
Interacting selectively and non-covalently with any polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
Interacting selectively and non-covalently with cellulose.
Modulates the activity of guanylate cyclase.
Binds to and increases the activity of guanylate cyclase.
Stops, prevents or reduces the activity of guanylate cyclase.
The regulated release of growth hormone from secretory granules into the blood.
The process in which proteins are secreted into the extracellular milieu via the type I secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
The process in which proteins are secreted into the extracellular milieu via the type I secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
The process in which proteins are secreted into the extracellular milieu via the type I secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the bacterial type III secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the bacterial type III secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the bacterial type III secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the bacterial type III secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
The process in which proteins are transferred into the extracellular milieu or directly into host cells by the bacterial type III secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins.
The process in which proteins are transferred into the extracellular milieu or directly into host cells, via the type IV protein secretion system.
The process in which proteins are transferred into the extracellular milieu or directly into host cells, via the type IV protein secretion system.
The process in which proteins are transferred into the extracellular milieu or directly into host cells, via the type IV protein secretion system.
A complex of three secretory proteins that carry out secretion in the type I secretion system: an inner membrane transport ATPase (termed ABC protein for ATP-binding cassette), which provides the energy for protein secretion; an outer membrane protein, which is exported via the sec pathway; and a membrane fusion protein, which is anchored in the inner membrane and spans the periplasmic space.
A complex of approximately 20 proteins, most of which are located in the cytoplasmic membrane that carries out protein secretion in the bacterial type III secretion system; type III secretion also requires a cytoplasmic, probably membrane-associated ATPase.
A complex of approximately 20 proteins, most of which are located in the cytoplasmic membrane that carries out protein secretion in the bacterial type III secretion system; type III secretion also requires a cytoplasmic, probably membrane-associated ATPase.
The covalent alteration of one or more fatty acids in a lipid, resulting in a change in the properties of the lipid.
Covalent attachment of a glycosyl residue to a lipid molecule.
The invasion by an organism of a cell of its host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The progressive compaction of dispersed interphase chromatin into threadlike chromosomes prior to mitotic or meiotic nuclear division, or during apoptosis, in eukaryotic cells.
The progressive compaction of dispersed interphase chromatin into threadlike chromosomes prior to mitotic or meiotic nuclear division, or during apoptosis, in eukaryotic cells.
The progressive compaction of dispersed interphase chromatin into threadlike chromosomes prior to mitotic or meiotic nuclear division, or during apoptosis, in eukaryotic cells.
The progressive compaction of dispersed interphase chromatin into threadlike chromosomes prior to mitotic or meiotic nuclear division, or during apoptosis, in eukaryotic cells.
Alterations undergone by nuclei at the molecular and morphological level as part of the execution phase of apoptosis.
The compaction of chromatin during apoptosis.
The breakdown of the nucleus into small membrane-bounded compartments, or blebs, each of which contain compacted DNA.
The breakdown of the nucleus into small membrane-bounded compartments, or blebs, each of which contain compacted DNA.
The breakdown of the nucleus into small membrane-bounded compartments, or blebs, each of which contain compacted DNA.
The series of molecular signals generated as a consequence of a rhodopsin molecule being activated by a photon, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a rhodopsin molecule being activated by a photon, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a rhodopsin molecule being activated by a photon, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a rhodopsin molecule being activated by a photon, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a rhodopsin molecule being activated by a photon, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
The series of molecular signals generated as a consequence of a rhodopsin molecule being activated by a photon, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent release of inositol trisphosphate (IP3) and diacylglycerol (DAG).
Catalysis of the reaction: (-)-quinate + NAD+ = (-)-3-dehydroquinate + NADH + H+.
Catalysis of the reaction: (-)-quinate + NAD+ = (-)-3-dehydroquinate + NADH + H+.
Catalysis of the reaction: (-)-quinate + NAD+ = (-)-3-dehydroquinate + NADH + H+.
Catalysis of the reaction: (-)-quinate + NAD+ = (-)-3-dehydroquinate + NADH + H+.
Catalysis of the reaction: (-)-quinate + NAD+ = (-)-3-dehydroquinate + NADH + H+.
Catalysis of the reaction: glycolate + NADP+ = glyoxylate + NADPH + H+.
Catalysis of the reaction: glycolate + NADP+ = glyoxylate + NADPH + H+.
Catalysis of the reaction: glycolate + NADP+ = glyoxylate + NADPH + H+.
Catalysis of the reaction: 5,10-methylenetetrahydromethanopterin + coenzyme F420 + 2 H(+) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + reduced coenzyme F420.
Catalysis of the reaction: 5,10-methylenetetrahydromethanopterin + coenzyme F420 + 2 H(+) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + reduced coenzyme F420.
Catalysis of the reaction: 5,10-methylenetetrahydromethanopterin + coenzyme F420 + 2 H(+) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + reduced coenzyme F420.
Catalysis of the reaction: 5,10-methylenetetrahydromethanopterin + coenzyme F420 + 2 H(+) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + reduced coenzyme F420.
Catalysis of the reaction: 5-methyltetrahydromethanopterin + coenzyme M = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M. 2-(methylthio)ethanesulfonate is also known as methyl-CoM.
Catalysis of the reaction: 5-methyltetrahydromethanopterin + coenzyme M = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M. 2-(methylthio)ethanesulfonate is also known as methyl-CoM.
Catalysis of the reaction: 5-methyltetrahydromethanopterin + coenzyme M = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M. 2-(methylthio)ethanesulfonate is also known as methyl-CoM.
Catalysis of the reaction: 5-methyltetrahydromethanopterin + coenzyme M = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M. 2-(methylthio)ethanesulfonate is also known as methyl-CoM.
Catalysis of the reaction: 5-methyltetrahydromethanopterin + coenzyme M = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M. 2-(methylthio)ethanesulfonate is also known as methyl-CoM.
Catalysis of the reaction: 5,6,7,8-tetrahydromethanopterin + N-formylmethanofuran + H(+) = N(5)-formyl-5,6,7,8-tetrahydromethanopterin + methanofuran.
Catalysis of the reaction: 5,6,7,8-tetrahydromethanopterin + N-formylmethanofuran + H(+) = N(5)-formyl-5,6,7,8-tetrahydromethanopterin + methanofuran.
Catalysis of the reaction: 5,6,7,8-tetrahydromethanopterin + N-formylmethanofuran + H(+) = N(5)-formyl-5,6,7,8-tetrahydromethanopterin + methanofuran.
Catalysis of the reaction: 5,6,7,8-tetrahydromethanopterin + N-formylmethanofuran + H(+) = N(5)-formyl-5,6,7,8-tetrahydromethanopterin + methanofuran.
Catalysis of the reaction: 5,6,7,8-tetrahydromethanopterin + N-formylmethanofuran + H(+) = N(5)-formyl-5,6,7,8-tetrahydromethanopterin + methanofuran.
Catalysis of the reaction: 5,6,7,8-tetrahydromethanopterin + N-formylmethanofuran + H(+) = N(5)-formyl-5,6,7,8-tetrahydromethanopterin + methanofuran.
Catalysis of the reaction: 5,6,7,8-tetrahydromethanopterin + N-formylmethanofuran + H(+) = N(5)-formyl-5,6,7,8-tetrahydromethanopterin + methanofuran.
Catalysis of the reaction: 5-formyltetrahydrofolate + ATP = 5,10-methenyltetrahydrofolate + ADP + H(+) + phosphate.
Catalysis of the reaction: 5-formyltetrahydrofolate + ATP = 5,10-methenyltetrahydrofolate + ADP + H(+) + phosphate.
Catalysis of the reaction: 5-formyltetrahydrofolate + ATP = 5,10-methenyltetrahydrofolate + ADP + H(+) + phosphate.
Catalysis of the reaction: 5-formyltetrahydrofolate + ATP = 5,10-methenyltetrahydrofolate + ADP + H(+) + phosphate.
Catalysis of the reaction: 5-formyltetrahydrofolate + ATP = 5,10-methenyltetrahydrofolate + ADP + H(+) + phosphate.
Catalysis of the reaction: 5-formyltetrahydrofolate + ATP = 5,10-methenyltetrahydrofolate + ADP + H(+) + phosphate.
Catalysis of the reaction: 5-formyltetrahydrofolate + ATP = 5,10-methenyltetrahydrofolate + ADP + H(+) + phosphate.
Combining with the cyclic peptide hormone melanin-concentrating hormone to initiate a change in cell activity.
Interacting selectively and non-covalently with a LIM domain (for Lin-11 Isl-1 Mec-3) of a protein, a domain with seven conserved cysteine residues and a histidine, that binds two zinc ions and acts as an interface for protein-protein interactions.
Interacting selectively and non-covalently with a LRR domain (leucine rich repeats) of a protein.
Interacting selectively and non-covalently with a clathrin heavy or light chain, the main components of the coat of coated vesicles and coated pits, and which also occurs in synaptic vesicles.
Protection of epithelial surfaces of the gastrointestinal tract from proteolytic and caustic digestive agents.
Any process that modulates the frequency, rate or extent of ossification, the formation of bone or of a bony substance or the conversion of fibrous tissue or of cartilage into bone or a bony substance.
Any process that modulates the frequency, rate or extent of ossification, the formation of bone or of a bony substance or the conversion of fibrous tissue or of cartilage into bone or a bony substance.
Any process that stops, prevents, or reduces the frequency, rate or extent of ossification, the formation of bone or of a bony substance or the conversion of fibrous tissue or of cartilage into bone or a bony substance.
Any process that stops, prevents, or reduces the frequency, rate or extent of ossification, the formation of bone or of a bony substance or the conversion of fibrous tissue or of cartilage into bone or a bony substance.
Any process that stops, prevents, or reduces the frequency, rate or extent of ossification, the formation of bone or of a bony substance or the conversion of fibrous tissue or of cartilage into bone or a bony substance.
Any process that stops, prevents, or reduces the frequency, rate or extent of ossification, the formation of bone or of a bony substance or the conversion of fibrous tissue or of cartilage into bone or a bony substance.
Any process that stops, prevents, or reduces the frequency, rate or extent of ossification, the formation of bone or of a bony substance or the conversion of fibrous tissue or of cartilage into bone or a bony substance.
Any process that stops, prevents, or reduces the frequency, rate or extent of ossification, the formation of bone or of a bony substance or the conversion of fibrous tissue or of cartilage into bone or a bony substance.
The action of a molecule that contributes to the structural integrity of an epidermal cutaneous structure.
The action of a molecule that contributes to the structural integrity of cutaneous epidermal structures such as hairs, scales, or feathers.
The deposition of hydroxyapatite, a form of calcium phosphate with the formula Ca10(PO4)6(OH)2, in bone tissue.
Catalysis of the reaction: testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H + H+.
Catalysis of the reaction: testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H + H+.
Catalysis of the reaction: testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H + H+.
Catalysis of the reaction: testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H + H+.
Catalysis of the reaction: testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H + H+.
Catalysis of the reaction: testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H + H+.
Combining with estrogen and transmitting the signal within the cell to trigger a change in cell activity or function.
The component of the synaptic vesicle membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
Any of several large complexes that contain two or three dynein heavy chains and several light chains, and have microtubule motor activity.
The region between the plasma membrane and the cell wall in organisms lacking an outer cell membrane such as yeast and Gram positive bacteria. The region is thinner than the equivalent in Gram negative bacteria.
The region between the plasma membrane and the cell wall in organisms lacking an outer cell membrane such as yeast and Gram positive bacteria. The region is thinner than the equivalent in Gram negative bacteria.
The region between the plasma membrane and the cell wall in organisms lacking an outer cell membrane such as yeast and Gram positive bacteria. The region is thinner than the equivalent in Gram negative bacteria.
The region between the plasma membrane and the cell wall in organisms lacking an outer cell membrane such as yeast and Gram positive bacteria. The region is thinner than the equivalent in Gram negative bacteria.
The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
A protein serine/threonine phosphatase complex formed by the catalytic subunit of protein phosphatase 4 plus one or more regulatory subunits.
Any of a group of peptide cofactors of enzymes for the lysosomal degradation of sphingolipids. They stimulate various enzymes, including glucosylceramidase, galactosylceramidase, cerebroside-sulfatase, alpha-galactosidase, beta-galactosidase, and sphingomyelin phosphodiesterase.
Stops, prevents or reduces the activity of a protein serine/threonine kinase.
Stops, prevents or reduces the activity of a protein tyrosine kinase.
Stops, prevents or reduces the activity of a receptor signaling protein tyrosine kinase.
Binds to and increases the activity of a protein kinase, an enzyme which phosphorylates a protein.
Increases the activity of a protein tyrosine kinase, an enzyme which phosphorylates a tyrosyl phenolic group on a protein.
Binds to and increases the activity of a receptor signaling protein tyrosine kinase.
Uptake of cholesterol into the blood by absorption from the small intestine.
Any process that modulates the frequency, rate or extent of absorption of cholesterol into the blood, and the exclusion of other sterols from absorption.
The directed movement of cholesterol, cholest-5-en-3-beta-ol, 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 deoxynucleotide, a deoxyribonucleoside in ester linkage to phosphate, commonly at the 5' position of deoxyribose, into, out of or within a cell.
Catalysis of the cleavage of heparan sulfate; can degrade both heparan sulfate and heparin glycosaminoglycan chains.
Interacting selectively and non-covalently with ARF, ADP-ribosylation factor, a small monomeric cytosolic GTPase that, when bound to GTP, binds to the membranes of cells.
Any process that activates or increases the frequency, rate, extent or direction of cell growth.
Any process that activates or increases the frequency, rate, extent or direction of cell growth.
Any process that activates or increases the frequency, rate, extent or direction of cell growth.
Any process that activates or increases the frequency, rate, extent or direction of cell growth.
Any process that activates or increases the frequency, rate, extent or direction of cell growth.
Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.
Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.
Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.
Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.
The chemical reactions and pathways involving poly-N-acetyllactosamine, a carbohydrate composed of N-acetyllactosamine repeats (Gal-beta-1,4-GlcNAc-beta-1,3)n.
The chemical reactions and pathways resulting in the breakdown of poly-N-acetyllactosamine, a carbohydrate composed of N-acetyllactosamine repeats (Gal-beta-1,4-GlcNAc-beta-1,3)n.
The chemical reactions and pathways resulting in the breakdown of poly-N-acetyllactosamine, a carbohydrate composed of N-acetyllactosamine repeats (Gal-beta-1,4-GlcNAc-beta-1,3)n.
The chemical reactions and pathways resulting in the breakdown of poly-N-acetyllactosamine, a carbohydrate composed of N-acetyllactosamine repeats (Gal-beta-1,4-GlcNAc-beta-1,3)n.
The chemical reactions and pathways resulting in the formation of poly-N-acetyllactosamine, a carbohydrate composed of N-acetyllactosamine repeats (Gal-beta-1,4-GlcNAc-beta-1,3)n.
The chemical reactions and pathways resulting in the formation of poly-N-acetyllactosamine, a carbohydrate composed of N-acetyllactosamine repeats (Gal-beta-1,4-GlcNAc-beta-1,3)n.
The chemical reactions and pathways resulting in the formation of poly-N-acetyllactosamine, a carbohydrate composed of N-acetyllactosamine repeats (Gal-beta-1,4-GlcNAc-beta-1,3)n.
The chemical reactions and pathways resulting in the formation of poly-N-acetyllactosamine, a carbohydrate composed of N-acetyllactosamine repeats (Gal-beta-1,4-GlcNAc-beta-1,3)n.
A structure that lies outside the plasma membrane and surrounds the entire cell or cells. This does not include the periplasmic space.
An envelope that surrounds a bacterial cell and includes the cytoplasmic membrane and everything external, encompassing the periplasmic space, cell wall, and outer membrane if present.
Complex formed in muscle cells between the membrane of the sarcoplasmic reticulum and invaginations of the plasma membrane (T-tubules).
Invagination of the plasma membrane of a muscle cell that extends inward from the cell surface around each myofibril. The ends of T-tubules make contact with the sarcoplasmic reticulum membrane.
Invagination of the plasma membrane of a muscle cell that extends inward from the cell surface around each myofibril. The ends of T-tubules make contact with the sarcoplasmic reticulum membrane.
The process in which a relatively unspecialized monocyte acquires the specialized features of an osteoclast. An osteoclast is a specialized phagocytic cell associated with the absorption and removal of the mineralized matrix of bone tissue.
Any process involved in the controlled movement of a flagellated sperm cell.
Any process involved in the controlled movement of a flagellated sperm cell.
Any process involved in the controlled movement of a flagellated sperm cell.
The process in which a relatively unspecialized cell acquires specialized features of a melanocyte.
The process in which a relatively unspecialized cell acquires specialized features of a melanocyte.
Any process involved in the maintenance of an internal steady state of divalent inorganic anions at the level of a cell.
Any process involved in the maintenance of an internal steady state of trivalent inorganic anions at the level of a cell.
Any process involved in the maintenance of an internal steady state of monovalent inorganic anions at the level of a cell.
The directed movement of chloride ions from one side of an epithelium to the other.
The accomplishment of a non-fluctuating 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.
The process whose specific outcome is the progression of the respiratory tube over time, from its formation to the mature structure. The respiratory tube is assumed to mean any tube in the respiratory tract.
The process whose specific outcome is the progression of the lung over time, from its formation to the mature structure. In all air-breathing vertebrates the lungs are developed from the ventral wall of the oesophagus as a pouch which divides into two sacs. In amphibians and many reptiles the lungs retain very nearly this primitive sac-like character, but in the higher forms the connection with the esophagus becomes elongated into the windpipe and the inner walls of the sacs become more and more divided, until, in the mammals, the air spaces become minutely divided into tubes ending in small air cells, in the walls of which the blood circulates in a fine network of capillaries. In mammals the lungs are more or less divided into lobes, and each lung occupies a separate cavity in the thorax.
The process whose specific outcome is the progression of the adrenal gland over time, from its formation to the mature structure. This gland can either be a discrete structure located bilaterally above each kidney, or a cluster of cells in the head kidney that perform the functions of the adrenal gland. In either case, this organ consists of two cells types, aminergic chromaffin cells and steroidogenic cortical cells.
The process, occurring in the embryo, by which the anatomical structures of the limb are generated and organized. A limb is an appendage of an animal used for locomotion or grasping.
The chemical reactions and pathways resulting in the breakdown of prenylated proteins.
The chemical reactions and pathways resulting in the breakdown of prenylated proteins.
The chemical reactions and pathways resulting in the breakdown of prenylated proteins.
The chemical reactions and pathways resulting in the breakdown of prenylcysteine, 3-methyl-2-buten-1-yl-cysteine, a derivative of the amino acid cysteine formed by the covalent addition of a prenyl residue.
The chemical reactions and pathways resulting in the breakdown of prenylcysteine, 3-methyl-2-buten-1-yl-cysteine, a derivative of the amino acid cysteine formed by the covalent addition of a prenyl residue.
The chemical reactions and pathways resulting in the breakdown of prenylcysteine, 3-methyl-2-buten-1-yl-cysteine, a derivative of the amino acid cysteine formed by the covalent addition of a prenyl residue.
The chemical reactions and pathways involving prenylcysteine, 3-methyl-2-buten-1-yl-cysteine, a derivative of the amino acid cysteine formed by the covalent addition of a prenyl residue.
A cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage.
A cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage.
A cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage.
A cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage.
A cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage.
Interacting selectively and non-covalently with an estrogen receptor.
Interacting selectively and non-covalently with cyclins, proteins whose levels in a cell varies markedly during the cell cycle, rising steadily until mitosis, then falling abruptly to zero. As cyclins reach a threshold level, they are thought to drive cells into G2 phase and thus to mitosis.
Any process that modulates the frequency, rate or extent of cell migration.
Any process that activates or increases the frequency, rate or extent of cell migration.
Any process that activates or increases the frequency, rate or extent of cell migration.
Any process that activates or increases the frequency, rate or extent of cell migration.
Any process that activates or increases the frequency, rate or extent of cell migration.
Any process that activates or increases the frequency, rate or extent of cell migration.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell migration.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell migration.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell migration.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell migration.
An enzyme regulator activity that increases the processivity of polymerization by DNA polymerase, by allowing the polymerase to move rapidly along DNA while remaining topologically bound to it.
An enzyme regulator activity that increases the processivity of polymerization by DNA polymerase, by allowing the polymerase to move rapidly along DNA while remaining topologically bound to it.
Catalysis of the reaction: CMP-N-acetylneuraminate + NADPH + H+ + O2 = CMP-N-glycoloylneuraminate + NADP+ + H2O.
Catalysis of the reaction: CMP-N-acetylneuraminate + NADPH + H+ + O2 = CMP-N-glycoloylneuraminate + NADP+ + H2O.
Catalysis of the reaction: CMP-N-acetylneuraminate + NADPH + H+ + O2 = CMP-N-glycoloylneuraminate + NADP+ + H2O.
Catalysis of the reaction: CMP-N-acetylneuraminate + NADPH + H+ + O2 = CMP-N-glycoloylneuraminate + NADP+ + H2O.
Catalysis of the reaction: CMP-N-acetylneuraminate + NADPH + H+ + O2 = CMP-N-glycoloylneuraminate + NADP+ + H2O.
Catalysis of the reaction: CMP-N-acetylneuraminate + NADPH + H+ + O2 = CMP-N-glycoloylneuraminate + NADP+ + H2O.
Catalysis of the reaction: CMP-N-acetylneuraminate + NADPH + H+ + O2 = CMP-N-glycoloylneuraminate + NADP+ + H2O.
Catalysis of the reaction: a long-chain-acyl ethyl ester + H2O = a long-chain carboxylic acid + ethanol.
Catalysis of the reaction: a long-chain-acyl ethyl ester + H2O = a long-chain carboxylic acid + ethanol.
Catalysis of the reaction: a long-chain-acyl ethyl ester + H2O = a long-chain carboxylic acid + ethanol.
Catalysis of the reaction: a long-chain-acyl ethyl ester + H2O = a long-chain carboxylic acid + ethanol.
Catalysis of the reaction: hyaluronate = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.
Catalysis of the reaction: hyaluronate = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.
Catalysis of the reaction: hyaluronate = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.
Catalysis of the reaction: hyaluronate = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.
Catalysis of the reaction: hyaluronate = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.
Catalysis of the eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.
Catalysis of the eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.
Catalysis of the eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.
Catalysis of the eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.
Catalysis of the eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.
Catalysis of the eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.
Catalysis of the hydroxylation of C-24 of 1-alpha,25-hydroxycholecalciferol (25-hydroxyvitamin D3; calcitriol).
Catalysis of the hydroxylation of C-24 of 1-alpha,25-hydroxycholecalciferol (25-hydroxyvitamin D3; calcitriol).
Catalysis of the reaction: vitamin D3 + NADPH + H+ + O2 = calcidiol + NADP+ + H2O.
The action of a molecule that contributes to the structural integrity of tooth enamel.
Interacting selectively and non-covalently with the enzyme protein phosphatase 2B.
Interacting selectively and non-covalently with the enzyme protein phosphatase 2B.
Interacting selectively and non-covalently with the SNAP receptor syntaxin-3.
Interacting selectively and non-covalently with the iron-responsive element, a regulatory sequence found in the 5'- and 3'-untranslated regions of mRNAs encoding many iron-binding proteins.
Catalysis of the reaction: inositol-1,3,4,5,6-pentakisphosphate + H2O = inositol-1,4,5,6-tetrakisphosphate + phosphate.
Catalysis of the reaction: inositol-1,4,5,6-tetrakisphosphate + H2O = inositol-1,4,5-trisphosphate + phosphate.
Interacts with the fibroblast growth factor receptor to reduce the action of another ligand, the agonist.
Interacts with the fibroblast growth factor receptor to reduce the action of another ligand, the agonist.
The action characteristic of melanin-concentrating hormone, a cyclic peptide hormone that, upon receptor binding, induces melanin aggregation in melanocytes, and is also involved in regulating food intake and energy balance in mammals.
Catalysis of the conversion of precursor Z to molybdopterin, the final step in molybdopterin biosynthesis.
Interacting selectively and non-covalently with the interleukin-17 receptor.
Interacting selectively and non-covalently with the interleukin-17 receptor.
Combining with any member of the interleukin-17 family of cytokines and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with any member of the interleukin-17 family of cytokines and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
Combining with ICAM-3, intercellular adhesion molecule 3, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. ICAM-3, or CD50, are constitutively expressed on monocytes, granulocytes and lymphocytes; on physiological stimulation, they become transiently phosphorylated on serine residues.
Interacting selectively and non-covalently with receptors for intercellular adhesion molecule-3 (ICAM-3), such as DC-SIGN and LFA-1.
Interacting selectively and non-covalently with receptors for intercellular adhesion molecule-3 (ICAM-3), such as DC-SIGN and LFA-1.
Interacting selectively and non-covalently with receptors for intercellular adhesion molecule-3 (ICAM-3), such as DC-SIGN and LFA-1.
Antagonizes ribosome-mediated translation of mRNA into a polypeptide.
Interacting selectively and non-covalently with the high molecular weight B cell growth factor receptor.
Interacting selectively and non-covalently with the high molecular weight B cell growth factor receptor.
Interacting selectively and non-covalently with the high molecular weight B cell growth factor receptor.
Interacting selectively and non-covalently with the high molecular weight B cell growth factor receptor.
Combining with a high molecular weight B cell growth factor and transmitting the signal to initiate a change in cell activity.
Combining with a high molecular weight B cell growth factor and transmitting the signal to initiate a change in cell activity.
Combining with a high molecular weight B cell growth factor and transmitting the signal to initiate a change in cell activity.
Combining with a high molecular weight B cell growth factor and transmitting the signal to initiate a change in cell activity.
The function of a transcription cofactor that activates transcription in conjuction with a ligand-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
The function of a transcription cofactor that activates transcription in conjuction with a ligand-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
The function of a transcription cofactor that activates transcription in conjuction with a ligand-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
The function of a transcription cofactor that activates transcription in conjuction with a ligand-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
The function of a transcription cofactor that activates transcription in conjuction with a ligand-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
The function of a transcription cofactor that activates transcription in conjunction with a thyroid hormone-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
The function of a transcription cofactor that activates transcription in conjunction with a thyroid hormone-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
The function of a transcription cofactor that activates transcription in conjunction with a thyroid hormone-dependent nuclear receptor from a RNA polymerase II promoter; does not bind DNA itself.
Combining with the urokinase plasminogen activator to initiate a change in cell activity.
Combining with the urokinase plasminogen activator to initiate a change in cell activity.
Combining with the urokinase plasminogen activator to initiate a change in cell activity.
Catalysis of the synthesis of free D-serine from L-serine.
Combining with neurotensin, a neuropeptide active in the central and peripheral nervous system in mammals, and transmitting the signal from one side of the membrane to the other by a mechanism independent of coupling to G proteins.
Combining with neurotensin, a neuropeptide active in the central and peripheral nervous system in mammals, and transmitting the signal from one side of the membrane to the other by a mechanism independent of coupling to G proteins.
Combining with neurotensin, a neuropeptide active in the central and peripheral nervous system in mammals, and transmitting the signal from one side of the membrane to the other by a mechanism independent of coupling to G proteins.
Combining with neurotensin, a neuropeptide active in the central and peripheral nervous system in mammals, and transmitting the signal from one side of the membrane to the other by a mechanism independent of coupling to G proteins.
Combining with neurotensin, a neuropeptide active in the central and peripheral nervous system in mammals, and transmitting the signal from one side of the membrane to the other by a mechanism independent of coupling to G proteins.
Interacting selectively and non-covalently with the interleukin-17E receptor.
Interacting selectively and non-covalently with the interleukin-17E receptor.
The regionalization process that gives rise to the structural pattern of a chorion-containing eggshell such as those found in insects.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of sperm mitochondria; the process in which they take on their characteristic morphology; they are flattened, elongated, and arranged circumferentially into a tight helical coil around the tail-dense fibers of the mature sperm.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of sperm mitochondria; the process in which they take on their characteristic morphology; they are flattened, elongated, and arranged circumferentially into a tight helical coil around the tail-dense fibers of the mature sperm.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of sperm mitochondria; the process in which they take on their characteristic morphology; they are flattened, elongated, and arranged circumferentially into a tight helical coil around the tail-dense fibers of the mature sperm.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism. The various forms of symbiosis include parasitism, in which the association is disadvantageous or destructive to one of the organisms; mutualism, in which the association is advantageous, or often necessary to one or both and not harmful to either; and commensalism, in which one member of the association benefits while the other is not affected. However, mutualism, parasitism, and commensalism are often not discrete categories of interactions and should rather be perceived as a continuum of interaction ranging from parasitism to mutualism. In fact, the direction of a symbiotic interaction can change during the lifetime of the symbionts due to developmental changes as well as changes in the biotic/abiotic environment in which the interaction occurs. Microscopic symbionts are often referred to as endosymbionts.
Catalysis of the two-electron reduction of the disulfide of thioredoxins with electrons from ferredoxin involving a 4Fe-4S cluster and an adjacent active-site disulfide.
A protein complex that possesses ferredoxin:thioredoxin reductase activity.
Catalysis of the phosphorylation of fructosamine to form fructosamine-3-kinase.
The chemical reactions and pathways involving fructose 1,6-bisphosphate, also known as FBP. The D enantiomer is a metabolic intermediate in glycolysis and gluconeogenesis.
The chemical reactions and pathways involving fructosamine, a fructose molecule containing an amino group in place of a hydroxyl group.
The chemical reactions and pathways resulting in the formation of fructosamine, a fructose molecule containing an amino group in place of a hydroxyl group.
The chemical reactions and pathways resulting in the formation of fructosamine, a fructose molecule containing an amino group in place of a hydroxyl group.
The chemical reactions and pathways resulting in the formation of fructosamine, a fructose molecule containing an amino group in place of a hydroxyl group.
The chemical reactions and pathways resulting in the formation of fructosamine, a fructose molecule containing an amino group in place of a hydroxyl group.
The chemical reactions and pathways resulting in the breakdown of fructosamine, a fructose molecule containing an amino group in place of a hydroxyl group.
The chemical reactions and pathways resulting in the breakdown of fructosamine, a fructose molecule containing an amino group in place of a hydroxyl group.
The chemical reactions and pathways resulting in the breakdown of fructosamine, a fructose molecule containing an amino group in place of a hydroxyl group.
The chemical reactions and pathways involving fructoselysine, a fructose molecule containing a lysine group in place of a hydroxyl group.
The chemical reactions and pathways involving fructoseglycine, a fructose molecule containing a glycine group in place of a hydroxyl group.
Interacting selectively and non-covalently with lactose, a disaccharide of glucose and galactose, the carbohydrate of milk.
The controlled breakdown of any cell membrane in the context of a normal process such as autophagy.
The controlled breakdown of any cell membrane in the context of a normal process such as autophagy.
The controlled breakdown of any cell membrane in the context of a normal process such as autophagy.
The controlled breakdown of the membranes of cargo-carrying vesicles formed during peroxisome degradation.
The controlled breakdown of the membranes of cargo-carrying vesicles formed during peroxisome degradation.
The controlled breakdown of the membranes of cargo-carrying vesicles formed during peroxisome degradation.
The controlled breakdown of the membranes of autophagosomes.
The controlled breakdown of the membranes of autophagosomes.
The controlled breakdown of the membranes of autophagosomes.
The controlled breakdown of the membranes of autophagosomes.
Catalysis of the transfer of a formimino group from 5-formimidoyltetrahydrofolate to an acceptor molecule such as an amino acid.
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + glycine = (6S)-5,6,7,8-tetrahydrofolate + N-formimidoylglycine.
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + glycine = (6S)-5,6,7,8-tetrahydrofolate + N-formimidoylglycine.
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + glycine = (6S)-5,6,7,8-tetrahydrofolate + N-formimidoylglycine.
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + glycine = (6S)-5,6,7,8-tetrahydrofolate + N-formimidoylglycine.
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate.
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate.
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate.
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate.
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate.
Catalysis of the reaction: 3 S-adenosyl-L-methionine(1+) = 3 S-methyl-5'-thioadenosine + 3 H(+) + nicotianamine.
Catalysis of the reaction: scytalone = 1,3,8-trihydroxynaphthalene + H(2)O.
Catalysis of the reaction: scytalone = 1,3,8-trihydroxynaphthalene + H(2)O.
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + 2 H(+) = 5,10-methenyltetrahydrofolate + NH(4)(+).
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + 2 H(+) = 5,10-methenyltetrahydrofolate + NH(4)(+).
Catalysis of the reaction: 5-formimidoyltetrahydrofolate + 2 H(+) = 5,10-methenyltetrahydrofolate + NH(4)(+).
A small peptide excreted by a naturally transformable bacterium (e.g. Bacillus subtilis) that transmits a signal required for the establishment of competence.
The chemical reactions and pathways involving methylamine (CH3NH2).
The chemical reactions and pathways involving methylamine (CH3NH2).
The chemical reactions and pathways involving methylamine (CH3NH2).
The chemical reactions and pathways involving nicotianamine, 2(S),3'2(S),3''(S)-N-(N-(3-amino-3-carboxypropyl)-3-amino-3-carboxypropyl)-azetidine-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of nicotianamine, 2(S),3'2(S),3''(S)-N-(N-(3-amino-3-carboxypropyl)-3-amino-3-carboxypropyl)-azetidine-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of nicotianamine, 2(S),3'2(S),3''(S)-N-(N-(3-amino-3-carboxypropyl)-3-amino-3-carboxypropyl)-azetidine-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of nicotianamine, 2(S),3'2(S),3''(S)-N-(N-(3-amino-3-carboxypropyl)-3-amino-3-carboxypropyl)-azetidine-2-carboxylic acid.
The chemical reactions and pathways resulting in the formation of nicotianamine, 2(S),3'2(S),3''(S)-N-(N-(3-amino-3-carboxypropyl)-3-amino-3-carboxypropyl)-azetidine-2-carboxylic acid.
The chemical reactions and pathways resulting in the breakdown of nicotianamine, 2(S),3'2(S),3''(S)-N-(N-(3-amino-3-carboxypropyl)-3-amino-3-carboxypropyl)-azetidine-2-carboxylic acid.
The chemical reactions and pathways resulting in the breakdown of nicotianamine, 2(S),3'2(S),3''(S)-N-(N-(3-amino-3-carboxypropyl)-3-amino-3-carboxypropyl)-azetidine-2-carboxylic acid.
The chemical reactions and pathways resulting in the breakdown of nicotianamine, 2(S),3'2(S),3''(S)-N-(N-(3-amino-3-carboxypropyl)-3-amino-3-carboxypropyl)-azetidine-2-carboxylic acid.
The process in which a naturally transformable bacterium acquires the ability to take up exogenous DNA. This term should be applied only to naturally transformable bacteria, and should not be used in the context of artificially induced bacterial transformation.
The expulsion of feces from the rectum.
Cleavage of double-stranded RNA to form small interfering RNA molecules (siRNAs) of 21-23 nucleotides, in the context of RNA interference.
Cleavage of double-stranded RNA to form small interfering RNA molecules (siRNAs) of 21-23 nucleotides, in the context of RNA interference.
Cleavage of double-stranded RNA to form small interfering RNA molecules (siRNAs) of 21-23 nucleotides, in the context of RNA interference.
The process in which small interfering RNAs target cognate mRNA molecules for degradation.
The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter.
A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
The migrating motile tip of a growing neuron projection, where actin accumulates, and the actin cytoskeleton is the most dynamic.
Any part of a cell where non-isotropic growth takes place.
Any part of a cell where non-isotropic growth takes place.
A structure composed of peptidoglycan and often chitin in addition to other materials. It usually forms perpendicular to the long axis of a cell or hypha and grows centripetally from the cell wall to the center of the cell and often functions in the compartmentalization of a cell into two daughter cells.
A structure composed of peptidoglycan and often chitin in addition to other materials. It usually forms perpendicular to the long axis of a cell or hypha and grows centripetally from the cell wall to the center of the cell and often functions in the compartmentalization of a cell into two daughter cells.
Catalysis of the reaction: L-kynurenine + H2O = anthranilate + L-alanine.
Catalysis of the reaction: L-kynurenine + H2O = anthranilate + L-alanine.
The cytoplasm of a host cell.
Any process in which an organism enters and maintains a periodic, readily reversible state of reduced awareness and metabolic activity. Usually accompanied by physical relaxation, the onset of sleep in humans and other mammals is marked by a change in the electrical activity of the brain.
Any process in which an organism enters and maintains a periodic, readily reversible state of reduced awareness and metabolic activity. Usually accompanied by physical relaxation, the onset of sleep in humans and other mammals is marked by a change in the electrical activity of the brain.
Any process in which an organism enters and maintains a periodic, readily reversible state of reduced awareness and metabolic activity. Usually accompanied by physical relaxation, the onset of sleep in humans and other mammals is marked by a change in the electrical activity of the brain.
A wavelike sequence of involuntary muscular contraction and relaxation that passes along a tubelike structure, such as the intestine, impelling the contents onwards.
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
The process in which a relatively unspecialized cell acquires the specialized features of a cellular spore, a cell form that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction.
The process in which a relatively unspecialized cell acquires the specialized features of a cellular spore, a cell form that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction.
The process in which a relatively unspecialized cell acquires the specialized features of a cellular spore, a cell form that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction.
The process in which a relatively unspecialized cell acquires the specialized features of a cellular spore, a cell form that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction.
The formation of spores derived from the products of an asexual cell division. Examples of this process are found in bacteria and fungi.
The formation of spores derived from the products of an asexual cell division. Examples of this process are found in bacteria and fungi.
The formation of spores derived from the products of an asexual cell division. Examples of this process are found in bacteria and fungi.
The formation of spores derived from the products of an asexual cell division. Examples of this process are found in bacteria and fungi.
The process in which cells that are products of meiosis acquire the specialized features of ascospores. Ascospores are generally found in clusters of four or eight spores within a single mother cell, the ascus, and are characteristic of the ascomycete fungi (phylum Ascomycota).
The process in which cells that are products of meiosis acquire the specialized features of ascospores. Ascospores are generally found in clusters of four or eight spores within a single mother cell, the ascus, and are characteristic of the ascomycete fungi (phylum Ascomycota).
The process in which cells that are products of meiosis acquire the specialized features of ascospores. Ascospores are generally found in clusters of four or eight spores within a single mother cell, the ascus, and are characteristic of the ascomycete fungi (phylum Ascomycota).
The process in which cells that are products of meiosis acquire the specialized features of ascospores. Ascospores are generally found in clusters of four or eight spores within a single mother cell, the ascus, and are characteristic of the ascomycete fungi (phylum Ascomycota).
The wall surrounding a cell of a dimorphic fungus growing in the single-cell budding yeast form, in contrast to the filamentous or hyphal form.
The cell wall surrounding a fungal hypha.
The process in which a multicellular organism, a unicellular organism or a group of unicellular organisms grow in a threadlike, filamentous shape.
Growth of fungi as threadlike, tubular structures that may contain multiple nuclei and may or may not be divided internally by septa, or cross-walls.
Any process that modulates the frequency, rate or extent of complement activation.
Any process that modulates the frequency, rate or extent of the classical pathway of complement activation.
Any process that modulates the frequency, rate or extent of the alternative pathway of complement activation.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spindle pole body (SPB). The SPB is the microtubule organizing center in fungi, and is functionally homologous to the animal cell centrosome.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spindle pole body (SPB). The SPB is the microtubule organizing center in fungi, and is functionally homologous to the animal cell centrosome.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spindle pole body (SPB). The SPB is the microtubule organizing center in fungi, and is functionally homologous to the animal cell centrosome.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spindle pole body (SPB). The SPB is the microtubule organizing center in fungi, and is functionally homologous to the animal cell centrosome.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spindle pole body (SPB). The SPB is the microtubule organizing center in fungi, and is functionally homologous to the animal cell centrosome.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spindle pole body (SPB). The SPB is the microtubule organizing center in fungi, and is functionally homologous to the animal cell centrosome.
The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins.
The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins.
The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins.
The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins.
The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins.
The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins.
The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins.
The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins.
The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins.
The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins.
The directed movement of the nucleus along microtubules within the cell, mediated by motor proteins.
Construction of a new spindle pole body.
Construction of a new spindle pole body.
Construction of a new spindle pole body.
Construction of a new spindle pole body.
Construction of a new spindle pole body.
Construction of a new spindle pole body.
Construction of a new spindle pole body.
Construction of a new spindle pole body.
Construction of a new spindle pole body.
The aggregation, arrangement and bonding together of a set of components to form an ascospore wall. During sporulation in Ascomycota, each ascospore nucleus becomes surrounded by a specialized spore wall, formed by deposition of spore wall components in the lumenal space between the outer and inner leaflets of the prospore membrane. An example of this process is found in Saccharomyces cerevisiae.
The aggregation, arrangement and bonding together of a set of components to form an ascospore wall. During sporulation in Ascomycota, each ascospore nucleus becomes surrounded by a specialized spore wall, formed by deposition of spore wall components in the lumenal space between the outer and inner leaflets of the prospore membrane. An example of this process is found in Saccharomyces cerevisiae.
Polarized accumulation of cytoskeletal proteins (including F-actin) and regulatory proteins in a cell. An example of this is the actin cap found in Saccharomyces cerevisiae.
An endocytic patch  that consists of an actin-containing structure found at the plasma membrane in cells; formed of networks of branched actin filaments that lie just beneath the plasma membrane and assemble, move, and disassemble rapidly. An example of this is the actin cortical patch found in Saccharomyces cerevisiae.
An endocytic patch  that consists of an actin-containing structure found at the plasma membrane in cells; formed of networks of branched actin filaments that lie just beneath the plasma membrane and assemble, move, and disassemble rapidly. An example of this is the actin cortical patch found in Saccharomyces cerevisiae.
The contractile fiber of smooth muscle cells.
The contractile fiber of smooth muscle cells.
Electron-dense region associated with a smooth muscle contractile fiber.
Catalysis of the reaction: 1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate.
The posttranscriptional addition of methyl groups to specific residues in a tRNA molecule.
Any process involved in the maturation of a precursor Small SubUnit (SSU) ribosomal RNA (rRNA) molecule into a mature SSU-rRNA molecule.
Any process involved in the maturation of a precursor Small SubUnit (SSU) ribosomal RNA (rRNA) molecule into a mature SSU-rRNA molecule.
The formation of a stable duplex DNA that contains one strand from each of the two recombining DNA molecules.
Interacting selectively and non-covalently with hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin.
Interacting selectively and non-covalently with hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin.
The chemical reactions and pathways involving a bacteriochlorophyll, 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, 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, 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, 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, any of the chlorophylls of photosynthetic bacteria. They differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the breakdown of bacteriochlorophyll, any of the chlorophylls of photosynthetic bacteria. They differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the breakdown of bacteriochlorophyll, any of the chlorophylls of photosynthetic bacteria. They differ structurally from the chlorophylls of higher plants.
The chemical reactions and pathways resulting in the breakdown of bacteriochlorophyll, any of the chlorophylls of photosynthetic bacteria. They differ structurally from the chlorophylls of higher plants.
A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis.
The elongation of a fatty acid chain by the sequential addition of two-carbon units.
Any process that modulates the frequency, rate or extent of bone mineralization.
Any process that activates or increases the frequency, rate or extent of bone mineralization.
Any process that activates or increases the frequency, rate or extent of bone mineralization.
Any process that activates or increases the frequency, rate or extent of bone mineralization.
Any process that activates or increases the frequency, rate or extent of bone mineralization.
Any process that activates or increases the frequency, rate or extent of bone mineralization.
Any process that stops, prevents, or reduces the frequency, rate or extent of bone mineralization.
Any process that stops, prevents, or reduces the frequency, rate or extent of bone mineralization.
Any process that stops, prevents, or reduces the frequency, rate or extent of bone mineralization.
Any process that stops, prevents, or reduces the frequency, rate or extent of bone mineralization.
Enables the transfer of inorganic diphosphate across a membrane.
The directed movement of inorganic diphosphate 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 ankyrin, a 200 kDa cytoskeletal protein that attaches other cytoskeletal proteins to integral membrane proteins.
Interacting selectively and non-covalently with spectrin, a protein that is the major constituent of the erythrocyte cytoskeletal network. It associates with band 4.1 (see band protein) and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. It is composed of nonhomologous chains, alpha and beta, which aggregate side-to-side in an antiparallel fashion to form dimers, tetramers, and higher polymers.
A series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family 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 member of the BMP (bone morphogenetic protein) family 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 member of the BMP (bone morphogenetic protein) family 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 member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
Any process that modulates the frequency, rate or extent of the activity of any BMP receptor signaling pathway.
Any process that modulates the frequency, rate or extent of the activity of any BMP receptor signaling pathway.
Any process that modulates the frequency, rate or extent of the activity of any BMP receptor signaling pathway.
Any process that modulates the frequency, rate or extent of the activity of any BMP receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of the BMP signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the BMP signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the BMP signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the BMP signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the BMP signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the BMP signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the BMP signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the BMP signaling pathway.
Interacting selectively and non-covalently with small nucleolar RNA.
Any process that modulates the rate, direction or extent of axon extension.
Any process that stops, prevents, or reduces the frequency, rate or extent of axon outgrowth.
Any process that stops, prevents, or reduces the frequency, rate or extent of axon outgrowth.
Any process that stops, prevents, or reduces the frequency, rate or extent of axon outgrowth.
Any process that stops, prevents, or reduces the frequency, rate or extent of axon outgrowth.
A series of molecular signals generated as a consequence of a intracellular steroid hormone receptor binding to one of its physiological ligands.
A series of molecular signals generated as a consequence of a intracellular steroid hormone receptor binding to one of its physiological ligands.
Interacting selectively and non-covalently with any part of a small nucleolar ribonucleoprotein particle.
Any series of molecular signals generated as a consequence of an intracellular estrogen receptor binding to one of its physiological ligands. The pathway begins with receptor-ligand binding, and ends with regulation of a downstream cellular process (e.g. transcription).
Any series of molecular signals generated as a consequence of an intracellular estrogen receptor binding to one of its physiological ligands. The pathway begins with receptor-ligand binding, and ends with regulation of a downstream cellular process (e.g. transcription).
Any series of molecular signals generated as a consequence of an androgen binding to its receptor.
Any series of molecular signals initiated by a ligand binding to an receptor located within a cell.
Any series of molecular signals initiated by a ligand binding to an receptor located within a cell.
Any series of molecular signals initiated by a ligand binding to an receptor located within a cell.
Catalysis of the reaction: acyl-CoA + dihydrolipoamide = CoA + S-acyldihydrolipoamide.
The heterodimeric receptor for granulocyte macrophage colony-stimulating factor.
The heterodimeric receptor for granulocyte macrophage colony-stimulating factor.
The action of a molecule that contributes to the structural integrity of chromatin.
The process, occurring in the embryo, by which the anatomical structures of the genitalia are generated and organized.
The process whose specific outcome is the progression of the male genitalia over time, from its formation to the mature structure.
The process whose specific outcome is the progression of the female genitalia over time, from formation to the mature structure.
Any process in which plasmids are segregated or distributed into daughter cells upon cell division.
The process in which copies of the 2-micrometer plasmid, found in fungi such as Saccharomyces, are distributed to daughter cells upon cell division.
Interacting selectively and non-covalently with Hsp70 proteins, any of a group of heat shock proteins around 70kDa in size.
The function of interacting (directly or indirectly) with receptors such that the proportion of receptors in the active form is changed.
The function of interacting (directly or indirectly) with receptors such that the proportion of receptors in the active form is increased.
The function of interacting (directly or indirectly) with receptors such that the proportion of receptors in the active form is decreased.
Interacting (directly or indirectly) with acetylcholine receptors such that the proportion of receptors in the active form is changed.
Interacting (directly or indirectly) with acetylcholine receptors such that the proportion of receptors in the active form is increased.
Interacting (directly or indirectly) with acetylcholine receptors such that the proportion of receptors in the active form is decreased.
Interacting selectively and non-covalently with a cyclic nucleotide, a nucleotide in which the phosphate group is in diester linkage to two positions on the sugar residue.
Interacting selectively and non-covalently with cAMP, the nucleotide cyclic AMP (adenosine 3',5'-cyclophosphate).
Interacting selectively and non-covalently with cAMP, the nucleotide cyclic AMP (adenosine 3',5'-cyclophosphate).
Interacting selectively and non-covalently with cAMP, the nucleotide cyclic AMP (adenosine 3',5'-cyclophosphate).
Interacting selectively and non-covalently with cAMP, the nucleotide cyclic AMP (adenosine 3',5'-cyclophosphate).
Interacting selectively and non-covalently with cGMP, the nucleotide cyclic GMP (guanosine 3',5'-cyclophosphate).
Interacting selectively and non-covalently with cGMP, the nucleotide cyclic GMP (guanosine 3',5'-cyclophosphate).
Interacting selectively and non-covalently with cGMP, the nucleotide cyclic GMP (guanosine 3',5'-cyclophosphate).
Interacting selectively and non-covalently with adenyl nucleotides, any compound consisting of adenosine esterified with (ortho)phosphate.
Specifies the site of a posttranscriptional modification in an rRNA molecule by base pairing with a short sequence around the target residue.
Specifies the site of a posttranscriptional modification in a tRNA molecule by base pairing with a short sequence around the target residue.
Specifies the site of pseudouridylation in an RNA molecule by base pairing with a short sequence around the target residue.
Specifies the site of pseudouridylation in an rRNA molecule by base pairing with a short sequence around the target residue.
Specifies the site of pseudouridylation in a tRNA molecule by base pairing with a short sequence around the target residue.
Specifies the site of 2'-O-ribose methylation in an RNA molecule by base pairing with a short sequence around the target residue.
Specifies the site of 2'-O-ribose methylation in an rRNA molecule by base pairing with a short sequence around the target residue.
Activity that provides specificity to a methylase by using base complementarity to guide site-specific 2'-O-ribose methylations to a small nuclear RNA molecule.
Specifies the site of 2'-O-ribose methylation in a tRNA molecule by base pairing with a short sequence around the target residue.
Activity that provides specificity to a pseudouridine synthetase by using base complementarity to guide site-specific pseudouridylations to a small nuclear RNA molecule.
Specifies the site of a posttranscriptional modification in an snRNA molecule by base pairing with a short sequence around the target residue.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Catalysis of the reaction involving the transfer of a phosphatidate (otherwise known as diacylglycerol 3-phosphosphate) group.
The chemical reactions and pathways resulting in the breakdown of bile acids, any of a group of steroid carboxylic acids occurring in bile.
The chemical reactions and pathways resulting in the breakdown of bile acids, any of a group of steroid carboxylic acids occurring in bile.
The chemical reactions and pathways resulting in the breakdown of bile acids, any of a group of steroid carboxylic acids occurring in bile.
The chemical reactions and pathways resulting in the breakdown of bile acids, any of a group of steroid carboxylic acids occurring in bile.
The chemical reactions and pathways resulting in the breakdown of bile acids, any of a group of steroid carboxylic acids occurring in bile.
The chemical reactions and pathways resulting in the breakdown of bile acids, any of a group of steroid carboxylic acids occurring in bile.
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of any of the extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of any of the extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of Cajal bodies, nuclear bodies that appear ultrastructurally as a tangle of coiled, electron-dense threads roughly 0.5 micrometers in diameter and are enriched in ribonucleoproteins, and certain general RNA polymerase II transcription factors.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of Cajal bodies, nuclear bodies that appear ultrastructurally as a tangle of coiled, electron-dense threads roughly 0.5 micrometers in diameter and are enriched in ribonucleoproteins, and certain general RNA polymerase II transcription factors.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of Lands, a class of nuclear body that react against SP140 auto-antibodies.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of Lands, a class of nuclear body that react against SP140 auto-antibodies.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of Lands, a class of nuclear body that react against SP140 auto-antibodies.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of PML bodies, a class of nuclear body; they react against SP100 auto-antibodies (PML = promyelocytic leukemia).
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of PML bodies, a class of nuclear body; they react against SP100 auto-antibodies (PML = promyelocytic leukemia).
The chemical reactions and pathways resulting in the breakdown of SMAD signaling proteins by ubiquitination and targeting to the proteasome.
The chemical reactions and pathways resulting in the breakdown of SMAD signaling proteins by ubiquitination and targeting to the proteasome.
The chemical reactions and pathways resulting in the breakdown of SMAD signaling proteins by ubiquitination and targeting to the proteasome.
Catalysis of the transfer of a methyl group from S-adenosylmethionine during the synthesis of quinone cofactors such as ubiquinone (coenzyme Q), menaquinone (vitamin K2), plastoquinone and phylloquinone (vitamin K1).
The directed movement of a symbiont's proteins within 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 a symbiont's proteins within a cell of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The process whose specific outcome is the progression of a reproductive fruiting body over time, from its formation to the mature structure. A reproductive fruiting body is a multicellular reproductive structure that contains spores.
The process whose specific outcome is the progression of the myxococcal fruiting body over time, from its formation to the mature structure. The process begins when myxococci respond to a lack of nutrients in the environment and ends when the myxococcal fruiting body is a mature structure.
The process whose specific outcome is the progression of the myxococcal fruiting body over time, from its formation to the mature structure. The process begins when myxococci respond to a lack of nutrients in the environment and ends when the myxococcal fruiting body is a mature structure.
The process whose specific outcome is the progression of the myxococcal fruiting body over time, from its formation to the mature structure. The process begins when myxococci respond to a lack of nutrients in the environment and ends when the myxococcal fruiting body is a mature structure.
The process whose specific outcome is the progression of a sporocarp over time, from its formation to the mature structure. The sporocarp is a spore bearing fruiting body organ. An example of this process is found in the Fungal species Coprinopsis cinerea.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: diphosphate + oxaloacetate = CO(2) + phosphate + phosphoenolpyruvate.
Catalysis of the reaction: [methionine synthase]-cob(II)alamin + NADPH + H+ + S-adenosyl methionine = [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+.
Catalysis of the reaction: [methionine synthase]-cob(II)alamin + NADPH + H+ + S-adenosyl methionine = [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+.
Catalysis of the reaction: [methionine synthase]-cob(II)alamin + NADPH + H+ + S-adenosyl methionine = [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+.
Catalysis of the reaction: [methionine synthase]-cob(II)alamin + NADPH + H+ + S-adenosyl methionine = [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+.
Catalysis of the reaction: [methionine synthase]-cob(II)alamin + NADPH + H+ + S-adenosyl methionine = [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+.
Catalysis of the reaction: [methionine synthase]-cob(II)alamin + NADPH + H+ + S-adenosyl methionine = [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + NADP+.
The process whose specific outcome is the progression of the sorocarp over time, from its formation to the mature structure. The process begins with the aggregation of individual cells and ends with the mature sorocarp. The sorocarp is a structure containing a spore-bearing sorus that sits on top of a stalk. An example of this process is found in Dictyostelium discoideum.
The process whose specific outcome is the progression of the sorocarp over time, from its formation to the mature structure. The process begins with the aggregation of individual cells and ends with the mature sorocarp. The sorocarp is a structure containing a spore-bearing sorus that sits on top of a stalk. An example of this process is found in Dictyostelium discoideum.
The process whose specific outcome is the progression of the sorocarp over time, from its formation to the mature structure. The process begins with the aggregation of individual cells and ends with the mature sorocarp. The sorocarp is a structure containing a spore-bearing sorus that sits on top of a stalk. An example of this process is found in Dictyostelium discoideum.
The process whose specific outcome is the progression of the sorocarp over time, from its formation to the mature structure. The process begins with the aggregation of individual cells and ends with the mature sorocarp. The sorocarp is a structure containing a spore-bearing sorus that sits on top of a stalk. An example of this process is found in Dictyostelium discoideum.
Partial constriction of the cytoplasm of an embryo to form a furrow that resembles a cleavage furrow but does not complete cytokinesis.
Formation of furrows in the cytoplasm between nuclei during cell cycles in embryos that contribute to the formation of the syncytial blastoderm. An example of this process is found in Drosophila melanogaster.
A process that occurs during the first cell cycle in an embryo, in which anterior cortical contractions culminate in a single partial constriction of the embryo called the pseudocleavage furrow. An example of this process is found in nematode worms.
Catalysis of the transfer of the ADP-ribose group of NAD+ to the amino group at N2 of 2'-deoxyguanosine to yield N2-(alpha-ADP-ribos-1-yl)-2'-deoxyguanosine and its beta form.
The covalent attachment of an ADP-ribosyl group to the amino group at N2 of a 2'-deoxyguanosine residue in double-stranded DNA.
The directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding.
The movement of a leukocyte in response to an external stimulus.
The movement of a leukocyte in response to an external stimulus.
Catalysis of the hydrolysis of terminal non-reducing alpha-L-rhamnose residues in alpha-L-rhamnosides.
Catalysis of the hydrolysis of terminal non-reducing alpha-L-rhamnose residues in alpha-L-rhamnosides.
Catalysis of the hydrolysis of terminal non-reducing alpha-L-rhamnose residues in alpha-L-rhamnosides.
Catalysis of the hydrolysis of N-glycosidic bonds in an RNA molecule.
Catalysis of the hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes or corresponding sites in 28S RNA from other species.
Catalysis of the hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes or corresponding sites in 28S RNA from other species.
Catalysis of the hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes or corresponding sites in 28S RNA from other species.
Catalysis of the hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes or corresponding sites in 28S RNA from other species.
Catalysis of the hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes or corresponding sites in 28S RNA from other species.
Catalysis of the hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes or corresponding sites in 28S RNA from other species.
Catalysis of the hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes or corresponding sites in 28S RNA from other species.
Catalysis of the hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes or corresponding sites in 28S RNA from other species.
Catalysis of the hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes or corresponding sites in 28S RNA from other species.
Catalysis of the hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes or corresponding sites in 28S RNA from other species.
Catalysis of the reaction: pectin + n H2O = n methanol + pectate.
Catalysis of the reaction: pectin + n H2O = n methanol + pectate.
Catalysis of the reaction: pectin + n H2O = n methanol + pectate.
Catalysis of the reaction: pectin + n H2O = n methanol + pectate.
Catalysis of the reaction: pectin + n H2O = n methanol + pectate.
Catalysis of the reaction: pectin + n H2O = n methanol + pectate.
Catalysis of the reaction: pectin + n H2O = n methanol + pectate.
Catalysis of the reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
Catalysis of the reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
Catalysis of the reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
Catalysis of the reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
Catalysis of the reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
Catalysis of the reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
Catalysis of the reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
Catalysis of the reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
Catalysis of the reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
Catalysis of the reaction: feruloyl-polysaccharide + H2O = ferulate + polysaccharide.
Catalysis of the reaction: H(2)O + oxaloacetate = acetate + H(+) + oxalate.
Catalysis of the reaction: H(2)O + oxaloacetate = acetate + H(+) + oxalate.
Catalysis of the reaction: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH.
Catalysis of the reaction: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH.
Catalysis of the reaction: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH.
Catalysis of the reaction: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH.
Catalysis of the reaction: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH.
Catalysis of the reaction: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH.
Catalysis of the interconversion of arsenate and arsenite.
Catalysis of the reaction: arsenate + thioredoxin = arsenite + thioredoxin disulfide. Thioredoxin disulfide is also known as oxidized thioredoxin.
Catalysis of an oxidation-reduction (redox) reaction in which a phosphorus- or arsenic-containing group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
Catalysis of an oxidation-reduction (redox) reaction in which a phosphorus- or arsenic-containing group acts as a hydrogen or electron donor and reduces a disulfide.
Interacting selectively and non-covalently with the U1 small nuclear RNA (U1 snRNA).
Interacting selectively and non-covalently with the U2 small nuclear RNA (U2 snRNA).
Interacting selectively and non-covalently with the U4 small nuclear RNA (U4 snRNA).
Interacting selectively and non-covalently with the U4atac small nuclear RNA (U4atac snRNA).
Interacting selectively and non-covalently with the U5 small nuclear RNA (U5 snRNA).
Interacting selectively and non-covalently with the U6atac small nuclear RNA (U6atac snRNA).
Interacting selectively and non-covalently with the U11 small nuclear RNA (U11 snRNA).
Interacting selectively and non-covalently with the U12 small nuclear RNA (U12 snRNA).
Interacting selectively and non-covalently with the pre-mRNA 5' splice site sequence.
Interacting selectively and non-covalently with the pre-mRNA 3' splice site sequence.
Interacting selectively and non-covalently with the 3' end of the U6 small nuclear RNA (U6 snRNA).
The incorporation of pyrrolysine, also known as lysine methylamine methyltransferase cofactor adduct, into a peptide; uses a special tRNA that recognizes the UAG codon as a modified lysine, rather than as a termination codon. Pyrrolysine may be synthesized as a free amino acid or synthesized from a lysine charged tRNA before its incorporation; it is not a posttranslational modification of peptidyl-lysine; this modification is found in several Methanosarcina methylamine methyltransferases.
The incorporation of pyrrolysine, also known as lysine methylamine methyltransferase cofactor adduct, into a peptide; uses a special tRNA that recognizes the UAG codon as a modified lysine, rather than as a termination codon. Pyrrolysine may be synthesized as a free amino acid or synthesized from a lysine charged tRNA before its incorporation; it is not a posttranslational modification of peptidyl-lysine; this modification is found in several Methanosarcina methylamine methyltransferases.
The chemical reactions and pathways resulting in the formation of D-alanine, the D-enantiomer of the amino acid alanine, i.e (2R)-2-aminopropanoic acid.
The chemical reactions and pathways resulting in the formation of D-alanine, the D-enantiomer of the amino acid alanine, i.e (2R)-2-aminopropanoic acid.
The chemical reactions and pathways resulting in the formation of D-alanine, the D-enantiomer of the amino acid alanine, i.e (2R)-2-aminopropanoic acid.
The chemical reactions and pathways resulting in the formation of D-alanine, the D-enantiomer of the amino acid alanine, i.e (2R)-2-aminopropanoic acid.
The chemical reactions and pathways resulting in the breakdown of D-alanine and related amino acids.
The chemical reactions and pathways resulting in the breakdown of D-alanine and related amino acids.
The chemical reactions and pathways resulting in the breakdown of D-alanine and related amino acids.
A pathway of carbon dioxide fixation in which one molecule of acetyl-CoA is completely synthesized from two molecules of carbon dioxide (CO2).
The chemical reactions and pathways involving polyketides, any of a diverse group of natural products synthesized via linear poly-beta-ketones, which are themselves formed by repetitive head-to-tail addition of acetyl (or substituted acetyl) units indirectly derived from acetate (or a substituted acetate) by a mechanism similar to that for fatty acid biosynthesis but without the intermediate reductive steps.
The chemical reactions and pathways resulting in the breakdown of polyketides, any of a diverse group of natural products synthesized via linear poly-beta-ketones, which are themselves formed by repetitive head-to-tail addition of acetyl (or substituted acetyl) units indirectly derived from acetate (or a substituted acetate) by a mechanism similar to that for fatty acid biosynthesis but without the intermediate reductive steps.
The chemical reactions and pathways resulting in the breakdown of polyketides, any of a diverse group of natural products synthesized via linear poly-beta-ketones, which are themselves formed by repetitive head-to-tail addition of acetyl (or substituted acetyl) units indirectly derived from acetate (or a substituted acetate) by a mechanism similar to that for fatty acid biosynthesis but without the intermediate reductive steps.
The chemical reactions and pathways resulting in the breakdown of polyketides, any of a diverse group of natural products synthesized via linear poly-beta-ketones, which are themselves formed by repetitive head-to-tail addition of acetyl (or substituted acetyl) units indirectly derived from acetate (or a substituted acetate) by a mechanism similar to that for fatty acid biosynthesis but without the intermediate reductive steps.
Any process involved in the maintenance of an internal equilibrium of hydrogen ions (protons) within a cell or between a cell and its external environment.
Any process involved in the maintenance of an internal equilibrium of hydrogen ions (protons) within a cell or between a cell and its external environment.
Any process involved in the maintenance of an internal steady state of sulfate ions at the level of a cell.
Any process involved in the maintenance of an internal steady state of phosphate ions at the level of a cell.
Any process involved in the maintenance of an internal steady state of chloride ions at the level of a cell.
The anaerobic chemical reactions and pathways resulting in the breakdown of glucose, with the production of acetic acid, butyric acid, carbon dioxide (CO2), and dihydrogen; effected by some saccharolytic species of Clostridium, e.g. C. butyricum.
The anaerobic chemical reactions and pathways resulting in the breakdown of glucose, with the production of acetic acid, butyric acid, carbon dioxide (CO2), and dihydrogen; effected by some saccharolytic species of Clostridium, e.g. C. butyricum.
The chemical reactions and pathways involving an aminoglycoside antibiotic, any member of a group of broad spectrum antibiotics, of similar toxicity and pharmacology, that contain an aminodeoxysugar, an amino- or guanidino-substituted inositol ring, and one or more residues of other sugars. The group includes streptomycin, neomycin, framycetin, kanamycin, paromomycin, and gentamicin.
The chemical reactions and pathways resulting in the formation of an aminoglycoside antibiotic, any member of a group of broad spectrum antibiotics, of similar toxicity and pharmacology, that contain an aminodeoxysugar, an amino- or guanidino-substituted inositol ring, and one or more residues of other sugars. The group includes streptomycin, neomycin, framycetin, kanamycin, paromomycin, and gentamicin.
The chemical reactions and pathways resulting in the formation of an aminoglycoside antibiotic, any member of a group of broad spectrum antibiotics, of similar toxicity and pharmacology, that contain an aminodeoxysugar, an amino- or guanidino-substituted inositol ring, and one or more residues of other sugars. The group includes streptomycin, neomycin, framycetin, kanamycin, paromomycin, and gentamicin.
The chemical reactions and pathways resulting in the formation of an aminoglycoside antibiotic, any member of a group of broad spectrum antibiotics, of similar toxicity and pharmacology, that contain an aminodeoxysugar, an amino- or guanidino-substituted inositol ring, and one or more residues of other sugars. The group includes streptomycin, neomycin, framycetin, kanamycin, paromomycin, and gentamicin.
The chemical reactions and pathways resulting in the formation of an aminoglycoside antibiotic, any member of a group of broad spectrum antibiotics, of similar toxicity and pharmacology, that contain an aminodeoxysugar, an amino- or guanidino-substituted inositol ring, and one or more residues of other sugars. The group includes streptomycin, neomycin, framycetin, kanamycin, paromomycin, and gentamicin.
The chemical reactions and pathways resulting in the breakdown of an aminoglycoside antibiotic, any member of a group of broad spectrum antibiotics, of similar toxicity and pharmacology, that contain an aminodeoxysugar, an amino- or guanidino-substituted inositol ring, and one or more residues of other sugars. The group includes streptomycin, neomycin, framycetin, kanamycin, paromomycin, and gentamicin.
The chemical reactions and pathways resulting in the breakdown of an aminoglycoside antibiotic, any member of a group of broad spectrum antibiotics, of similar toxicity and pharmacology, that contain an aminodeoxysugar, an amino- or guanidino-substituted inositol ring, and one or more residues of other sugars. The group includes streptomycin, neomycin, framycetin, kanamycin, paromomycin, and gentamicin.
The chemical reactions and pathways resulting in the breakdown of an aminoglycoside antibiotic, any member of a group of broad spectrum antibiotics, of similar toxicity and pharmacology, that contain an aminodeoxysugar, an amino- or guanidino-substituted inositol ring, and one or more residues of other sugars. The group includes streptomycin, neomycin, framycetin, kanamycin, paromomycin, and gentamicin.
The chemical reactions and pathways involving peptides with antibiotic activity.
The chemical reactions and pathways resulting in the formation of peptides with antibiotic activity.
The chemical reactions and pathways resulting in the formation of peptides with antibiotic activity.
The chemical reactions and pathways resulting in the formation of peptides with antibiotic activity.
The chemical reactions and pathways resulting in the formation of peptides with antibiotic activity.
The chemical reactions and pathways resulting in the breakdown of peptides with antibiotic activity.
The chemical reactions and pathways resulting in the breakdown of peptides with antibiotic activity.
The chemical reactions and pathways resulting in the breakdown of peptides with antibiotic activity.
The chemical reactions and pathways involving a beta-lactam antibiotic, any member of a class of natural or semisynthetic antibiotics whose characteristic feature is a strained, four-membered beta-lactam ring. They include the penicillins and many of the cephalosporins.
The chemical reactions and pathways resulting in the formation of a beta-lactam antibiotic, any member of a class of natural or semisynthetic antibiotics whose characteristic feature is a strained, four-membered beta-lactam ring. They include the penicillins and many of the cephalosporins.
The chemical reactions and pathways resulting in the formation of a beta-lactam antibiotic, any member of a class of natural or semisynthetic antibiotics whose characteristic feature is a strained, four-membered beta-lactam ring. They include the penicillins and many of the cephalosporins.
The chemical reactions and pathways resulting in the formation of a beta-lactam antibiotic, any member of a class of natural or semisynthetic antibiotics whose characteristic feature is a strained, four-membered beta-lactam ring. They include the penicillins and many of the cephalosporins.
The chemical reactions and pathways resulting in the formation of a beta-lactam antibiotic, any member of a class of natural or semisynthetic antibiotics whose characteristic feature is a strained, four-membered beta-lactam ring. They include the penicillins and many of the cephalosporins.
The chemical reactions and pathways resulting in the breakdown of a beta-lactam antibiotic, any member of a class of natural or semisynthetic antibiotics whose characteristic feature is a strained, four-membered beta-lactam ring. They include the penicillins and many of the cephalosporins.
The chemical reactions and pathways resulting in the breakdown of a beta-lactam antibiotic, any member of a class of natural or semisynthetic antibiotics whose characteristic feature is a strained, four-membered beta-lactam ring. They include the penicillins and many of the cephalosporins.
The chemical reactions and pathways resulting in the breakdown of a beta-lactam antibiotic, any member of a class of natural or semisynthetic antibiotics whose characteristic feature is a strained, four-membered beta-lactam ring. They include the penicillins and many of the cephalosporins.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving a vitamin, 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.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving a coenzyme.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving a coenzyme.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving a coenzyme.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving a prosthetic group.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving a prosthetic group.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving a prosthetic group.
The lipid bilayer surrounding a cytoplasmic vesicle.
The lipid bilayer surrounding a vesicle associated with the Golgi apparatus.
The lipid bilayer surrounding a chitosome.
The lipid bilayer surrounding a coated vesicle.
The lipid bilayer surrounding a COPI-coated vesicle.
The lipid bilayer surrounding a clathrin-coated vesicle.
The lipid bilayer surrounding an endocytic vesicle.
The lipid bilayer surrounding a dense granule of the type found in apicomplexan parasites.
The lipid bilayer surrounding a clathrin-coated endocytic vesicle.
The lipid bilayer surrounding a phagocytic vesicle.
The lipid bilayer surrounding a clathrin-coated phagocytic vesicle.
The lipid bilayer surrounding a synaptic vesicle.
The portion of the plasma membrane surrounding an axon; it is a specialized trilaminar random mosaic of protein molecules floating within a fluid matrix of highly mobile phospholipid molecules, 7-8 nm in thickness.
Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Rac family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase.
A ribonucleoprotein complex that catalyzes cleavage of the leader sequence of precursor tRNAs (pre-tRNAs), generating the mature 5' end of tRNAs.
A ribonuclease P complex located in the mitochondrion of a eukaryotic cell, where it catalyzes the 5' endonucleolytic cleavage of precursor tRNAs to yield mature tRNAs. The subunit composition of mitochondrial ribonuclease P complexes varies between species, but the complex often contains a single RNA molecule and a single protein molecule.
A ribonuclease P complex located in the cyanelle, where it catalyzes the 5' endonucleolytic cleavage of precursor tRNAs to yield mature tRNAs. The best characterized cyanelle ribonuclease P complex, from the alga Cyanophora paradoxa, contains a single RNA molecule that is necessary but not sufficient for catalysis, and several protein molecules.
A ribonuclease P complex that contains a single RNA molecule that is necessary and usually sufficient for catalysis, and a single protein molecule. Examples of this complex are found in Bacterial species.
A ribonuclease P complex that generally contains a single RNA molecule and several protein molecules. Examples of this complex are found in Archaeal species.
Any process, either active or passive, by which an organism avoids or tolerates the effects of its host organism's defense response. The host defense response is mounted by the host in response to the presence of the organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process, either active or passive, by which a virus avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any complex of pre-rRNAs, ribosomal proteins, and associated proteins formed during ribosome biogenesis.
Any complex of pre-rRNAs, ribosomal proteins, and associated proteins formed in the nucleolus during ribosome biogenesis.
A large ribonucleoprotein complex considered to be the earliest preribosomal complex. In S. cerevisiae, it has a size of 90S and consists of the 35S pre-rRNA, early-associating ribosomal proteins most of which are part of the small ribosomal subunit, the U3 snoRNA and associated proteins.
A preribosomal complex consisting of 27SA, 27SB, and/or 7S pre-rRNA, 5S rRNA, ribosomal proteins including late-associating large subunit proteins, and associated proteins; a precursor of the eukaryotic cytoplasmic large ribosomal subunit.
A preribosomal complex consisting of 20S pre-rRNA, ribosomal proteins including late-associating small subunit proteins, and associated proteins; a precursor of the eukaryotic cytoplasmic small ribosomal subunit.
Any of several heterodimers containing one or two Noc proteins, associated with preribosomal complexes; involved in ribosome biogenesis.
A heterodimer associated with 90S and 66S preribosomes. Predominantly, but not exclusively, nucleolar; involved in ribosomal large subunit biogenesis.
A heterodimer associated with 66S preribosomes; predominantly nucleoplasmic, but also locates to the nucleolus; involved in ribosomal large subunit biogenesis.
A heterodimer associated with precursors of the eukaryotic small ribosomal subunit, including the 90S preribosome; involved in small subunit biogenesis.
A heterodimer associated with precursors of the eukaryotic small ribosomal subunit, including the 90S preribosome; involved in small subunit biogenesis.
The central portion of the bacterial-type flagellar basal body, which spans the periplasm and threads through the rings.
The central portion of the bacterial-type flagellar basal body, which spans the periplasm and threads through the rings.
Modulates the rate of GTP hydrolysis by a GTPase.
Modulates the rate of GTP hydrolysis by a GTPase.
Modulates the rate of GTP hydrolysis by a GTPase.
Catalysis of the transfer of a methyl group from a donor to the C5 atom of the uridine residue at position 54 in a tRNA molecule.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing thymine at position U54 of a transfer RNA. This occurs in most Gram-negative bacteria, some archae, and eukaryotes.
Catalysis of the transfer of a methyl group from 5,10-methylenetetrahydrofolate to the C5 atom of the uridine residue at position 54 in a tRNA molecule. This occurs in most Gram-positive bacteria and some Gram-negative bacteria.
Catalysis of the reaction: acetyl phosphate + H(2)O + NH(4)(+) + thioredoxin disulfide = glycine + H(+) + phosphate + thioredoxin.
Complex that possesses glycine reductase activity; usually comprises three subunits, of which two are selenoproteins; the subunits are typically designated selenoprotein A, selenoprotein B and protein C.
Catalysis of the reaction: NAD+ + [dinitrogen reductase] = nicotinamide + ADP-D-ribosyl-[dinitrogen reductase].
Catalysis of the reaction: NAD+ + [dinitrogen reductase] = nicotinamide + ADP-D-ribosyl-[dinitrogen reductase].
Catalysis of the reaction: NAD+ + [dinitrogen reductase] = nicotinamide + ADP-D-ribosyl-[dinitrogen reductase].
Catalysis of the reaction: NAD+ + [dinitrogen reductase] = nicotinamide + ADP-D-ribosyl-[dinitrogen reductase].
Catalysis of the reaction: NAD+ + [dinitrogen reductase] = nicotinamide + ADP-D-ribosyl-[dinitrogen reductase].
Repression of transcription of centromeric DNA by altering the structure of chromatin.
Repression of transcription of centromeric DNA by altering the structure of chromatin.
Repression of transcription of centromeric DNA by altering the structure of chromatin.
Construction of the eggshell, a product of the somatic follicle cell epithelium and a structure that supports the egg in a hostile environment, minimizing water loss whilst allowing gas exchanges essential for embryonic respiration.
Construction of the vitelline membrane portion of the egg shell, a rigid structure required to maintain the shape of the egg.
The directed movement of substances along cytoskeletal fibers such as microfilaments or microtubules within a cell.
The process in which one relatively unspecialized immature cystocyte of the germ-line cyst in the germarium acquires the specialized features of an oocyte. An example of this process can be found in Drosophila melanogaster.
The process that occurs during oogenesis involving the ovarian follicle cells, somatic cells which surround the germ cells of an ovary. An example of this is found in Drosophila melanogaster.
Formation of a single follicular epithelium around the germ-line derived cells of a cyst formed in the germarium. An example of this process is found in Drosophila melanogaster.
The delamination process that results in the splitting off of border cells from the anterior epithelium, prior to border cell migration.
Any process that regulates the frequency, rate or extent of border cell delamination.
Any process that increases the frequency, rate or extent of border cell delamination.
Any process that increases the frequency, rate or extent of border cell delamination.
Any process that increases the frequency, rate or extent of border cell delamination.
Any process that increases the frequency, rate or extent of border cell delamination.
Any process that increases the frequency, rate or extent of border cell delamination.
Any process that increases the frequency, rate or extent of border cell delamination.
Any process that decreases the frequency, rate or extent of border cell delamination.
Any process that decreases the frequency, rate or extent of border cell delamination.
Any process that decreases the frequency, rate or extent of border cell delamination.
Any process that decreases the frequency, rate or extent of border cell delamination.
Any process that decreases the frequency, rate or extent of border cell delamination.
Development of ovarian follicle cells to create the interfollicular stalks that connect the egg chambers of progressive developmental stages. An example of this process is found in Drosophila melanogaster.
Polarization of the follicle cells of an insect ovary along the anterior/posterior axis.
The increase in volume of an oocyte during the growth phase of the egg chamber, once the egg chamber has left the germarium. An example of this process is found in Drosophila melanogaster.
The process in which a cell becomes capable of differentiating autonomously into an oocyte cell regardless of its environment; upon determination, the cell fate cannot be reversed.
The chromosome organization process in which meiotic chromosomes in the oocyte nucleus cluster together to form a compact spherical structure called the karyosome.
Any process by which an organism or tissue maintains a population of germ-line stem cells.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of polar granules, cytoplasmic, non-membranous RNA/protein complex aggregates in the primordial germ cells of many higher eukaryotes.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of polar granules, cytoplasmic, non-membranous RNA/protein complex aggregates in the primordial germ cells of many higher eukaryotes.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of polar granules, cytoplasmic, non-membranous RNA/protein complex aggregates in the primordial germ cells of many higher eukaryotes.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of polar granules, cytoplasmic, non-membranous RNA/protein complex aggregates in the primordial germ cells of many higher eukaryotes.
Directed movement of the oocyte, following its specification, from its original central position in the cyst to a posterior position relative to the nurse cells of the egg chamber, and its maintenance in this posterior location. This is the first sign of anterior-posterior asymmetry in the developing egg chamber.
Directed movement of the oocyte, following its specification, from its original central position in the cyst to a posterior position relative to the nurse cells of the egg chamber, and its maintenance in this posterior location. This is the first sign of anterior-posterior asymmetry in the developing egg chamber.
Directed movement of the oocyte, following its specification, from its original central position in the cyst to a posterior position relative to the nurse cells of the egg chamber, and its maintenance in this posterior location. This is the first sign of anterior-posterior asymmetry in the developing egg chamber.
Directed movement of the oocyte, following its specification, from its original central position in the cyst to a posterior position relative to the nurse cells of the egg chamber, and its maintenance in this posterior location. This is the first sign of anterior-posterior asymmetry in the developing egg chamber.
Directed movement of the oocyte, following its specification, from its original central position in the cyst to a posterior position relative to the nurse cells of the egg chamber, and its maintenance in this posterior location. This is the first sign of anterior-posterior asymmetry in the developing egg chamber.
Directed movement of the oocyte, following its specification, from its original central position in the cyst to a posterior position relative to the nurse cells of the egg chamber, and its maintenance in this posterior location. This is the first sign of anterior-posterior asymmetry in the developing egg chamber.
Directed movement of the oocyte, following its specification, from its original central position in the cyst to a posterior position relative to the nurse cells of the egg chamber, and its maintenance in this posterior location. This is the first sign of anterior-posterior asymmetry in the developing egg chamber.
Directed movement of the oocyte, following its specification, from its original central position in the cyst to a posterior position relative to the nurse cells of the egg chamber, and its maintenance in this posterior location. This is the first sign of anterior-posterior asymmetry in the developing egg chamber.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spectrosome, a germline specific spherical organelle that is the precursor to the fusome.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the spectrosome, a germline specific spherical organelle that is the precursor to the fusome.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fusome of ovarian cells, an organelle derived from the spectrosome. It anchors the mitotic spindle pole to provide orientation during cystoblast cell divisions.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fusome of ovarian cells, an organelle derived from the spectrosome. It anchors the mitotic spindle pole to provide orientation during cystoblast cell divisions.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fusome of testicular cells, an organelle derived from the spectrosome.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fusome of testicular cells, an organelle derived from the spectrosome.
Assembly of the cytoplasmic bridges between developing spermatogonial or oogonial cysts.
Formation of the intercellular bridges that connect the germ-line cells of a male cyst.
Formation of the intercellular bridges that connect the germ-line cells of a male cyst.
Formation, in a germarium, of a group of interconnected cells derived from a single female gonial founder cell (a cystoblast). The germarium is the most anterior portion of an insect ovariole. An example of this process is found in Drosophila melanogaster.
The release of a mature ovum/oocyte from an ovary.
Catalysis of the reaction: acetoacetate + ATP + CoA = acetoacetyl-CoA + AMP + diphosphate + H(+).
Catalysis of the reaction: acetoacetate + ATP + CoA = acetoacetyl-CoA + AMP + diphosphate + H(+).
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
The process of binding or confining any triester of glycerol such that it is separated from other components of a biological system.
Catalysis of the reaction: S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine.
Catalysis of the reaction: S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine.
Catalysis of the reaction: S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine.
Catalysis of the reaction: S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine.
Catalysis of the reaction: S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine.
Catalysis of the reaction: S-adenosyl-L-methionine + a fatty acid = S-adenosyl-L-homocysteine + a fatty acid methyl ester.
Catalysis of the reaction: S-adenosyl-L-methionine + a fatty acid = S-adenosyl-L-homocysteine + a fatty acid methyl ester.
Catalysis of the reaction: S-adenosyl-L-methionine + a fatty acid = S-adenosyl-L-homocysteine + a fatty acid methyl ester.
Catalysis of the reaction: S-adenosyl-L-methionine + 1,4-N1-D-glucooligosaccharide = S-adenosyl-L-homocysteine + oligosaccharide containing 6-methyl-D-glucose units.
Catalysis of the reaction: S-adenosyl-L-methionine + 1,4-N1-D-glucooligosaccharide = S-adenosyl-L-homocysteine + oligosaccharide containing 6-methyl-D-glucose units.
Catalysis of the reaction: S-adenosyl-L-methionine + 1,4-N1-D-glucooligosaccharide = S-adenosyl-L-homocysteine + oligosaccharide containing 6-methyl-D-glucose units.
Catalysis of the reaction: S-adenosyl-L-methionine + carnosine = S-adenosyl-L-homocysteine + anserine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + phenol = S-adenosyl-L-homocysteine + anisole + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + phenol = S-adenosyl-L-homocysteine + anisole + H(+).
Catalysis of the reaction: 2-iodophenol + S-adenosyl-L-methionine = 1-iodo-2-methoxybenzene + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + tyramine = N-methyltyramine + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + tyramine = N-methyltyramine + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + tyramine = N-methyltyramine + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + tyramine = N-methyltyramine + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + O-demethylpuromycin = S-adenosyl-L-homocysteine + puromycin.
Catalysis of the reaction: S-adenosyl-L-methionine + O-demethylpuromycin = S-adenosyl-L-homocysteine + puromycin.
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-3-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-3-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-3-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-3-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-3-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-3-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-3-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-1-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-1-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-1-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-1-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-1-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-1-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-1-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) when at least one of the interacting partners is in the GTP-bound state.
Catalysis of the reaction: S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing a single residue of 2'-O-methyladenosine.
Catalysis of the reaction: S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing a single residue of 2'-O-methyladenosine.
Catalysis of the reaction: S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing a single residue of 2'-O-methyladenosine.
Catalysis of the reaction: S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing a single residue of 2'-O-methyladenosine.
Catalysis of the reaction: S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing a single residue of 2'-O-methyladenosine.
Catalysis of the reaction: S-adenosyl-L-methionine + luteolin = 4',5,7-trihydroxy-3'-methoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + luteolin = 4',5,7-trihydroxy-3'-methoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + luteolin = 4',5,7-trihydroxy-3'-methoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + luteolin = 4',5,7-trihydroxy-3'-methoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + luteolin = 4',5,7-trihydroxy-3'-methoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + luteolin = 4',5,7-trihydroxy-3'-methoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + luteolin = 4',5,7-trihydroxy-3'-methoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + N-alpha,N-alpha-dimethyl-L-histidine = S-adenosyl-L-homocysteine + N-alpha,N-alpha,N-alpha-trimethyl-L-histidine.
Catalysis of the reaction: S-adenosyl-L-methionine + N-alpha,N-alpha-dimethyl-L-histidine = S-adenosyl-L-homocysteine + N-alpha,N-alpha,N-alpha-trimethyl-L-histidine.
Catalysis of the reaction: S-adenosyl-L-methionine + N-alpha,N-alpha-dimethyl-L-histidine = S-adenosyl-L-homocysteine + N-alpha,N-alpha,N-alpha-trimethyl-L-histidine.
Catalysis of the reaction: S-adenosyl-L-methionine + N-alpha,N-alpha-dimethyl-L-histidine = S-adenosyl-L-homocysteine + N-alpha,N-alpha,N-alpha-trimethyl-L-histidine.
Catalysis of the reaction: S-adenosyl-L-methionine + isoflavone = S-adenosyl-L-homocysteine + 4'-O-methylisoflavone.
Catalysis of the reaction: S-adenosyl-L-methionine + isoflavone = S-adenosyl-L-homocysteine + 4'-O-methylisoflavone.
Catalysis of the reaction: S-adenosyl-L-methionine + isoflavone = S-adenosyl-L-homocysteine + 4'-O-methylisoflavone.
Catalysis of the reaction: S-adenosyl-L-methionine + isoflavone = S-adenosyl-L-homocysteine + 4'-O-methylisoflavone.
Catalysis of the reaction: S-adenosyl-L-methionine + (indol-3-yl)pyruvate = S-adenosyl-L-homocysteine + (S)-3-(indol-3-yl)-2-oxobutanoate.
Catalysis of the reaction: S-adenosyl-L-methionine + (indol-3-yl)pyruvate = S-adenosyl-L-homocysteine + (S)-3-(indol-3-yl)-2-oxobutanoate.
Catalysis of the reaction: S-adenosyl-L-methionine + (indol-3-yl)pyruvate = S-adenosyl-L-homocysteine + (S)-3-(indol-3-yl)-2-oxobutanoate.
Catalysis of the reaction: S-adenosyl-L-methionine + (indol-3-yl)pyruvate = S-adenosyl-L-homocysteine + (S)-3-(indol-3-yl)-2-oxobutanoate.
Catalysis of the reaction: S-adenosyl-L-methionine + (indol-3-yl)pyruvate = S-adenosyl-L-homocysteine + (S)-3-(indol-3-yl)-2-oxobutanoate.
Catalysis of the reaction: S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine.
Catalysis of the reaction: S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine.
Catalysis of the reaction: S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine.
Catalysis of the reaction: S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine.
Catalysis of the reaction: S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine.
Catalysis of the reaction: S-adenosyl-L-methionine + loganate = S-adenosyl-L-homocysteine + loganin.
Catalysis of the reaction: S-adenosyl-L-methionine + loganate = S-adenosyl-L-homocysteine + loganin.
Catalysis of the reaction: S-adenosyl-L-methionine + loganate = S-adenosyl-L-homocysteine + loganin.
Catalysis of the reaction: S-adenosyl-L-methionine + putrescine = N-methylputrescine + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + putrescine = N-methylputrescine + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + licodione = 2'-O-methyllicodione + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L-homocysteine + 5-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L-homocysteine + 5-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L-homocysteine + 5-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L-homocysteine + 5-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L-homocysteine + 5-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L-homocysteine + 5-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L-homocysteine + 5-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L-homocysteine + 5-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L-homocysteine + 5-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L-homocysteine + 5-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L-homocysteine + 5-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + xanthotoxin. Xanthotoxol is also known as 8-hydroxyfuranocoumarin and xanthotoxin as 8-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + xanthotoxin. Xanthotoxol is also known as 8-hydroxyfuranocoumarin and xanthotoxin as 8-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + xanthotoxin. Xanthotoxol is also known as 8-hydroxyfuranocoumarin and xanthotoxin as 8-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + xanthotoxin. Xanthotoxol is also known as 8-hydroxyfuranocoumarin and xanthotoxin as 8-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + xanthotoxin. Xanthotoxol is also known as 8-hydroxyfuranocoumarin and xanthotoxin as 8-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + xanthotoxin. Xanthotoxol is also known as 8-hydroxyfuranocoumarin and xanthotoxin as 8-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + xanthotoxin. Xanthotoxol is also known as 8-hydroxyfuranocoumarin and xanthotoxin as 8-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + xanthotoxin. Xanthotoxol is also known as 8-hydroxyfuranocoumarin and xanthotoxin as 8-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + xanthotoxin. Xanthotoxol is also known as 8-hydroxyfuranocoumarin and xanthotoxin as 8-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + xanthotoxin. Xanthotoxol is also known as 8-hydroxyfuranocoumarin and xanthotoxin as 8-methoxyfuranocoumarin.
Catalysis of the reaction: S-adenosyl-L-methionine + 5,7,4'-trihydroxyflavone = S-adenosyl-L-homocysteine + 4'-methoxy-5,7-dihydroxyflavone.
Catalysis of the reaction: S-adenosyl-L-methionine + 5,7,4'-trihydroxyflavone = S-adenosyl-L-homocysteine + 4'-methoxy-5,7-dihydroxyflavone.
Catalysis of the reaction: S-adenosyl-L-methionine + 5,7,4'-trihydroxyflavone = S-adenosyl-L-homocysteine + 4'-methoxy-5,7-dihydroxyflavone.
Catalysis of the reaction: S-adenosyl-L-methionine + 3,5,7,3',4'-pentahydroxyflavone = S-adenosyl-L-homocysteine + 3-methoxy-5,7,3',4'-tetrahydroxy-flavone.
Catalysis of the reaction: S-adenosyl-L-methionine + 3,5,7,3',4'-pentahydroxyflavone = S-adenosyl-L-homocysteine + 3-methoxy-5,7,3',4'-tetrahydroxy-flavone.
Catalysis of the reaction: S-adenosyl-L-methionine + 3,5,7,3',4'-pentahydroxyflavone = S-adenosyl-L-homocysteine + 3-methoxy-5,7,3',4'-tetrahydroxy-flavone.
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + isoorientin = S-adenosyl-L-homocysteine + H(+) + isoscoparin.
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + isoorientin = S-adenosyl-L-homocysteine + H(+) + isoscoparin.
Catalysis of the reaction: 3',4',5,7-tetrahydroxy-3-methoxyflavone + S-adenosyl-L-methionine(1+) = 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 3',4',5,7-tetrahydroxy-3-methoxyflavone + S-adenosyl-L-methionine(1+) = 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 3',4',5,7-tetrahydroxy-3-methoxyflavone + S-adenosyl-L-methionine(1+) = 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 3',4',5,7-tetrahydroxy-3-methoxyflavone + S-adenosyl-L-methionine(1+) = 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 3',4',5,7-tetrahydroxy-3-methoxyflavone + S-adenosyl-L-methionine(1+) = 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 3',4',5,7-tetrahydroxy-3-methoxyflavone + S-adenosyl-L-methionine(1+) = 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine(1+) = 3',5-dihydroxy-3,4',7-trimethoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine(1+) = 3',5-dihydroxy-3,4',7-trimethoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine(1+) = 3',5-dihydroxy-3,4',7-trimethoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine(1+) = 3',5-dihydroxy-3,4',7-trimethoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine(1+) = 3',5-dihydroxy-3,4',7-trimethoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine(1+) = 3',5-dihydroxy-3,4',7-trimethoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3',4',5,6-tetrahydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine(1+) = 3',4',5-trihydroxy-3,6,7-trimethoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3',4',5,6-tetrahydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine(1+) = 3',4',5-trihydroxy-3,6,7-trimethoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3',4',5,6-tetrahydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine(1+) = 3',4',5-trihydroxy-3,6,7-trimethoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3',4',5,6-tetrahydroxy-3,7-dimethoxyflavone + S-adenosyl-L-methionine(1+) = 3',4',5-trihydroxy-3,6,7-trimethoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + pyridine = N-methylpyridinium + S-adenosyl-L-homocysteine.
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + pyridine = N-methylpyridinium + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 3,3',4',5,7,8-hexahydroxyflavone + S-adenosyl-L-methionine(1+) = 3,3',4',5,7-pentahydroxy-8-methoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3,3',4',5,7,8-hexahydroxyflavone + S-adenosyl-L-methionine(1+) = 3,3',4',5,7-pentahydroxy-8-methoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3,3',4',5,7,8-hexahydroxyflavone + S-adenosyl-L-methionine(1+) = 3,3',4',5,7-pentahydroxy-8-methoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3,3',4',5,7,8-hexahydroxyflavone + S-adenosyl-L-methionine(1+) = 3,3',4',5,7-pentahydroxy-8-methoxyflavone + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: (S)-tetrahydrocolumbamine + S-adenosyl-L-methionine(1+) = S-adenosyl-L-homocysteine + H(+) + tetrahydropalmatine.
Catalysis of the reaction: (S)-tetrahydrocolumbamine + S-adenosyl-L-methionine(1+) = S-adenosyl-L-homocysteine + H(+) + tetrahydropalmatine.
Catalysis of the reaction: 2-methylpropanal oxime + S-adenosyl-L-methionine = 2-methylpropanal O-methyloxime + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 2-methylpropanal oxime + S-adenosyl-L-methionine = 2-methylpropanal O-methyloxime + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 2-methylpropanal oxime + S-adenosyl-L-methionine = 2-methylpropanal O-methyloxime + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 2-methylpropanal oxime + S-adenosyl-L-methionine = 2-methylpropanal O-methyloxime + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + 11-O-demethyl-17-O-deacetylvindoline = S-adenosyl-L-homocysteine + 17-O-deacetylvindoline.
Catalysis of the reaction: S-adenosyl-L-methionine + 11-O-demethyl-17-O-deacetylvindoline = S-adenosyl-L-homocysteine + 17-O-deacetylvindoline.
Catalysis of the reaction: S-adenosyl-L-methionine + 11-O-demethyl-17-O-deacetylvindoline = S-adenosyl-L-homocysteine + 17-O-deacetylvindoline.
Catalysis of the reaction: S-adenosyl-L-methionine + 11-O-demethyl-17-O-deacetylvindoline = S-adenosyl-L-homocysteine + 17-O-deacetylvindoline.
Catalysis of the reaction: 3-hydroxyanthranilate + S-adenosyl-L-methionine = 3-hydroxy-4-methylanthranilate + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 3-hydroxyanthranilate + S-adenosyl-L-methionine = 3-hydroxy-4-methylanthranilate + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: (3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + deacetoxyvindoline + H(+).
Catalysis of the reaction: (3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + deacetoxyvindoline + H(+).
Catalysis of the reaction: (3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + deacetoxyvindoline + H(+).
Catalysis of the reaction: (3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + deacetoxyvindoline + H(+).
Catalysis of the reaction: (3R)-3-hydroxy-16-methoxy-2,3-dihydrotabersonine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + deacetoxyvindoline + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + macrocin = S-adenosyl-L-homocysteine + H(+) + tylosin.
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + macrocin = S-adenosyl-L-homocysteine + H(+) + tylosin.
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + macrocin = S-adenosyl-L-homocysteine + H(+) + tylosin.
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + demethylmacrocin = S-adenosyl-L-homocysteine + H(+) + macrocin.
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + demethylmacrocin = S-adenosyl-L-homocysteine + H(+) + macrocin.
Catalysis of the reaction: N-benzoyl-4-hydroxyanthranilate + S-adenosyl-L-methionine(1+) = N-benzoyl-4-methoxyanthranilate + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: N-benzoyl-4-hydroxyanthranilate + S-adenosyl-L-methionine(1+) = N-benzoyl-4-methoxyanthranilate + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: N-benzoyl-4-hydroxyanthranilate + S-adenosyl-L-methionine(1+) = N-benzoyl-4-methoxyanthranilate + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + L-tryptophan = S-adenosyl-L-homocysteine + L-2-methyltryptophan + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + L-tryptophan = S-adenosyl-L-homocysteine + L-2-methyltryptophan + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + L-tryptophan = S-adenosyl-L-homocysteine + L-2-methyltryptophan + H(+).
Catalysis of the reaction: 6-hydroxymellein + S-adenosyl-L-methionine = 6-methoxymellein + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 6-hydroxymellein + S-adenosyl-L-methionine = 6-methoxymellein + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + anthranilate = N-methylanthranilate + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + anthranilate = N-methylanthranilate + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + glucuronoxylan D-glucuronate = S-adenosyl-L-homocysteine + glucuronoxylan 4-O-methyl-D-glucuronate.
Catalysis of the reaction: S-adenosyl-L-methionine + (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline = S-adenosyl-L-homocysteine + N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline.
Catalysis of the reaction: S-adenosyl-L-methionine + (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline = S-adenosyl-L-homocysteine + N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline.
Catalysis of the reaction: S-adenosyl-L-methionine + (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline = S-adenosyl-L-homocysteine + N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline.
Catalysis of the reaction: (S)-scoulerine + S-adenosyl-L-methionine(1+) = (S)-tetrahydrocolumbamine + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: (S)-scoulerine + S-adenosyl-L-methionine(1+) = (S)-tetrahydrocolumbamine + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + columbamine = S-adenosyl-L-homocysteine + H(+) + palmatine.
Catalysis of the reaction: 10-hydroxydihydrosanguinarine + S-adenosyl-L-methionine(1+) = S-adenosyl-L-homocysteine + dihydrochelirubine + H(+).
Catalysis of the reaction: 12-hydroxydihydrochelirubine + S-adenosyl-L-methionine(1+) = S-adenosyl-L-homocysteine + dihydromacarpine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + 6-O-methylnorlaudanosoline = S-adenosyl-L-homocysteine + nororientaline.
Catalysis of the reaction: S-adenosyl-L-methionine + (S)-7,8,13,14-tetrahydroprotoberberine = S-adenosyl-L-homocysteine + cis-N-methyl-(S)-7,8,13,14-tetrahydroprotoberberine.
Catalysis of the reaction: S-adenosyl-L-methionine + (S)-7,8,13,14-tetrahydroprotoberberine = S-adenosyl-L-homocysteine + cis-N-methyl-(S)-7,8,13,14-tetrahydroprotoberberine.
Catalysis of the reaction: S-adenosyl-L-methionine + [cytochrome c]-methionine = S-adenosyl-L-homocysteine + [cytochrome c]-S-methyl-methionine.
Catalysis of the reaction: S-adenosyl-L-methionine + [cytochrome c]-methionine = S-adenosyl-L-homocysteine + [cytochrome c]-S-methyl-methionine.
Catalysis of the reaction: S-adenosyl-L-methionine + 3'-hydroxy-N-methyl-(S)-coclaurine = S-adenosyl-L-homocysteine + (S)-reticuline.
Catalysis of the reaction: S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine = S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine.
Catalysis of the reaction: S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine = S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine.
Catalysis of the reaction: S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine = S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine.
Catalysis of the reaction: S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine = S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine.
Catalysis of the reaction: S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine = S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine.
Catalysis of the reaction: S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine = S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine.
Catalysis of the reaction: S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine = S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine.
Catalysis of the reaction: S-adenosyl-L-methionine + (RS)-norcoclaurine = S-adenosyl-L-homocysteine + (RS)-coclaurine.
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-4-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-4-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-4-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine(1+) + myo-inositol = 1D-4-O-methyl-myo-inositol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + precorrin-2 = S-adenosyl-L-homocysteine + H(+) + precorrin-3A.
Catalysis of the reaction: S-adenosyl-L-methionine + precorrin-2 = S-adenosyl-L-homocysteine + H(+) + precorrin-3A.
Catalysis of the reaction: S-adenosyl-L-methionine + precorrin-3B = S-adenosyl-L-homocysteine + precorrin 4.
Catalysis of the reaction: S-adenosyl-L-methionine + precorrin-3B = S-adenosyl-L-homocysteine + precorrin 4.
Catalysis of the reaction: S-adenosyl-L-methionine + precorrin-3B = S-adenosyl-L-homocysteine + precorrin 4.
Catalysis of the reaction: S-adenosyl-L-methionine + precorrin-3B = S-adenosyl-L-homocysteine + precorrin 4.
Catalysis of the reaction: S-adenosyl-L-methionine + trichlorophenol = S-adenosyl-L-homocysteine + trichloroanisole.
Catalysis of the reaction: S-adenosyl-L-methionine + trichlorophenol = S-adenosyl-L-homocysteine + trichloroanisole.
Catalysis of the reaction: S-adenosyl-L-methionine + trichlorophenol = S-adenosyl-L-homocysteine + trichloroanisole.
Catalysis of the reaction: S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate.
Catalysis of the reaction: S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate.
Catalysis of the reaction: S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate.
Catalysis of the reaction: S-adenosyl-L-methionine + methylarsonite = S-adenosyl-L-homocysteine + dimethylarsinate.
Catalysis of the reaction: 3'-demethylstaurosporine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + H(+) + staurosporine.
Catalysis of the reaction: 3'-demethylstaurosporine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + H(+) + staurosporine.
Catalysis of the reaction: 3'-demethylstaurosporine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + H(+) + staurosporine.
Catalysis of the reaction: S-adenosyl-L-methionine + (S)-coclaurine = S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine.
Catalysis of the reaction: S-adenosyl-L-methionine + jasmonate = S-adenosyl-L-homocysteine + methyljasmonate.
Catalysis of the reaction: S-adenosyl-L-methionine + jasmonate = S-adenosyl-L-homocysteine + methyljasmonate.
Catalysis of the reaction: S-adenosyl-L-methionine + jasmonate = S-adenosyl-L-homocysteine + methyljasmonate.
Catalysis of the reaction: S-adenosyl-L-methionine + jasmonate = S-adenosyl-L-homocysteine + methyljasmonate.
Catalysis of the reaction: S-adenosyl-L-methionine + cycloartenol = (24R)-24-methylcycloart-25-en-3beta-ol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + cycloartenol = (24R)-24-methylcycloart-25-en-3beta-ol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 24-methylidenelophenol + S-adenosyl-L-methionine(1+) = (Z)-24-ethylidenelophenol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 24-methylidenelophenol + S-adenosyl-L-methionine(1+) = (Z)-24-ethylidenelophenol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 24-methylidenelophenol + S-adenosyl-L-methionine(1+) = (Z)-24-ethylidenelophenol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 24-methylidenelophenol + S-adenosyl-L-methionine(1+) = (Z)-24-ethylidenelophenol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: 24-methylidenelophenol + S-adenosyl-L-methionine(1+) = (Z)-24-ethylidenelophenol + S-adenosyl-L-homocysteine + H(+).
Catalysis of the reaction: S-adenosyl-L-methionine + trans-aconitate = (E)-3-(methoxycarbonyl)pent-2-enedioate + S-adenosyl-L-homocysteine.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of cyclic nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of cyclic nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of cyclic nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of nucleotides.
Any process that stops, prevents, or reduces the frequency, rate or extent of an adenylate cyclase-activating adrenergic receptor protein signaling pathway activity. An adrenergic receptor signaling pathway is the series of molecular signals generated as a consequence of an adrenergic receptor binding to one of its physiological ligands.
Any process that stops, prevents, or reduces the frequency, rate or extent of an adenylate cyclase-activating adrenergic receptor protein signaling pathway activity. An adrenergic receptor signaling pathway is the series of molecular signals generated as a consequence of an adrenergic receptor binding to one of its physiological ligands.
Any process that modulates the frequency, rate or extent of the assembly of actin filaments by the addition of actin monomers to a filament.
Any process that modulates the frequency, rate or extent of the disassembly of actin filaments by the removal of actin monomers from a filament.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin depolymerization.
Any process that activates or increases the frequency, rate or extent of actin depolymerization.
Any process that activates or increases the frequency, rate or extent of actin depolymerization.
Any process that activates or increases the frequency, rate or extent of actin depolymerization.
Any process that activates or increases the frequency, rate or extent of actin depolymerization.
Any process that activates or increases the frequency, rate or extent of actin depolymerization.
Any process that activates or increases the frequency, rate or extent of actin depolymerization.
Any process that activates or increases the frequency, rate or extent of actin depolymerization.
Any process that activates or increases the frequency, rate or extent of actin depolymerization.
Any process that activates or increases the frequency, rate or extent of actin depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
Any process that activates or increases the frequency, rate or extent of actin polymerization.
Any process that activates or increases the frequency, rate or extent of actin polymerization.
Any process that activates or increases the frequency, rate or extent of actin polymerization.
Any process that activates or increases the frequency, rate or extent of actin polymerization.
Any process that activates or increases the frequency, rate or extent of actin polymerization.
Any process that activates or increases the frequency, rate or extent of actin polymerization.
Any process that activates or increases the frequency, rate or extent of actin polymerization.
Any process that modulates the frequency, rate or extent of the assembly of intermediate filaments by the addition of monomers to a filament.
Any process that stops, prevents, or reduces the frequency, rate or extent of intermediate filament polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of intermediate filament polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of intermediate filament polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of intermediate filament polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of intermediate filament polymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament polymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament polymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament polymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament polymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament polymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament polymerization.
Any process that modulates the frequency, rate or extent of the disassembly of intermediate filaments by the removal of monomers from a filament.
Any process that stops, prevents, or reduces the frequency, rate or extent of intermediate filament depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of intermediate filament depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of intermediate filament depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of intermediate filament depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of intermediate filament depolymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament depolymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament depolymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament depolymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament depolymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament depolymerization.
Any process that activates or increases the frequency, rate or extent of intermediate filament depolymerization.
A G protein-coupled receptor signaling pathway which proceeds with inhibition of phospholipase C (PLC) activity and a subsequent decrease in the levels of cellular inositol trisphosphate (IP3) and diacylglycerol (DAG).
A G protein-coupled receptor signaling pathway which proceeds with inhibition of phospholipase C (PLC) activity and a subsequent decrease in the levels of cellular inositol trisphosphate (IP3) and diacylglycerol (DAG).
A G protein-coupled receptor signaling pathway which proceeds with inhibition of phospholipase C (PLC) activity and a subsequent decrease in the levels of cellular inositol trisphosphate (IP3) and diacylglycerol (DAG).
A G protein-coupled receptor signaling pathway which proceeds with inhibition of phospholipase C (PLC) activity and a subsequent decrease in the levels of cellular inositol trisphosphate (IP3) and diacylglycerol (DAG).
A G protein-coupled receptor signaling pathway which proceeds with inhibition of phospholipase C (PLC) activity and a subsequent decrease in the levels of cellular inositol trisphosphate (IP3) and diacylglycerol (DAG).
A G protein-coupled receptor signaling pathway which proceeds with inhibition of phospholipase C (PLC) activity and a subsequent decrease in the levels of cellular inositol trisphosphate (IP3) and diacylglycerol (DAG).
A G protein-coupled receptor signaling pathway which proceeds with inhibition of phospholipase C (PLC) activity and a subsequent decrease in the levels of cellular inositol trisphosphate (IP3) and diacylglycerol (DAG).
The process in which transcription of polyadenylated RNA polymerase II transcripts is terminated; cleavage and polyadenylylation of the mRNA 3' end is coupled to transcription termination.
The process in which transcription of polyadenylated RNA polymerase II transcripts is terminated; cleavage and polyadenylylation of the mRNA 3' end is coupled to transcription termination.
The process in which transcription of polyadenylated RNA polymerase II transcripts is terminated; cleavage and polyadenylylation of the mRNA 3' end is coupled to transcription termination.
The process in which transcription of nonpolyadenylated RNA polymerase II transcripts is terminated; coupled to the maturation of the RNA 3'-end.
The process in which transcription of nonpolyadenylated RNA polymerase II transcripts is terminated; coupled to the maturation of the RNA 3'-end.
The process in which transcription of nonpolyadenylated RNA polymerase II transcripts is terminated; coupled to the maturation of the RNA 3'-end.
Catalysis of the reaction: (3S)-3-hydroxy-L-aspartate = NH(4)(+) + oxaloacetate.
Catalysis of the reaction: (3S)-3-hydroxy-L-aspartate = NH(4)(+) + oxaloacetate.
Catalysis of the reaction: (3S)-3-hydroxy-L-aspartate = NH(4)(+) + oxaloacetate.
Catalysis of the reaction: (3S)-3-hydroxy-L-aspartate = NH(4)(+) + oxaloacetate.
Catalysis of the reaction: (3S)-3-hydroxy-L-aspartate = NH(4)(+) + oxaloacetate.
Any chromosome other than a sex chromosome.
The process whose specific outcome is the progression of the prostate gland over time, from its formation to the mature structure. The prostate gland is a partly muscular, partly glandular body that is situated near the base of the mammalian male urethra and secretes an alkaline viscid fluid which is a major constituent of the ejaculatory fluid.
The process in which a myeloid precursor cell acquires the specialized features of a granulocyte. Granulocytes are a class of leukocytes characterized by the presence of granules in their cytoplasm. These cells are active in allergic immune reactions such as arthritic inflammation and rashes. This class includes basophils, eosinophils and neutrophils.
Any process that modulates the frequency, rate or extent of granulocyte differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of granulocyte differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of granulocyte differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of granulocyte differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of granulocyte differentiation.
Any process that activates or increases the frequency, rate or extent of granulocyte differentiation.
Any process that activates or increases the frequency, rate or extent of granulocyte differentiation.
Any process that activates or increases the frequency, rate or extent of granulocyte differentiation.
Any process that activates or increases the frequency, rate or extent of granulocyte differentiation.
Any process that activates or increases the frequency, rate or extent of granulocyte differentiation.
The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium.
Any process that modulates the frequency, rate or extent of epithelial cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of epithelial cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of epithelial cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of epithelial cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of epithelial cell differentiation.
Any process that activates or increases the frequency, rate or extent of epithelial cell differentiation.
Any process that activates or increases the frequency, rate or extent of epithelial cell differentiation.
Any process that activates or increases the frequency, rate or extent of epithelial cell differentiation.
Any process that activates or increases the frequency, rate or extent of epithelial cell differentiation.
Any process that activates or increases the frequency, rate or extent of epithelial cell differentiation.
The process in which a relatively unspecialized cell acquires specialized features of a polarized epithelial cell. The polarized epithelial cell can be any of the cells within an epithelium where the epithelial sheet is oriented with respect to the planar axis.
Any process that modulates the frequency, rate or extent of polarized epithelial cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of polarized epithelial cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of polarized epithelial cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of polarized epithelial cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of polarized epithelial cell differentiation.
Any process that activates or increases the rate or extent of polarized epithelial cell differentiation.
Any process that activates or increases the rate or extent of polarized epithelial cell differentiation.
Any process that activates or increases the rate or extent of polarized epithelial cell differentiation.
Any process that activates or increases the rate or extent of polarized epithelial cell differentiation.
Any process that activates or increases the rate or extent of polarized epithelial cell differentiation.
The portion of the cytoskeleton that lies just beneath the plasma membrane.
The portion of the actin cytoskeleton, comprising filamentous actin and associated proteins, that lies just beneath the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane.
The lipid bilayer surrounding the rough endoplasmic reticulum.
The lipid bilayer surrounding the rough endoplasmic reticulum.
The lipid bilayer surrounding the smooth endoplasmic reticulum.
The lipid bilayer surrounding the smooth endoplasmic reticulum.
A protein complex that mediates transcriptional silencing at the rDNA locus (the name derives from regulator of nucleolar silencing and telophase). In Saccharomyces the complex contains Net1p, Sir2p, Cdc14p, and at least one more subunit.
Trimeric protein complex that possesses endonuclease activity; involved in meiotic recombination, DNA repair and checkpoint signaling. In Saccharomyces cerevisiae, the complex comprises Mre11p, Rad50p, and Xrs2p; complexes identified in other species generally contain proteins orthologous to the Saccharomyces cerevisiae proteins.
Trimeric protein complex that possesses endonuclease activity; involved in meiotic recombination, DNA repair and checkpoint signaling. In Saccharomyces cerevisiae, the complex comprises Mre11p, Rad50p, and Xrs2p; complexes identified in other species generally contain proteins orthologous to the Saccharomyces cerevisiae proteins.
Trimeric protein complex that possesses endonuclease activity; involved in meiotic recombination, DNA repair and checkpoint signaling. In Saccharomyces cerevisiae, the complex comprises Mre11p, Rad50p, and Xrs2p; complexes identified in other species generally contain proteins orthologous to the Saccharomyces cerevisiae proteins.
Trimeric protein complex that possesses endonuclease activity; involved in meiotic recombination, DNA repair and checkpoint signaling. In Saccharomyces cerevisiae, the complex comprises Mre11p, Rad50p, and Xrs2p; complexes identified in other species generally contain proteins orthologous to the Saccharomyces cerevisiae proteins.
Trimeric protein complex that possesses endonuclease activity; involved in meiotic recombination, DNA repair and checkpoint signaling. In Saccharomyces cerevisiae, the complex comprises Mre11p, Rad50p, and Xrs2p; complexes identified in other species generally contain proteins orthologous to the Saccharomyces cerevisiae proteins.
Trimeric protein complex that possesses endonuclease activity; involved in meiotic recombination, DNA repair and checkpoint signaling. In Saccharomyces cerevisiae, the complex comprises Mre11p, Rad50p, and Xrs2p; complexes identified in other species generally contain proteins orthologous to the Saccharomyces cerevisiae proteins.
The portion of nuclear chromatin associated with the nucleolus; includes the DNA encoding the ribosomal RNA.
Any of the tandem arrays of rDNA localized at the periphery of the nucleus and protruding into the nucleolus, and associated proteins. May be visible as a single or double spot by DAPI staining.
A protein complex composed of an alpha and a beta receptor subunit and an interleukin ligand. In human, Interleukin-19, -20 and -24 bind IL20RA/IL20RB receptor subunits and Interleukin-20 and -24 bind IL22RA1/IL20RB receptor subunits.
A cytoplasmic protein complex containing glycogen synthase kinase-3-beta (GSK-3-beta), the adenomatous polyposis coli protein (APC), and the scaffolding protein axin, among others; phosphorylates beta-catenin, targets it for degradation by the proteasome.
A cytoplasmic protein complex containing glycogen synthase kinase-3-beta (GSK-3-beta), the adenomatous polyposis coli protein (APC), and the scaffolding protein axin, among others; phosphorylates beta-catenin, targets it for degradation by the proteasome.
A cytoplasmic protein complex containing glycogen synthase kinase-3-beta (GSK-3-beta), the adenomatous polyposis coli protein (APC), and the scaffolding protein axin, among others; phosphorylates beta-catenin, targets it for degradation by the proteasome.
A cytoplasmic protein complex containing glycogen synthase kinase-3-beta (GSK-3-beta), the adenomatous polyposis coli protein (APC), and the scaffolding protein axin, among others; phosphorylates beta-catenin, targets it for degradation by the proteasome.
A cytoplasmic protein complex containing glycogen synthase kinase-3-beta (GSK-3-beta), the adenomatous polyposis coli protein (APC), and the scaffolding protein axin, among others; phosphorylates beta-catenin, targets it for degradation by the proteasome.
A cytoplasmic protein complex containing glycogen synthase kinase-3-beta (GSK-3-beta), the adenomatous polyposis coli protein (APC), and the scaffolding protein axin, among others; phosphorylates beta-catenin, targets it for degradation by the proteasome.
A cytoplasmic protein complex containing glycogen synthase kinase-3-beta (GSK-3-beta), the adenomatous polyposis coli protein (APC), and the scaffolding protein axin, among others; phosphorylates beta-catenin, targets it for degradation by the proteasome.
The process whose specific outcome is the progression of the thyroid gland over time, from its formation to the mature structure. The thyroid gland is an endoderm-derived gland that produces thyroid hormone.
The process whose specific outcome is the progression of the mammary gland over time, from its formation to the mature structure. The mammary gland is a large compound sebaceous gland that in female mammals is modified to secrete milk. Its development starts with the formation of the mammary line and ends as the mature gland cycles between nursing and weaning stages.
Any complex that possesses RNA polymerase activity; generally comprises a catalytic subunit and one or more additional subunits.
Interacting selectively and non-covalently with beta-2-microglobulin.
Interacting selectively and non-covalently with a lipid antigen.
Interacting selectively and non-covalently with an endogenous cellular lipid antigen.
Interacting selectively and non-covalently with an exogenous lipid antigen (examples include microbial lipids and glycolipids).
Any process that modulates the frequency or rate of myeloid dendritic cell activation.
Any process that stops, prevents, or reduces the frequency, rate or extent of myeloid dendritic cell activation.
Any process that stops, prevents, or reduces the frequency, rate or extent of myeloid dendritic cell activation.
Any process that stops, prevents, or reduces the frequency, rate or extent of myeloid dendritic cell activation.
Any process that stops, prevents, or reduces the frequency, rate or extent of myeloid dendritic cell activation.
Any process that stimulates, induces or increases the rate of myeloid dendritic cell activation.
Any process that stimulates, induces or increases the rate of myeloid dendritic cell activation.
Any process that stimulates, induces or increases the rate of myeloid dendritic cell activation.
Any process that stimulates, induces or increases the rate of myeloid dendritic cell activation.
Any process that stimulates, induces or increases the rate of myeloid dendritic cell activation.
Any process that modulates the frequency, rate or extent of B cell proliferation.
Any process that modulates the frequency, rate or extent of B cell proliferation.
Any process that modulates the frequency, rate or extent of B cell proliferation.
Any process that stops, prevents or reduces the rate or extent of B cell proliferation.
Any process that stops, prevents or reduces the rate or extent of B cell proliferation.
Any process that stops, prevents or reduces the rate or extent of B cell proliferation.
Any process that stops, prevents or reduces the rate or extent of B cell proliferation.
Any process that stops, prevents or reduces the rate or extent of B cell proliferation.
Any process that stops, prevents or reduces the rate or extent of B cell proliferation.
Any process that stops, prevents or reduces the rate or extent of B cell proliferation.
Any process that activates or increases the rate or extent of B cell proliferation.
Any process that activates or increases the rate or extent of B cell proliferation.
Any process that activates or increases the rate or extent of B cell proliferation.
Any process that activates or increases the rate or extent of B cell proliferation.
Any process that activates or increases the rate or extent of B cell proliferation.
Any process that activates or increases the rate or extent of B cell proliferation.
Any process that activates or increases the rate or extent of B cell proliferation.
Any process that activates or increases the rate or extent of B cell proliferation.
A protein complex that possesses ubiquitin ligase activity; the complex is usually pentameric; for example, in mammals the subunits are pVHL, elongin B, elongin C, cullin-2 (Cul2), and Rbx1.
A protein complex that possesses ubiquitin ligase activity; the complex is usually pentameric; for example, in mammals the subunits are pVHL, elongin B, elongin C, cullin-2 (Cul2), and Rbx1.
A protein complex that possesses ubiquitin ligase activity; the complex is usually pentameric; for example, in mammals the subunits are pVHL, elongin B, elongin C, cullin-2 (Cul2), and Rbx1.
A cohesin complex that mediates sister chromatid cohesion during mitosis; has a subunit composition distinct from that of the meiotic cohesin complex.
A cohesin complex that mediates sister chromatid cohesion during meiosis; has a subunit composition distinct from that of the mitotic cohesin complex.
A multi-component enzymatic machine at the replication fork which mediates DNA replication. Includes DNA primase, one or more DNA polymerases, DNA helicases, and other proteins.
A multi-component enzymatic machine at the replication fork which mediates DNA replication. Includes DNA primase, one or more DNA polymerases, DNA helicases, and other proteins.
A multi-component enzymatic machine at the replication fork which mediates DNA replication. Includes DNA primase, one or more DNA polymerases, DNA helicases, and other proteins.
Protein complex that mediates editing of the mRNA encoding apolipoprotein B; catalyzes the deamination of C to U (residue 6666 in the human mRNA). Contains a catalytic subunit, APOBEC-1, and other proteins (e.g. human ASP; rat ASP and KSRP).
Protein complex that mediates editing of the mRNA encoding apolipoprotein B; catalyzes the deamination of C to U (residue 6666 in the human mRNA). Contains a catalytic subunit, APOBEC-1, and other proteins (e.g. human ASP; rat ASP and KSRP).
Conserved heterotrimeric complex of PCNA-like proteins that is loaded onto DNA at sites of DNA damage.
Conserved heterotrimeric complex of PCNA-like proteins that is loaded onto DNA at sites of DNA damage.
A multimeric protein complex that associates with the vacuolar membrane, late endosomal (multivesicular body) and lysosomal membranes. HOPS is a tethering complex involved in vesicle fusion.
Catalysis of the reaction: ATP + H2O = ADP + phosphate. This reaction requires the presence of an actin filament to accelerate release of ADP and phosphate.
Catalysis of the reaction: ATP + H2O = ADP + phosphate. This reaction requires the presence of calcium ion (Ca2+).
The process whose specific outcome is the progression of the forebrain over time, from its formation to the mature structure. The forebrain is the anterior of the three primary divisions of the developing chordate brain or the corresponding part of the adult brain (in vertebrates, includes especially the cerebral hemispheres, the thalamus, and the hypothalamus and especially in higher vertebrates is the main control center for sensory and associative information processing, visceral functions, and voluntary motor functions).
The process whose specific outcome is the progression of the midbrain over time, from its formation to the mature structure. The midbrain is the middle division of the three primary divisions of the developing chordate brain or the corresponding part of the adult brain (in vertebrates, includes a ventral part containing the cerebral peduncles and a dorsal tectum containing the corpora quadrigemina and that surrounds the aqueduct of Sylvius connecting the third and fourth ventricles).
The process whose specific outcome is the progression of the hindbrain over time, from its formation to the mature structure. The hindbrain is the posterior of the three primary divisions of the developing chordate brain, or the corresponding part of the adult brain (in vertebrates, includes the cerebellum, pons, and medulla oblongata and controls the autonomic functions and equilibrium).
The process whose specific outcome is the progression of the notochord over time, from its formation to the mature structure. The notochord is a mesoderm-derived structure located ventral of the developing nerve cord. In vertebrates, the notochord serves as a core around which other mesodermal cells form the vertebrae. In the most primitive chordates, which lack vertebrae, the notochord persists as a substitute for a vertebral column.
A conserved hetero-pentameric membrane-associated complex involved in retrograde transport from endosomes to the Golgi apparatus. The budding yeast retromer comprises Vps35p, Vps29p, Vps26p, Vps5p, and Vps17p. The mammalian complex shows slight variation in composition compared to yeast, and comprises SNX1 or SNX2, SNX5 or SNX6, VPS26A or VPS26B, VPS29, and VPS35.
The dimeric subcomplex of the retromer, believed to be peripherally associated with the membrane. This dimeric complex is responsible for remodelling endosomal membranes to form a tube-structure to which cargo molecules are selected for recycling. The budding yeast complex comprises Vps5p and Vps17p, and may contain multiple copies of a Vps5p/Vps17p dimer. The mammalian complex contains SNX1 or SNX2 dimerized with SNX5 or SNX6.
The dimeric subcomplex of the retromer, believed to be peripherally associated with the membrane. This dimeric complex is responsible for remodelling endosomal membranes to form a tube-structure to which cargo molecules are selected for recycling. The budding yeast complex comprises Vps5p and Vps17p, and may contain multiple copies of a Vps5p/Vps17p dimer. The mammalian complex contains SNX1 or SNX2 dimerized with SNX5 or SNX6.
The dimeric subcomplex of the retromer, believed to be peripherally associated with the membrane. This dimeric complex is responsible for remodelling endosomal membranes to form a tube-structure to which cargo molecules are selected for recycling. The budding yeast complex comprises Vps5p and Vps17p, and may contain multiple copies of a Vps5p/Vps17p dimer. The mammalian complex contains SNX1 or SNX2 dimerized with SNX5 or SNX6.
The trimeric subcomplex of the retromer, believed to be closely associated with the membrane. This trimeric complex is responsible for recognizing and binding to cargo molecules. The complex comprises three Vps proteins in both yeast and mammalian cells: Vps35p, Vps29p, and Vps26p in yeast, and VPS35, VPS29 and VPS26A or VPS26B in mammals.
The trimeric subcomplex of the retromer, believed to be closely associated with the membrane. This trimeric complex is responsible for recognizing and binding to cargo molecules. The complex comprises three Vps proteins in both yeast and mammalian cells: Vps35p, Vps29p, and Vps26p in yeast, and VPS35, VPS29 and VPS26A or VPS26B in mammals.
The trimeric subcomplex of the retromer, believed to be closely associated with the membrane. This trimeric complex is responsible for recognizing and binding to cargo molecules. The complex comprises three Vps proteins in both yeast and mammalian cells: Vps35p, Vps29p, and Vps26p in yeast, and VPS35, VPS29 and VPS26A or VPS26B in mammals.
The trimeric subcomplex of the retromer, believed to be closely associated with the membrane. This trimeric complex is responsible for recognizing and binding to cargo molecules. The complex comprises three Vps proteins in both yeast and mammalian cells: Vps35p, Vps29p, and Vps26p in yeast, and VPS35, VPS29 and VPS26A or VPS26B in mammals.
The trimeric subcomplex of the retromer, believed to be closely associated with the membrane. This trimeric complex is responsible for recognizing and binding to cargo molecules. The complex comprises three Vps proteins in both yeast and mammalian cells: Vps35p, Vps29p, and Vps26p in yeast, and VPS35, VPS29 and VPS26A or VPS26B in mammals.
A protein complex that binds to the Mlu1 cell cycle box (MCB) promoter element, consensus sequence ACGCGN, and is involved in regulation of transcription during the G1/S transition of the cell cycle. In Saccharomyces, the complex contains a heterodimer of the DNA binding protein Mbp1p and the activator Swi4p, and is associated with additional proteins known as Nrm1p, Msa1p, and Msa2p; in Schizosaccharomyces the complex contains Res1p, Res2p, and Cdc10p.
A protein complex that binds to the Mlu1 cell cycle box (MCB) promoter element, consensus sequence ACGCGN, and is involved in regulation of transcription during the G1/S transition of the cell cycle. In Saccharomyces, the complex contains a heterodimer of the DNA binding protein Mbp1p and the activator Swi4p, and is associated with additional proteins known as Nrm1p, Msa1p, and Msa2p; in Schizosaccharomyces the complex contains Res1p, Res2p, and Cdc10p.
A protein complex that binds to the Mlu1 cell cycle box (MCB) promoter element, consensus sequence ACGCGN, and is involved in regulation of transcription during the G1/S transition of the cell cycle. In Saccharomyces, the complex contains a heterodimer of the DNA binding protein Mbp1p and the activator Swi4p, and is associated with additional proteins known as Nrm1p, Msa1p, and Msa2p; in Schizosaccharomyces the complex contains Res1p, Res2p, and Cdc10p.
The post-translational removal of peptide sequences from within a protein sequence.
The post-translational removal of peptide sequences from within a protein sequence, by a process not involving inteins.
The formation of a thickening of the neural ectoderm in the head region of the vertebrate embryo which develops into the olfactory region of the nasal cavity.
Interacting selectively and non-covalently with a tetratricopeptide repeat (TPR) domain of a protein, the consensus sequence of which is defined by a pattern of small and large hydrophobic amino acids and a structure composed of helices.
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 deep water stimulus, being immersed in standing deep water throughout the life cycle.
Formation of the junction between an axon and the glial cell that forms the myelin sheath. Paranodal junctions form at each paranode, i.e. at the ends of the unmyelinated nodes of Ranvier.
Formation of the junction between an axon and the glial cell that forms the myelin sheath. Paranodal junctions form at each paranode, i.e. at the ends of the unmyelinated nodes of Ranvier.
Formation of the junction between an axon and the glial cell that forms the myelin sheath. Paranodal junctions form at each paranode, i.e. at the ends of the unmyelinated nodes of Ranvier.
A large multiprotein complex that possesses histone acetyltransferase and is involved in regulation of transcription. The composition is similar to that of the SAGA complex; for example, the human complex contains the transcription-transformation cofactor TRRAP, hGCN5L acetylase, novel human ADA-like and SPT-like cofactors, and a subset of TAFs.
A large multiprotein complex that possesses histone acetyltransferase and is involved in regulation of transcription. The composition is similar to that of the SAGA complex; for example, the human complex contains the transcription-transformation cofactor TRRAP, hGCN5L acetylase, novel human ADA-like and SPT-like cofactors, and a subset of TAFs.
A conserved complex that contains a heterodimer of SMC proteins (Smc5p and Smc6p, or homologs thereof) and several other proteins, and is involved in DNA repair and maintaining cell cycle arrest following DNA damage. In S. cerevisiae, this is an octameric complex called Mms21-Smc5-Smc6 complex, with at least five of its subunits conserved in fission yeast and humans.
The process resulting in the transition of the otic placode into the otic vesicle, a transient embryonic structure formed during development of the vertebrate inner ear.
The process resulting in the transition of the otic placode into the otic vesicle, a transient embryonic structure formed during development of the vertebrate inner ear.
The process whose specific outcome is the progression of the midbrain-hindbrain boundary over time, from its formation to the mature structure. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages.
The process whose specific outcome is the progression of the midbrain-hindbrain boundary over time, from its formation to the mature structure. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages.
The process whose specific outcome is the progression of the midbrain-hindbrain boundary over time, from its formation to the mature structure. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages.
The process whose specific outcome is the progression of the midbrain-hindbrain boundary over time, from its formation to the mature structure. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages.
The process whose specific outcome is the progression of the midbrain-hindbrain boundary over time, from its formation to the mature structure. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages.
The acetylation of peptidyl-serine to form peptidyl-O-acetyl-L-serine.
The acetylation of peptidyl-serine.
The oxidation of the C alpha-C beta bond of peptidyl-tyrosine to form peptidyl-(Z)-2,3-didehydrotyrosine coupled with cyclization of neighboring residues.
The oxidation of the C alpha-C beta bond of peptidyl-tyrosine to form peptidyl-(E)-2,3-didehydrotyrosine coupled with cyclization of neighboring residues.
The formation of a cluster of several metal atoms, including manganese or calcium, with one or more bridging (mu-bond) oxygen atoms; amino acids residues in proteins that may ligate the metal oxygen cluster are histidine, aspartate, and glutamate.
The incorporation of manganese into a metallo-oxygen cluster.
The incorporation of calcium into a metallo-oxygen cluster.
The incorporation of calcium into a 4Mn-Ca-4O complex by bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide as in the photosystem II catalytic site.
The incorporation of manganese into a 4Mn-Ca-4O complex by bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide as in the photosystem II catalytic site.
Complex that possesses ADPG pyrophosphorylase activity. In all organisms where it has been found, the complex is a tetramer. In bacteria, it is a homotetramer. In plants, the complex is a heterotetramer composed small and large subunits.
A protein complex composed of four identical subunits that possesses ADPG pyrophosphorylase activity. Examples of this component are found in Bacterial species.
A protein complex composed of four different subunits that possesses ADPG pyrophosphorylase activity. An example of this process is found in Mus musculus.
An ADPG pyrophosphorylase complex found in the amyloplast.
An ADPG pyrophosphorylase complex found in the chloroplast.
Any collagen complex which links one collagen assembly, such as a collagen fibril or sheet, to other structures.
Any collagen complex which links one collagen assembly, such as a collagen fibril or sheet, to other structures.
sheet-forming collagen trimer
Any collagen trimer that passes through a lipid bilayer membrane.
A collagen homotrimer of alpha1(XVII) chains; type XVII collagen triple helices span the plasma membrane and associate with hemidesmosomes and the basal lamina where they bind laminin.
A collagen homotrimer of alpha1(XVIII) chains.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a day length that exceeds a particular duration known as the 'critical day length'. The critical day length varies between species. Although the term long-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness falls short of the number of hours defined by 24 hours minus the critical day length.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a day length that exceeds a particular duration known as the 'critical day length'. The critical day length varies between species. Although the term long-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness falls short of the number of hours defined by 24 hours minus the critical day length.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a day length that exceeds a particular duration known as the 'critical day length'. The critical day length varies between species. Although the term long-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness falls short of the number of hours defined by 24 hours minus the critical day length.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a day length that exceeds a particular duration known as the 'critical day length'. The critical day length varies between species. Although the term long-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness falls short of the number of hours defined by 24 hours minus the critical day length.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a day length that falls short of a particular duration known as the 'critical day length'. The critical day length varies between species. Although the term short-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness exceeds the number of hours defined by 24 hours minus the critical day length.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a day length that falls short of a particular duration known as the 'critical day length'. The critical day length varies between species. Although the term short-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness exceeds the number of hours defined by 24 hours minus the critical day length.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a day length that falls short of a particular duration known as the 'critical day length'. The critical day length varies between species. Although the term short-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness exceeds the number of hours defined by 24 hours minus the critical day length.
Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a day length that falls short of a particular duration known as the 'critical day length'. The critical day length varies between species. Although the term short-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness exceeds the number of hours defined by 24 hours minus the critical day length.
Interacting selectively and non-covalently with a chloroplast targeting sequence, a specific peptide sequence that acts as a signal to localize the protein within the chloroplast.
Interacting selectively and non-covalently with an endoplasmic reticulum signal peptide, a specific peptide sequence that acts as a signal to localize the protein within the endoplasmic reticulum.
Interacting selectively and non-covalently with a mitochondrion targeting sequence, a specific peptide sequence that acts as a signal to localize the protein within the mitochondrion.
Interacting selectively and non-covalently with a KDEL sequence, the C terminus tetrapeptide sequence Asp-Asp-Glu-Leu found in proteins that are to be retained in the endoplasmic reticulum.
The catalysis of phosphate removal from a phosphotyrosine using cysteine as a nucleophile and proceed by means of a thiol-phosphate intermediate.
Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate. This reaction requires metal ions.
Any process that modulates the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that modulates the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that modulates the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any process that activates or increases the frequency, rate or extent of vascular endothelial growth factor receptor signaling pathway activity.
Any cellular process that results in the specification, formation or maintenance of polarized actin-based cytoskeletal structures.
Any cellular process that results in the specification, formation or maintenance of polarized microtubule-based cytoskeletal structures.
Any cellular process that results in the specification, formation or maintenance of polarized cytoskeletal structures.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of astral microtubules, any of the spindle microtubules that radiate in all directions from the spindle poles.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of astral microtubules, any of the spindle microtubules that radiate in all directions from the spindle poles.
The 'de novo' formation of an astral microtubule, in which tubulin heterodimers form metastable oligomeric aggregates, some of which go on to support formation of a complete microtubule.
Interacting selectively and non-covalently with potassium (K+) ions.
A protein complex that possesses glutamyl-tRNA(Gln) amidotransferase activity, and therefore creates Gln-tRNA by amidating Glu-tRNA; usually composed of 3 subunits: A, B, and C. Note that the C subunit may not be required in all organisms.
A protein complex that possesses glutamyl-tRNA(Gln) amidotransferase activity, and therefore creates Gln-tRNA by amidating Glu-tRNA; usually composed of 3 subunits: A, B, and C. Note that the C subunit may not be required in all organisms.
A protein complex that possesses glutamyl-tRNA(Gln) amidotransferase activity, and therefore creates Gln-tRNA by amidating Glu-tRNA; usually composed of 3 subunits: A, B, and C. Note that the C subunit may not be required in all organisms.
Interacting selectively and non-covalently with Tat, a viral transactivating regulatory protein from the human immunodeficiency virus, or the equivalent protein from another virus.
A protein complex required for heterochromatin assembly; contains an Argonaute homolog, a chromodomain protein, and at least one additional protein; named for RNA-induced initiation of transcriptional gene silencing.
The modification of two peptidyl-tyrosines to form a 3'-(3'-L-tyrosinyl)-L-tyrosine protein cross-link.
The modification of two peptidyl-tyrosines to form a 3'-(O4'-L-tyrosinyl)-L-tyrosine protein cross-link.
The hydroxylation of peptidyl-arginine to form peptidyl-hydroxyarginine.
The dihydroxylation of peptidyl-arginine to form peptidyl-3,4-dihydroxy-L-arginine.
The dihydroxylation of peptidyl-lysine to peptidyl-4,5-dihydroxy-L-lysine.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone.
The transfer of electrons from NADH to the quinone pool that occurs during oxidative phosphorylation and results in the generation of a proton gradient, mediated by the enzyme known as NADH-quinone oxidoreductase.
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon.
The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon.
The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon.
Interacting selectively and non-covalently with molybdate (MoO4 2-) ions.
The process in which thiamine pyrophosphate is transported across a membrane.
The process in which thiamine pyrophosphate is transported across a membrane.
The process in which thiamine pyrophosphate is transported across a membrane.
The process in which thiamine pyrophosphate is transported across a membrane.
The process in which thiamine pyrophosphate is transported across a membrane.
Interacting selectively and non-covalently with thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.
Interacting selectively and non-covalently with thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.
Interacting selectively and non-covalently with thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
Interacting selectively and non-covalently with thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
Interacting selectively and non-covalently with thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
Interacting selectively and non-covalently with thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
Interacting selectively and non-covalently with thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
Interacting selectively and non-covalently with taurine.
The chemical reactions and pathways involving alpha-glucans, compounds composed of glucose residues linked by alpha-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of alpha-glucans, compounds composed of glucose residues linked by alpha-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of alpha-glucans, compounds composed of glucose residues linked by alpha-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of alpha-glucans, compounds composed of glucose residues linked by alpha-D-glucosidic bonds.
The chemical reactions and pathways resulting in the formation of alpha-glucans, compounds composed of glucose residues linked by alpha-D-glucosidic bonds.
The chemical reactions and pathways resulting in the breakdown of alpha-glucans.
The chemical reactions and pathways resulting in the breakdown of alpha-glucans.
The chemical reactions and pathways resulting in the breakdown of alpha-glucans.
The portion of the microtubule cytoskeleton that lies just beneath the plasma membrane.
A process involved in the controlled movement of a bacterial cell powered by the rearward secretion of carbohydrate slime.
Interacting selectively and non-covalently with double-stranded DNA containing one or more mismatches.
Interacting selectively and non-covalently with double-stranded DNA containing one or more mismatches.
Interacting selectively and non-covalently with double-stranded DNA containing one or more mismatches.
Interacting selectively and non-covalently with a kininogen, any of a group of plasma proteins that are kinin precursors.
Interacting selectively and non-covalently with a kininogen of high molecular mass.
Interacting selectively and non-covalently with a kininogen of high molecular mass.
Interacting selectively and non-covalently with a kininogen of low molecular mass.
Interacting selectively and non-covalently with a kininogen of low molecular mass.
Interacting selectively and non-covalently with a high molecular weight kininogen receptor.
A protein complex that acts as a receptor for high molecular weight kininogens. In humans, this receptor includes the CK1 and uPAR proteins.
Oscillatory movement of the nucleus involved in meiosis I. This oscillatory movement is led by an astral microtubule array emanating from the spindle pole body, and driven by the microtubule motor cytoplasmic dynein.
Oscillatory movement of the nucleus involved in meiosis I. This oscillatory movement is led by an astral microtubule array emanating from the spindle pole body, and driven by the microtubule motor cytoplasmic dynein.
Oscillatory movement of the nucleus involved in meiosis I. This oscillatory movement is led by an astral microtubule array emanating from the spindle pole body, and driven by the microtubule motor cytoplasmic dynein.
A nonmembrane-bound oligomeric protein complex that participates in bidirectional transport of molecules (cargo) along axonemal microtubules.
A nonmembrane-bound oligomeric protein complex that participates in bidirectional transport of molecules (cargo) along axonemal microtubules.
A nonmembrane-bound oligomeric protein complex that participates in bidirectional transport of molecules (cargo) along axonemal microtubules.
The smaller subcomplex of the intraciliary transport particle; characterized complexes have molecular weights of 710-760 kDa.
The smaller subcomplex of the intraciliary transport particle; characterized complexes have molecular weights of 710-760 kDa.
The smaller subcomplex of the intraciliary transport particle; characterized complexes have molecular weights of 710-760 kDa.
The smaller subcomplex of the intraciliary transport particle; characterized complexes have molecular weights of 710-760 kDa.
The larger subcomplex of the intraciliary transport particle; characterized complexes have molecular weights around 550 kDa.
The larger subcomplex of the intraciliary transport particle; characterized complexes have molecular weights around 550 kDa.
The larger subcomplex of the intraciliary transport particle; characterized complexes have molecular weights around 550 kDa.
The larger subcomplex of the intraciliary transport particle; characterized complexes have molecular weights around 550 kDa.
A kinesin complex found in eukaryotic axonemes that contains two distinct plus end-directed kinesin motor proteins and at least one accessory subunit, and that functions in the anterograde transport of molecules (cargo) from the basal body to the distal tip of the axoneme.
Dissolution of the primary septum during cell separation.
Dissolution of the primary septum during cell separation.
Dissolution of the primary septum during cell separation.
The chemical reactions and pathways resulting in the dissolution of the septum edging during cell separation.
The chemical reactions and pathways resulting in the dissolution of the septum edging during cell separation.
The chemical reactions and pathways resulting in the dissolution of the septum edging during cell separation.
The chemical reactions and pathways resulting in the dissolution of the septum edging during cell separation.
Any process that modulates the extent to which the two centrioles within a centrosome remain tightly paired; may be mediated by the assembly and disassembly of a proteinaceous linker.
A proteinaceous scaffold associated with S. pombe chromosomes during meiotic prophase. Linear elements have a structure related to but not equivalent to the synaptonemal complex.
The cell cycle process in which a proteinaceous scaffold, related to the synaptonemal complex, is assembled in association with S. pombe chromosomes during meiotic prophase.
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 caffeine stimulus. Caffeine is an alkaloid found in numerous plant species, where it acts as a natural pesticide that paralyzes and kills certain insects feeding upon them.
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 brefeldin A stimulus.
A cellular structure consisting of parallel, hexagonally arranged actin tubules, comprising filamentous actin and associated proteins. Actin rod structures are found in diverse organisms, having been observed in spores of Dictyostelium discoideum, Drosophila melanogaster oocytes, as well as in numerous animal cells under stress conditions.
A cellular structure, approximately 13 nm in diameter, consisting of three actin filaments bundled together.
Protein complex that carries out the reaction: ATP + H2O + K+(out) = ADP + phosphate + K+(in). It is a high affinity potassium uptake system. The E. coli complex consists of 4 proteins: KdpA is the potassium ion translocase, KdpB is the ATPase, and KdpC and KdpF seem to be involved in assembly and stabilization of the complex.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.
An ADPG pyrophosphorylase complex found in a plastid.
Any nuclear protein complex that contains an ATPase subunit of the imitation switch (ISWI) family. ISWI ATPases are involved in assembling chromatin and in sliding and spacing nucleosomes to regulate transcription of nuclear RNA polymerases I, II, and III and also DNA replication, recombination and repair.
A multisubunit protein complex that contains the Ino80p ATPase; exhibits chromatin remodeling activity and 3' to 5' DNA helicase activity.
A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
Interacting selectively and non-covalently with troponin I, the inhibitory subunit of the troponin complex.
Interacting selectively and non-covalently with troponin T, the tropomyosin-binding subunit of the troponin complex.
The central substructure of the nuclear pore complex (NPC), through which nucleocytoplasmic transport of RNAs, proteins and small molecules occurs. The central transport channel is filled with FG-nucleoporins, which form a selective barrier and provide a series of binding sites for transporter proteins. Characterized S. cerevisiae FG-nucleoporins include Nup159p, Nup145Np, Nup116p, Nup100p, Nsp1p, Nup57p, Nup49p, Nup42p, Nup53p, Nup59p/Asm4p, Nup60p and Nup1. Characterized vertebrate FG-nucleoporins include Nup214, Nup98, Nup62, Nup54, Nup58/45, NLP1, and Nup153.
The central substructure of the nuclear pore complex (NPC), through which nucleocytoplasmic transport of RNAs, proteins and small molecules occurs. The central transport channel is filled with FG-nucleoporins, which form a selective barrier and provide a series of binding sites for transporter proteins. Characterized S. cerevisiae FG-nucleoporins include Nup159p, Nup145Np, Nup116p, Nup100p, Nsp1p, Nup57p, Nup49p, Nup42p, Nup53p, Nup59p/Asm4p, Nup60p and Nup1. Characterized vertebrate FG-nucleoporins include Nup214, Nup98, Nup62, Nup54, Nup58/45, NLP1, and Nup153.
The central substructure of the nuclear pore complex (NPC), through which nucleocytoplasmic transport of RNAs, proteins and small molecules occurs. The central transport channel is filled with FG-nucleoporins, which form a selective barrier and provide a series of binding sites for transporter proteins. Characterized S. cerevisiae FG-nucleoporins include Nup159p, Nup145Np, Nup116p, Nup100p, Nsp1p, Nup57p, Nup49p, Nup42p, Nup53p, Nup59p/Asm4p, Nup60p and Nup1. Characterized vertebrate FG-nucleoporins include Nup214, Nup98, Nup62, Nup54, Nup58/45, NLP1, and Nup153.
The central substructure of the nuclear pore complex (NPC), through which nucleocytoplasmic transport of RNAs, proteins and small molecules occurs. The central transport channel is filled with FG-nucleoporins, which form a selective barrier and provide a series of binding sites for transporter proteins. Characterized S. cerevisiae FG-nucleoporins include Nup159p, Nup145Np, Nup116p, Nup100p, Nsp1p, Nup57p, Nup49p, Nup42p, Nup53p, Nup59p/Asm4p, Nup60p and Nup1. Characterized vertebrate FG-nucleoporins include Nup214, Nup98, Nup62, Nup54, Nup58/45, NLP1, and Nup153.
The process whose specific outcome is the progression of the pancreas over time, from its formation to the mature structure. The pancreas is an endoderm derived structure that produces precursors of digestive enzymes and blood glucose regulating enzymes.
The process whose specific outcome is the progression of the exocrine pancreas over time, from its formation to the mature structure. The exocrine pancreas produces and store zymogens of digestive enzymes, such as chymotrypsinogen and trypsinogen in the acinar cells.
The process whose specific outcome is the progression of the endocrine pancreas over time, from its formation to the mature structure. The endocrine pancreas is made up of islet cells that produce insulin, glucagon and somatostatin.
An mRNA editing complex found in the mitochondrion. The best characterized example is that of Trypanosoma brucei, which catalyzes the insertion and deletion of uridylates.
An mRNA editing complex found in a plastid.
A microtubule organizing center found in interphase cells, which organize a longitudinal array of three to five MT bundles from the nuclear envelope during interphase. Each MT bundle is composed of two to seven MTs arranged in an antiparallel configuration, with the dynamic MT plus ends extending toward the cell tips and stable minus ends near the nucleus.
A microtubule organizing center found in interphase cells, which organize a longitudinal array of three to five MT bundles from the nuclear envelope during interphase. Each MT bundle is composed of two to seven MTs arranged in an antiparallel configuration, with the dynamic MT plus ends extending toward the cell tips and stable minus ends near the nucleus.
A microtubule organizing center found in interphase cells, which organize a longitudinal array of three to five MT bundles from the nuclear envelope during interphase. Each MT bundle is composed of two to seven MTs arranged in an antiparallel configuration, with the dynamic MT plus ends extending toward the cell tips and stable minus ends near the nucleus.
The directed movement of the nucleus along microfilaments within the cell, mediated by motor proteins.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a microtubule organizing center, a structure from which microtubules grow.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a microtubule organizing center, a structure from which microtubules grow.
The aggregation, arrangement and bonding together of a set of components, including gamma-tubulin and other proteins, to form an interphase microtubule organizing center.
The aggregation, arrangement and bonding together of a set of components, including gamma-tubulin and other proteins, to form an interphase microtubule organizing center.
The aggregation, arrangement and bonding together of a set of components, including gamma-tubulin and other proteins, to form an interphase microtubule organizing center.
The aggregation, arrangement and bonding together of a set of components, including gamma-tubulin and other proteins, to form an interphase microtubule organizing center.
The process in which the equatorial microtubule organizing center is disassembled at the end of mitosis.
A complex that possesses glutamate synthase activity.
A protein complex that in yeast consists of a large and a small subunit. Possesses glutamate synthase (NADH) activity.
The series of molecular signals, mediated by the small GTPase Ras, that results in the initiation of contraction of the contractile ring, at the beginning of cytokinesis and cell division by septum formation. The pathway coordinates chromosome segregation with mitotic exit and cytokinesis.
The series of molecular signals, mediated by the small GTPase Ras, that results in the initiation of contraction of the contractile ring, at the beginning of cytokinesis and cell division by septum formation. The pathway coordinates chromosome segregation with mitotic exit and cytokinesis.
The series of molecular signals, mediated by the small GTPase Ras, that results in the initiation of contraction of the contractile ring, at the beginning of cytokinesis and cell division by septum formation. The pathway coordinates chromosome segregation with mitotic exit and cytokinesis.
The series of molecular signals, mediated by the small GTPase Ras, that results in the initiation of contraction of the contractile ring, at the beginning of cytokinesis and cell division by septum formation. The pathway coordinates chromosome segregation with mitotic exit and cytokinesis.
Any process that modulates the frequency, rate or extent of septation initiation signaling.
Any process that modulates the frequency, rate or extent of septation initiation signaling.
Any process that modulates the frequency, rate or extent of septation initiation signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of septation initiation signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of septation initiation signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of septation initiation signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of septation initiation signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of septation initiation signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of septation initiation signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of septation initiation signaling.
Any process that activates or increases the frequency, rate or extent of septation initiation signaling.
Any process that activates or increases the frequency, rate or extent of septation initiation signaling.
Any process that activates or increases the frequency, rate or extent of septation initiation signaling.
Any process that activates or increases the frequency, rate or extent of septation initiation signaling.
Any process that activates or increases the frequency, rate or extent of septation initiation signaling.
Any process that activates or increases the frequency, rate or extent of septation initiation signaling.
Any process that activates or increases the frequency, rate or extent of septation initiation signaling.
Any process that activates or increases the frequency, rate or extent of septation initiation signaling.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures containing both actin and myosin or paramyosin. The myosin may be organized into filaments.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures containing both actin and myosin or paramyosin. The myosin may be organized into filaments.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures containing both actin and myosin or paramyosin. The myosin may be organized into filaments.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a filament composed of myosin molecules.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a filament composed of myosin molecules.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a filament composed of myosin molecules.
The aggregation, arrangement and bonding together of a filament composed of myosin molecules.
The disassembly of a filament composed of myosin molecules.
The formation of a bipolar filament composed of myosin II molecules.
The disassembly of a bipolar filament composed of myosin II molecules.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a bipolar filament composed of myosin II molecules.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a bipolar filament composed of myosin II molecules.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a bipolar filament composed of myosin II molecules.
A membrane-bounded organelle of ciliated protozoan cells that contains polyploid copies of a portion of the cell's complete genome. Transcription of genes occurs in macronuclei. Some ciliate species may contain multiple macronuclei per cell.
A membrane-bounded organelle of ciliated protozoan cells that contains a diploid copy of the cell's complete genome. Sections of contiguous sequence in the macronucleus are often interrupted by internal eliminated sequences (IES), and may be permuted, in micronuclei. Genic transcription is not found in micronuclei. Some ciliate species may contain multiple micronuclei per cell.
The stepwise addition of carbohydrate or carbohydrate derivative residues to the initially added O-linked residue (usually GalNAc) to form the core 5 O-glycan structure, GalNAc-alpha-(1->3)-GalNAc.
The stepwise addition of carbohydrate or carbohydrate derivative residues to the initially added O-linked residue (usually GalNAc) to form the core 6 O-glycan structure, GlcNAc-beta-(1->6)-GalNAc.
The stepwise addition of carbohydrate or carbohydrate derivative residues to the initially added O-linked residue (usually GalNAc) to form the core 7 O-glycan structure, GalNAc-alpha-(1->6)-GalNAc.
The stepwise addition of carbohydrate or carbohydrate derivative residues to the initially added O-linked residue (usually GalNAc) to form the core 8 O-glycan structure, Gal-alpha-(1->3)-GalNAc.
Electron-dense organelle with a granular internal matrix; contains proteins destined to be secreted.
Any process in which RNA molecules inactivate expression of target genes.
Repression of transcription by conversion of large regions of DNA into heterochromatin, directed by small RNAs sharing sequence identity to the repressed region.
Repression of transcription by conversion of large regions of DNA into heterochromatin, directed by small RNAs sharing sequence identity to the repressed region.
Repression of transcription by conversion of large regions of DNA into heterochromatin, directed by small RNAs sharing sequence identity to the repressed region.
Repression of transcription by conversion of large regions of DNA into heterochromatin, directed by small RNAs sharing sequence identity to the repressed region.
Repression of transcription by conversion of large regions of DNA into heterochromatin, directed by small RNAs sharing sequence identity to the repressed region.
Repression of transcription by conversion of large regions of DNA into heterochromatin, directed by small RNAs sharing sequence identity to the repressed region.
Repression of transcription by conversion of large regions of DNA into heterochromatin, directed by small RNAs sharing sequence identity to the repressed region.
The DNA metabolic process in which micronuclear-limited sequences, internal eliminated sequences (IES) and breakage eliminated sequences (BES) are removed from the developing macronucleus (anlage) of a ciliate.
Cleavage of double-stranded RNA molecules by an RNaseIII-family enzyme to produce small RNAs (generally 20-30 nucleotides, depending on species) with biological function.
Cleavage of double-stranded RNA molecules by an RNaseIII-family enzyme to produce small RNAs (generally 20-30 nucleotides, depending on species) with biological function.
Cleavage of noncoding, double-stranded RNAs transcribed from the micronuclear genome to produce scnRNAs, small RNAs (~28 nucleotides) that direct the deletion of micronuclear-limited sequences from the developing macronuclear genome.
Regulated cleavage of the developing macronuclear genome at a limited number of chromosome breakage sites (CBS). The macronuclear destined segment (MDS) sequence adjacent to the CBS (or separated from it by a BES) receives a macronuclear telomere following chromosome breakage.
Any process involved in the conversion of a primary microRNA transcript into a pre-microRNA molecule.
Any process involved in the conversion of a primary microRNA transcript into a pre-microRNA molecule.
Any process involved in the conversion of a pre-microRNA transcript into a mature microRNA molecule.
Dynamic structural changes in centromeric DNA.
Any process that modulates the frequency, rate or extent of the covalent alteration of a histone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent alteration of a histone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent alteration of a histone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent alteration of a histone.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent alteration of a histone.
Any process that activates or increases the frequency, rate or extent of the covalent alteration of a histone.
Any process that activates or increases the frequency, rate or extent of the covalent alteration of a histone.
Any process that activates or increases the frequency, rate or extent of the covalent alteration of a histone.
Any process that activates or increases the frequency, rate or extent of the covalent alteration of a histone.
Any process that activates or increases the frequency, rate or extent of the covalent alteration of a histone.
The removal of acetyl groups from histones in centromeric DNA.
Any process that modulates the frequency, rate or extent of the covalent addition of methyl groups to histones.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent addition of methyl groups to histones.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent addition of methyl groups to histones.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent addition of methyl groups to histones.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent addition of methyl groups to histones.
Any process that activates or increases the frequency, rate or extent of the covalent addition of methyl groups to histones.
Any process that activates or increases the frequency, rate or extent of the covalent addition of methyl groups to histones.
Any process that activates or increases the frequency, rate or extent of the covalent addition of methyl groups to histones.
Any process that activates or increases the frequency, rate or extent of the covalent addition of methyl groups to histones.
Any process that activates or increases the frequency, rate or extent of the covalent addition of methyl groups to histones.
Any process that modulates the frequency, rate or extent of the removal of acetyl groups from histones.
Any process that stops, prevents, or reduces the frequency, rate or extent of the removal of acetyl groups from histones.
Any process that stops, prevents, or reduces the frequency, rate or extent of the removal of acetyl groups from histones.
Any process that stops, prevents, or reduces the frequency, rate or extent of the removal of acetyl groups from histones.
Any process that stops, prevents, or reduces the frequency, rate or extent of the removal of acetyl groups from histones.
Any process that activates or increases the frequency, rate or extent of the removal of acetyl groups from histones.
Any process that activates or increases the frequency, rate or extent of the removal of acetyl groups from histones.
Any process that activates or increases the frequency, rate or extent of the removal of acetyl groups from histones.
Any process that activates or increases the frequency, rate or extent of the removal of acetyl groups from histones.
Any process that activates or increases the frequency, rate or extent of the removal of acetyl groups from histones.
Any process that modulates the frequency, rate or extent of the removal of acetyl groups from histones in centromeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the removal of acetyl groups to histones in centromeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the removal of acetyl groups to histones in centromeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the removal of acetyl groups to histones in centromeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the removal of acetyl groups to histones in centromeric DNA.
Any process that activates or increases the frequency, rate or extent of the removal of acetyl groups from histones in centromeric DNA.
Any process that activates or increases the frequency, rate or extent of the removal of acetyl groups from histones in centromeric DNA.
Any process that activates or increases the frequency, rate or extent of the removal of acetyl groups from histones in centromeric DNA.
Any process that activates or increases the frequency, rate or extent of the removal of acetyl groups from histones in centromeric DNA.
Any process that activates or increases the frequency, rate or extent of the removal of acetyl groups from histones in centromeric DNA.
The process in which the anatomical structures of the hair follicle are generated and organized.
The biogenesis of a snoRNA molecule which resides within, and is processed from, the intron of a pre-mRNA.
Catalysis of the reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine.
Catalysis of the reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine.
Catalysis of the reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine.
Catalysis of the reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine.
Catalysis of the reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine.
Catalysis of the hydroxylation of cholesterol at position 26 of the side chain, to produce 26-hydroxycholesterol.
Any complex that acts to move proteins or RNAs into or out of the nucleus through nuclear pores.
The process occurring during the embryonic phase whose specific outcome is the progression of the eye over time, from its formation to the mature structure.
The process occurring during the post-embryonic phase whose specific outcome is the progression of the camera-type eye over time, from its formation to the mature structure.
Catalysis of the reaction: histone H3 N6-acetyl-L-lysine (position 14) + H2O = histone H3 L-lysine (position 14) + acetate. This reaction represents the removal of an acetyl group from lysine at position 14 of the histone H3 protein.
A subcomplex of the nuclear pore complex (NPC) that forms the outer rings of the core scaffold, a lattice-like structure that gives the NPC its shape and strength. In S. cerevisiae, the two outer rings each contain multiple copies of the following proteins: Nup133p, Nup120p, Nup145Cp, Nup85p, Nup84p, Seh1p, and Sec13p. In vertebrates, the two outer rings each contain multiple copies of the following proteins: Nup133, Nup160, Nup96, Nup75, Nup107, Seh1, Sec13, Nup43, Nup37, and ALADIN. Components are arranged in 8-fold symmetrical 'spokes' around the central transport channel. A single 'spoke', can be isolated and is sometimes referred to as the Nup84 complex (S. cerevisiae) or the Nup107-160 complex (vertebrates).
A subcomplex of the nuclear pore complex (NPC) that forms the outer rings of the core scaffold, a lattice-like structure that gives the NPC its shape and strength. In S. cerevisiae, the two outer rings each contain multiple copies of the following proteins: Nup133p, Nup120p, Nup145Cp, Nup85p, Nup84p, Seh1p, and Sec13p. In vertebrates, the two outer rings each contain multiple copies of the following proteins: Nup133, Nup160, Nup96, Nup75, Nup107, Seh1, Sec13, Nup43, Nup37, and ALADIN. Components are arranged in 8-fold symmetrical 'spokes' around the central transport channel. A single 'spoke', can be isolated and is sometimes referred to as the Nup84 complex (S. cerevisiae) or the Nup107-160 complex (vertebrates).
A subcomplex of the nuclear pore complex (NPC) that forms the outer rings of the core scaffold, a lattice-like structure that gives the NPC its shape and strength. In S. cerevisiae, the two outer rings each contain multiple copies of the following proteins: Nup133p, Nup120p, Nup145Cp, Nup85p, Nup84p, Seh1p, and Sec13p. In vertebrates, the two outer rings each contain multiple copies of the following proteins: Nup133, Nup160, Nup96, Nup75, Nup107, Seh1, Sec13, Nup43, Nup37, and ALADIN. Components are arranged in 8-fold symmetrical 'spokes' around the central transport channel. A single 'spoke', can be isolated and is sometimes referred to as the Nup84 complex (S. cerevisiae) or the Nup107-160 complex (vertebrates).
Any process that establishes the spatial arrangement of nuclear pores within the nuclear envelope.
Any of several protein complexes required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes, platelet dense granules, and other related organelles; acronym for biogenesis of lysosomal-related organelles complex.
A protein complex required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. Many of the protein subunits are conserved between mouse and human; the mouse complex contains the Pallidin, Muted, Cappuccino, Dysbindin, Snapin, BLOS1, BLOS2, AND BLOS3 proteins.
A protein complex required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. The human complex contains the Hps3, Hps5, and Hps6 proteins; the mouse complex contains ru2 and ru.
A protein complex required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. The human complex contains the Hps1 and Hps4 proteins.
A pathway of degradation of nuclear-transcribed mRNAs that proceeds through a series of steps that is independent of deadenylation, but requires decapping followed by transcript decay, and that can regulate mRNA stability.
A pathway of degradation of nuclear-transcribed mRNAs that proceeds through a series of steps that is independent of deadenylation, but requires decapping followed by transcript decay, and that can regulate mRNA stability.
A pathway of degradation of nuclear-transcribed mRNAs that proceeds through a series of steps that is independent of deadenylation, but requires decapping followed by transcript decay, and that can regulate mRNA stability.
A pathway of degradation of nuclear-transcribed mRNAs that proceeds through a series of steps that is independent of deadenylation, but requires decapping followed by transcript decay, and that can regulate mRNA stability.
A pathway of degradation of nuclear-transcribed mRNAs that proceeds through a series of steps that is independent of deadenylation, but requires decapping followed by transcript decay, and that can regulate mRNA stability.
A pathway of degradation of nuclear-transcribed mRNAs that proceeds through a series of steps that is independent of deadenylation, but requires decapping followed by transcript decay, and that can regulate mRNA stability.
A pathway of degradation of nuclear-transcribed mRNAs that proceeds through a series of steps that is independent of deadenylation, but requires decapping followed by transcript decay, and that can regulate mRNA stability.
A pathway of degradation of nuclear-transcribed mRNAs that proceeds through a series of steps that is independent of deadenylation, but requires decapping followed by transcript decay, and that can regulate mRNA stability.
A pathway of degradation of nuclear-transcribed mRNAs that proceeds through a series of steps that is independent of deadenylation, but requires decapping followed by transcript decay, and that can regulate mRNA stability.
A pathway of degradation of nuclear-transcribed mRNAs that proceeds through a series of steps that is independent of deadenylation, but requires decapping followed by transcript decay, and that can regulate mRNA stability.
Cleavage of the 5'-cap of a nuclear-transcribed mRNA that is independent of poly(A) tail shortening.
Cleavage of the 5'-cap of a nuclear-transcribed mRNA that is independent of poly(A) tail shortening.
The lipid bilayer surrounding the platelet dense granule.
The volume enclosed by the membrane of the platelet dense granule.
A membrane that is one of the two lipid bilayers of an organelle envelope or the outermost membrane of single membrane bound organelle.
A secretory organelle found in blood platelets, which is unique in that it exhibits further compartmentalization and acquires its protein content via two distinct mechanisms: (1) biosynthesis predominantly at the megakaryocyte (MK) level (with some vestigial platelet synthesis) (e.g. platelet factor 4) and (2) endocytosis and pinocytosis at both the MK and circulating platelet levels (e.g. fibrinogen (Fg) and IgG).
The lipid bilayer surrounding the platelet alpha granule.
The volume enclosed by the membrane of the platelet alpha granule.
A network of membrane-bounded compartments found in blood platelets, where they regulate platelet activation by sequestering or releasing calcium. The dense tubular network exists as thin elongated membranes in resting platelets, and undergoes a major ultrastructural change, to a rounded vesicular form, upon addition of thrombin.
The lipid bilayer surrounding the platelet dense tubular network.
The volume enclosed by the membranes of the platelet dense tubular network.
A medial cortical band overlaying the nucleus which acts as a landmark for contractile ring positioning and plays a role in cell cycle regulation.
A series of molecular signals in which a stress-activated protein kinase (SAPK) cascade relays one or more of the signals.
A series of molecular signals in which a stress-activated protein kinase (SAPK) cascade relays one or more of the signals.
A series of molecular signals in which a stress-activated protein kinase (SAPK) cascade relays one or more of the signals.
A series of molecular signals in which a stress-activated protein kinase (SAPK) cascade relays one or more of the signals.
A series of molecular signals in which a stress-activated protein kinase (SAPK) cascade relays one or more of the signals.
A series of molecular signals in which a stress-activated protein kinase (SAPK) cascade relays one or more of the signals.
The regrowth of a lost or destroyed body part, such as an organ or tissue. This process may occur via renewal, repair, and/or growth alone (i.e. increase in size or mass).
The regrowth of a lost or destroyed animal organ.
The regrowth of fin tissue following its loss or destruction.
The regrowth of neuronal processes such as axons or dendrites in response to their loss or damage.
The regrowth of axons following their loss or damage.
The regrowth of dendrites in response to their loss or damage.
A protein complex containing septins.  Typically, these complexes contain multiple septins and are oligomeric.
Control of the formation, spatial distribution, and breakdown of the septin ring.
The controlled breakdown of a septin ring.
The chemical reactions and pathways resulting in the formation of holo-[acyl-carrier protein].
The chemical reactions and pathways resulting in the formation of holo-[acyl-carrier protein].
The chemical reactions and pathways resulting in the formation of holo-[acyl-carrier protein].
The chemical reactions and pathways resulting in the formation of holo-[acyl-carrier protein].
The chemical reactions and pathways resulting in the formation of holo-[acyl-carrier protein].
Assembly or disassembly of microtubules by the addition or removal of tubulin heterodimers from a microtubule.
Any process that modulates the frequency, rate or extent of microtubule polymerization or depolymerization by the addition or removal of tubulin heterodimers from a microtubule.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule polymerization or depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule polymerization or depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule polymerization or depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule polymerization or depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule polymerization or depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule polymerization or depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule polymerization or depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule polymerization or depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule polymerization or depolymerization.
Any process that modulates the frequency, rate or extent of microtubule polymerization.
Any process that modulates the frequency, rate or extent of microtubule depolymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule polymerization.
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule polymerization.
Any process that activates or increases the frequency, rate or extent of microtubule polymerization.
Any process that activates or increases the frequency, rate or extent of microtubule polymerization.
Any process that activates or increases the frequency, rate or extent of microtubule polymerization.
Any process that activates or increases the frequency, rate or extent of microtubule polymerization.
Any process that activates or increases the frequency, rate or extent of microtubule polymerization.
Any process that activates or increases the frequency, rate or extent of microtubule depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule depolymerization.
Any process that activates or increases the frequency, rate or extent of microtubule depolymerization.
The intramolecular conversion of uridine to pseudouridine in an rRNA molecule.
The intramolecular conversion of uridine to pseudouridine in a tRNA molecule.
The intramolecular conversion of uridine to pseudouridine in an snRNA molecule.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of structures formed of microtubules and associated proteins at the midpoint of a cell.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of structures formed of microtubules and associated proteins at the midpoint of a cell.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of structures formed of microtubules and associated proteins in the cytoplasm of a cell.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of structures formed of microtubules and associated proteins in the cytoplasm of a cell.
Any process involved in forming the mature 3' end of an RNA molecule.
Any process involved in forming the mature 3' end of an mRNA molecule.
Any process involved in forming the mature 3' end of an rRNA molecule.
Any process involved in forming the mature 3' end of a snoRNA molecule.
Catalysis of the transfer of an L-fucosyl group from GDP-beta-L-fucose to an acceptor molecule to form an alpha-(1->2) linkage.
Catalysis of the transfer of an L-fucosyl group from GDP-beta-L-fucose to an acceptor molecule to form an alpha-(1->2) linkage.
A developmental process involving two tissues in which one tissue (the inducer) produces a signal that directs cell fate commitment of cells in the second tissue (the responder).
Signaling at short range between cells of different ancestry and developmental potential that results in one cell or group of cells effecting a developmental change in the other. This is often done by secretion of proteins by one cell which affects the neighboring cells and causes them to adopt a certain fate.
The process in which one cell or group of cells receives, transduces, and responds to a signal generated by another cell or group of cells of different ancestry and developmental potential, such that the recipient cell(s) undergo a developmental change.
Catalysis of the reaction: L-serine + NADP(+) = L-alpha-formylglycine + 2 H(+) + NADPH.
Any process that modulates the rate, direction or extent of axon growth such that the correct diameter is attained and maintained.
The cell cycle process in which sister chromatids establish stable attachments to microtubules emanating from opposite spindle poles.
The cell cycle process in which sister chromatids establish stable attachments to microtubules emanating from opposite spindle poles.
Any process that decreases the rate of conjugation.
Any process that decreases the rate of conjugation.
Any process that decreases the rate of conjugation.
Any process that decreases the rate of conjugation.
Any process that increases the rate or frequency of conjugation.
Any process that increases the rate or frequency of conjugation.
Any process that increases the rate or frequency of conjugation.
Any process that increases the rate or frequency of conjugation.
Any process that increases the rate or frequency of conjugation.
Any process that modulates the rate or frequency of conjugation with cellular fusion.
Any process that decreases the rate or frequency of conjugation with cellular fusion.
Any process that decreases the rate or frequency of conjugation with cellular fusion.
Any process that decreases the rate or frequency of conjugation with cellular fusion.
Any process that decreases the rate or frequency of conjugation with cellular fusion.
Any process that increases the rate or frequency of conjugation with cellular fusion.
Any process that increases the rate or frequency of conjugation with cellular fusion.
Any process that increases the rate or frequency of conjugation with cellular fusion.
Any process that increases the rate or frequency of conjugation with cellular fusion.
Any process that increases the rate or frequency of conjugation with cellular fusion.
The process in which a cell initiates conjugation with cellular fusion upon starvation for one or more nutrients.
The process in which a cell initiates conjugation with cellular fusion upon carbon starvation.
The process in which a cell initiates conjugation with cellular fusion upon nitrogen starvation.
A temporary protrusion or retractile process of a cell, associated with flowing movements of the protoplasm, and serving for locomotion and feeding.
Any process in which the proteasome is transported to, or maintained in, a specific location.
Any process in which the proteasome is transported to, or maintained in, a specific location.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by the anaphase-promoting complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by an SCF (Skp1/Cul1/F-box protein) complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by an SCF (Skp1/Cul1/F-box protein) complex, and mediated by the proteasome.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by an SCF (Skp1/Cul1/F-box protein) complex, and mediated by the proteasome.
The chemical reactions and pathways involving 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one, also known as DIF-1, differentiation-inducing factor-1. DIF-1 is a secreted chlorinated molecule that controls cell fate during development of Dictyostelium cells.
The chemical reactions and pathways involving 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one, also known as DIF-1, differentiation-inducing factor-1. DIF-1 is a secreted chlorinated molecule that controls cell fate during development of Dictyostelium cells.
The chemical reactions and pathways involving 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one, also known as DIF-1, differentiation-inducing factor-1. DIF-1 is a secreted chlorinated molecule that controls cell fate during development of Dictyostelium cells.
The chemical reactions and pathways resulting in the formation of 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one, also known as DIF-1, differentiation-inducing factor-1. DIF-1 is a secreted chlorinated molecule that controls cell fate during development of Dictyostelium cells.
The chemical reactions and pathways resulting in the formation of 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one, also known as DIF-1, differentiation-inducing factor-1. DIF-1 is a secreted chlorinated molecule that controls cell fate during development of Dictyostelium cells.
The chemical reactions and pathways resulting in the formation of 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one, also known as DIF-1, differentiation-inducing factor-1. DIF-1 is a secreted chlorinated molecule that controls cell fate during development of Dictyostelium cells.
The chemical reactions and pathways resulting in the formation of 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one, also known as DIF-1, differentiation-inducing factor-1. DIF-1 is a secreted chlorinated molecule that controls cell fate during development of Dictyostelium cells.
The chemical reactions and pathways resulting in the formation of 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one, also known as DIF-1, differentiation-inducing factor-1. DIF-1 is a secreted chlorinated molecule that controls cell fate during development of Dictyostelium cells.
The chemical reactions and pathways resulting in the formation of 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one, also known as DIF-1, differentiation-inducing factor-1. DIF-1 is a secreted chlorinated molecule that controls cell fate during development of Dictyostelium cells.
The process in which a relatively unspecialized cell acquires specialized features of a sorocarp stalk cell, any of the cellulose-covered cells that form the stalk of a sorocarp. An example of this process is found in Dictyostelium discoideum.
The process whose specific outcome is the progression of the sorocarp stalk over time, from its formation to the mature structure. 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.
The process whose specific outcome is the progression of the sorocarp stalk over time, from its formation to the mature structure. 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.
The process whose specific outcome is the progression of the sorocarp stalk over time, from its formation to the mature structure. 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 reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 79) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 79). This reaction is the addition of a methyl group onto lysine at position 79 of the histone H3 protein.
Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 79) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 79). This reaction is the addition of a methyl group onto lysine at position 79 of the histone H3 protein.
The process whose specific outcome is the progression of the aggregate over time, from its formation to the point when a slug is formed. Aggregate development begins in response to starvation and continues by the chemoattractant-mediated movement of cells toward each other. The aggregate is a multicellular structure that gives rise to the slug.
The process whose specific outcome is the progression of the aggregate over time, from its formation to the point when a slug is formed. Aggregate development begins in response to starvation and continues by the chemoattractant-mediated movement of cells toward each other. The aggregate is a multicellular structure that gives rise to the slug.
The process whose specific outcome is the progression of the slug over time, from its formation to the mature structure. Slug development begins when the aggregate rises upwards to form a finger-shaped structure and ends when culmination begins. Slug development begins after aggregation and ends before culmination in sorocarp development.
The process whose specific outcome is the progression of the slug over time, from its formation to the mature structure. Slug development begins when the aggregate rises upwards to form a finger-shaped structure and ends when culmination begins. Slug development begins after aggregation and ends before culmination in sorocarp development.
The process whose specific outcome is the progression of the slug over time, from its formation to the mature structure. Slug development begins when the aggregate rises upwards to form a finger-shaped structure and ends when culmination begins. Slug development begins after aggregation and ends before culmination in sorocarp development.
The process whose specific outcome is the progression of the slug over time, from its formation to the mature structure. Slug development begins when the aggregate rises upwards to form a finger-shaped structure and ends when culmination begins. Slug development begins after aggregation and ends before culmination in sorocarp development.
The process whose specific outcome is the progression of the slug over time, from its formation to the mature structure. Slug development begins when the aggregate rises upwards to form a finger-shaped structure and ends when culmination begins. Slug development begins after aggregation and ends before culmination in sorocarp development.
The process whose specific outcome is the progression of the slug over time, from its formation to the mature structure. Slug development begins when the aggregate rises upwards to form a finger-shaped structure and ends when culmination begins. Slug development begins after aggregation and ends before culmination in sorocarp development.
The process whose specific outcome is the progression of the culminant over time, from its formation to the mature structure. Culmination begins with a morphogenetic change of the finger-like or migratory slug giving rise to an organized structure containing a stalk and a sorus. This process is the final stage of sorocarp development.
The process whose specific outcome is the progression of the culminant over time, from its formation to the mature structure. Culmination begins with a morphogenetic change of the finger-like or migratory slug giving rise to an organized structure containing a stalk and a sorus. This process is the final stage of sorocarp development.
The process whose specific outcome is the progression of the culminant over time, from its formation to the mature structure. Culmination begins with a morphogenetic change of the finger-like or migratory slug giving rise to an organized structure containing a stalk and a sorus. This process is the final stage of sorocarp development.
Any process that modulates the frequency, rate or extent of reproductive fruiting body development.
Any process that modulates the frequency, rate or extent of sorocarp development. An example of this process is found in Dictyostelium discoideum.
Any process that modulates the frequency, rate or extent of sorocarp development. An example of this process is found in Dictyostelium discoideum.
Any process that modulates the size of the aggregate formed during sorocarp formation.
Any process that modulates the size of the aggregate formed during sorocarp formation.
Any process that decreases the size of the aggregate formed during sorocarp formation.
Any process that decreases the size of the aggregate formed during sorocarp formation.
Any process that decreases the size of the aggregate formed during sorocarp formation.
Any process that decreases the size of the aggregate formed during sorocarp formation.
Any process that increases the size of the aggregate formed during sorocarp formation.
Any process that increases the size of the aggregate formed during sorocarp formation.
Any process that increases the size of the aggregate formed during sorocarp formation.
Any process that increases the size of the aggregate formed during sorocarp formation.
Any process that increases the size of the aggregate formed during sorocarp formation.
The specialized envelope lying outside the cell membrane of a spore.
The chemical reactions and pathways resulting in the breakdown of phosphatidylinositol, any glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the breakdown of phosphatidylinositol, any glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the breakdown of phosphatidylinositol, any glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the breakdown of phosphatidylinositol, any glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The chemical reactions and pathways resulting in the breakdown of phosphatidylinositol, any glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
The incorporation of exogenous sulfur into a metallo-sulfur cluster.
The incorporation of a metal and exogenous sulfur into a metallo-sulfur cluster.
The incorporation of a metal and exogenous sulfur into a metallo-sulfur cluster.
The incorporation of a metal and exogenous sulfur into a metallo-sulfur cluster.
The lipid bilayer surrounding the contractile vacuole.
The component of the contractile vacuolar membrane consisting of gene products that have some part that penetrates at least one leaflet of the membrane bilayer. This component includes gene products that are buried in the bilayer with no exposure outside the bilayer.
The component of the vacuolar membrane consisting of gene products and protein complexes that have some part that penetrates at least one leaflet of the membrane bilayer. May also refer to the state of being buried in the bilayer with no exposure outside the bilayer.
The posttranscriptional addition of methyl groups to specific residues in an rRNA molecule.
The chemical reactions and pathways involving a ferrichrome. 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 chemical reactions and pathways resulting in the formation of a ferrichrome. 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 chemical reactions and pathways resulting in the formation of a ferrichrome. 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 chemical reactions and pathways resulting in the formation of a ferrichrome. 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 chemical reactions and pathways resulting in the formation of a ferrichrome. 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 chemical reactions and pathways resulting in the formation of a ferrichrome. 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 chemical reactions and pathways resulting in the formation of a ferrichrome. 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 chemical reactions and pathways resulting in the formation of a ferrichrome. 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 chemical reactions and pathways resulting in the formation of a ferrichrome. 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 chemical reactions and pathways involving ferricrocin, a cyclic hexapeptide siderophore with the structure Gly-Ser-Gly-(N5-acetyl-N5-hydroxyornithine)3.
The chemical reactions and pathways resulting in the formation of ferricrocin, a cyclic hexapeptide siderophore with the structure Gly-Ser-Gly-(N5-acetyl-N5-hydroxyornithine)3.
The chemical reactions and pathways resulting in the formation of ferricrocin, a cyclic hexapeptide siderophore with the structure Gly-Ser-Gly-(N5-acetyl-N5-hydroxyornithine)3.
The chemical reactions and pathways resulting in the formation of ferricrocin, a cyclic hexapeptide siderophore with the structure Gly-Ser-Gly-(N5-acetyl-N5-hydroxyornithine)3.
The chemical reactions and pathways resulting in the formation of ferricrocin, a cyclic hexapeptide siderophore with the structure Gly-Ser-Gly-(N5-acetyl-N5-hydroxyornithine)3.
The chemical reactions and pathways resulting in the formation of ferricrocin, a cyclic hexapeptide siderophore with the structure Gly-Ser-Gly-(N5-acetyl-N5-hydroxyornithine)3.
The chemical reactions and pathways resulting in the formation of ferricrocin, a cyclic hexapeptide siderophore with the structure Gly-Ser-Gly-(N5-acetyl-N5-hydroxyornithine)3.
The chemical reactions and pathways resulting in the formation of ferricrocin, a cyclic hexapeptide siderophore with the structure Gly-Ser-Gly-(N5-acetyl-N5-hydroxyornithine)3.
The chemical reactions and pathways resulting in the formation of ferricrocin, a cyclic hexapeptide siderophore with the structure Gly-Ser-Gly-(N5-acetyl-N5-hydroxyornithine)3.
Catalysis of the reaction: L-ornithine + O2 + H+ = N5-hydroxy-L-ornithine + H2O.
The formation of otoliths during embryogenesis with completion in early postembryonic development. Formation occurs by precipitation of specific crystal forms of calcium carbonate around an organic core of extracellular matrix proteins. Otoconia (otoliths) are small (~10 micron) dense extracellular particles present in the otolith end organs of the vertebrate inner ear.
The formation of otoliths during embryogenesis with completion in early postembryonic development. Formation occurs by precipitation of specific crystal forms of calcium carbonate around an organic core of extracellular matrix proteins. Otoconia (otoliths) are small (~10 micron) dense extracellular particles present in the otolith end organs of the vertebrate inner ear.
The formation and growth of otoliths throughout the life of the organism. Otoliths are the large extracellular ear-stones of the fish inner ear, produced by precipitation of specific crystal forms of calcium carbonate on organic matrices. The otolith enlarges throughout the life of the fish, as layers of calcium carbonate are added.
The process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
The process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
The process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
The process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
The process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Catalysis of the endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Interacting selectively and non-covalently with phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).
The covalent alteration of one or more amino acid residues within a peptide, resulting in a change in the properties of that peptide.
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. One well-characterized example is the neuronal SNARE complex formed of synaptobrevin 2, syntaxin 1a, and SNAP-25.
The process in which the signal sequence of a translated protein binds to and forms a complex with the Sec complex.
The process in which the signal sequence of a translated protein binds to and forms a complex with the Sec complex.
The process in which the signal sequence of a translated protein binds to and forms a complex with the Sec complex.
The process in which a protein translocates through the ER membrane posttranslationally.
The process in which a protein translocates through the ER membrane posttranslationally.
An endoplasmic reticulum membrane-associated complex involved in the translocation of proteins that are targeted to the ER. In yeast, this complex consists of two subcomplexes, namely, the Sec61 complex and the Sec62/Sec63 complex.
A protein complex involved in the posttranslational targeting of proteins to the ER. In yeast, it is a tetrameric complex consisting of Sec62p, Sec63p, Sec71p and Sec72p.
A protein complex involved in the posttranslational targeting of proteins to the ER. In yeast, it is a tetrameric complex consisting of Sec62p, Sec63p, Sec71p and Sec72p.
Interacting selectively and non-covalently with a POZ (poxvirus and zinc finger) domain of a protein, a protein-protein interaction domain found in many transcription factors.
Interacting selectively and non-covalently with a POZ (poxvirus and zinc finger) domain of a protein, a protein-protein interaction domain found in many transcription factors.
A pentameric complex that includes orthologues of human PIR121, Nap1, Abi, SCAR, and HSPC300 and regulates actin polymerization and/or depolymerization through small GTPase mediated signal transduction.
A pentameric complex that includes orthologues of human PIR121, Nap1, Abi, SCAR, and HSPC300 and regulates actin polymerization and/or depolymerization through small GTPase mediated signal transduction.
A pentameric complex that includes orthologues of human PIR121, Nap1, Abi, SCAR, and HSPC300 and regulates actin polymerization and/or depolymerization through small GTPase mediated signal transduction.
Interacting selectively and non-covalently with phosphatidylcholine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of choline.
A complex of the endoplasmic reticulum that catalyzes S-palmitoylation, the addition of palmitate (C16:0) or other long-chain fatty acids to proteins at a cysteine residue.
An ISWI complex that contains an ATPase subunit of the ISWI family (SNF2H in mammals) and an RSF1 homolog. It mediates nucleosome deposition and generates regularly spaced nucleosome arrays. In mammals, RSF is involved in regulation of transcription from RNA polymerase II promoters).
Formation of hard tissues that consist mainly of inorganic compounds, and also contain a small amounts of organic matrices that are believed to play important roles in their formation.
Formation of hard tissues that consist mainly of inorganic compounds, and also contain a small amounts of organic matrices that are believed to play important roles in their formation.
Formation of hard tissues that consist mainly of inorganic compounds, and also contain a small amounts of organic matrices that are believed to play important roles in their formation.
The precipitation of calcium carbonate onto the organic matrix of a shell, such as a mollusc shell.
Catalysis of the hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).
Catalysis of the hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).
Catalysis of the hydrolysis of (1->4) linkages in (1->4)-beta-D-glucans, to remove successive glucose units.
Catalysis of the hydrolysis of (1->4) linkages in (1->4)-beta-D-glucans, to remove successive glucose units.
Catalysis of the hydrolysis of (1->4) linkages in (1->4)-beta-D-glucans, to remove successive glucose units.
Catalysis of the hydrolysis of (1->4) linkages in (1->4)-beta-D-glucans, to remove successive glucose units.
Catalysis of the hydrolysis of (1->4) linkages in (1->4)-beta-D-glucans, to remove successive glucose units.
Catalysis of the hydrolysis of (1->4) linkages in (1->4)-beta-D-glucans, to remove successive glucose units.
Catalysis of the hydrolysis of (1->4) linkages in (1->4)-beta-D-glucans, to remove successive glucose units.
Catalysis of the hydrolysis of (1->4) linkages in (1->4)-beta-D-glucans, to remove successive glucose units.
Catalysis of the hydrolysis of (1->4) linkages in (1->4)-beta-D-glucans, to remove successive glucose units.
Catalysis of the endohydrolysis of (1->4)-beta-D-galactosidic linkages in arabinogalactans.
Catalysis of the endohydrolysis of (1->4)-beta-D-galactosidic linkages in arabinogalactans.
Catalysis of the endohydrolysis of (1->4)-beta-D-galactosidic linkages in arabinogalactans.
Catalysis of the endohydrolysis of (1->4)-beta-D-galactosidic linkages in arabinogalactans.
Catalysis of the random hydrolysis of 2,6-beta-D-fructofuranosidic linkages in 2,6-beta-D-fructans (levans) containing more than 3 fructose units.
Catalysis of the random hydrolysis of 2,6-beta-D-fructofuranosidic linkages in 2,6-beta-D-fructans (levans) containing more than 3 fructose units.
Catalysis of the reaction: maltodextrin = glucose-1-phosphate.
The chemical reactions and pathways involving arabinan, a polysaccharide composed of arabinose residues.
The chemical reactions and pathways resulting in the breakdown of arabinan, a polysaccharide composed of arabinose residues.
The chemical reactions and pathways resulting in the breakdown of arabinan, a polysaccharide composed of arabinose residues.
The chemical reactions and pathways resulting in the breakdown of arabinan, a polysaccharide composed of arabinose residues.
The behavior of an organism in response to a sound.
The behavior of an organism in response to a sound.
The behavior of an organism in response to a sound.
The component of a membrane consisting of the gene products having some covalently attached portion, for example part of a peptide sequence or some other covalently attached group such as a GPI anchor, which spans or is embedded in one or both leaflets of the membrane.
The component of the plasma 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 endoplasmic reticulum 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 Golgi 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 nuclear inner 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 cell 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 peroxisomal 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 a plasma 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 a plasma 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 a plasma membrane consisting of gene products and protein complexes that penetrate the external side of the plasma membrane only, either directly or via some covalently attached hydrophobic anchor.
The component of a plasma membrane consisting of gene products and protein complexes that penetrate the external side of the plasma membrane only, either directly or via some covalently attached hydrophobic anchor.
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region.
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region.
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region.
The component of a plasma membrane consisting of gene products and protein complexes that have some covalently attached part (e.g. peptide sequence or GPI anchor) which is embedded in the cytoplasmic side of the plasma membrane only.
The component of a plasma membrane consisting of gene products and protein complexes that have some covalently attached part (e.g. peptide sequence or GPI anchor) which is embedded in the cytoplasmic side of the plasma membrane only.
The component of a plasma membrane consisting of gene products and protein complexes that have some covalently attached part (e.g. peptide sequence or GPI anchor) which is embedded in the cytoplasmic side of the plasma membrane only.
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its periplasmic surface, but not integrated into the hydrophobic region.
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its periplasmic surface, but not integrated into the hydrophobic region.
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its periplasmic surface, but not integrated into the hydrophobic region.
The component of a plasma membrane consisting of gene products and protein complexes that penetrate the periplasmic side of the plasma membrane only, either directly or via some covalently attached hydrophobic anchor.
The component of a plasma membrane consisting of gene products and protein complexes that penetrate the periplasmic side of the plasma membrane only, either directly or via some covalently attached hydrophobic anchor.
The component of a plasma membrane consisting of gene products and protein complexes that penetrate the periplasmic side of the plasma membrane only, either directly or via some covalently attached hydrophobic anchor.
The side of the outer membrane that is opposite to the side that faces the periplasm of the cell.
The side of the outer membrane that is opposite to the side that faces the periplasm of the cell.
The side (leaflet) of the outer membrane that faces the periplasm of the cell.
The side (leaflet) of the outer membrane that faces the periplasm of the cell.
The side (leaflet) of the outer membrane that faces the periplasm of the cell.
The component of a cell outer 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 a cell outer 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 a cell outer 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 the cell outer membrane consisting of the gene products and protein complexes that penetrate the external side of the cell outer membrane only, either directly or via some covalently attached hydrophobic anchor.
The component of the cell outer membrane consisting of the gene products and protein complexes that penetrate the external side of the cell outer membrane only, either directly or via some covalently attached hydrophobic anchor.
The component of the cell outer membrane consisting of the gene products and protein complexes that penetrate the external side of the cell outer membrane only, either directly or via some covalently attached hydrophobic anchor.
The component of the cell 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 the cell outer membrane consisting of gene products and protein complexes that are loosely bound to periplasmic surface, but not integrated into the hydrophobic region.
The component of the cell outer membrane consisting of gene products and protein complexes that are loosely bound to periplasmic surface, but not integrated into the hydrophobic region.
The component of the cell outer membrane consisting of gene products and protein complexes that are loosely bound to periplasmic surface, but not integrated into the hydrophobic region.
The component of the cell outer membrane consisting of gene products and protein complexes that are loosely bound to periplasmic surface, but not integrated into the hydrophobic region.
The component of the cell outer membrane consisting of the gene products that that penetrate the periplasmic side of the cell outer membrane only, either directly or via some covalently attached hydrophobic anchor.
The component of the cell outer membrane consisting of the gene products that that penetrate the periplasmic side of the cell outer membrane only, either directly or via some covalently attached hydrophobic anchor.
The component of the cell outer membrane consisting of the gene products that that penetrate the periplasmic side of the cell outer membrane only, either directly or via some covalently attached hydrophobic anchor.
The component of the cell outer membrane consisting of the gene products that that penetrate the periplasmic side of the cell outer membrane only, either directly or via some covalently attached hydrophobic anchor.
The assembly of actin rods, a cellular structure consisting of parallel, hexagonally arranged actin tubules.
A complex that catalyzes the transfer of an acetyl group to a protein acceptor molecule.
Interacting selectively and non-covalently with denatured proteins.
An enzyme complex composed of 4 subunits, 2 copies of the large protein (nrdD in E. coli) and 2 copies of the small protein (nrdG in E. coli). It catalyzes the generation of 2'deoxyribonucleotides under anaerobic growth conditions. The larger subunit is the catalytic unit that is activated by the smaller iron-binding subunit.
A complex that possesses poly(A)-specific ribonuclease activity; catalyzes the message-specific shortening of mRNA poly(A) tails. Contains at least two subunits, known as Pan2p and Pan3p in Saccharomyces.
The area of a motile cell closest to the direction of movement.
The area of a motile cell closest to the direction of movement.
The portion of the plasma membrane surrounding a plasma membrane bounded cell surface projection.
The portion of the plasma membrane surrounding a plasma membrane bounded cell surface projection.
The area of a motile cell opposite to the direction of movement.
The area of a motile cell opposite to the direction of movement.
The area of a motile cell perpendicular to the direction of movement.
The portion of the plasma membrane surrounding the leading edge of a motile cell.
The portion of the plasma membrane surrounding the trailing edge of a motile cell.
The portion of the plasma membrane surrounding a lamellipodium.
The portion of the plasma membrane surrounding a uropod.
The portion of the plasma membrane surrounding a pseudopodium.
A protein-DNA complex assembled at eukaryotic DNA replication origins immediately prior to the initiation of DNA replication. The preinitiation complex is formed by the assembly of additional proteins onto an existing prereplicative complex. In budding yeast, the additional proteins might include Cdc45p, Sld2p, Sld3p, Dpb11p, DNA polymerases, and others; in fission yeast the GINS complex is present.
A protein complex conserved among eukaryotes that forms part of the kinetochore and plays an essential role in forming stable kinetochore-microtubule attachments. The complex contains proteins known in several species, including budding and fission yeasts, as Ndc80p, Nuf2p, Spc24p, and Spc25p. In vertebrates it is part of the outer plate of the kinetochore.
Catalysis of the reaction: ATP + H2O + amine(out) = ADP + phosphate + amine(in).
A protein complex formed by the association of signaling proteins with a death receptor upon ligand binding. The complex includes procaspases and death domain-containing proteins in addition to the ligand-bound receptor, and may control the activation of caspases 8 and 10.
A protein complex formed by the association of signaling proteins with a death receptor upon ligand binding. The complex includes procaspases and death domain-containing proteins in addition to the ligand-bound receptor, and may control the activation of caspases 8 and 10.
A protein complex formed by the association of signaling proteins with a death receptor upon ligand binding. The complex includes procaspases and death domain-containing proteins in addition to the ligand-bound receptor, and may control the activation of caspases 8 and 10.
A protein complex formed by the association of signaling proteins with a death receptor upon ligand binding. The complex includes procaspases and death domain-containing proteins in addition to the ligand-bound receptor, and may control the activation of caspases 8 and 10.
A protein complex formed by the association of signaling proteins with a death receptor upon ligand binding. The complex includes procaspases and death domain-containing proteins in addition to the ligand-bound receptor, and may control the activation of caspases 8 and 10.
A protein complex formed upon binding of Fas/CD95/APO-1 to its ligand. The complex includes FADD/Mort1, procaspase-8/10 and c-FLIP in addition to the ligand-bound receptor.
A protein complex formed upon binding of Fas/CD95/APO-1 to its ligand. The complex includes FADD/Mort1, procaspase-8/10 and c-FLIP in addition to the ligand-bound receptor.
A protein complex formed upon binding of Fas/CD95/APO-1 to its ligand. The complex includes FADD/Mort1, procaspase-8/10 and c-FLIP in addition to the ligand-bound receptor.
A protein complex formed upon binding of TRAIL to its ligand. The complex includes FADD/Mort1 and procaspase-8 addition to the ligand-bound receptor.
A protein complex formed upon binding of TRAIL to its ligand. The complex includes FADD/Mort1 and procaspase-8 addition to the ligand-bound receptor.
Interacting selectively and non-covalently with a small monomeric GTPase.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a pseudopodium, a temporary protrusion or retractile process of a cell, associated with cellular movement.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a pseudopodium, a temporary protrusion or retractile process of a cell, associated with cellular movement.
The assembly of a pseudopodium by rearrangement of the actin cytoskeleton and overlying membrane.
The assembly of a pseudopodium by rearrangement of the actin cytoskeleton and overlying membrane.
The myosin-based contraction and retraction of the pseudopodium.
The extension of a pseudopodium from the lateral area of a cell.
Any process that modulates the frequency, rate or extent of the assembly of pseudopodia.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of pseudopodia.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of pseudopodia.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of pseudopodia.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of pseudopodia.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of pseudopodia.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia.
Any process that modulates the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Any process that activates or increases the frequency, rate or extent of the assembly of pseudopodia from the lateral side of the cell.
Catalysis of the transfer of a galactose residue from a donor molecule, such as GDP-galactose or UDP-galactose, to an oligosaccharide, forming an alpha-1,2-linkage.
Any process that modulates the frequency, rate or extent of cyclase activity.
Any process that stops or reduces the activity of a cyclase.
Any process that stops or reduces the activity of a cyclase.
Any process that stops or reduces the activity of a cyclase.
Any process that stops or reduces the activity of a cyclase.
Any process that activates or increases the activity of a cyclase.
Any process that activates or increases the activity of a cyclase.
Any process that activates or increases the activity of a cyclase.
Any process that activates or increases the activity of a cyclase.
Any process that activates or increases the activity of a cyclase.
Any process that modulates the frequency, rate or extent of guanylate cyclase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of guanylate cyclase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of guanylate cyclase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of guanylate cyclase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of guanylate cyclase activity.
Any process that activates or increases the frequency, rate or extent of guanylate cyclase activity.
Any process that activates or increases the frequency, rate or extent of guanylate cyclase activity.
Any process that activates or increases the frequency, rate or extent of guanylate cyclase activity.
Any process that activates or increases the frequency, rate or extent of guanylate cyclase activity.
Any process that activates or increases the frequency, rate or extent of guanylate cyclase activity.
Any process that modulates the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
Any process that stops, prevents, or reduces the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
Any process that stops, prevents, or reduces the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
Any process that stops, prevents, or reduces the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
Any process that stops, prevents, or reduces the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
Any process that stops, prevents, or reduces the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
Any process that activates or increases the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
Any process that activates or increases the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
Any process that activates or increases the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
Any process that activates or increases the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
Any process that activates or increases the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
Any process that activates or increases the frequency, rate or extent of sorocarp stalk cell differentiation. An example of this process is found in Dictyostelium discoideum.
The process in which the sorocarp is generated and organized. An example of this process is found in Dictyostelium discoideum.
The transfer of one or more phosphate groups to an actin molecule.
The process in which the migration of an axon growth cone of a retinal ganglion cell (RGC) is directed to its target in the brain in response to a combination of attractive and repulsive cues.
A series of molecular signals within the cell that are mediated by a member of the Ran family of proteins switching to a GTP-bound active state.
The 5' to 3' exonucleolytic resection of the DNA at the site of the break at the mating-type locus to form a 3' single-strand DNA overhang.
The proteolytic cleavage of a transmembrane protein leading to the release of an intracellular domain.
The process of providing, via surface-bound receptor-ligand pairs, a second, antigen-independent, signal in addition to that provided by the B- or T cell receptor to augment B- or T cell activation.
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 T cell activation.
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 T cell activation.
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 T cell activation.
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 T cell activation.
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 T cell activation.
The process of providing, via surface-bound receptor-ligand pairs, a second, antigen-independent, signal in addition to that provided by the B cell receptor to augment B cell activation.
The process of providing, via surface-bound receptor-ligand pairs, a second, antigen-independent, signal in addition to that provided by the B cell receptor to augment B cell activation.
The process of providing, via surface-bound receptor-ligand pairs, a second, antigen-independent, signal in addition to that provided by the B cell receptor to augment B cell activation.
The process of providing, via surface-bound receptor-ligand pairs, a second, antigen-independent, signal in addition to that provided by the B cell receptor to augment B cell activation.
The process of providing, via surface-bound receptor-ligand pairs, a second, antigen-independent, signal in addition to that provided by the B cell receptor to augment B cell activation.
The process of providing, via surface-bound receptor-ligand pairs, a second, antigen-independent, signal in addition to that provided by the B cell receptor to augment B cell activation.
The process of providing, via surface-bound receptor-ligand pairs, a second, antigen-independent, signal in addition to that provided by the B cell receptor to augment B cell activation.
The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.
The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.
The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.
The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.
The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.
The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.
The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.
The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.
The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.
The process in which a DNA replication fork that has stalled is restored to a functional state and replication is restarted. The stalling may be due to DNA damage, DNA secondary structure, bound proteins, dNTP shortage, or other causes.
A protein complex conserved in eukaryotes and associated with the replication fork; the complex stabilizes stalled replication forks and is thought to be involved in coordinating leading- and lagging-strand synthesis and in replication checkpoint signaling.
A protein complex conserved in eukaryotes and associated with the replication fork; the complex stabilizes stalled replication forks and is thought to be involved in coordinating leading- and lagging-strand synthesis and in replication checkpoint signaling.
A protein complex conserved in eukaryotes and associated with the replication fork; the complex stabilizes stalled replication forks and is thought to be involved in coordinating leading- and lagging-strand synthesis and in replication checkpoint signaling.
Catalysis of the reaction: pyruvate + taurine = L-alanine + sulfoacetaldehyde.
Catalysis of the reaction: pyruvate + taurine = L-alanine + sulfoacetaldehyde.
The component of the organelle 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 organelle 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 endosome 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 endosome 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 mitochondrial inner 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 mitochondrial inner 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 mitochondrial 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 mitochondrial 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 nuclear 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 nuclear 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 vacuolar 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 contractile vacuolar 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 an organelle membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
The component of an endosome 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 mitochondrial 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 mitochondrial 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 a nuclear 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.
A complex consisting of two membrane proteins and one extracytoplasmic solute receptor. Such transporters transport a variety of substrates without direct ATP power, instead using energy from ion gradients.
A complex consisting of two membrane proteins and one extracytoplasmic solute receptor. Such transporters transport a variety of substrates without direct ATP power, instead using energy from ion gradients.
The series of events in which a folic acid stimulus is received by a cell and converted into a molecular signal.
The series of events in which a folic acid stimulus is received by a cell and converted into a molecular signal.
The series of events in which a folic acid stimulus is received by a cell and converted into a molecular signal.
The series of events in which a folic acid stimulus is received by a cell and converted into a molecular signal.
The series of events in which a folic acid stimulus is received by a cell and converted into a molecular signal.
The series of events in which a cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus is received by a cell and converted into a molecular signal; cAMP is the nucleotide cyclic AMP.
The series of events in which a cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus is received by a cell and converted into a molecular signal; cAMP is the nucleotide cyclic AMP.
The series of events in which a cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus is received by a cell and converted into a molecular signal; cAMP is the nucleotide cyclic AMP.
The series of events in which a cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus is received by a cell and converted into a molecular signal; cAMP is the nucleotide cyclic AMP.
The series of events in which a cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus is received by a cell and converted into a molecular signal; cAMP is the nucleotide cyclic AMP.
The series of events in which a cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus is received by a cell and converted into a molecular signal; cAMP is the nucleotide cyclic AMP.
The series of events in which a cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus is received by a cell and converted into a molecular signal; cAMP is the nucleotide cyclic AMP.
The series of events in which a cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus is received by a cell and converted into a molecular signal; cAMP is the nucleotide cyclic AMP.
The series of events in which a cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus is received by a cell and converted into a molecular signal; cAMP is the nucleotide cyclic AMP.
Catalysis of the reaction: hexitol + acceptor = hexose + reduced acceptor.
During ascospore formation, the process in which each haploid nucleus becomes encapsulated by a double membrane.
During ascospore formation, the process in which each haploid nucleus becomes encapsulated by a double membrane.
A spindle pole body (SPB) organization process that takes place during the second meiotic division during ascospore formation and results in the structural reorganization of the SPB; includes the recruitment of sporulation-specific proteins to the outer plaque to form the meiotic outer plaque (MOP).
A spindle pole body (SPB) organization process that takes place during the second meiotic division during ascospore formation and results in the structural reorganization of the SPB; includes the recruitment of sporulation-specific proteins to the outer plaque to form the meiotic outer plaque (MOP).
A spindle pole body (SPB) organization process that takes place during the second meiotic division during ascospore formation and results in the structural reorganization of the SPB; includes the recruitment of sporulation-specific proteins to the outer plaque to form the meiotic outer plaque (MOP).
A spindle pole body (SPB) organization process that takes place during the second meiotic division during ascospore formation and results in the structural reorganization of the SPB; includes the recruitment of sporulation-specific proteins to the outer plaque to form the meiotic outer plaque (MOP).
A spindle pole body (SPB) organization process that takes place during the second meiotic division during ascospore formation and results in the structural reorganization of the SPB; includes the recruitment of sporulation-specific proteins to the outer plaque to form the meiotic outer plaque (MOP).
A spindle pole body (SPB) organization process that takes place during the second meiotic division during ascospore formation and results in the structural reorganization of the SPB; includes the recruitment of sporulation-specific proteins to the outer plaque to form the meiotic outer plaque (MOP).
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways by which individual cells transform chemical substances.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
Any protein complex that mediates the effects of small interfering RNAs on gene expression. Most known examples contain one or more members of the Argonaute family of proteins.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein complex assembly.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein complex assembly.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein complex assembly.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein complex assembly.
Any process that activates or increases the frequency, rate or extent of protein complex assembly.
Any process that activates or increases the frequency, rate or extent of protein complex assembly.
Any process that activates or increases the frequency, rate or extent of protein complex assembly.
Any process that activates or increases the frequency, rate or extent of protein complex assembly.
Any process that activates or increases the frequency, rate or extent of protein complex assembly.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving sulfur amino acids.
Any process that modulates the frequency, rate or extent of vesicle fusion.
Any process that stops, prevents, or reduces the frequency, rate or extent of vesicle fusion.
Any process that stops, prevents, or reduces the frequency, rate or extent of vesicle fusion.
Any process that stops, prevents, or reduces the frequency, rate or extent of vesicle fusion.
Any process that stops, prevents, or reduces the frequency, rate or extent of vesicle fusion.
Any process that activates or increases the frequency, rate or extent of vesicle fusion.
Any process that activates or increases the frequency, rate or extent of vesicle fusion.
Any process that activates or increases the frequency, rate or extent of vesicle fusion.
Any process that activates or increases the frequency, rate or extent of vesicle fusion.
Any process that activates or increases the frequency, rate or extent of vesicle fusion.
Any process that modulates the frequency, rate or extent of cell killing, the process in which a cell brings about the death of another cell, either in the same or a different organism.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell killing.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell killing.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell killing.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell killing.
Any process that activates or increases the frequency, rate or extent of cell killing.
Any process that activates or increases the frequency, rate or extent of cell killing.
Any process that activates or increases the frequency, rate or extent of cell killing.
Any process that activates or increases the frequency, rate or extent of cell killing.
Any process that activates or increases the frequency, rate or extent of cell killing.
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that stops, prevents, or reduces the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that stops, prevents, or reduces the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that stops, prevents, or reduces the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that stops, prevents, or reduces the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that stops, prevents, or reduces the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that stops, prevents, or reduces the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that activates or increases the frequency, rate or extent of the process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that activates or increases the frequency, rate or extent of the process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that activates or increases the frequency, rate or extent of the process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that activates or increases the frequency, rate or extent of the process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that activates or increases the frequency, rate or extent of the process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that activates or increases the frequency, rate or extent of the process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that activates or increases the frequency, rate or extent of the process involved in the formation, arrangement of constituent parts, or disassembly of cell projections.
Any process that modulates the frequency, rate or extent of a defense response.
Any process that stops, prevents, or reduces the frequency, rate or extent of a defense response.
Any process that stops, prevents, or reduces the frequency, rate or extent of a defense response.
Any process that stops, prevents, or reduces the frequency, rate or extent of a defense response.
Any process that stops, prevents, or reduces the frequency, rate or extent of a defense response.
Any process that activates or increases the frequency, rate or extent of a defense response.
Any process that activates or increases the frequency, rate or extent of a defense response.
Any process that activates or increases the frequency, rate or extent of a defense response.
Any process that activates or increases the frequency, rate or extent of a defense response.
Any process that activates or increases the frequency, rate or extent of a defense response.
The component of the plastid 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 plastid 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 plastid inner 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 plastid inner 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 plastid 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 plastid 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 chloroplast inner 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 chloroplast inner 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 chloroplast 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 chloroplast 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 thylakoid 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 thylakoid 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 plasma membrane consisting of the gene products that are tethered to the external side of 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 plasma membrane consisting of the gene products that are tethered to the external side of 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 removal of an amino group from the N-terminal amino acid residue of a protein.
The removal of an amino group from the side chain of an N-terminal asparagine or glutamine residue of a protein.
The alteration of the N-terminal amino acid residue in a protein.
The alteration of the N-terminal amino acid residue in a protein.
The alteration of the N-terminal amino acid residue in a protein.
The removal of an amino group from the side chain of an N-terminal asparagine residue of a protein.
The removal of an amino group from the side chain of an N-terminal glutamine residue of a protein.
Interacting selectively and non-covalently with a translation initiation factor, any polypeptide factor involved in the initiation of ribosome-mediated translation.
Interacting selectively and non-covalently with eukaryotic initiation factor 4G, a polypeptide factor involved in the initiation of ribosome-mediated translation.
Any complex that possesses ubiquitin conjugating enzyme activity.
A heterodimeric ubiquitin conjugating enzyme complex that catalyzes assembly of K63-linked polyubiquitin chains, which act as a signal to promote error-free DNA postreplication repair; in Saccharomyces the complex comprises Ubc13p and Mms2p.
A protein complex that possesses RNA-directed RNA polymerase activity.
A complex required for RNAi mediated heterochromatin assembly. In S. pombe this contains RNA-directed RNA polymerase, a putative helicase and a protein containing a pap25 associated domain.
A complex required for RNAi mediated heterochromatin assembly. In S. pombe this contains RNA-directed RNA polymerase, a putative helicase and a protein containing a pap25 associated domain.
A virus-specific protein complex that possesses RNA-dependent RNA polymerase activity and replicates the genome of an RNA virus.
The aggregation, arrangement and bonding together of a set of components to form a cell projection in response to mating pheromone. This process is observed in unicellular fungi.
Any process that modulates the frequency, rate, or extent of mating projection formation by unicellular fungi.
Any process that modulates the frequency, rate, or extent of the start of mating projection formation by unicellular fungi.
Any process that modulates the frequency, rate, or extent of the end of mating projection formation by unicellular fungi.
A complex consisting of a Cdc2-class (also known as Cdc28) cyclin-dependent kinase and an M-phase cyclin such as S. pombe Cdc13. The MPF complex phosphorylates and activates the anaphase promoting complex (APC).
The process of introducing one or more phosphate groups into an organic acid.
A pentameric protein complex related to replication factor C, which loads a trimeric complex of checkpoint proteins (known as the checkpoint clamp or 9-1-1 complex) onto DNA at damage sites; functions in DNA damage cell cycle checkpoints. In Schizosaccharomyces pombe the subunits are known as Rad17, Rfc2, Rfc3, Rfc4, and Rfc5, while in Saccharomyces cerevisiae the subunits are known as Rad24p, Rfc2p, Rfc3p, Rfc4p, and Rfc5p.
A pentameric protein complex related to replication factor C, which loads a trimeric complex of checkpoint proteins (known as the checkpoint clamp or 9-1-1 complex) onto DNA at damage sites; functions in DNA damage cell cycle checkpoints. In Schizosaccharomyces pombe the subunits are known as Rad17, Rfc2, Rfc3, Rfc4, and Rfc5, while in Saccharomyces cerevisiae the subunits are known as Rad24p, Rfc2p, Rfc3p, Rfc4p, and Rfc5p.
A pentameric protein complex related to replication factor C, which loads a trimeric complex of checkpoint proteins (known as the checkpoint clamp or 9-1-1 complex) onto DNA at damage sites; functions in DNA damage cell cycle checkpoints. In Schizosaccharomyces pombe the subunits are known as Rad17, Rfc2, Rfc3, Rfc4, and Rfc5, while in Saccharomyces cerevisiae the subunits are known as Rad24p, Rfc2p, Rfc3p, Rfc4p, and Rfc5p.
A pentameric protein complex related to replication factor C, which loads a trimeric complex of checkpoint proteins (known as the checkpoint clamp or 9-1-1 complex) onto DNA at damage sites; functions in DNA damage cell cycle checkpoints. In Schizosaccharomyces pombe the subunits are known as Rad17, Rfc2, Rfc3, Rfc4, and Rfc5, while in Saccharomyces cerevisiae the subunits are known as Rad24p, Rfc2p, Rfc3p, Rfc4p, and Rfc5p.
A heptameric complex related to replication factor C, which loads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) onto DNA and plays a vital role in chromosome cohesion. In Saccharomyces the subunits are known as Ctf18p, Rfc2p, Rfc3p, Rfc4p, Rfc5p, Dcc1p, and Ctf8p.
A heptameric complex related to replication factor C, which loads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) onto DNA and plays a vital role in chromosome cohesion. In Saccharomyces the subunits are known as Ctf18p, Rfc2p, Rfc3p, Rfc4p, Rfc5p, Dcc1p, and Ctf8p.
A heptameric complex related to replication factor C, which loads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) onto DNA and plays a vital role in chromosome cohesion. In Saccharomyces the subunits are known as Ctf18p, Rfc2p, Rfc3p, Rfc4p, Rfc5p, Dcc1p, and Ctf8p.
A pentameric replication factor C (RLC) complex, which unloads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) from chromatin and has roles in telomere length regulation and other aspects of genome stability. In Saccharomyces the subunits are known as Elg1p, Rfc2p, Rfc3p, Rfc4p, and Rfc5p.
A pentameric replication factor C (RLC) complex, which unloads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) from chromatin and has roles in telomere length regulation and other aspects of genome stability. In Saccharomyces the subunits are known as Elg1p, Rfc2p, Rfc3p, Rfc4p, and Rfc5p.
A pentameric replication factor C (RLC) complex, which unloads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) from chromatin and has roles in telomere length regulation and other aspects of genome stability. In Saccharomyces the subunits are known as Elg1p, Rfc2p, Rfc3p, Rfc4p, and Rfc5p.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of prostaglandin.
A neuropeptide hormone secreted by the central nervous system of insects that stimulates the tanning and sclerotization of the adult cuticle following eclosion. The active hormone consists of an obligate heterodimer of the alpha and beta subunits.
Any process that modulates the frequency, rate or extent of the addition of ubiquitin groups to a protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein.
Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein.
Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein.
Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein.
Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein.
Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein.
Any process that modulates the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein.
Any process that stops, prevents, or reduces the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein.
Any process that activates or increases the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein.
Any process that activates or increases the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein.
Any process that activates or increases the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein.
Any process that activates or increases the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein.
Any process that activates or increases the frequency, rate or extent of the covalent alteration of one or more amino acid residues within a protein.
Interacting selectively and non-covalently with sodium ions (Na+).
Interacting selectively and non-covalently with lithium ions (Li+).
Interacting selectively and non-covalently with chloride ions (Cl-).
Interacting selectively and non-covalently with lipoic acid, 1,2-dithiolane-3-pentanoic acid.
Interacting selectively and non-covalently with a carboxylic acid, any organic acid containing one or more carboxyl (COOH) groups or anions (COO-).
The chemical reactions and pathways involving any oxylipin, any of a group of biologically active compounds formed by oxidative metabolism of polyunsaturated fatty acids.
The chemical reactions and pathways resulting in the formation of any oxylipin, any of a group of biologically active compounds formed by oxidative metabolism of polyunsaturated fatty acids.
The chemical reactions and pathways resulting in the formation of any oxylipin, any of a group of biologically active compounds formed by oxidative metabolism of polyunsaturated fatty acids.
The chemical reactions and pathways resulting in the formation of any oxylipin, any of a group of biologically active compounds formed by oxidative metabolism of polyunsaturated fatty acids.
The chemical reactions and pathways resulting in the formation of any oxylipin, any of a group of biologically active compounds formed by oxidative metabolism of polyunsaturated fatty acids.
Interacting selectively and non-covalently with a pigment, any general or particular coloring matter in living organisms, e.g. melanin.
A vesicle found in the cytoplasm of a cell.
A vesicle found in the cytoplasm of a cell.
A vesicle found in the cytoplasm of a cell.
A vesicle found in the cytoplasm of a cell.
An intracellular non-membrane-bounded organelle; a hollow structure made of protein, which usually has the form of a cylindrical tube closed by conical end caps. By regulating their relative gas vesicle content, aquatic microbes are able to perform vertical migrations.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a gas vesicle. A gas vesicle is a hollow structure made of protein, which usually has the form of a cylindrical tube closed by conical end caps.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a gas vesicle. A gas vesicle is a hollow structure made of protein, which usually has the form of a cylindrical tube closed by conical end caps.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a gas vesicle. A gas vesicle is a hollow structure made of protein, which usually has the form of a cylindrical tube closed by conical end caps.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a gas vesicle. A gas vesicle is a hollow structure made of protein, which usually has the form of a cylindrical tube closed by conical end caps.
Any process that modulates an organism's tendency or ability to rise or float in a fluid medium such as water or air, often through the use of stored gases.
A complex that catalyzes the transfer of an acetyl group to the N-terminal residue of a protein acceptor molecule.
A conserved complex that catalyzes the transfer of an acetyl group to an N-terminal Ser, Ala, Gly, or Thr residue of a protein acceptor molecule. In Saccharomyces the complex includes Nat1p and Ard1p, and may contain additional proteins.
A conserved complex that catalyzes the transfer of an acetyl group to the N-terminal residue of a protein acceptor molecule that has a Met-Glu, Met-Asp, Met-Asn, or Met-Met N-terminus. In Saccharomyces the complex includes Nat3p and Mdm20p.
A conserved complex that catalyzes the transfer of an acetyl group to the N-terminal residue of a protein acceptor molecule that has a Met-Ile, Met-Leu, Met-Trp, or Met-Phe N-terminus. In Saccharomyces the complex includes Mak3p, Mak10p, and Mak31p.
Interacting selectively and non-covalently with L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.
Interacting selectively and non-covalently with L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.
Interacting selectively and non-covalently with cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
Interacting selectively and non-covalently with any alkali metal ion; alkali metals are those elements in group Ia of the periodic table, with the exception of hydrogen.
A complex formed by a recombinase, a regulatory protein, and the DNA sequences bound by each protein; catalyzes a reversible site-specific recombination reaction that results in the alternate expression of one or more genes in various contexts.
A complex containing a RecQ family helicase and a topoisomerase III homologue; may also include one or more additional proteins; conserved from E. coli to human.
Interacting selectively and non-covalently with a hexon, the major protein component of the icosahedral capsid of an adenovirus.
The process in which the cytoplasm of the outermost cells of the vertebrate epidermis is replaced by keratin. Keratinization occurs in the stratum corneum, feathers, hair, claws, nails, hooves, and horns.
The conversion of a primary RNA molecule transcribed from a chloroplast genome into one or more mature RNA molecules.
The conversion of a primary mRNA transcript containing more than one complete protein-coding region into individual mature mRNA molecules.
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 methotrexate stimulus. Methotrexate is 4-amino-10-methylformic acid, a folic acid analogue that is a potent competitive inhibitor of dihydrofolate reductase.
A ribonucleoprotein complex containing small nucleolar RNA of the box C/D type that can carry out ribose-2'-O-methylation of target RNAs.
A ribonucleoprotein complex containing small nucleolar RNA of the box C/D type that can carry out ribose-2'-O-methylation of target RNAs.
A ribonucleoprotein complex containing small nucleolar RNA of the box C/D type that can carry out ribose-2'-O-methylation of target RNAs.
A box H/ACA RNP complex that is located in the nucleolus.
A box H/ACA RNP complex that is located in the nucleolus.
The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines.
The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines.
The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines.
The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines.
A heterodimeric protein complex required for the activation of DNA replication origins; comprises a catalytic subunit and a regulatory subunit (in Saccharomyces, Cdc7p and Dbf4p, respectively); complexes identified in other species generally contain proteins related to the Saccharomyces proteins.
A heterodimeric protein complex required for the activation of DNA replication origins; comprises a catalytic subunit and a regulatory subunit (in Saccharomyces, Cdc7p and Dbf4p, respectively); complexes identified in other species generally contain proteins related to the Saccharomyces proteins.
A heterodimeric protein complex required for the activation of DNA replication origins; comprises a catalytic subunit and a regulatory subunit (in Saccharomyces, Cdc7p and Dbf4p, respectively); complexes identified in other species generally contain proteins related to the Saccharomyces proteins.
Interacting selectively and non-covalently with titin, any of a family of giant proteins found in striated and smooth muscle. In striated muscle, single titin molecules span half the sarcomere, with their N- and C-termini in the Z-disc and M-line, respectively.
Interacting selectively and non-covalently with telethonin, a protein found in the Z disc of striated muscle and which is a substrate of the titin kinase.
Interacting selectively and non-covalently with a mitogen-activated protein kinase kinase, any protein that can phosphorylate a MAP kinase.
Interacting selectively and non-covalently with a mitogen-activated protein kinase kinase kinase, any protein that can phosphorylate a MAP kinase kinase.
A heterodimeric complex comprising BRCA1 and BARD1, which possesses ubiquitin ligase activity and is involved in genome maintenance, possibly by functioning in surveillance for DNA damage.
Any process that modulates the frequency, rate or extent of mRNA cleavage, any process in which a pre-mRNA or mRNA molecule is cleaved at specific sites or in a regulated manner.
Any process that stops, prevents, or reduces the frequency, rate or extent of mRNA cleavage.
Any process that stops, prevents, or reduces the frequency, rate or extent of mRNA cleavage.
Any process that stops, prevents, or reduces the frequency, rate or extent of mRNA cleavage.
Any process that stops, prevents, or reduces the frequency, rate or extent of mRNA cleavage.
Any process that activates or increases the frequency, rate or extent of mRNA cleavage.
Any process that activates or increases the frequency, rate or extent of mRNA cleavage.
Any process that activates or increases the frequency, rate or extent of mRNA cleavage.
Any process that activates or increases the frequency, rate or extent of mRNA cleavage.
Any process that activates or increases the frequency, rate or extent of mRNA cleavage.
Any process that modulates the frequency, rate or extent of mRNA 3'-end processing, any process involved in forming the mature 3' end of an mRNA molecule.
Any process that stops, prevents, or reduces the frequency, rate or extent of mRNA 3'-end processing.
Any process that stops, prevents, or reduces the frequency, rate or extent of mRNA 3'-end processing.
Any process that stops, prevents, or reduces the frequency, rate or extent of mRNA 3'-end processing.
Any process that stops, prevents, or reduces the frequency, rate or extent of mRNA 3'-end processing.
Any process that activates or increases the frequency, rate or extent of mRNA 3'-end processing.
Any process that activates or increases the frequency, rate or extent of mRNA 3'-end processing.
Any process that activates or increases the frequency, rate or extent of mRNA 3'-end processing.
Any process that activates or increases the frequency, rate or extent of mRNA 3'-end processing.
Any process that activates or increases the frequency, rate or extent of mRNA 3'-end processing.
A process in which force is generated within fast-twitch skeletal muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. The fast-twitch skeletal muscle is characterized by fast time parameters, high force development and fatiguability.
A process in which force is generated within fast-twitch skeletal muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. The fast-twitch skeletal muscle is characterized by fast time parameters, high force development and fatiguability.
A process in which force is generated within fast-twitch skeletal muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. The fast-twitch skeletal muscle is characterized by fast time parameters, high force development and fatiguability.
A process in which force is generated within fast-twitch skeletal muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. The fast-twitch skeletal muscle is characterized by fast time parameters, high force development and fatiguability.
A process in which force is generated within fast-twitch skeletal muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. The fast-twitch skeletal muscle is characterized by fast time parameters, high force development and fatiguability.
A process in which force is generated within slow-twitch skeletal muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. The slow-twitch skeletal muscle is characterized by slow time parameters, low force development and resistance to fatigue.
Any process that modulates the frequency, rate, extent or location of heterochromatin formation.
Any process that modulates the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of fast-twitch skeletal muscle contraction.
Any process that modulates the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that activates or increases the frequency, rate or extent of slow-twitch skeletal muscle contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of heterochromatin formation.
Any process that stops, prevents, or reduces the frequency, rate or extent of heterochromatin formation.
Any process that stops, prevents, or reduces the frequency, rate or extent of heterochromatin formation.
Any process that stops, prevents, or reduces the frequency, rate or extent of heterochromatin formation.
Any process that stops, prevents, or reduces the frequency, rate or extent of heterochromatin formation.
Any process that activates or increases the frequency, rate or extent of heterochromatin formation.
Any process that activates or increases the frequency, rate or extent of heterochromatin formation.
Any process that activates or increases the frequency, rate or extent of heterochromatin formation.
Any process that activates or increases the frequency, rate or extent of heterochromatin formation.
Any process that activates or increases the frequency, rate or extent of heterochromatin formation.
Any process that activates or increases the frequency, rate or extent of heterochromatin formation.
Any process that modulates the extent or location of heterochromatin formation.
Any process that modulates the extent or location of heterochromatin formation.
The chemical reactions and pathways involving glycine betaine, N-trimethylglycine.
The chemical reactions and pathways involving glycine betaine, N-trimethylglycine.
The chemical reactions and pathways involving glycine betaine, N-trimethylglycine.
The chemical reactions and pathways resulting in the formation of glycine betaine, N-trimethylglycine.
The chemical reactions and pathways resulting in the formation of glycine betaine, N-trimethylglycine.
The chemical reactions and pathways resulting in the formation of glycine betaine, N-trimethylglycine.
The chemical reactions and pathways resulting in the formation of glycine betaine, N-trimethylglycine.
The chemical reactions and pathways resulting in the formation of glycine betaine, N-trimethylglycine.
The chemical reactions and pathways resulting in the formation of glycine betaine, N-trimethylglycine.
The chemical reactions and pathways resulting in the breakdown of glycine betaine, N-trimethylglycine.
The chemical reactions and pathways resulting in the breakdown of glycine betaine, N-trimethylglycine.
The chemical reactions and pathways resulting in the breakdown of glycine betaine, N-trimethylglycine.
The chemical reactions and pathways resulting in the breakdown of glycine betaine, N-trimethylglycine.
The chemical reactions and pathways resulting in the breakdown of glycine betaine, N-trimethylglycine.
Catalysis of the reaction: ATP + H2O + a betaine(out) = ADP + phosphate + a betaine(in).
Catalysis of the reaction: ATP + H2O + glycine betaine(out) = ADP + phosphate + glycine betaine(in).
Catalysis of the reaction: ATP + H2O + glycine betaine(out) = ADP + phosphate + glycine betaine(in).
The directed movement of glycine betaine, N-trimethylglycine, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any ubiquitin ligase complex in which the catalytic core consists of a member of the cullin family and a RING domain protein; the core is associated with one or more additional proteins that confer substrate specificity.
Any ubiquitin ligase complex in which the catalytic core consists of a member of the cullin family and a RING domain protein; the core is associated with one or more additional proteins that confer substrate specificity.
Any ubiquitin ligase complex in which the catalytic core consists of a member of the cullin family and a RING domain protein; the core is associated with one or more additional proteins that confer substrate specificity.
A ubiquitin ligase complex in which a cullin from the Cul2 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul2 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul2 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul2 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul2 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul2 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul2 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul2 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul3 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a BTB-domain-containing protein.
A ubiquitin ligase complex in which a cullin from the Cul3 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a BTB-domain-containing protein.
A ubiquitin ligase complex in which a cullin from the Cul3 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a BTB-domain-containing protein.
A ubiquitin ligase complex in which a cullin from the Cul3 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a BTB-domain-containing protein.
A ubiquitin ligase complex in which a cullin from the Cul3 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a BTB-domain-containing protein.
A ubiquitin ligase complex in which a cullin from the Cul3 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a BTB-domain-containing protein.
A ubiquitin ligase complex in which a cullin from the Cul4A subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein.
A ubiquitin ligase complex in which a cullin from the Cul4A subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein.
A ubiquitin ligase complex in which a cullin from the Cul4A subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein.
A ubiquitin ligase complex in which a cullin from the Cul4A subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein.
A ubiquitin ligase complex in which a cullin from the Cul4A subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein.
A ubiquitin ligase complex in which a cullin from the Cul4A subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein.
A ubiquitin ligase complex in which a cullin from the Cul4B subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by unknown subunits.
A ubiquitin ligase complex in which a cullin from the Cul5 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul5 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul5 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul5 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul5 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein.
A ubiquitin ligase complex in which a cullin from the Cul7 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a Skp1 linker and an F-box protein.
A ubiquitin ligase complex in which a cullin from the Cul7 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a Skp1 linker and an F-box protein.
A ubiquitin ligase complex in which a cullin from the Cul7 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a Skp1 linker and an F-box protein.
A ubiquitin ligase complex in which a cullin from the Cul7 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a Skp1 linker and an F-box protein.
The reformation of the nuclear envelope following its breakdown in the context of a normal process.
An organelle found in bacteria consisting of a proteinaceous coat containing metabolic enzymes whose purpose is the sequestration or concentration of metabolites and which has the appearance of a polygonal granule by electron microscopy.
An organelle consisting of a proteinaceous coat and enzymes for the fixation of carbon dioxide including mechanisms for the concentration of carbonate to increase the efficiency of fixation under low-carbon dioxide conditions.
An organelle found in bacteria consisting of a proteinaceous coat containing enzymes for the degradation of ethanolamine whose purpose is the protection of the rest of the cell from the toxic acetaldehyde product of the enzyme ethanolamine ammonia lyase.
An organelle found in bacteria consisting of a proteinaceous coat containing enzymes for the degradation of 1,2-propanediol whose purpose is the protection of the rest of the cell from the toxic propionaldehyde product of the enzyme diol dehydratase.
Interacting selectively and non-covalently with a class III myosin; myosin III is monomeric and has an N terminal kinase domain.
A myosin complex containing one or more class IV myosin heavy chains and associated light chains; myosin IV is relatively uncharacterized, but is predicted to have a single motor domain, one IQ motif and a tail with a Myosin Tail Homology (myTH4) domain homologous to that in the tails of myosins VII and XV.
A myosin complex containing a dimer of class V myosin heavy chains and associated light chains; involved in intracellular transport. Myosin V is a dimeric molecule consisting of conserved motor domains followed by 6 IQ motifs which bind specific light chains and calmodulin. The tail domain is important for cellular localization and cargo binding and can be divided into an alpha-helical coiled coil region and a C-terminal globular region.
A myosin complex containing one or more class VI myosin heavy chains and associated light chains. Myosin VI has a single IQ motif in the neck and a tail region with a coiled coil domain followed by a unique globular domain; a unique insertion that enables myosin VI to move towards the pointed or minus end of actin filaments.
A myosin complex containing a dimer of class VII myosin heavy chains and associated light chains. Myosin VII (240 kDa) is predicted to be a dimeric molecule with 5 IQ motifs and a tail region with a short stretch of coiled coil followed by two myosin-tail homology (MyTH4) domains, two talin-binding (FERM) domains and an SH3-domain.
A myosin complex containing a dimer of class VIII myosin heavy chains and associated light chains. Myosin VIII is predicted to be dimeric, and contain an unusual 100-190 residue N-terminal extension prior to their motor domains, 3-4 IQ motifs, a short region (~70 residues) of predicted alpha-helical coiled coil and a C-terminal domain.
A myosin complex containing a class IX myosin heavy chain and associated light chains. Myosin IX is monomeric with a motor domain containing an N-terminal extension and an insert in the actin binding interface, followed by four to six IQ motifs and a tail region that contains a zinc binding motif and a domain with homology to GTPase activating proteins (GAPs) of the Rho family of G-proteins.
A myosin complex containing one or more class X myosin heavy chains and associated light chains.
A myosin complex containing a dimer of class XI myosin heavy chains and associated light chains. Myosin XI heavy chain sizes are similar in molecular structure to the class V myosins with 5 to 6 IQ motifs and tail regions with predicted coiled coil domains (forming dimeric molecules) and large C-terminal regions.
A myosin complex containing one or more class XII myosin heavy chains and associated light chains; myosin XII contains a large tail region with two MyTH4 domains and a short region of coiled coil.
A myosin complex containing one or more class XIII myosin heavy chains and associated light chains.
A myosin complex containing a class XIV myosin heavy chain and associated light chains; myosin XIV heavy chains are the simplest known, containing a motor domain, no classic IQ motif and variable length tails.
A myosin complex containing a class XV myosin heavy chain and associated light chains. Myosin XV is single headed, and has a large extension (1200aa) at the N-terminus of the motor domain, two IQ motifs and a tail with a similar domain structure to that of the tail of myosin VII.
A myosin complex containing a class XVI myosin heavy chains and associated light chains; myosin XVI heavy chains contain ankyrin repeat.
A myosin complex containing one or more class XVII myosin heavy chains and associated light chains.
A myosin complex containing a class XVIII myosin heavy chain and associated light chains; myosin XVIII heavy chains contain an N-terminal PDZ domain.
Interacting selectively and non-covalently with a class V myosin; myosin V is a dimeric molecule involved in intracellular transport.
Interacting selectively and non-covalently with DNA that is assembled into chromatin.
Interacting selectively and non-covalently with a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.
Interacting selectively and non-covalently with the DNA portion of a nucleosome.
Interacting selectively and non-covalently with a histone that is assembled into a nucleosome.
Any process that modulates the frequency, rate or extent of mating type switching, the conversion of a single-cell organism from one mating type to another by the precise replacement of a DNA sequence at the expressed mating type locus with a copy of a sequence from a donor locus.
Any process that stops, prevents, or reduces the frequency, rate or extent of mating type switching.
Any process that stops, prevents, or reduces the frequency, rate or extent of mating type switching.
Any process that stops, prevents, or reduces the frequency, rate or extent of mating type switching.
Any process that stops, prevents, or reduces the frequency, rate or extent of mating type switching.
Any process that activates or increases the frequency, rate or extent of mating type switching.
Any process that activates or increases the frequency, rate or extent of mating type switching.
Any process that activates or increases the frequency, rate or extent of mating type switching.
Any process that activates or increases the frequency, rate or extent of mating type switching.
Any process that activates or increases the frequency, rate or extent of mating type switching.
The controlled breakdown of chromatin from a higher order structure into its simpler subcomponents, DNA, histones, other proteins, and sometimes RNA.
A multiprotein complex having distributive polyadenylation activity of a variety of RNA substrates including hypomodified and incorrectly folded tRNAs, pre-snRNAs, pre-snoRNAs, incorrectly spliced or processed pre-mRNAs, cryptic unstable transcripts (CUTs), pre-rRNAs and rRNA fragments released as part of rRNA processing. In S. cerevisiae, the complex consists of either Pap2 (also known as Trf4) or Trf5, Air1 or Air2, and Mtr4, and is involved in RNA 3'-end processing and in RNA surveillance and quality control.
A multiprotein complex having distributive polyadenylation activity of a variety of RNA substrates including hypomodified and incorrectly folded tRNAs, pre-snRNAs, pre-snoRNAs, incorrectly spliced or processed pre-mRNAs, cryptic unstable transcripts (CUTs), pre-rRNAs and rRNA fragments released as part of rRNA processing. In S. cerevisiae, the complex consists of either Pap2 (also known as Trf4) or Trf5, Air1 or Air2, and Mtr4, and is involved in RNA 3'-end processing and in RNA surveillance and quality control.
A multiprotein complex having distributive polyadenylation activity of a variety of RNA substrates including hypomodified and incorrectly folded tRNAs, pre-snRNAs, pre-snoRNAs, incorrectly spliced or processed pre-mRNAs, cryptic unstable transcripts (CUTs), pre-rRNAs and rRNA fragments released as part of rRNA processing. In S. cerevisiae, the complex consists of either Pap2 (also known as Trf4) or Trf5, Air1 or Air2, and Mtr4, and is involved in RNA 3'-end processing and in RNA surveillance and quality control.
A multiprotein complex having distributive polyadenylation activity of a variety of RNA substrates including hypomodified and incorrectly folded tRNAs, pre-snRNAs, pre-snoRNAs, incorrectly spliced or processed pre-mRNAs, cryptic unstable transcripts (CUTs), pre-rRNAs and rRNA fragments released as part of rRNA processing. In S. cerevisiae, the complex consists of either Pap2 (also known as Trf4) or Trf5, Air1 or Air2, and Mtr4, and is involved in RNA 3'-end processing and in RNA surveillance and quality control.
A multiprotein complex having distributive polyadenylation activity of a variety of RNA substrates including hypomodified and incorrectly folded tRNAs, pre-snRNAs, pre-snoRNAs, incorrectly spliced or processed pre-mRNAs, cryptic unstable transcripts (CUTs), pre-rRNAs and rRNA fragments released as part of rRNA processing. In S. cerevisiae, the complex consists of either Pap2 (also known as Trf4) or Trf5, Air1 or Air2, and Mtr4, and is involved in RNA 3'-end processing and in RNA surveillance and quality control.
A high molecular weight complex characterized in S. pombe containing the cell-end anchoring protein Tea1. This complex is transported to the cell ends by microtubules and is involved in bipolar growth and the maintennce of normal cell polarity.
A complex that posseses mannosyltransferase activity.
A complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity; usually includes members of the PMT1 and PMT2 protein subfamilies.
A complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity; usually includes members of the PMT1 and PMT2 protein subfamilies.
A localization process that acts on a protein complex; the complex is transported to, or maintained in, a specific location.
A localization process that acts on a protein complex; the complex is transported to, or maintained in, a specific location.
A localization process that acts on a protein complex; the complex is transported to, or maintained in, a specific location.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the peptidoglycan-based cell wall.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the peptidoglycan-based cell wall.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall.
The chemical reactions and pathways resulting in the formation of cell wall glycoproteins, any cell wall protein that contains covalently bound sugar residues.
The chemical reactions and pathways resulting in the formation of cell wall glycoproteins, any cell wall protein that contains covalently bound sugar residues.
The chemical reactions and pathways resulting in the formation of cell wall glycoproteins, any cell wall protein that contains covalently bound sugar residues.
The chemical reactions and pathways resulting in the formation of cell wall glycoproteins, any cell wall protein that contains covalently bound sugar residues.
The assembly of chromatin into heterochromatin, a compact and highly condensed form that is often, but not always, transcriptionally silent.
The assembly of chromatin into heterochromatin, a compact and highly condensed form that is often, but not always, transcriptionally silent.
The assembly of chromatin into heterochromatin that is located adjacent to the CENP-A rich centromere 'central core' and characterized by the modified histone H3K9me3.
The assembly of chromatin into heterochromatin that is located adjacent to the CENP-A rich centromere 'central core' and characterized by the modified histone H3K9me3.
The assembly of chromatin into heterochromatin that is located adjacent to the CENP-A rich centromere 'central core' and characterized by the modified histone H3K9me3.
The assembly of chromatin into heterochromatin at the telomere.
A conserved heterodimeric complex with SUMO activating enzyme activity.
A conserved heterodimeric complex with SUMO activating enzyme activity.
A protein complex that forms part of the inner centromere, which is involved in the loading of the centromeric histone h3 variant CENP-A onto centromeres and in centromere specific heterochromatin formation. The complex contains about 12 proteins, of which two are known as Mis6 and Sim4 in S. pombe and CENP-I and CENP-H in human.
A protein complex that forms part of the inner centromere, which is involved in the loading of the centromeric histone h3 variant CENP-A onto centromeres and in centromere specific heterochromatin formation. The complex contains about 12 proteins, of which two are known as Mis6 and Sim4 in S. pombe and CENP-I and CENP-H in human.
A protein complex that forms part of the inner centromere, which is involved in the loading of the centromeric histone h3 variant CENP-A onto centromeres and in centromere specific heterochromatin formation. The complex contains about 12 proteins, of which two are known as Mis6 and Sim4 in S. pombe and CENP-I and CENP-H in human.
A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.
A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.
A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.
A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.
A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.
A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.
A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.
A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.
A protein complex involved in the catalysis of the formation of the modified nucleotide 1-methyladenosine (m1A) in tRNA. In yeast, it is a heterotetramer of two subunits, Gcd10p and Gcd14p, while in bacteria and archaea it is a homotetramer.
The function of absorbing and responding to electromagnetic radiation with a wavelength of approximately 730nm. The response may involve a change in conformation.
The function of absorbing and responding to electromagnetic radiation with a wavelength of approximately 660nm. The response may involve a change in conformation.
A multisubunit protein complex that binds to centromeric DNA and initiates kinetochore assembly. In yeast, this complex consists of four subunits, namely Ctf13p, Skp1p, Cep3p and Cbf2p.
A chromatin-associated multiprotein complex containing Polycomb Group proteins. In Drosophila, Polycomb group proteins are involved in the long-term maintenance of gene repression, and PcG protein complexes associate with Polycomb group response elements (PREs) in target genes to regulate higher-order chromatin structure.
The portion of the plasma membrane surrounding the cell tip.
Structure within the hyphal tip of filamentous fungi that acts as an organizing center for hyphal tip growth; may function to supply vesicles to the elongating tip and/or to organize cytoskeletal microfilaments.
A transmembrane protein complex involved in the translocation of proteins across the cytoplasmic membrane. In Gram-negative bacteria, Sec-translocated proteins are subsequently secreted via the type II, IV, or V secretion systems. Sec complex components include SecA, D, E, F, G, Y and YajC.
A transmembrane protein complex involved in the translocation of proteins across the cytoplasmic membrane. In Gram-negative bacteria, Sec-translocated proteins are subsequently secreted via the type II, IV, or V secretion systems. Sec complex components include SecA, D, E, F, G, Y and YajC.
A transmembrane protein complex involved in the translocation of proteins across the cytoplasmic membrane. In Gram-negative bacteria, Sec-translocated proteins are subsequently secreted via the type II, IV, or V secretion systems. Sec complex components include SecA, D, E, F, G, Y and YajC.
A transmembrane protein complex involved in the translocation of proteins across the cytoplasmic membrane. In Gram-negative bacteria, Sec-translocated proteins are subsequently secreted via the type II, IV, or V secretion systems. Sec complex components include SecA, D, E, F, G, Y and YajC.
A multisubunit complex consisting of Myb and other proteins that regulates site specific DNA replication, gene amplification and transcriptional repression.
The chemical reactions and pathways involving menthol, the monoterpene 2-isopropyl-5-methylcyclohexanol.
The chemical reactions and pathways resulting in the formation of menthol, the monoterpene 2-isopropyl-5-methylcyclohexanol.
The chemical reactions and pathways resulting in the formation of menthol, the monoterpene 2-isopropyl-5-methylcyclohexanol.
The chemical reactions and pathways resulting in the formation of menthol, the monoterpene 2-isopropyl-5-methylcyclohexanol.
The chemical reactions and pathways resulting in the formation of menthol, the monoterpene 2-isopropyl-5-methylcyclohexanol.
The portion of the plasma membrane surrounding the brush border.
The portion of the plasma membrane surrounding a filopodium.
The portion of the plasma membrane surrounding a microvillus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a ruffle, a projection at the leading edge of a crawling cell.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a ruffle, a projection at the leading edge of a crawling cell.
Interacting selectively and non-covalently with a receptor for gonadotropin-releasing hormone (GnRH), a peptide hormone that is synthesized and released by the hypothalamus and is responsible for the release of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) from the anterior pituitary.
Interacting selectively and non-covalently with a receptor for gonadotropin-releasing hormone (GnRH), a peptide hormone that is synthesized and released by the hypothalamus and is responsible for the release of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) from the anterior pituitary.
Interacting selectively and non-covalently with a receptor for thyrotropin-releasing hormone, a tripeptide hormone that is produced by the hypothalamus and stimulates the release of thyroid-stimulating hormone (TSH) and prolactin by the anterior pituitary.
Interacting selectively and non-covalently with a receptor for thyrotropin-releasing hormone, a tripeptide hormone that is produced by the hypothalamus and stimulates the release of thyroid-stimulating hormone (TSH) and prolactin by the anterior pituitary.
Interacting selectively and non-covalently with a receptor for thyrotropin-releasing hormone, a tripeptide hormone that is produced by the hypothalamus and stimulates the release of thyroid-stimulating hormone (TSH) and prolactin by the anterior pituitary.
A process that is carried out at the cellular level which results in dynamic structural changes to the arrangement of constituent parts of cytoskeletal structures comprising actin filaments and their associated proteins.
A process that is carried out at the cellular level which results in dynamic structural changes to the arrangement of constituent parts of cytoskeletal structures comprising actin filaments and their associated proteins.
A process that is carried out at the cellular level which results in dynamic structural changes to the arrangement of constituent parts of cytoskeletal structures comprising actin filaments and their associated proteins.
A protein complex that consists of an RNA 5' triphosphatase and a guanyl transferase (Cet1p and Ceg1p in S. cerevisiae; Pct1 and Ceg1 in S. pombe) and is involved in mRNA capping.
A protein complex that consists of an RNA 5' triphosphatase and a guanyl transferase (Cet1p and Ceg1p in S. cerevisiae; Pct1 and Ceg1 in S. pombe) and is involved in mRNA capping.
The movement of one microtubule along another microtubule, where the motion is directed towards the minus ends of the microtubules.
The movement of one microtubule along another microtubule, where the motion is directed towards the plus ends of the microtubules.
Any process that activates or increases the rate of progression from anaphase/telophase (high mitotic CDK activity) to G1 (low mitotic CDK activity).
Any process that activates or increases the rate of progression from anaphase/telophase (high mitotic CDK activity) to G1 (low mitotic CDK activity).
Any process that activates or increases the rate of progression from anaphase/telophase (high mitotic CDK activity) to G1 (low mitotic CDK activity).
Any process that activates or increases the rate of progression from anaphase/telophase (high mitotic CDK activity) to G1 (low mitotic CDK activity).
Any process that activates or increases the rate of progression from anaphase/telophase (high mitotic CDK activity) to G1 (low mitotic CDK activity).
Any process that modulates the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that activates or increases the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that activates or increases the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that activates or increases the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that activates or increases the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that activates or increases the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that activates or increases the frequency, rate or extent of chemical reactions and pathways involving anthocyanins.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of anthocyanins.
Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl trans-3-hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl trans-4-hydroxy-L-proline + succinate + CO2.
Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl trans-4-hydroxy-L-proline + succinate + CO2.
Interacting selectively and non-covalently with the brain-derived neurotrophic factor receptor.
Interacting selectively and non-covalently with the brain-derived neurotrophic factor receptor.
The series of molecular signals generated as a consequence of a brain-derived neurotrophic factor receptor binding to one of its physiological ligands.
The series of molecular signals generated as a consequence of a brain-derived neurotrophic factor receptor binding to one of its physiological ligands.
The series of molecular signals generated as a consequence of a brain-derived neurotrophic factor receptor binding to one of its physiological ligands.
Any process that modulates the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that modulates the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that modulates the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that activates or increases the frequency, rate or extent of signaling via the brain-derived neurotrophic factor receptor signaling pathway.
Any process that modulates the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that modulates the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that activates or increases the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that activates or increases the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that activates or increases the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that activates or increases the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that activates or increases the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that activates or increases the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that activates or increases the frequency, rate or extent of brain-derived neurotrophic factor-activated receptor activity.
Any process that modulates the frequency, rate, extent, or location of DNA-templated transcription termination, the process in which transcription is completed; the formation of phosphodiester bonds ceases, the RNA-DNA hybrid dissociates, and RNA polymerase releases the DNA.
Any process that modulates the frequency, rate, extent, or location of DNA-templated transcription termination, the process in which transcription is completed; the formation of phosphodiester bonds ceases, the RNA-DNA hybrid dissociates, and RNA polymerase releases the DNA.
Any process that modulates the frequency, rate, extent, or location of DNA-templated transcription termination, the process in which transcription is completed; the formation of phosphodiester bonds ceases, the RNA-DNA hybrid dissociates, and RNA polymerase releases the DNA.
Any process that modulates the frequency, rate, extent, or location of DNA-templated transcription termination, the process in which transcription is completed; the formation of phosphodiester bonds ceases, the RNA-DNA hybrid dissociates, and RNA polymerase releases the DNA.
Regulation of transcription through variation in where transcription termination occurs.
A type of transcriptional regulation at the level of early termination. This process can occur only in prokaryotes, where transcription of an operon into messenger RNA and translation of that mRNA into polypeptides occur simultaneously. The general principle is that alternative mRNA secondary structures occur under different physiological conditions such as available amount of a particular amino acid. One set of conditions favors early termination of transcription. In the classic example of the trp biosynthesis operon, translation of the gene for a short, trp-containing polypeptide called the trp operon leader peptide pauses either at a trp codon (if tryptophan is scarce) or the stop codon (if trp is readily available). In the former situation transcription continues, but in the latter a Rho-independent terminator forms and reduces, or attenuates, expression of the tryptophan biosynthesis genes. Although the polypeptides encoded by leader peptide genes appear not to be stable once their translation is complete, it is suggested by recent studies that their nascent polypeptide chains interact specifically with ribosomes, specific uncharged tRNAs, or other cellular components to inhibit release at the stop codon and improve the function of transcriptional attenuation as a regulatory switch.
Catalysis of the cyclization of (S)-2,3-epoxysqualene to form a triterpene.
Protein complex that has a role in determining cell polarity, found at the neck of a fungal bud before and during cytokinesis.
Protein complex that has a role in determining cell polarity, found at the tip of a growing fungal bud.
Protein complex that has a role in determining cell polarity, found at the tip of a growing fungal hypha.
Protein complex that has a role in determining cell polarity, found at the tip of the mating projection in unicellular fungi exposed to mating pheromone.
Regulation of transcription by a mechanism that allows RNA polymerase to continue transcription beyond termination site(s).
The cell cycle process in which the contractile ring is maintained in response to the cytokinesis checkpoint; that is when cytokinesis is delayed awaiting completion of nuclear division or the correct formation of cytokinetic structures. This process occurs in the context of cytokinesis that takes place as part of a cell cycle.
The cell cycle process in which the contractile ring is maintained in response to the cytokinesis checkpoint; that is when cytokinesis is delayed awaiting completion of nuclear division or the correct formation of cytokinetic structures. This process occurs in the context of cytokinesis that takes place as part of a cell cycle.
The mitotic cell cycle checkpoint that delays or arrests cell cycle progression until cells have reached a critical size.
A mitotic cell cycle checkpoint that monitors cell size, and negatively regulates cell cycle progression between G1 and S phase until a critical size is reached.
A mitotic cell cycle checkpoint that monitors cell size, and negatively regulates cell cycle progression between G1 and S phase until a critical size is reached.
A mitotic cell cycle checkpoint that monitors cell size, and negatively regulates cell cycle progression between G2 and M phase until a critical size is reached.
A mitotic cell cycle checkpoint that monitors cell size, and negatively regulates cell cycle progression between G2 and M phase until a critical size is reached.
A mitotic cell cycle checkpoint that monitors cell size, and negatively regulates cell cycle progression between G2 and M phase until a critical size is reached.
A cell cycle process that controls cell cycle progression in response to changes in DNA structure by monitoring the integrity of the DNA. The DNA integrity checkpoint begins with detection of DNA damage, defects in DNA structure or DNA replication, and progresses through signal transduction and ends with cell cycle effector processes.
A mitotic cell cycle checkpoint that detects and negatively regulates progression through the G1/S transition of the cell cycle in response to DNA damage.
A cell cycle checkpoint that detects and negatively regulates progression from G2 to M phase in the cell cycle in response to DNA damage.
A mitotic cell cycle checkpoint that slows DNA synthesis in response to DNA damage by the prevention of new origin firing and the stabilization of slow replication fork progression.
A mitotic cell cycle checkpoint that slows DNA synthesis in response to DNA damage by the prevention of new origin firing and the stabilization of slow replication fork progression.
A cell cycle checkpoint that originates from the mitotic or meiotic spindle.
A cell cycle checkpoint that monitors and signals errors in the placement or orientation of the spindle in the cell. This delays the completion of anaphase until errors are corrected.
A cell cycle checkpoint that monitors and signals errors in the placement or orientation of the spindle in the cell. This delays the completion of anaphase until errors are corrected.
A cell cycle checkpoint that monitors and signals errors in the placement or orientation of the spindle in the cell. This delays the completion of anaphase until errors are corrected.
A cell cycle checkpoint that monitors and signals errors in the placement or orientation of the spindle in the cell. This delays the completion of anaphase until errors are corrected.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of membrane rafts, small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of membrane rafts, small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of membrane rafts, small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes.
The process that establishes the spatial arrangement of membrane rafts within a cellular membrane.
Assembly of hemidesmosomes, integrin-containing protein complexes that bind to laminin in the basal lamina. Hemidesmosomes form the contact between the basal surface of epithelial cells and the underlying basal lamina.
A process that impedes the progress of the DNA replication fork at natural replication fork pausing sites within the eukaryotic rDNA repeat spacer.
A process that impedes the progress of the DNA replication fork at natural replication fork pausing sites within the eukaryotic rDNA repeat spacer.
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase D (PLD) and a subsequent increase in cellular levels of phosphatidic acid (PA).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase D (PLD) and a subsequent increase in cellular levels of phosphatidic acid (PA).
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase D (PLD) and a subsequent increase in cellular levels of phosphatidic acid (PA).
Any process that initiates the activity of inactive phospholipase D.
Any process that modulates the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that modulates the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that activates or increases the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that activates or increases the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that activates or increases the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that activates or increases the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that activates or increases the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that activates or increases the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
Any process that activates or increases the frequency, rate or extent of the activity of the inositol 1,4,5-trisphosphate-sensitive calcium-release channel.
A protein complex that possesses nucleotide-dependent protein kinase activity. The nucleotide can be AMP (in S. pombe and human) or ADP (in S. cerevisiae).
A protein complex that possesses nucleotide-dependent protein kinase activity. The nucleotide can be AMP (in S. pombe and human) or ADP (in S. cerevisiae).
A protein complex that possesses nucleotide-dependent protein kinase activity. The nucleotide can be AMP (in S. pombe and human) or ADP (in S. cerevisiae).
A protein complex that possesses nucleotide-dependent protein kinase activity. The nucleotide can be AMP (in S. pombe and human) or ADP (in S. cerevisiae).
A protein complex that possesses nucleotide-dependent protein kinase activity. The nucleotide can be AMP (in S. pombe and human) or ADP (in S. cerevisiae).
A protein complex that possesses nucleotide-dependent protein kinase activity. The nucleotide can be AMP (in S. pombe and human) or ADP (in S. cerevisiae).
A protein complex that possesses nucleotide-dependent protein kinase activity. The nucleotide can be AMP (in S. pombe and human) or ADP (in S. cerevisiae).
The attachment of a cell to the underlying substrate via adhesion molecules.
The chemical reactions and pathways involving wybutosine, 3H-imidazo[1,2-alpha]purine-7-butanoic acid, 4,9-dihydro- alpha-[(methoxycarbonyl)amino]- 4,6-dimethyl-9-oxo- 3-beta-D-ribofuranosyl methyl ester, a modified nucleoside found in some tRNA molecules.
The chemical reactions and pathways involving wybutosine, 3H-imidazo[1,2-alpha]purine-7-butanoic acid, 4,9-dihydro- alpha-[(methoxycarbonyl)amino]- 4,6-dimethyl-9-oxo- 3-beta-D-ribofuranosyl methyl ester, a modified nucleoside found in some tRNA molecules.
The chemical reactions and pathways involving wybutosine, 3H-imidazo[1,2-alpha]purine-7-butanoic acid, 4,9-dihydro- alpha-[(methoxycarbonyl)amino]- 4,6-dimethyl-9-oxo- 3-beta-D-ribofuranosyl methyl ester, a modified nucleoside found in some tRNA molecules.
The chemical reactions and pathways resulting in the formation of wybutosine, 3H-imidazo[1,2-alpha]purine-7-butanoic acid, 4,9-dihydro- alpha-[(methoxycarbonyl)amino]- 4,6-dimethyl-9-oxo- 3-beta-D-ribofuranosyl methyl ester, a modified nucleoside found in some tRNA molecules.
The chemical reactions and pathways resulting in the formation of wybutosine, 3H-imidazo[1,2-alpha]purine-7-butanoic acid, 4,9-dihydro- alpha-[(methoxycarbonyl)amino]- 4,6-dimethyl-9-oxo- 3-beta-D-ribofuranosyl methyl ester, a modified nucleoside found in some tRNA molecules.
An amorphous structure surrounding the core of the centrosome, from which microtubules are nucleated; contains gamma-tubulin.
Interacting selectively and non-covalently with a protein upon poly-ubiquitination of the target protein.
The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential.
The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential.
A proteasome found in the nucleus of a cell.
A proteasome complex found in the cytosol of a cell.
The regulatory subcomplex of a proteasome located in the nucleus of a cell.
A multisubunit complex located in the cytosol of a cell, which caps one or both ends of the proteasome core complex. This complex recognizes, unfolds ubiquitinated proteins and translocates them to the proteasome core complex.
The core complex of a proteasome located in the nucleus of a cell.
The core complex of a proteasome located in the cytosol of a cell.
The subunits forming the outer ring of the core complex of a proteasome located in the nucleus of a cell.
The proteasome core subcomplex that constitutes the two outer rings of the cytosolic proteasome core complex.
The subunits forming the inner ring of the core complex of a proteasome located in the nucleus of a cell.
The proteasome core subcomplex that constitutes the two inner rings of the cytosolic proteasome core complex.
The subunits of the regulatory particle that directly associate with the core complex of a proteasome located in the nucleus of a cell.
The subcomplex of the proteasome regulatory particle that directly associates with the proteasome core complex located in the cytosol of the cell.
The subunits that form the peripheral lid of the regulatory particle of a proteasome located in the nucleus of a cell.
The subcomplex of the cytosolic proteasome regulatory particle that forms the peripheral lid, which is added on top of the base subcomplex.
A centrosome from which one pole of a mitotic or meiotic spindle is organized.
A supercomplex formed by the association of two subcomplexes (known as MIND and Ndc80 in Schizosaccharomyces) with additional proteins at the kinetochores of condensed nuclear chromosomes.
A supercomplex formed by the association of two subcomplexes (known as MIND and Ndc80 in Schizosaccharomyces) with additional proteins at the kinetochores of condensed nuclear chromosomes.
A supercomplex formed by the association of two subcomplexes (known as MIND and Ndc80 in Schizosaccharomyces) with additional proteins at the kinetochores of condensed nuclear chromosomes.
Nuclear heterochromatin that is located adjacent to the CENP-A rich centromere 'central core' and characterized by the modified histone H3K9me3.
Nuclear heterochromatin that is located adjacent to the CENP-A rich centromere 'central core' and characterized by the modified histone H3K9me3.
Nuclear heterochromatin that is located adjacent to the CENP-A rich centromere 'central core' and characterized by the modified histone H3K9me3.
The cell cycle process in which the sister centromeres of one chromosome attach to microtubules that emanate from the same spindle pole, which ensures that homologous maternal and paternal chromosomes are pulled in opposite directions at anaphase of meiosis I.
The cell cycle process in which the sister centromeres of one chromosome attach to microtubules that emanate from the same spindle pole, which ensures that homologous maternal and paternal chromosomes are pulled in opposite directions at anaphase of meiosis I.
Any process that modulates the rate or extent of fever generation.
Any process that stops, prevents, or reduces the rate or extent of fever generation.
Any process that stops, prevents, or reduces the rate or extent of fever generation.
Any process that stops, prevents, or reduces the rate or extent of fever generation.
Any process that stops, prevents, or reduces the rate or extent of fever generation.
Any process that stops, prevents, or reduces the rate or extent of fever generation.
Any process that activates or increases the frequency, rate, or extent of fever generation.
Any process that activates or increases the frequency, rate, or extent of fever generation.
Any process that activates or increases the frequency, rate, or extent of fever generation.
Any process that activates or increases the frequency, rate, or extent of fever generation.
Any process that activates or increases the frequency, rate, or extent of fever generation.
Any process that activates or increases the frequency, rate, or extent of fever generation.
A receptor-mediated endocytosis process that results in the movement of receptors from the plasma membrane to the inside of the cell. The process begins when cell surface receptors are monoubiquitinated following ligand-induced activation. Receptors are subsequently taken up into endocytic vesicles from where they are either targeted to the lysosome or vacuole for degradation or recycled back to the plasma membrane.
Interacting selectively and non-covalently with a ubiquitin conjugating enzyme, any of the E2 proteins.
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
Interacting selectively and non-covalently with beta-endorphin, a peptide generated by the cleavage of pro-opiomelanocortin.
The process in which linear telomeric DNA is remodeled into duplex loops, by the invasion of a 3' single-stranded overhang into the duplex region.
The process in which linear telomeric DNA is remodeled into duplex loops, by the invasion of a 3' single-stranded overhang into the duplex region.
The process in which linear telomeric DNA is remodeled into duplex loops, by the invasion of a 3' single-stranded overhang into the duplex region.
The process in which linear telomeric DNA is remodeled into duplex loops, by the invasion of a 3' single-stranded overhang into the duplex region.
Interacting selectively and non-covalently with an opioid receptor.
Fusion of the membrane of a synaptic vesicle with the presynaptic active zone membrane, thereby releasing its cargo neurotransmitters into the synaptic cleft.
Fusion of the membrane of a synaptic vesicle with the presynaptic active zone membrane, thereby releasing its cargo neurotransmitters into the synaptic cleft.
Fusion of the membrane of a synaptic vesicle with the presynaptic active zone membrane, thereby releasing its cargo neurotransmitters into the synaptic cleft.
Any process that modulates the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that modulates the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that stops, prevents, or reduces the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that activates or increases the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that activates or increases the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that activates or increases the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that activates or increases the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that activates or increases the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that activates or increases the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that activates or increases the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that activates or increases the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
Any process that activates or increases the frequency, rate or extent of synaptic vesicle fusion to the presynaptic membrane.
A chromatophore containing yellow pigment.
Interacting selectively and non-covalently with replication fork barriers, sites that inhibit the progress of replication forks.
The series of molecular signals generated as a consequence of an opioid receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of an opioid receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The series of molecular signals generated as a consequence of an opioid receptor binding to its physiological ligand, where the pathway proceeds with inhibition of adenylyl cyclase and a subsequent decrease in the concentration of cyclic AMP (cAMP).
The process in which a neurotrophic factor induces neuronal synaptic plasticity, the ability of neuronal synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
The proteolytic processing of an inactive enzyme to an active form.
The process in which inactive plasminogen is processed to active plasmin. This process includes cleavage at an internal Arg-Val site to form an N-terminal A-chain and C-terminal B-chain held together by a disulfide bond, and can include further proteolytic cleavage events to remove the preactivation peptide.
Any process in an organism that results in the killing of cells of another organism, including in some cases the death of the other organism. Killing here refers to the induction of death in one cell by another cell, not cell-autonomous death due to internal or other environmental conditions.
Any process in an organism that results in the killing of cells of another organism, including in some cases the death of the other organism. Killing here refers to the induction of death in one cell by another cell, not cell-autonomous death due to internal or other environmental conditions.
Any process in an organism that results in the killing of cells of another organism, including in some cases the death of the other organism. Killing here refers to the induction of death in one cell by another cell, not cell-autonomous death due to internal or other environmental conditions.
Any process that modulates the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
Any process that activates or increases the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
Any process that activates or increases the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
Any process that activates or increases the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
Any process that activates or increases the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
Any process that activates or increases the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
Any process that modulates the frequency, rate or extent of a neurophysiological process, an organ system process carried out by any of the organs or tissues of neurological system.
Any process that modulates the frequency, rate or extent of a neurophysiological process, an organ system process carried out by any of the organs or tissues of neurological system.
Any process that stops, prevents, or reduces the frequency, rate or extent of a neurophysiological process.
Any process that stops, prevents, or reduces the frequency, rate or extent of a neurophysiological process.
Any process that stops, prevents, or reduces the frequency, rate or extent of a neurophysiological process.
Any process that stops, prevents, or reduces the frequency, rate or extent of a neurophysiological process.
Any process that stops, prevents, or reduces the frequency, rate or extent of a neurophysiological process.
Any process that stops, prevents, or reduces the frequency, rate or extent of a neurophysiological process.
Any process that activates or increases the frequency, rate or extent of a neurophysiological process.
Any process that activates or increases the frequency, rate or extent of a neurophysiological process.
Any process that activates or increases the frequency, rate or extent of a neurophysiological process.
Any process that activates or increases the frequency, rate or extent of a neurophysiological process.
Any process that activates or increases the frequency, rate or extent of a neurophysiological process.
Any process that activates or increases the frequency, rate or extent of a neurophysiological process.
Any process that activates or increases the frequency, rate or extent of a neurophysiological process.
Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation.
Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation.
Any homeostatic process in which an organism produces heat, thereby raising its internal temperature.
Any process that modulates the rate or extent of heat generation.
Any process that stops, prevents, or reduces the rate or extent of heat generation.
Any process that stops, prevents, or reduces the rate or extent of heat generation.
Any process that stops, prevents, or reduces the rate or extent of heat generation.
Any process that stops, prevents, or reduces the rate or extent of heat generation.
Any process that activates or increases the rate or extent of heat generation.
Any process that activates or increases the rate or extent of heat generation.
Any process that activates or increases the rate or extent of heat generation.
Any process that activates or increases the rate or extent of heat generation.
Any process that activates or increases the rate or extent of heat generation.
Any homeostatic process in which an organism releases excess heat to the environment, thereby lowering its internal temperature.
Any process that modulates the rate or extent of heat dissipation.
Any process that stops, prevents, or reduces the rate or extent of heat dissipation.
Any process that stops, prevents, or reduces the rate or extent of heat dissipation.
Any process that stops, prevents, or reduces the rate or extent of heat dissipation.
Any process that stops, prevents, or reduces the rate or extent of heat dissipation.
Any process that activates or increases the rate or extent of heat dissipation.
Any process that activates or increases the rate or extent of heat dissipation.
Any process that activates or increases the rate or extent of heat dissipation.
Any process that activates or increases the rate or extent of heat dissipation.
Any process that activates or increases the rate or extent of heat dissipation.
Any process that modulates the frequency, rate or extent of cyclin-dependent protein serine/threonine kinase activity contributing to the G2/M transition of the cell cycle.
Any process that modulates the frequency, rate or extent of cyclin-dependent protein serine/threonine kinase activity contributing to the G2/M transition of the cell cycle.
Any process that modulates the frequency, rate or extent of cyclin-dependent protein serine/threonine kinase activity contributing to the G2/M transition of the cell cycle.
Any process that stops, prevents, or reduces the frequency, rate or extent of cyclin-dependent protein serine/threonine kinase activity contributing to the G2/M transition of the cell cycle.
Any process that stops, prevents, or reduces the frequency, rate or extent of cyclin-dependent protein serine/threonine kinase activity contributing to the G2/M transition of the cell cycle.
Any process that stops, prevents, or reduces the frequency, rate or extent of cyclin-dependent protein serine/threonine kinase activity contributing to the G2/M transition of the cell cycle.
Any process that stops, prevents, or reduces the frequency, rate or extent of cyclin-dependent protein serine/threonine kinase activity contributing to the G2/M transition of the cell cycle.
Any process that stops, prevents, or reduces the frequency, rate or extent of cyclin-dependent protein serine/threonine kinase activity contributing to the G2/M transition of the cell cycle.
Any process that stops, prevents, or reduces the frequency, rate or extent of cyclin-dependent protein serine/threonine kinase activity contributing to the G2/M transition of the cell cycle.
Any process that stops, prevents, or reduces the frequency, rate or extent of cyclin-dependent protein serine/threonine kinase activity contributing to the G2/M transition of the cell cycle.
A series of molecular signals initiated by the binding of a lipopolysaccharide (LPS) to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription. Lipopolysaccharides are major components of the outer membrane of Gram-negative bacteria, making them prime targets for recognition by the immune system.
A series of molecular signals initiated by the binding of a lipopolysaccharide (LPS) to a receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription. Lipopolysaccharides are major components of the outer membrane of Gram-negative bacteria, making them prime targets for recognition by the immune system.
Any process that modulates the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that modulates the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that stops, prevents, or reduces the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that activates or increases the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that activates or increases the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that activates or increases the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that activates or increases the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that activates or increases the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that activates or increases the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
Any process that activates or increases the frequency, rate or extent of signaling in response to detection of lipopolysaccharide.
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 the presence, absence, or concentration of nutrients.
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 extracellular 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 stimulus reflecting the presence, absence, or concentration of nutrients.
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 nutrient stimulus.
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a primary cell septum following nuclear division.
The dark-staining region of a sarcomere, in which myosin thick filaments are present; the center is traversed by the paler H zone, which in turn contains the M line.
The dark-staining region of a sarcomere, in which myosin thick filaments are present; the center is traversed by the paler H zone, which in turn contains the M line.
The dark-staining region of a sarcomere, in which myosin thick filaments are present; the center is traversed by the paler H zone, which in turn contains the M line.
The dark-staining region of a sarcomere, in which myosin thick filaments are present; the center is traversed by the paler H zone, which in turn contains the M line.
A relatively pale zone traversing the center of the A band of a sarcomere, visible in relaxed muscle fibers; consists of the central portion of thick (myosin) filaments that are not overlapped by thin (actin) filaments.
A relatively pale zone traversing the center of the A band of a sarcomere, visible in relaxed muscle fibers; consists of the central portion of thick (myosin) filaments that are not overlapped by thin (actin) filaments.
A region of a sarcomere that appears as a light band on each side of the Z disc, comprising a region of the sarcomere where thin (actin) filaments are not overlapped by thick (myosin) filaments; contains actin, troponin, and tropomyosin; each sarcomere includes half of an I band at each end.
A region of a sarcomere that appears as a light band on each side of the Z disc, comprising a region of the sarcomere where thin (actin) filaments are not overlapped by thick (myosin) filaments; contains actin, troponin, and tropomyosin; each sarcomere includes half of an I band at each end.
A region of a sarcomere that appears as a light band on each side of the Z disc, comprising a region of the sarcomere where thin (actin) filaments are not overlapped by thick (myosin) filaments; contains actin, troponin, and tropomyosin; each sarcomere includes half of an I band at each end.
The pigmented membrane of a plasma membrane-derived thylakoid.
Catalysis of the reaction: NADH + H+ + plastoquinone = NAD+ + plastoquinol.
Catalysis of the reaction: NADH + H+ + plastoquinone = NAD+ + plastoquinol.
The heterodimer formed by the beta and gamma subunits of a heterotrimeric G protein, which dissociates from the alpha subunit upon guanine nuclotide exchange.
The heterodimer formed by the beta and gamma subunits of a heterotrimeric G protein, which dissociates from the alpha subunit upon guanine nuclotide exchange.
Interacting selectively and non-covalently with a G-protein beta subunit.
Interacting selectively and non-covalently with a G-protein gamma subunit.
Interacting selectively and non-covalently with a complex of G-protein beta/gamma subunits.
Interacting selectively and non-covalently with an adenosine receptor.
Interacting selectively and non-covalently with an A1 adenosine receptor.
Interacting selectively and non-covalently with an A2A adenosine receptor.
Interacting selectively and non-covalently with an A2B adenosine receptor.
Interacting selectively and non-covalently with an A3 adenosine receptor.
Interacting selectively and non-covalently with an adrenergic receptor.
Interacting selectively and non-covalently with an alpha-1A adrenergic receptor.
Interacting selectively and non-covalently with an alpha-1B adrenergic receptor.
Interacting selectively and non-covalently with an alpha-1D adrenergic receptor.
Interacting selectively and non-covalently with an alpha-2A adrenergic receptor.
Interacting selectively and non-covalently with an alpha-2B adrenergic receptor.
Interacting selectively and non-covalently with an alpha-2C adrenergic receptor.
Interacting selectively and non-covalently with a beta-1 adrenergic receptor.
Interacting selectively and non-covalently with a beta-2 adrenergic receptor.
Interacting selectively and non-covalently with a beta-3 adrenergic receptor.
Interacting selectively and non-covalently with an adrenomedullin receptor.
Interacting selectively and non-covalently with an angiotensin receptor.
Interacting selectively and non-covalently with a type 1 angiotensin receptor.
Interacting selectively and non-covalently with a type 1 angiotensin receptor.
Interacting selectively and non-covalently with a type 2 angiotensin receptor.
Interacting selectively and non-covalently with a type 2 angiotensin receptor.
Interacting selectively and non-covalently with a bombesin receptor.
Interacting selectively and non-covalently with a subtype 3 bombesin receptor.
Interacting selectively and non-covalently with an endothelin A receptor.
Interacting selectively and non-covalently with an endothelin A receptor.
Interacting selectively and non-covalently with an endothelin B receptor.
Interacting selectively and non-covalently with a gastrin-releasing peptide receptor.
Interacting selectively and non-covalently with a gastrin-releasing peptide receptor.
Interacting selectively and non-covalently with a neuromedin B receptor.
Interacting selectively and non-covalently with a bradykinin receptor.
Interacting selectively and non-covalently with a B1 bradykinin receptor.
Interacting selectively and non-covalently with a B2 bradykinin receptor.
Interacting selectively and non-covalently with a C5a anaphylatoxin chemotactic receptor.
Interacting selectively and non-covalently with a C5L2 anaphylatoxin chemotactic receptor.
Interacting selectively and non-covalently with a calcitonin receptor.
Interacting selectively and non-covalently with a cannabinoid receptor.
Interacting selectively and non-covalently with a type 1 cannabinoid receptor.
Interacting selectively and non-covalently with a type 2 cannabinoid receptor.
Interacting selectively and non-covalently with a haptoglobin, any alpha2 globulin of blood plasma that can combine with free oxyhemoglobin to form a stable complex.
Interacting selectively and non-covalently with a hemoglobin alpha chain.
Interacting selectively and non-covalently with a hemoglobin beta chain.
Interacting selectively and non-covalently with a CXCR4 chemokine receptor.
Interacting selectively and non-covalently with a CXCR4 chemokine receptor.
Interacting selectively and non-covalently with a CXCR5 chemokine receptor.
Interacting selectively and non-covalently with a CXCR5 chemokine receptor.
Interacting selectively and non-covalently with a CXCR6 chemokine receptor.
Interacting selectively and non-covalently with a CXCR6 chemokine receptor.
Interacting selectively and non-covalently with a CXCR6 chemokine receptor.
Interacting selectively and non-covalently with a CCR1 chemokine receptor.
Interacting selectively and non-covalently with a CCR1 chemokine receptor.
Interacting selectively and non-covalently with a CCR2 chemokine receptor.
Interacting selectively and non-covalently with a CCR2 chemokine receptor.
Interacting selectively and non-covalently with a CCR3 chemokine receptor.
Interacting selectively and non-covalently with a CCR3 chemokine receptor.
Interacting selectively and non-covalently with a CCR4 chemokine receptor.
Interacting selectively and non-covalently with a CCR5 chemokine receptor.
Interacting selectively and non-covalently with a CCR6 chemokine receptor.
Interacting selectively and non-covalently with a CCR6 chemokine receptor.
Interacting selectively and non-covalently with a CCR7 chemokine receptor.
Interacting selectively and non-covalently with a CCR7 chemokine receptor.
Interacting selectively and non-covalently with a CCR7 chemokine receptor.
Interacting selectively and non-covalently with a CCR8 chemokine receptor.
Interacting selectively and non-covalently with a CCR9 chemokine receptor.
Interacting selectively and non-covalently with a CCR10 chemokine receptor.
Interacting selectively and non-covalently with a CCR11 chemokine receptor.
Interacting selectively and non-covalently with a CX3C chemokine receptor.
Interacting selectively and non-covalently with a CX3C chemokine receptor.
Interacting selectively and non-covalently with a XCR1 chemokine receptor.
Interacting selectively and non-covalently with a XCR1 chemokine receptor.
Interacting selectively and non-covalently with a cholecystokinin receptor.
Interacting selectively and non-covalently with a type A cholecystokinin receptor.
Interacting selectively and non-covalently with a type B gastrin/cholecystokinin receptor.
Interacting selectively and non-covalently with a cysteinyl leukotriene receptor.
Interacting selectively and non-covalently with a type 1 cysteinyl leukotriene receptor.
Interacting selectively and non-covalently with a type 2 cysteinyl leukotriene receptor.
Interacting selectively and non-covalently with a D1 dopamine receptor.
Interacting selectively and non-covalently with a D1 dopamine receptor.
Interacting selectively and non-covalently with a D2 dopamine receptor.
Interacting selectively and non-covalently with a D3 dopamine receptor.
Interacting selectively and non-covalently with a D4 dopamine receptor.
Interacting selectively and non-covalently with a D5 dopamine receptor.
Interacting selectively and non-covalently with a D5 dopamine receptor.
Interacting selectively and non-covalently with an endothelial differentiation G protein-coupled receptor.
Interacting selectively and non-covalently with an endothelial differentiation G protein-coupled receptor.
Interacting selectively and non-covalently with an Edg-1 sphingosine 1-phosphate receptor.
Interacting selectively and non-covalently with an Edg-2 lysophosphatidic acid receptor.
Interacting selectively and non-covalently with an Edg-2 lysophosphatidic acid receptor.
Interacting selectively and non-covalently with an Edg-3 sphingosine 1-phosphate receptor.
Interacting selectively and non-covalently with an Edg-4 lysophosphatidic acid receptor.
Interacting selectively and non-covalently with an Edg-4 lysophosphatidic acid receptor.
Interacting selectively and non-covalently with an Edg-5 sphingosine 1-phosphate receptor.
Interacting selectively and non-covalently with an Edg-6 sphingosine 1-phosphate receptor.
Interacting selectively and non-covalently with an Edg-7 lysophosphatidic acid receptor.
Interacting selectively and non-covalently with an Edg-7 lysophosphatidic acid receptor.
Interacting selectively and non-covalently with a fMet-Leu-Phe receptor.
Interacting selectively and non-covalently with a fMet-Leu-Phe receptor.
Interacting selectively and non-covalently with a follicle-stimulating hormone receptor.
Interacting selectively and non-covalently with a follicle-stimulating hormone receptor.
Interacting selectively and non-covalently with a follicle-stimulating hormone receptor.
Interacting selectively and non-covalently with a galanin receptor.
Interacting selectively and non-covalently with a type 1 galanin receptor.
Interacting selectively and non-covalently with a type 2 galanin receptor.
Interacting selectively and non-covalently with a type 3 galanin receptor.
Interacting selectively and non-covalently with a gastric inhibitory polypeptide receptor.
Interacting selectively and non-covalently with a ghrelin receptor.
Interacting selectively and non-covalently with a ghrelin receptor.
Interacting selectively and non-covalently with a glucagon receptor.
Interacting selectively and non-covalently with a growth hormone-releasing hormone receptor.
Interacting selectively and non-covalently with a type 1 hypocretin receptor.
Interacting selectively and non-covalently with a type 1 hypocretin receptor.
Interacting selectively and non-covalently with a type 2 hypocretin receptor.
Interacting selectively and non-covalently with a type 2 hypocretin receptor.
Interacting selectively and non-covalently with a kisspeptin receptor.
Interacting selectively and non-covalently with a kisspeptin receptor.
Interacting selectively and non-covalently with a kisspeptin receptor.
Interacting selectively and non-covalently with a kisspeptin receptor.
Interacting selectively and non-covalently with a kisspeptin receptor.
Interacting selectively and non-covalently with a kisspeptin receptor.
Interacting selectively and non-covalently with a leukotriene receptor.
Interacting selectively and non-covalently with a lutropin-choriogonadotropic hormone receptor.
Interacting selectively and non-covalently with a melanin-concentrating hormone receptor.
Interacting selectively and non-covalently with a type 1 melanin-concentrating hormone receptor.
Interacting selectively and non-covalently with a type 2 melanin-concentrating hormone receptor.
Interacting selectively and non-covalently with a melanocortin receptor.
Interacting selectively and non-covalently with a corticotropin hormone receptor.
Interacting selectively and non-covalently with a corticotropin hormone receptor.
Interacting selectively and non-covalently with a corticotropin hormone receptor.
Interacting selectively and non-covalently with a corticotropin hormone receptor.
Interacting selectively and non-covalently with a corticotropin hormone receptor.
Interacting selectively and non-covalently with a corticotropin hormone receptor.
Interacting selectively and non-covalently with a type 3 melanocortin receptor.
Interacting selectively and non-covalently with a type 4 melanocortin receptor.
Interacting selectively and non-covalently with a type 5 melanocortin receptor.
Interacting selectively and non-covalently with a melatonin receptor.
Interacting selectively and non-covalently with a type 1A melatonin receptor.
Interacting selectively and non-covalently with a type 1B melatonin receptor.
Interacting selectively and non-covalently with a H9 melatonin receptor.
Interacting selectively and non-covalently with a motilin receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) GABA receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) GABA receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) GABA receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) GABA receptor.
Interacting selectively and non-covalently with a type 1 metabotropic GABA receptor.
Interacting selectively and non-covalently with a type 2 metabotropic GABA receptor.
Interacting selectively and non-covalently with a type 1 metabotropic glutamate receptor.
Interacting selectively and non-covalently with a type 2 metabotropic glutamate receptor.
Interacting selectively and non-covalently with a type 3 metabotropic glutamate receptor.
Interacting selectively and non-covalently with a type 4 metabotropic glutamate receptor.
Interacting selectively and non-covalently with a type 5 metabotropic glutamate receptor.
Interacting selectively and non-covalently with a type 6 metabotropic glutamate receptor.
Interacting selectively and non-covalently with a type 7 metabotropic glutamate receptor.
Interacting selectively and non-covalently with a type 8 metabotropic glutamate receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) histamine receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) histamine receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) histamine receptor.
Interacting selectively and non-covalently with a H1 histamine receptor.
Interacting selectively and non-covalently with a H2 histamine receptor.
Interacting selectively and non-covalently with a H3 histamine receptor.
Interacting selectively and non-covalently with a H4 histamine receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) nucleotide receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) nucleotide receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) nucleotide receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) nucleotide receptor.
Interacting selectively and non-covalently with a P2Y1 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y2 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y4 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y5 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y6 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y8 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y9 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y10 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y11 nucleotide receptor.
Interacting selectively and non-covalently with a metabotropic serotonin receptor.
Interacting selectively and non-covalently with a metabotropic serotonin receptor.
Interacting selectively and non-covalently with a metabotropic serotonin receptor.
Interacting selectively and non-covalently with a metabotropic serotonin receptor.
Interacting selectively and non-covalently with a type 1B serotonin receptor.
Interacting selectively and non-covalently with a type 1B serotonin receptor.
Interacting selectively and non-covalently with a type 1D serotonin receptor.
Interacting selectively and non-covalently with a type 1D serotonin receptor.
Interacting selectively and non-covalently with a type 1E serotonin receptor.
Interacting selectively and non-covalently with a type 1E serotonin receptor.
Interacting selectively and non-covalently with a type 1F serotonin receptor.
Interacting selectively and non-covalently with a type 1F serotonin receptor.
Interacting selectively and non-covalently with a type 2A serotonin receptor.
Interacting selectively and non-covalently with a type 2A serotonin receptor.
Interacting selectively and non-covalently with a type 2B serotonin receptor.
Interacting selectively and non-covalently with a type 2B serotonin receptor.
Interacting selectively and non-covalently with a type 2C serotonin receptor.
Interacting selectively and non-covalently with a type 2C serotonin receptor.
Interacting selectively and non-covalently with a type 4 serotonin receptor.
Interacting selectively and non-covalently with a type 4 serotonin receptor.
Interacting selectively and non-covalently with a type 5A serotonin receptor.
Interacting selectively and non-covalently with a type 5A serotonin receptor.
Interacting selectively and non-covalently with a type 5B serotonin receptor.
Interacting selectively and non-covalently with a type 5B serotonin receptor.
Interacting selectively and non-covalently with a type 6 serotonin receptor.
Interacting selectively and non-covalently with a type 6 serotonin receptor.
Interacting selectively and non-covalently with a type 7 serotonin receptor.
Interacting selectively and non-covalently with a type 7 serotonin receptor.
Interacting selectively and non-covalently with a neurokinin receptor.
Interacting selectively and non-covalently with a substance P receptor.
Interacting selectively and non-covalently with a substance P receptor.
Interacting selectively and non-covalently with a neuromedin K receptor.
Interacting selectively and non-covalently with a neuromedin K receptor.
Interacting selectively and non-covalently with a substance K receptor.
Interacting selectively and non-covalently with a substance K receptor.
A protein complex formed by the stable binding of a haptoglobin to hemoglobin.
Interacting selectively and non-covalently with a type 1 neuromedin U receptor.
Interacting selectively and non-covalently with a type 2 neuromedin U receptor.
Interacting selectively and non-covalently with a neuropeptide Y receptor.
Interacting selectively and non-covalently with a neuropeptide Y receptor.
Interacting selectively and non-covalently with a type 1 neuropeptide Y receptor.
Interacting selectively and non-covalently with a type 2 neuropeptide Y receptor.
Interacting selectively and non-covalently with a type 4 neuropeptide Y receptor.
Interacting selectively and non-covalently with a type 4 neuropeptide Y receptor.
Interacting selectively and non-covalently with a type 5 neuropeptide Y receptor.
Interacting selectively and non-covalently with a neurotensin receptor.
Interacting selectively and non-covalently with a type 1 neurotensin receptor.
A process that prevents non-homologous end joining at telomere, thereby ensuring that telomeres do not fuse.
Interacting selectively and non-covalently with an olfactory receptor.
Interacting selectively and non-covalently with a delta-type opioid receptor.
Interacting selectively and non-covalently with a delta-type opioid receptor.
Interacting selectively and non-covalently with a kappa-type opioid receptor.
Interacting selectively and non-covalently with a kappa-type opioid receptor.
Interacting selectively and non-covalently with a mu-type opioid receptor.
Interacting selectively and non-covalently with a mu-type opioid receptor.
Interacting selectively and non-covalently with a nociceptin receptor.
Interacting selectively and non-covalently with an orexigenic neuropeptide QRFP receptor.
Interacting selectively and non-covalently with an oxytocin receptor.
Interacting selectively and non-covalently with a parathyroid hormone receptor.
Interacting selectively and non-covalently with a type 1 parathyroid hormone receptor.
Interacting selectively and non-covalently with a pituitary adenylate cyclase-activating polypeptide receptor.
Interacting selectively and non-covalently with a pituitary adenylate cyclase-activating polypeptide receptor.
Interacting selectively and non-covalently with a pituitary adenylate cyclase-activating polypeptide receptor.
Interacting selectively and non-covalently with a platelet activating factor receptor.
The formation of the single stranded telomeric 3' overhang, a conserved feature that ranges in length from 12 nt in budding yeast to approximately 500 nt in humans.
The formation of the single stranded telomeric 3' overhang, a conserved feature that ranges in length from 12 nt in budding yeast to approximately 500 nt in humans.
Interacting selectively and non-covalently with a prolactin-releasing peptide receptor.
Interacting selectively and non-covalently with a prostanoid receptor.
Interacting selectively and non-covalently with a prostaglandin D2 receptor.
Interacting selectively and non-covalently with a prostaglandin D2 receptor.
Interacting selectively and non-covalently with an EP1 subtype prostaglandin E2 receptor.
Interacting selectively and non-covalently with an EP1 subtype prostaglandin E2 receptor.
Interacting selectively and non-covalently with an EP2 subtype prostaglandin E2 receptor.
Interacting selectively and non-covalently with an EP2 subtype prostaglandin E2 receptor.
Interacting selectively and non-covalently with an EP3 subtype prostaglandin E2 receptor.
Interacting selectively and non-covalently with an EP3 subtype prostaglandin E2 receptor.
Interacting selectively and non-covalently with an EP4 subtype prostaglandin E2 receptor.
Interacting selectively and non-covalently with an EP4 subtype prostaglandin E2 receptor.
Interacting selectively and non-covalently with a prostaglandin F2-alpha receptor.
Interacting selectively and non-covalently with a prostaglandin F2-alpha receptor.
Interacting selectively and non-covalently with a prostacyclin receptor.
Interacting selectively and non-covalently with a prostacyclin receptor.
Interacting selectively and non-covalently with a thromboxane A2 receptor.
Interacting selectively and non-covalently with a thromboxane A2 receptor.
Interacting selectively and non-covalently with a proteinase activated receptor.
Interacting selectively and non-covalently with a type 1 proteinase activated receptor.
Interacting selectively and non-covalently with a type 1 proteinase activated receptor.
Interacting selectively and non-covalently with a type 2 proteinase activated receptor.
Interacting selectively and non-covalently with a type 3 proteinase activated receptor.
Interacting selectively and non-covalently with a type 4 proteinase activated receptor.
Interacting selectively and non-covalently with a secretin receptor.
Interacting selectively and non-covalently with a somatostatin receptor.
Interacting selectively and non-covalently with a type 1 somatostatin receptor.
Interacting selectively and non-covalently with a type 2 somatostatin receptor.
Interacting selectively and non-covalently with a type 3 somatostatin receptor.
Interacting selectively and non-covalently with a type 4 somatostatin receptor.
Interacting selectively and non-covalently with a type 5 somatostatin receptor.
Interacting selectively and non-covalently with a taste receptor.
Interacting selectively and non-covalently with a type 1 member 1 taste receptor.
Interacting selectively and non-covalently with a type 1 member 2 taste receptor.
Interacting selectively and non-covalently with a type 1 member 3 taste receptor.
Interacting selectively and non-covalently with a type 1 member 3 taste receptor.
The directed movement of a lipid droplet along a microtubule, mediated by motor proteins.
The directed movement of a lipid droplet along a microtubule, mediated by motor proteins.
The directed movement of a lipid droplet along a microtubule, mediated by motor proteins.
Interacting selectively and non-covalently with a urotensin receptor.
Interacting selectively and non-covalently with a vasoactive intestinal polypeptide receptor.
Interacting selectively and non-covalently with a vasoactive intestinal polypeptide receptor.
Interacting selectively and non-covalently with a type 1 vasoactive intestinal polypeptide receptor.
Interacting selectively and non-covalently with a type 1 vasoactive intestinal polypeptide receptor.
Interacting selectively and non-covalently with a type 2 vasoactive intestinal polypeptide receptor.
Interacting selectively and non-covalently with a type 2 vasoactive intestinal polypeptide receptor.
Interacting selectively and non-covalently with a vasopressin receptor.
Interacting selectively and non-covalently with a V1A vasopressin receptor.
Interacting selectively and non-covalently with a V1B vasopressin receptor.
Interacting selectively and non-covalently with a V2 vasopressin receptor.
The translocon of the inner envelope of chloroplasts, which facilitates the import of proteins across the chloroplast inner membrane.
The double lipid bilayer enclosing the chromoplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
The inner, i.e. lumen-facing, lipid bilayer of the chromoplast envelope; also faces the chromoplast stroma.
The outer, i.e. cytoplasm-facing, lipid bilayer of the chromoplast envelope.
The lipid bilayer surrounding an early endosome.
The lipid bilayer surrounding a late endosome.
The lipid bilayer surrounding a microbody.
The volume enclosed by the membrane of an endosome.
The volume enclosed by the membrane of an early endosome.
The volume enclosed by the membrane of a late endosome.
The volume enclosed by the membranes of a microbody.
The volume enclosed by the membranes of a glyoxysome.
Stable, specialized structure for the ingestion of food by the cell into phagosomes.
Stable, specialized structure for extrusion of waste by the cell into the surrounding medium.
Complex basket- or funnel-like structure used by the cell to collect food and channel it to the cytostome; includes specialized sub-structures made up of closely-spaced cilia and underlying basal bodies and fibrillar systems.
Stable structure that regulates the flow of liquid between the contractile vacuole and the surrounding medium.
A process that decreases synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
A process that decreases synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
A process that decreases synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
A process that decreases synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
A process that increases synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
A process that increases synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
A process that increases synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
A process that increases synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
A process that increases synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
A process that modulates synaptic metaplasticity. Metaplasticity is a higher-order form of plasticity and is manifest as a change in the ability to induce subsequent synaptic plasticity that is the ability of synapses to change as circumstances require.
A process that decreases synaptic metaplasticity. Metaplasticity is a higher-order form of plasticity and is manifest as a change in the ability to induce subsequent synaptic plasticity that is the ability of synapses to change as circumstances require.
A process that decreases synaptic metaplasticity. Metaplasticity is a higher-order form of plasticity and is manifest as a change in the ability to induce subsequent synaptic plasticity that is the ability of synapses to change as circumstances require.
A process that decreases synaptic metaplasticity. Metaplasticity is a higher-order form of plasticity and is manifest as a change in the ability to induce subsequent synaptic plasticity that is the ability of synapses to change as circumstances require.
A process that decreases synaptic metaplasticity. Metaplasticity is a higher-order form of plasticity and is manifest as a change in the ability to induce subsequent synaptic plasticity that is the ability of synapses to change as circumstances require.
A process that increases synaptic metaplasticity. Metaplasticity is a higher-order form of plasticity and is manifest as a change in the ability to induce subsequent synaptic plasticity that is the ability of synapses to change as circumstances require.
A process that increases synaptic metaplasticity. Metaplasticity is a higher-order form of plasticity and is manifest as a change in the ability to induce subsequent synaptic plasticity that is the ability of synapses to change as circumstances require.
A process that increases synaptic metaplasticity. Metaplasticity is a higher-order form of plasticity and is manifest as a change in the ability to induce subsequent synaptic plasticity that is the ability of synapses to change as circumstances require.
A process that increases synaptic metaplasticity. Metaplasticity is a higher-order form of plasticity and is manifest as a change in the ability to induce subsequent synaptic plasticity that is the ability of synapses to change as circumstances require.
A process that increases synaptic metaplasticity. Metaplasticity is a higher-order form of plasticity and is manifest as a change in the ability to induce subsequent synaptic plasticity that is the ability of synapses to change as circumstances require.
The directed movement of any of the vitamin B6 compounds -- pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate -- 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 pyridoxal into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Pyridoxal, 3-hydroxy-5-(hydroxymethyl)-2-methyl-4-pyridinecarboxaldehyde, is 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 directed movement of pyridoxal phosphate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore; pyridoxal phosphate is pyridoxal phosphorylated at the hydroxymethyl group of C-5, and is the active form of vitamin B6.
The directed movement of pyridoxamine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Pyridoxamine, 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol, is 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 directed movement of pyridoxine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Pyridoxine, 2-methyl-3-hydroxy-4,5-bis(hydroxymethyl)pyridine, is 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.
Enables the transfer of any of the vitamin B6 compounds, pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate, from one side of a membrane to the other.
Enables the transfer of pyridoxal from one side of a membrane to the other. Pyridoxal, 3-hydroxy-5-(hydroxymethyl)-2-methyl-4-pyridinecarboxaldehyde, is 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.
Enables the transfer of pyridoxal phosphate from one side of a membrane to the other. Pyridoxal phosphate is pyridoxal phosphorylated at the hydroxymethyl group of C-5, and is the active form of vitamin B6.
Enables the transfer of pyridoxamine from one side of a membrane to the other. Pyridoxamine, 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol, is 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.
Enables the transfer of pyridoxine from one side of a membrane to the other. Pyridoxine, 2-methyl-3-hydroxy-4,5-bis(hydroxymethyl)pyridine, is 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.
A series of molecular signals mediated by TOR (Target of rapamycin) proteins, members of the phosphoinositide (PI) 3-kinase related kinase (PIKK) family that act as serine/threonine kinases in response to nutrient availability or growth factors.
A series of molecular signals mediated by TOR (Target of rapamycin) proteins, members of the phosphoinositide (PI) 3-kinase related kinase (PIKK) family that act as serine/threonine kinases in response to nutrient availability or growth factors.
A series of molecular signals mediated by TOR (Target of rapamycin) proteins, members of the phosphoinositide (PI) 3-kinase related kinase (PIKK) family that act as serine/threonine kinases in response to nutrient availability or growth factors.
A series of molecular signals mediated by TOR (Target of rapamycin) proteins, members of the phosphoinositide (PI) 3-kinase related kinase (PIKK) family that act as serine/threonine kinases in response to nutrient availability or growth factors.
A series of molecular signals mediated by TOR (Target of rapamycin) proteins, members of the phosphoinositide (PI) 3-kinase related kinase (PIKK) family that act as serine/threonine kinases in response to nutrient availability or growth factors.
A series of molecular signals mediated by TOR (Target of rapamycin) proteins, members of the phosphoinositide (PI) 3-kinase related kinase (PIKK) family that act as serine/threonine kinases in response to nutrient availability or growth factors.
A series of molecular signals that forms a pathway of communication from the mitochondria to the nucleus and initiates cellular changes in response to changes in mitochondrial function.
A series of molecular signals that forms a pathway of communication from the mitochondria to the nucleus and initiates cellular changes in response to changes in mitochondrial function.
A series of molecular signals that forms a pathway of communication from the mitochondria to the nucleus and initiates cellular changes in response to changes in mitochondrial function.
A series of molecular signals that forms a pathway of communication from the mitochondria to the nucleus and initiates cellular changes in response to changes in mitochondrial function.
A protein complex that contains at least TOR (target of rapamycin) and Raptor (regulatory-associated protein of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of S6K. In Saccharomyces, the complex contains Kog1p, Lst8p, Tco89p, and either Tor1p or Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Raptor (regulatory-associated protein of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of S6K. In Saccharomyces, the complex contains Kog1p, Lst8p, Tco89p, and either Tor1p or Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Raptor (regulatory-associated protein of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of S6K. In Saccharomyces, the complex contains Kog1p, Lst8p, Tco89p, and either Tor1p or Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Raptor (regulatory-associated protein of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of S6K. In Saccharomyces, the complex contains Kog1p, Lst8p, Tco89p, and either Tor1p or Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Raptor (regulatory-associated protein of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of S6K. In Saccharomyces, the complex contains Kog1p, Lst8p, Tco89p, and either Tor1p or Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Raptor (regulatory-associated protein of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of S6K. In Saccharomyces, the complex contains Kog1p, Lst8p, Tco89p, and either Tor1p or Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Raptor (regulatory-associated protein of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of S6K. In Saccharomyces, the complex contains Kog1p, Lst8p, Tco89p, and either Tor1p or Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Raptor (regulatory-associated protein of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of S6K. In Saccharomyces, the complex contains Kog1p, Lst8p, Tco89p, and either Tor1p or Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Rictor (rapamycin-insensitive companion of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of PKB (also called AKT). In Saccharomyces, the complex contains Avo1p, Avo2p, Tsc11p, Lst8p, Bit61p, Slm1p, Slm2p, and Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Rictor (rapamycin-insensitive companion of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of PKB (also called AKT). In Saccharomyces, the complex contains Avo1p, Avo2p, Tsc11p, Lst8p, Bit61p, Slm1p, Slm2p, and Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Rictor (rapamycin-insensitive companion of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of PKB (also called AKT). In Saccharomyces, the complex contains Avo1p, Avo2p, Tsc11p, Lst8p, Bit61p, Slm1p, Slm2p, and Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Rictor (rapamycin-insensitive companion of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of PKB (also called AKT). In Saccharomyces, the complex contains Avo1p, Avo2p, Tsc11p, Lst8p, Bit61p, Slm1p, Slm2p, and Tor2p.
A protein complex that contains at least TOR (target of rapamycin) and Rictor (rapamycin-insensitive companion of TOR), or orthologs of, in complex with other signaling components. Mediates the phosphorylation and activation of PKB (also called AKT). In Saccharomyces, the complex contains Avo1p, Avo2p, Tsc11p, Lst8p, Bit61p, Slm1p, Slm2p, and Tor2p.
Heterochromatic regions of the chromosome found at the telomeres.
Heterochromatic regions of the chromosome found at silenced mating-type loci.
Any process that affects the rate, extent or location of chromatin silencing.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing.
Any process that activates or increases the frequency, rate or extent of chromatin silencing.
Any process that activates or increases the frequency, rate or extent of chromatin silencing.
Any process that activates or increases the frequency, rate or extent of chromatin silencing.
Any process that activates or increases the frequency, rate or extent of chromatin silencing.
Any process that activates or increases the frequency, rate or extent of chromatin silencing.
Any process that activates or increases the frequency, rate or extent of chromatin silencing.
Any process that affects the rate, extent or location of chromatin silencing at telomeres.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing at telomeres.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing at telomeres.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing at telomeres.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing at telomeres.
Any process that stops, prevents, or reduces the frequency, rate or extent of chromatin silencing at telomeres.
Any process that activates or increases the frequency, rate or extent of chromatin silencing at telomeres.
Any process that activates or increases the frequency, rate or extent of chromatin silencing at telomeres.
Any process that activates or increases the frequency, rate or extent of chromatin silencing at telomeres.
Any process that activates or increases the frequency, rate or extent of chromatin silencing at telomeres.
Any process that activates or increases the frequency, rate or extent of chromatin silencing at telomeres.
Any process that activates or increases the frequency, rate or extent of chromatin silencing at telomeres.
A two-stranded helical polymer of the protein actin.
Protease complex of the mitochondrial inner membrane whose catalytic residues lie on the intermembrane space side of the inner membrane; involved in mitochondrial protein turnover. Contains a subunit belonging to the AAA family of ATP-dependent metalloproteases.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving glucocorticoids.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glucocorticoids.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glucocorticoids.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glucocorticoids.
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of glucocorticoids.
Any process that modulates the frequency, rate or extent of addition of the phosphorylation by a protein of one or more of its own residues.
Any process that stops, prevents or decreases the rate of the phosphorylation by a protein of one or more of its own residues.
Any process that stops, prevents or decreases the rate of the phosphorylation by a protein of one or more of its own residues.
Any process that stops, prevents or decreases the rate of the phosphorylation by a protein of one or more of its own residues.
Any process that stops, prevents or decreases the rate of the phosphorylation by a protein of one or more of its own residues.
Any process that stops, prevents or decreases the rate of the phosphorylation by a protein of one or more of its own residues.
Any process that activates or increases the frequency, rate or extent of the phosphorylation by a protein of one or more of its own residues.
Any process that activates or increases the frequency, rate or extent of the phosphorylation by a protein of one or more of its own residues.
Any process that activates or increases the frequency, rate or extent of the phosphorylation by a protein of one or more of its own residues.
Any process that activates or increases the frequency, rate or extent of the phosphorylation by a protein of one or more of its own residues.
Any process that activates or increases the frequency, rate or extent of the phosphorylation by a protein of one or more of its own residues.
Any process that activates or increases the frequency, rate or extent of the phosphorylation by a protein of one or more of its own residues.
Catalysis of the reaction: ATP + a short-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA; short-chain fatty acids are fatty acids with a chain length of less than C6.
Catalysis of the reaction: ATP + a short-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA; short-chain fatty acids are fatty acids with a chain length of less than C6.
Catalysis of the reaction: ATP + a short-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA; short-chain fatty acids are fatty acids with a chain length of less than C6.
Catalysis of the reaction: ATP + a medium-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA; a medium-chain fatty acid is any fatty acid with a chain length of between C6 and C12.
Catalysis of the reaction: ATP + a medium-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA; a medium-chain fatty acid is any fatty acid with a chain length of between C6 and C12.
Catalysis of the reaction: ATP + a medium-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA; a medium-chain fatty acid is any fatty acid with a chain length of between C6 and C12.
Catalysis of the reaction: ATP + a very-long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA; a very long-chain fatty acid is a fatty acid which has a chain length greater than C22.
Catalysis of the reaction: ATP + a very-long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA; a very long-chain fatty acid is a fatty acid which has a chain length greater than C22.
Catalysis of the reaction: ATP + a very-long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA; a very long-chain fatty acid is a fatty acid which has a chain length greater than C22.
Any series of molecular signals generated as a consequence of a corticosteroid binding to its receptor.
Any series of molecular signals generated as a consequence of a mineralocorticoid binding to its receptor.
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 corticosteroid hormone stimulus. A corticosteroid is a steroid hormone that is produced in the adrenal cortex. Corticosteroids are involved in a wide range of physiologic systems such as stress response, immune response and regulation of inflammation, carbohydrate metabolism, protein catabolism, blood electrolyte levels, and behavior. They include glucocorticoids and mineralocorticoids.
Interacting selectively and non-covalently with a cortisol receptor.
Interacting selectively and non-covalently with a mineralocorticoid receptor.
Combining with cortisol and transmitting the signal within the cell to trigger a change in cell activity or function.
Catalysis of the reaction: N-beta-alanyl histamine + H2O = histamine + beta-alanine.
Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
A double membrane structure enclosing an organelle, including two lipid bilayers and the region between them. In some cases, an organelle envelope may have more than two membranes.
The outer, i.e. cytoplasm-facing in a cellular organelle, lipid bilayer of an organelle envelope.
Either of the lipid bilayers that surround a chloroplast and form the chloroplast envelope.
The region between the inner and outer lipid bilayers of an organelle envelope.
The region between the inner and outer lipid bilayers of a chloroplast envelope.
The region between the inner and outer lipid bilayers of a chromoplast envelope.
The enclosed volume within a sealed membrane or between two sealed membranes. Encompasses the volume enclosed by the membranes of a particular organelle, e.g. endoplasmic reticulum lumen, or the space between the two lipid bilayers of a double membrane surrounding an organelle, e.g. nuclear envelope lumen.
A multilayered structure surrounding all or part of a cell; encompasses one or more lipid bilayers, and may include a cell wall layer; also includes the space between layers.
Any thylakoid within a plastid.
The volume enclosed by a thylakoid membrane.
The volume enclosed by a plastid thylakoid membrane.
The volume enclosed by a plasma membrane-derived thylakoid.
The volume enclosed by the nuclear inner membrane.
Any small, fluid-filled, spherical organelle enclosed by membrane.
Any small, fluid-filled, spherical organelle enclosed by membrane.
Any small, fluid-filled, spherical organelle enclosed by membrane.
The volume enclosed by the membrane or protein that forms a vesicle.
A compartment that consists of a lumen and an enclosing membrane, and is part of an organelle.
Any of the thin, flattened membrane-bounded compartments that form the central portion of the Golgi complex.
A leucoplast in which protein is stored.
Self-propelled movement of a cell or organism from one location to another in a behavioral context; the aspect of locomotory behavior having to do with movement.
The series of molecular signals generated as a consequence of a bombesin receptor binding to one of its physiological ligands.
The directed movement of mRNA from the nucleus to the cytoplasm during a heat stimulus, a temperature stimulus above the optimal temperature for the organism; in particular, a process that enables an organism withstand exposure to temperatures that would otherwise lethally impair poly(A)+ mRNA-nucleus export.
The directed movement of mRNA from the nucleus to the cytoplasm during a heat stimulus, a temperature stimulus above the optimal temperature for the organism; in particular, a process that enables an organism withstand exposure to temperatures that would otherwise lethally impair poly(A)+ mRNA-nucleus export.
Any process that modulates the frequency, rate or extent of contraction of the actomyosin ring involved in cytokinesis that takes place as part of a cell cycle.
Any process that modulates the frequency, rate or extent of contraction of the actomyosin ring involved in cytokinesis that takes place as part of a cell cycle.
The biological transducer activity that accepts energy and converts it to another form, often by transfer to another molecule within the cell.
The biological transducer activity that accepts energy and converts it to another form, often by transfer to another molecule within the cell.
Absorbing energy from one or more photons and transferring their energy to another molecule, usually a protein, within the cell.
Interacting selectively and non-covalently with insulin-like growth factor I.
Interacting selectively and non-covalently with insulin-like growth factor II.
Interacting selectively and non-covalently with any thioesterase enzyme.
Interacting selectively and non-covalently with the N-terminus of a protein that has the potential to be, or has been, modified by N-terminal myristoylation. Binding affinity is typically altered by myristoylation; for example, N-terminal myristoylation of HIV Nef increases its affinity for calmodulin.
Any process that modulates the frequency, rate or extent of fatty acid bbeta-oxidation.
Any process that stops, prevents, or reduces the frequency, rate or extent of fatty acid beta-oxidation.
Any process that stops, prevents, or reduces the frequency, rate or extent of fatty acid beta-oxidation.
Any process that stops, prevents, or reduces the frequency, rate or extent of fatty acid beta-oxidation.
Any process that stops, prevents, or reduces the frequency, rate or extent of fatty acid beta-oxidation.
Any process that activates or increases the frequency, rate or extent of fatty acid beta-oxidation.
Any process that activates or increases the frequency, rate or extent of fatty acid beta-oxidation.
Any process that activates or increases the frequency, rate or extent of fatty acid beta-oxidation.
Any process that activates or increases the frequency, rate or extent of fatty acid beta-oxidation.
Any process that activates or increases the frequency, rate or extent of fatty acid beta-oxidation.
Catalysis of the transfer an alpha-D-glucosyl residue in a (1->4)-alpha-D-glucan to the primary hydroxy group of glucose, free or combined in a (1->4)-alpha-D-glucan.
Catalysis of the transfer an alpha-D-glucosyl residue in a (1->4)-alpha-D-glucan to the primary hydroxy group of glucose, free or combined in a (1->4)-alpha-D-glucan.
Catalysis of the transfer an alpha-D-glucosyl residue in a (1->4)-alpha-D-glucan to the primary hydroxy group of glucose, free or combined in a (1->4)-alpha-D-glucan.
Catalysis of the transfer an alpha-D-glucosyl residue in a (1->4)-alpha-D-glucan to the primary hydroxy group of glucose, free or combined in a (1->4)-alpha-D-glucan.
Catalysis of the transfer an alpha-D-glucosyl residue in a (1->4)-alpha-D-glucan to the primary hydroxy group of glucose, free or combined in a (1->4)-alpha-D-glucan.
A protein complex that binds interleukin-28 and interleukin-29. It is composed of an alpha and a beta receptor subunit (in human IFNLR1/IL28Ralpha & IL10RB) and either Interleukin-28 (IFNL2 or IFNL3) or Interleukin-29 (IFNL1).
Interacting selectively and non-covalently with the interleukin-28 receptor.
Interacting selectively and non-covalently with the interleukin-28 receptor.
The series of molecular signals that bring about the relay, amplification or dampening of a signal generated in response to a cue, such as starvation or pheromone exposure, in organisms that undergo conjugation with cellular fusion.
Any process that modulates the frequency, rate or extent of TOR signaling.
Any process that modulates the frequency, rate or extent of TOR signaling.
Any process that modulates the frequency, rate or extent of TOR signaling.
Any process that modulates the frequency, rate or extent of TOR signaling.
Any process that modulates the frequency, rate or extent of TOR signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling.
Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling.
Any process that activates or increases the frequency, rate or extent of TOR signaling.
Any process that activates or increases the frequency, rate or extent of TOR signaling.
Any process that activates or increases the frequency, rate or extent of TOR signaling.
Any process that activates or increases the frequency, rate or extent of TOR signaling.
Any process that activates or increases the frequency, rate or extent of TOR signaling.
Any process that activates or increases the frequency, rate or extent of TOR signaling.
Any process that activates or increases the frequency, rate or extent of TOR signaling.
Any process that activates or increases the frequency, rate or extent of TOR signaling.
Any process that activates or increases the frequency, rate or extent of TOR signaling.
Any process that activates or increases the frequency, rate or extent of TOR signaling.
A membrane-bounded intracellular vesicle as initially formed upon the ingestion of particulate material by phagocytosis.
A membrane-bounded intracellular vesicle formed by maturation of an early phagosome following the ingestion of particulate material by phagocytosis; during maturation, phagosomes acquire markers of late endosomes and lysosomes.
A membrane-bounded intracellular vesicle formed by maturation of an early phagosome following the ingestion of particulate material by phagocytosis; during maturation, phagosomes acquire markers of late endosomes and lysosomes.
A series of molecular signals within the cell that are mediated by a member of the ARF family of proteins switching to a GTP-bound active state.
Any process that modulates the frequency, rate or extent of ARF protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of ARF protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of ARF protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of ARF protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of ARF protein signal transduction.
Any process that activates or increases the frequency, rate or extent of ARF protein signal transduction.
Any process that activates or increases the frequency, rate or extent of ARF protein signal transduction.
Any process that activates or increases the frequency, rate or extent of ARF protein signal transduction.
Any process that activates or increases the frequency, rate or extent of ARF protein signal transduction.
Any process that activates or increases the frequency, rate or extent of ARF protein signal transduction.
Any process that modulates the frequency, rate or extent of Ran protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Ran protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Ran protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Ran protein signal transduction.
Any process that stops, prevents, or reduces the frequency, rate or extent of Ran protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Ran protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Ran protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Ran protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Ran protein signal transduction.
Any process that activates or increases the frequency, rate or extent of Ran protein signal transduction.
Catalysis of the reaction: 2-methylbutanol + NADP+ = 2-methylbutanal + NADPH + H+.
Catalysis of the reaction: 2-methylbutanol + NADP+ = 2-methylbutanal + NADPH + H+.
A prominent mass in the cytoplasm of previtellogenic oocytes. The cloud contains both mitochondria and electron-dense granulofibrillar material (GFM) and is the source of germinal granule material.
A prominent mass in the cytoplasm of previtellogenic oocytes. The cloud contains both mitochondria and electron-dense granulofibrillar material (GFM) and is the source of germinal granule material.
The covalent addition to a protein of ISG15, a ubiquitin-like protein.
A complex of five proteins, designated NELF-A, -B, -C, -D, and -E in human, that can physically associate with RNP polymerase II to induce transcriptional pausing.
The proteolytic processing of trypsinogen to the active form, trypsin.
Any process that activates or increases the frequency, rate or extent of the regulated release of insulin.
Any process that activates or increases the frequency, rate or extent of the regulated release of insulin.
Any process that activates or increases the frequency, rate or extent of the regulated release of insulin.
Any process that activates or increases the frequency, rate or extent of the regulated release of insulin.
Any process that activates or increases the frequency, rate or extent of the regulated release of insulin.
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 cobalt 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 magnesium ion stimulus.
Interacting selectively and non-covalently with a light chain of a myosin complex.
Interacting selectively and non-covalently with the head/neck region of a myosin heavy chain.
Interacting selectively and non-covalently with the tail region of a myosin heavy chain.
Interacting selectively and non-covalently with a light chain of a myosin I complex.
Interacting selectively and non-covalently with the head/neck region of a myosin I heavy chain.
Interacting selectively and non-covalently with the tail region of a myosin I heavy chain.
Interacting selectively and non-covalently with a light chain of a myosin II complex.
Interacting selectively and non-covalently with the head/neck region of a myosin II heavy chain.
Interacting selectively and non-covalently with the tail region of a myosin II heavy chain.
Interacting selectively and non-covalently with a heavy chain of a myosin complex.
Interacting selectively and non-covalently with a heavy chain of a myosin I complex.
Interacting selectively and non-covalently with a heavy chain of a myosin II complex.
A protein complex that stably associates with the C-terminus of RNA polymerase II and mediates 3'-end processing of small nuclear RNAs generated by RNA polymerase II.
A large ribonucleoprotein complex that is an early preribosomal complex. In S. cerevisiae, it has a size of 80S and consists of the 35S pre-rRNA, early-associating ribosomal proteins most of which are part of the small ribosomal subunit, the U3 snoRNA and associated proteins.
A large ribonucleoprotein complex that is an early preribosomal complex. In S. cerevisiae, it has a size of 80S and consists of the 35S pre-rRNA, early-associating ribosomal proteins most of which are part of the small ribosomal subunit, the U3 snoRNA and associated proteins.
Catalysis of the reaction: histone H3 N6-acetyl-L-lysine (position 14) + H2O = histone H3 L-lysine (position 14) + acetate. This reaction requires the presence of NAD, and represents the removal of an acetyl group from lysine at position 14 of the histone H3 protein.
The chemical reactions and pathways involving mitochondrial DNA.
The chemical reactions and pathways involving mitochondrial DNA.
The chemical reactions and pathways involving mitochondrial DNA.
The chemical reactions and pathways resulting in the breakdown of mitochondrial DNA.
The chemical reactions and pathways resulting in the breakdown of mitochondrial DNA.
The chemical reactions and pathways resulting in the breakdown of mitochondrial DNA.
The chemical reactions and pathways resulting in the breakdown of mitochondrial DNA.
The chemical reactions and pathways resulting in the breakdown of mitochondrial DNA.
The chemical reactions and pathways resulting in the breakdown of mitochondrial DNA.
The chemical reactions and pathways resulting in the breakdown of mitochondrial DNA.
A heterodimeric protein complex formed of Spt4 and Spt5 proteins which is expressed in eukaryotes from yeast to man. DSIF is an inhibitory elongation factor that promotes RNA polymerase II transcriptional pausing, but can also stimulate transcriptional elongation under certain conditions, and may play a role in RNA processing via its physical association with mRNA capping enzymes.
A heterodimeric protein complex formed of Spt4 and Spt5 proteins which is expressed in eukaryotes from yeast to man. DSIF is an inhibitory elongation factor that promotes RNA polymerase II transcriptional pausing, but can also stimulate transcriptional elongation under certain conditions, and may play a role in RNA processing via its physical association with mRNA capping enzymes.
A heterodimeric protein complex formed of Spt4 and Spt5 proteins which is expressed in eukaryotes from yeast to man. DSIF is an inhibitory elongation factor that promotes RNA polymerase II transcriptional pausing, but can also stimulate transcriptional elongation under certain conditions, and may play a role in RNA processing via its physical association with mRNA capping enzymes.
A heterodimeric protein complex formed of Spt4 and Spt5 proteins which is expressed in eukaryotes from yeast to man. DSIF is an inhibitory elongation factor that promotes RNA polymerase II transcriptional pausing, but can also stimulate transcriptional elongation under certain conditions, and may play a role in RNA processing via its physical association with mRNA capping enzymes.
A protein complex that stimulates the exchange of guanyl nucleotides associated with a GTPase.
A membrane-bounded flattened sac that is formed during micropexophagy between the membrane tips of an engulfing vacuole, completing the engulfment and sequestration of peroxisomes from the cytosol, and forming a micropexophagic body within the lumen of the vacuole.
A membrane-bounded flattened sac that is formed during micropexophagy between the membrane tips of an engulfing vacuole, completing the engulfment and sequestration of peroxisomes from the cytosol, and forming a micropexophagic body within the lumen of the vacuole.
A double-membrane-bounded organelle that functions in iron-sulfur protein maturation; evolutionarily derived from mitochondria. The mitosome has been detected only in anaerobic or microaerophilic organisms that do not have mitochondria, such as Entamoeba histolytica, Giardia intestinalis and several species of Microsporidia. These organisms are not capable of gaining energy from oxidative phosphorylation, which is normally performed by mitochondria.
The chemical reactions and pathways involving cardiolipin, 1,3-bis(3-phosphatidyl)glycerol.
The chemical reactions and pathways involving cardiolipin, 1,3-bis(3-phosphatidyl)glycerol.
The chemical reactions and pathways involving cardiolipin, 1,3-bis(3-phosphatidyl)glycerol.
The chemical reactions and pathways resulting in the formation of cardiolipin, 1,3-bis(3-phosphatidyl)glycerol.
The chemical reactions and pathways resulting in the formation of cardiolipin, 1,3-bis(3-phosphatidyl)glycerol.
Interacting selectively and non-covalently with a clathrin heavy chain.
Interacting selectively and non-covalently with a clathrin light chain.
Interacting selectively and non-covalently with bile acids, any of a group of steroid carboxylic acids occurring in bile.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a ciliary basal body, a short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum).
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a ciliary basal body, a short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum).
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a ciliary basal body, a short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum).
Any process that stops, prevents or reduces the rate of translation as a result of a stimulus indicating the organism is under stress.
Any process that stops, prevents or reduces the rate of translation as a result of a stimulus indicating the organism is under stress.
Any process that stops, prevents or reduces the rate of translation as a result of a stimulus indicating the organism is under stress.
Any process that stops, prevents or reduces the rate of translation as a result of a stimulus indicating the organism is under stress.
Any process that activates or increases the frequency, rate or extent of translation as a result of a stimulus indicating the organism is under stress.
Any process that activates or increases the frequency, rate or extent of translation as a result of a stimulus indicating the organism is under stress.
Any process that activates or increases the frequency, rate or extent of translation as a result of a stimulus indicating the organism is under stress.
Any process that activates or increases the frequency, rate or extent of translation as a result of a stimulus indicating the organism is under stress.
Any process that activates or increases the frequency, rate or extent of translation as a result of a stimulus indicating the organism is under stress.
Any process that stops, prevents or reduces the rate of translation initiation as a result of a stimulus indicating the organism is under stress.
Any process that stops, prevents or reduces the rate of translation initiation as a result of a stimulus indicating the organism is under stress.
Any process that stops, prevents or reduces the rate of translation initiation as a result of a stimulus indicating the organism is under stress.
Any process that stops, prevents or reduces the rate of translation initiation as a result of a stimulus indicating the organism is under stress.
Any process that activates or increases the frequency, rate or extent of translation initiation as a result of a stimulus indicating the organism is under stress.
Any process that activates or increases the frequency, rate or extent of translation initiation as a result of a stimulus indicating the organism is under stress.
Any process that activates or increases the frequency, rate or extent of translation initiation as a result of a stimulus indicating the organism is under stress.
Any process that activates or increases the frequency, rate or extent of translation initiation as a result of a stimulus indicating the organism is under stress.
Any process that activates or increases the frequency, rate or extent of translation initiation as a result of a stimulus indicating the organism is under stress.
A cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Blebs are formed during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses.
The assembly of a bleb, a cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Plasma membrane blebbing occurs during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses.
The assembly of a bleb, a cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Plasma membrane blebbing occurs during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses.
The assembly of a bleb, a cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Plasma membrane blebbing occurs during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses.
The assembly of a bleb, a cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Plasma membrane blebbing occurs during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses.
The assembly of a bleb, a cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Plasma membrane blebbing occurs during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses.
Any process that stops, prevents or reduces the rate of translation as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that stops, prevents or reduces the rate of translation as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that stops, prevents or reduces the rate of translation as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that stops, prevents or reduces the rate of translation as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that activates or increases the frequency, rate or extent of translation as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that activates or increases the frequency, rate or extent of translation as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that activates or increases the frequency, rate or extent of translation as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that activates or increases the frequency, rate or extent of translation as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that activates or increases the frequency, rate or extent of translation as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that stops, prevents or reduces the rate of translation initiation, as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that stops, prevents or reduces the rate of translation initiation, as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that stops, prevents or reduces the rate of translation initiation, as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that stops, prevents or reduces the rate of translation initiation, as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that activates or increases the frequency, rate or extent of translation initiation, as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that activates or increases the frequency, rate or extent of translation initiation, as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that activates or increases the frequency, rate or extent of translation initiation, as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that activates or increases the frequency, rate or extent of translation initiation, as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
Any process that activates or increases the frequency, rate or extent of translation initiation, as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
A process in which a protein or protein complex is maintained in a specific location in the cell cortex.
Catalysis of the endonucleolytic cleavage of DNA in a site specific manner. Cleavage is dependent on the presence of a specific recognition site in the DNA which must be modified (e.g. methylated, hydroxymethylated, glucosyl-hydroxymethylated).
A complex consisting of two proteins which acts as an endonuclease in DNA sequences containing a specific modified recognition site. Modifications may include methylation, hydroxymethylation, and glucosyl-hydroxymethylation.
Any process that modulates the frequency, rate or extent of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that modulates the frequency, rate or extent of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that modulates the frequency, rate or extent of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that modulates the frequency, rate or extent of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that modulates the frequency, rate or extent of a restriction endodeoxyribonuclease activity, the catalysis of endonucleolytic cleavage of DNA in a site-specific manner, resulting in double-strand breaks.
Any process that stops or reduces the rate of a restriction endodeoxyribonuclease activity, the catalysis of endonucleolytic cleavage of DNA in a site-specific manner, resulting in double-strand breaks.
Any process that stops or reduces the rate of a restriction endodeoxyribonuclease activity, the catalysis of endonucleolytic cleavage of DNA in a site-specific manner, resulting in double-strand breaks.
Any process that stops or reduces the rate of a restriction endodeoxyribonuclease activity, the catalysis of endonucleolytic cleavage of DNA in a site-specific manner, resulting in double-strand breaks.
Any process that stops or reduces the rate of a restriction endodeoxyribonuclease activity, the catalysis of endonucleolytic cleavage of DNA in a site-specific manner, resulting in double-strand breaks.
Any process that stops or reduces the rate of a restriction endodeoxyribonuclease activity, the catalysis of endonucleolytic cleavage of DNA in a site-specific manner, resulting in double-strand breaks.
Any process that stops or reduces the rate of a restriction endodeoxyribonuclease activity, the catalysis of endonucleolytic cleavage of DNA in a site-specific manner, resulting in double-strand breaks.
Any process that stops or reduces the rate of a restriction endodeoxyribonuclease activity, the catalysis of endonucleolytic cleavage of DNA in a site-specific manner, resulting in double-strand breaks.
Any process that stops or reduces the rate of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that stops or reduces the rate of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that stops or reduces the rate of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that stops or reduces the rate of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that stops or reduces the rate of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that activates or increases the frequency, rate or extent of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that activates or increases the frequency, rate or extent of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that activates or increases the frequency, rate or extent of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that activates or increases the frequency, rate or extent of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that activates or increases the frequency, rate or extent of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that activates or increases the frequency, rate or extent of nuclease activity, the hydrolysis of ester linkages within nucleic acids.
Any process that stops or reduces the rate of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that stops or reduces the rate of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that stops or reduces the rate of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that stops or reduces the rate of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that stops or reduces the rate of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that stops or reduces the rate of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that activates or increases the frequency, rate or extent of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that activates or increases the frequency, rate or extent of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that activates or increases the frequency, rate or extent of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that activates or increases the frequency, rate or extent of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that activates or increases the frequency, rate or extent of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that activates or increases the frequency, rate or extent of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that activates or increases the frequency, rate or extent of deoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid.
Any process that stops or reduces the rate of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that stops or reduces the rate of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that stops or reduces the rate of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that stops or reduces the rate of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that stops or reduces the rate of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that activates or increases the frequency, rate or extent of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that activates or increases the frequency, rate or extent of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that activates or increases the frequency, rate or extent of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that activates or increases the frequency, rate or extent of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that activates or increases the frequency, rate or extent of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that activates or increases the frequency, rate or extent of endodeoxyribonuclease activity, the hydrolysis of ester linkages within deoxyribonucleic acid by creating internal breaks.
Any process that stops or reduces the rate of type I restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type I restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type I restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type I restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type I restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type I restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type I restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type II restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type II restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type II restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type II restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type II restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type II restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type II restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type III restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type III restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type III restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type III restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type III restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type III restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type III restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type IV restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type IV restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type IV restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type IV restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type IV restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type IV restriction endodeoxyribonuclease activity.
Any process that stops or reduces the rate of type IV restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type I restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type I restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type I restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type II restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type II restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type II restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type III restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type III restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type III restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type IV restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type IV restriction endodeoxyribonuclease activity.
Any process that modulates the frequency, rate or extent of a type IV restriction endodeoxyribonuclease activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the transcription factor NF-kappaB.
Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the transcription factor NF-kappaB.
Interacting selectively and non-covalently with a NACHT (NAIP, CIITA, HET-E and TP1) domain. The NACHT domain consists of seven distinct conserved motifs, including an ATP/GTPase specific P-loop, a Mg(2+)-binding site and five more specific motifs.
Interacting selectively and non-covalently with a Pyrin (PAAD/DAPIN) domain, a protein-protein interaction domain that has the same fold as the Death domain.
Interacting selectively and non-covalently with a Pyrin (PAAD/DAPIN) domain, a protein-protein interaction domain that has the same fold as the Death domain.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.
Any process that activates or increases the frequency, rate or extent of protein binding.
Any process that activates or increases the frequency, rate or extent of protein binding.
Any process that activates or increases the frequency, rate or extent of protein binding.
Any process that activates or increases the frequency, rate or extent of protein binding.
Any process that activates or increases the frequency, rate or extent of protein binding.
Interacting selectively and non-covalently with a SAM (Sterile Alpha Motif) domain, which is a 70-amino acid protein sequence that participates in protein-protein, protein-lipid, and protein-RNA interactions and is conserved from lower to higher eukaryotes.
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 food stimulus; food is anything which, when taken into the body, serves to nourish or build up the tissues or to supply body heat.
Any process that modulates the frequency, rate or extent of a response to a food stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to a food stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to a food stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to a food stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to a food stimulus.
Any process that activates, maintains, or increases the rate of a response to a food stimulus.
Any process that activates, maintains, or increases the rate of a response to a food stimulus.
Any process that activates, maintains, or increases the rate of a response to a food stimulus.
Any process that activates, maintains, or increases the rate of a response to a food stimulus.
Any process that activates, maintains, or increases the rate of a response to a food stimulus.
Any process which modulates appetite, the desire or physical craving for food.
Any process that reduces appetite.
Any process that reduces appetite.
Any process that reduces appetite.
Any process that reduces appetite.
Any process that reduces appetite.
Any process that reduces appetite.
Any process that increases appetite.
Any process that increases appetite.
Any process that increases appetite.
Any process that increases appetite.
Any process that increases appetite.
Any process that increases appetite.
Any process that increases appetite.
Any process that modulates the frequency, rate or extent of a response to an external stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to an external stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to an external stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to an external stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to an external stimulus.
Any process that activates, maintains or increases the rate of a response to an external stimulus.
Any process that activates, maintains or increases the rate of a response to an external stimulus.
Any process that activates, maintains or increases the rate of a response to an external stimulus.
Any process that activates, maintains or increases the rate of a response to an external stimulus.
Any process that activates, maintains or increases the rate of a response to an external stimulus.
Any process that modulates the frequency, rate or extent of a response to an extracellular stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to an extracellular stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to an extracellular stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to an extracellular stimulus.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to an extracellular stimulus.
Any process that activates, maintains or increases the rate of a response to an extracellular stimulus.
Any process that activates, maintains or increases the rate of a response to an extracellular stimulus.
Any process that activates, maintains or increases the rate of a response to an extracellular stimulus.
Any process that activates, maintains or increases the rate of a response to an extracellular stimulus.
Any process that activates, maintains or increases the rate of a response to an extracellular stimulus.
Any process that modulates the frequency, rate or extent of a response to nutrient levels.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to nutrient levels.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to nutrient levels.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to nutrient levels.
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to nutrient levels.
Any process that activates or increases the frequency, rate or extent of a response to nutrient levels.
Any process that activates or increases the frequency, rate or extent of a response to nutrient levels.
Any process that activates or increases the frequency, rate or extent of a response to nutrient levels.
Any process that activates or increases the frequency, rate or extent of a response to nutrient levels.
Any process that activates or increases the frequency, rate or extent of a response to nutrient levels.
Any process that modulates the frequency, rate or extent of protein histidine kinase activity.
Any process that initiates the activity of an inactive protein histidine kinase.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein histidine kinase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein histidine kinase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein histidine kinase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein histidine kinase activity.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein histidine kinase activity.
Any process that modulates the frequency, rate or extent of carbohydrate phosphatase activity, the catalysis of the hydrolysis of phosphate from a carbohydrate phosphate.
Any process that modulates the frequency, rate or extent of glucose-6-phosphatase activity, the catalysis of the reaction: D-glucose 6-phosphate + H2O = D-glucose + phosphate.
Catalysis of the reaction: D-glucitol + NADP(+) = L-sorbose + H(+) + NADPH. The reaction may occur, to a minor extent, in the reverse direction.
Catalysis of the reaction: D-glucitol + NADP(+) = L-sorbose + H(+) + NADPH. The reaction may occur, to a minor extent, in the reverse direction.
A protein complex required for the loading of a structural maintenance of chromosome (SMC) complex, such as cohesin, condensin or SMC5/SMC6, onto DNA. Appears to be eukaryotically conserved.
A protein complex required for the loading of a structural maintenance of chromosome (SMC) complex, such as cohesin, condensin or SMC5/SMC6, onto DNA. Appears to be eukaryotically conserved.
A protein complex required for the loading of a structural maintenance of chromosome (SMC) complex, such as cohesin, condensin or SMC5/SMC6, onto DNA. Appears to be eukaryotically conserved.
An array of astral microtubules that emanates from the spindle pole body during meiosis and facilitates horsetail nuclear movement.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the horsetail-astral array, a structure of astral microtubules that emanates from the spindle pole body during meiosis.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the horsetail-astral array, a structure of astral microtubules that emanates from the spindle pole body during meiosis.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the horsetail-astral array, a structure of astral microtubules that emanates from the spindle pole body during meiosis.
The process of binding or confining zinc ions such that they are separated from other components of a biological system.
The process in which the nascent membrane forms at the meiotic outer plaque and grows until closure occurs and forespores, or prospores, are formed.
The process in which the nascent membrane forms at the meiotic outer plaque and grows until closure occurs and forespores, or prospores, are formed.
The process in which the nascent membrane forms at the meiotic outer plaque and grows until closure occurs and forespores, or prospores, are formed.
The process in which the nascent membrane forms at the meiotic outer plaque and grows until closure occurs and forespores, or prospores, are formed.
The process in which the nascent membrane forms at the meiotic outer plaque and grows until closure occurs and forespores, or prospores, are formed.
The meiotic cell cycle process in which physical connections are formed between telomeric heterochromatin and the spindle pole body, facilitating bouquet formation.
The meiotic cell cycle process in which physical connections are formed between telomeric heterochromatin and the spindle pole body, facilitating bouquet formation.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the oral apparatus. The oral apparatus is a funnel-like structure used by the cell to collect food and channel it to the cytostome, characteristic of ciliate protozoans.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the oral apparatus. The oral apparatus is a funnel-like structure used by the cell to collect food and channel it to the cytostome, characteristic of ciliate protozoans.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the oral apparatus. The oral apparatus is a funnel-like structure used by the cell to collect food and channel it to the cytostome, characteristic of ciliate protozoans.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the oral apparatus. The oral apparatus is a funnel-like structure used by the cell to collect food and channel it to the cytostome, characteristic of ciliate protozoans.
Inward projections of the cytoskeletal structures of the oral apparatus, which form a fiber that extends past the cytostome into the cytoplasm.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the macronucleus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the macronucleus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the macronucleus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the micronucleus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the micronucleus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the micronucleus.
A cell part that is composed of the eisosome membrane or MCC domain, a furrow-like plasma membrane sub-domain and associated integral transmembrane proteins, and the proteins (eisosome filaments) that form a scaffolding lattice on the cytoplasmic face. Eisosomes broadly affect overall plasma membrane organization.
The lipid bilayer surrounding a dense core granule.
Non-sexual aggregation of single-celled organisms mediated by polymers (polysaccharides, proteins, and/or nucleic acids) secreted into the extracellular environment.
Non-sexual aggregation of single-celled organisms mediated by polymers (polysaccharides, proteins, and/or nucleic acids) secreted into the extracellular environment.
Catalysis of the reaction: histone H3 N6-acetyl-L-lysine (position 9) + H2O = histone H3 L-lysine (position 9) + acetate. This reaction represents the removal of an acetyl group from lysine at position 9 of the histone H3 protein.
The assembly of a sterol-rich region of the plasma membrane at the cell surface overlying the contractile ring.
Interacting selectively and non-covalently with alkylated residues in DNA.
Interacting selectively and non-covalently with O6-alkylguanine adducts in DNA.
A eukaryotically conserved protein complex that localizes to kinetochores in early mitosis, the spindle mid-zone in anaphase B and to the telophase midbody. It has been proposed that the passenger complex coordinates various events based on its location to different structures during the course of mitosis. Complex members include the BIR-domain-containing protein Survivin, Aurora kinase, INCENP and Borealin.
A eukaryotically conserved protein complex that localizes to kinetochores in early mitosis, the spindle mid-zone in anaphase B and to the telophase midbody. It has been proposed that the passenger complex coordinates various events based on its location to different structures during the course of mitosis. Complex members include the BIR-domain-containing protein Survivin, Aurora kinase, INCENP and Borealin.
A eukaryotically conserved protein complex that localizes to kinetochores in early mitosis, the spindle mid-zone in anaphase B and to the telophase midbody. It has been proposed that the passenger complex coordinates various events based on its location to different structures during the course of mitosis. Complex members include the BIR-domain-containing protein Survivin, Aurora kinase, INCENP and Borealin.
Interacting selectively and non-covalently with double-stranded DNA containing insertions or deletions.
Interacting selectively and non-covalently with double-stranded DNA containing insertions or deletions.
Interacting selectively and non-covalently with double-stranded DNA containing an A/C mispair.
Interacting selectively and non-covalently with double-stranded DNA containing an A/C mispair.
Interacting selectively and non-covalently with double-stranded DNA containing an A/C mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a G/T mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a G/T mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a G/T mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a single base insertion or deletion.
Interacting selectively and non-covalently with double-stranded DNA containing a dinucleotide insertion or deletion.
Interacting selectively and non-covalently with double-stranded DNA containing a single adenine insertion or a deletion that results in an unpaired adenine.
Interacting selectively and non-covalently with double-stranded DNA containing a single cytosine insertion or a deletion that results in an unpaired cytosine.
Interacting selectively and non-covalently with double-stranded DNA containing a single guanine insertion or a deletion that results in an unpaired guanine.
Interacting selectively and non-covalently with double-stranded DNA containing a single thymine insertion or a deletion that results in an unpaired thymine.
A homodimeric protein complex that possesses 4-aminobutyrate transaminase activity.
A homodimeric protein complex that possesses 4-aminobutyrate transaminase activity.
A homodimeric protein complex that possesses 4-aminobutyrate transaminase activity.
Interacting selectively and non-covalently with succinate-semialdehyde dehydrogenase.
Any process that initiates the activity of an inactive protein kinase.
Any process that initiates the activity of the inactive enzyme protein kinase B.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a rhamnose 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 rhamnose stimulus.
The chemical reactions and pathways resulting in the formation of ubiquinone, beginning with the conversion of chorismate to 4-hydroxybenzoate.
A heterooligomeric septin complex that acts during mitotic cell division.
A heterooligomeric septin complex that acts during meiotic cell division.
The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
The cleavage furrow is a plasma membrane invagination at the cell division site. The cleavage furrow begins as a shallow groove and eventually deepens to divide the cytoplasm.
Any constituent part of the cell division plane, the eventual plane of cell division in a dividing cell.
The part of the cytoskeleton (the internal framework of a cell) composed of septins and associated proteins. Includes septin cytoskeleton-associated complexes.
A contractile ring, i.e. a cytoskeletal structure composed of actin filaments and myosin, that forms beneath the plasma membrane of the prospore envelope in meiotic cells in preparation for completing cytokinesis.
A contractile ring, i.e. a cytoskeletal structure composed of actin filaments and myosin, that forms beneath the plasma membrane of the prospore envelope in meiotic cells in preparation for completing cytokinesis.
A contractile ring, i.e. a cytoskeletal structure composed of actin filaments and myosin, that forms beneath the plasma membrane of the prospore envelope in meiotic cells in preparation for completing cytokinesis.
A diffuse ring composed of a series of septin bars that run parallel to the long axis of the cell. This type of septin structure has been observed in a number of locations associated with polarized grown and/or deposition of new membrane, but not with cytokinesis, such as at the shmoo (mating projection) neck, at the junction between the mother cell and the germ tube (hypha) of a fungal cell growing filamentously.
A faint structure formed of septins found at the leading edge of growth in germ tubes and hyphae in fungal cells growing filamentously. This cap of septins colocalizes with a region of the plasma membrane that is rich in ergosterol.
Arrays of septin filaments, or bars, found in a series of filamentous structures. Such structures have been observed in the prospore membrane during spore formation in S. cerevisiae and in the chlamydospore membrane during chlamydospore formation in C. albicans.
Any of a series of structures composed of septins and septin-associated proteins localized to the cleavage plane which are involved in cytokinesis.
A septin band, i.e. a diffuse ring composed of a series of septin bars running parallel to the long axis of the cell, located at the neck of a shmoo (mating projection).
A septin band, i.e. a diffuse ring composed of a series of septin bars running parallel to the long axis of the cell, located at the junction between the mother cell and the germ tube (hypha) of a fungal cell growing filamentously.
A faint structure formed of septins found at the leading edge of growth in hyphae of fungal cells growing filamentously. This cap of septins colocalizes with a region of the plasma membrane that is rich in ergosterol.
Arrays of septin filaments, or bars, found in a series of filamentous structures; observed in the prospore membrane during spore formation.
Arrays of septin filaments, or bars, found in a series of filamentous structures. Observed in the chlamydospore membrane during chlamydospore formation.
A tight ring-shaped structure that forms in the division plane within hyphae of filamentous fungi at sites where a septum will form; composed of septins as well as septin-associated proteins.
A tight ring-shaped structure that forms in the division plane at the site of cytokinesis in a prospore; composed of septins as well as septin-associated proteins.
A tight ring-shaped structure that forms in the division plane at the junction between the mother cell and a pseudohyphal projection; composed of septins as well as septin-associated proteins.
A faint structure formed of septins found at the leading edge of growth in germ tubes of fungal cells growing filamentously. This cap of septins colocalizes with a region of the plasma membrane that is rich in ergosterol.
A tight ring-shaped structure that forms in the division plane within the germ tube of filamentous fungi at sites where a septum will form; composed of septins as well as septin-associated proteins.
A tubular, hourglass-shaped structure composed of highly ordered arrays of septin filaments; in budding yeast cells, the septin collar forms from the initial septin ring by expanding into the daughter cell.
A tubular structure with flared ends, shaped like an hourglass and composed of highly ordered arrays of septin filaments, that forms at the bud neck of a dividing cell. In S. cerevisiae, this structure is located at the bud neck throughout most of the cell cycle and the septins are fixed within the structure, not exchanging with soluble septins. This septin structure acts as a scaffold for other proteins that function at the bud neck.
A septin ring, i.e. a ring-shaped structure composed of septins and septin-associated proteins, located at the neck of a shmoo (mating projection). The septin ring in the neck of a shmoo may act as a barrier to localize mating factors in the shmoo tip.
A pair of rings that flank the site of cell division, formed by splitting of the septin ring (or collar) prior to cytokinesis; this double ring structure is thought to trap proteins needed for cytokinesis or the formation of the new membrane or cell wall between the two septin rings. Split septin rings are known to occur in budding yeast cells and probably occur in other cell types as well.
Two separate septin rings that are formed from the septin collar at the time of cytokinesis in cells that divide by budding. These two rings are thought to delineate a special compartment in which factors involved in cytokinesis are concentrated.
A sterol-rich region of the plasma membrane which forms at the cell surface overlying the contractile ring and spreads into the invaginating plasma membrane surrounding the septum.
The slender tubular outgrowth first produced by most spores in germination.
The chemical reactions and pathways resulting in the formation of ubiquinone, beginning with the conversion of tyrosine to 4-hydroxybenzoate.
Interacting selectively and non-covalently with double-stranded DNA containing a dinucleotide repeat insertion or a deletion resulting in unpaired dinucleotide repeats.
Interacting selectively and non-covalently with a small conjugating protein such as ubiquitin or a ubiquitin-like protein.
Interacting selectively and non-covalently with the small ubiquitin-like protein SUMO.
Interacting selectively and non-covalently with the small ubiquitin-like protein SUMO.
Interacting selectively and non-covalently with a polymer of the small ubiquitin-like protein SUMO.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising septin complexes and their associated proteins.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising septin complexes and their associated proteins.
Control of the formation, spatial distribution, and breakdown of a septin ring located at the bud neck.
The process in which a contractile ring is assembled and/or maintained in a specific location, in the context of cytokinesis that takes place as part of a cell cycle.
The process in which a contractile ring is assembled and/or maintained in a specific location, in the context of cytokinesis that takes place as part of a cell cycle.
The process in which a contractile ring is assembled in a specific location as part of a process of cell cycle cytokinesis.
The process in which a contractile ring is assembled in a specific location as part of a process of cell cycle cytokinesis.
The process in which a contractile ring is assembled in a specific location as part of a process of cell cycle cytokinesis.
The process in which a contractile ring is assembled in a specific location as part of a process of cell cycle cytokinesis.
The process in which a contractile ring is assembled in a specific location as part of a process of cell cycle cytokinesis.
The process in which a contractile ring is assembled in a specific location as part of a process of cell cycle cytokinesis.
Any process in which an actomyosin contractile ring is maintained in a location and prevented from moving elsewhere.
Any process in which an actomyosin contractile ring is maintained in a location and prevented from moving elsewhere.
Any process in which an actomyosin contractile ring is maintained in a location and prevented from moving elsewhere.
Any process in which an actomyosin contractile ring is maintained in a location and prevented from moving elsewhere.
Interacting selectively and non-covalently with acrosin, a protein that is found in the acrosomes of sperm and possesses protease and carbohydrate binding activities.
Interacting selectively and non-covalently with acrosin, a protein that is found in the acrosomes of sperm and possesses protease and carbohydrate binding activities.
Interacting selectively and non-covalently with acrosin, a protein that is found in the acrosomes of sperm and possesses protease and carbohydrate binding activities.
Interacting selectively and non-covalently with acrosin, a protein that is found in the acrosomes of sperm and possesses protease and carbohydrate binding activities.
The chemical reactions and pathways resulting in the formation of ubiquinone, via the intermediates 2-polyprenylphenol and 2-polyprenyl-6-hydroxyphenol.
The chemical reactions and pathways resulting in the formation of ubiquinone, via the intermediates 3,4-dihydroxy-5-polyprenylbenzoate and 3-methoxy-4-hydroxy-5-polyprenylbenzoate.
A membrane-bounded intracellular vesicle formed late in the endocytic pathway when the pH in the vacuole becomes neutral prior to exocytosis.
Any process involved in mediating the movement of discrete segments of DNA between nonhomologous sites.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in a type of transpositional recombination which occurs via an RNA intermediate.
Any process involved in the transposition of miniature inverted-repeat transposable elements (MITEs).
The synthesis of DNA from an RNA transposon intermediate.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of telomeres, terminal regions of a linear chromosome that include the telomeric DNA repeats and associated proteins.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of telomeres, terminal regions of a linear chromosome that include the telomeric DNA repeats and associated proteins.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of telomeres, terminal regions of a linear chromosome that include the telomeric DNA repeats and associated proteins.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of telomeres, terminal regions of a linear chromosome that include the telomeric DNA repeats and associated proteins.
The process in which telomeric DNA is synthesized semi-conservatively by the conventional replication machinery and telomeric accessory factors as part of cell cycle DNA replication.
The process in which telomeric DNA is synthesized semi-conservatively by the conventional replication machinery and telomeric accessory factors as part of cell cycle DNA replication.
The process in which telomeric DNA is synthesized semi-conservatively by the conventional replication machinery and telomeric accessory factors as part of cell cycle DNA replication.
A cellular process that results in the aggregation, arrangement and bonding together of a set of components to form a telomere at a non-telomeric double-stranded DNA end. A telomere is a terminal region of a linear chromosome that includes telomeric DNA repeats and associated proteins.
A cellular process that results in the formation of a telomere at a non-telomeric double-stranded DNA end that involves the activity of a telomerase enzyme.
Any process that modulates the frequency, rate or extent of a process that affects and monitors the activity of telomeric proteins and the length of telomeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of a process that affects and monitors the activity of telomeric proteins and the length of telomeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of a process that affects and monitors the activity of telomeric proteins and the length of telomeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of a process that affects and monitors the activity of telomeric proteins and the length of telomeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of a process that affects and monitors the activity of telomeric proteins and the length of telomeric DNA.
Any process that activates or increases the frequency, rate or extent of a process that affects and monitors the activity of telomeric proteins and the length of telomeric DNA.
Any process that activates or increases the frequency, rate or extent of a process that affects and monitors the activity of telomeric proteins and the length of telomeric DNA.
Any process that activates or increases the frequency, rate or extent of a process that affects and monitors the activity of telomeric proteins and the length of telomeric DNA.
Any process that activates or increases the frequency, rate or extent of a process that affects and monitors the activity of telomeric proteins and the length of telomeric DNA.
Any process that activates or increases the frequency, rate or extent of a process that affects and monitors the activity of telomeric proteins and the length of telomeric DNA.
Any process that modulates the frequency, rate or extent of a recombinational process involved in the maintenance of proper telomeric length.
Any process that stops, prevents, or reduces the frequency, rate or extent of a recombinational process involved in the maintenance of proper telomeric length.
Any process that stops, prevents, or reduces the frequency, rate or extent of a recombinational process involved in the maintenance of proper telomeric length.
Any process that stops, prevents, or reduces the frequency, rate or extent of a recombinational process involved in the maintenance of proper telomeric length.
Any process that stops, prevents, or reduces the frequency, rate or extent of a recombinational process involved in the maintenance of proper telomeric length.
Any process that activates or increases the frequency, rate or extent of a recombinational process involved in the maintenance of proper telomeric length.
Any process that activates or increases the frequency, rate or extent of a recombinational process involved in the maintenance of proper telomeric length.
Any process that activates or increases the frequency, rate or extent of a recombinational process involved in the maintenance of proper telomeric length.
Any process that activates or increases the frequency, rate or extent of a recombinational process involved in the maintenance of proper telomeric length.
Any process that activates or increases the frequency, rate or extent of a recombinational process involved in the maintenance of proper telomeric length.
Any process that modulates the frequency, rate or extent of the addition of telomeric repeats by telomerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of telomeric repeats by telomerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of telomeric repeats by telomerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of telomeric repeats by telomerase.
Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of telomeric repeats by telomerase.
Any process that activates or increases the frequency, rate or extent of the addition of telomeric repeats by telomerase.
Any process that activates or increases the frequency, rate or extent of the addition of telomeric repeats by telomerase.
Any process that activates or increases the frequency, rate or extent of the addition of telomeric repeats by telomerase.
Any process that activates or increases the frequency, rate or extent of the addition of telomeric repeats by telomerase.
Any process that activates or increases the frequency, rate or extent of the addition of telomeric repeats by telomerase.
Any process that modulates the frequency, rate or extent of the semi-conservative replication of telomeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the semi-conservative replication of telomeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the semi-conservative replication of telomeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the semi-conservative replication of telomeric DNA.
Any process that stops, prevents, or reduces the frequency, rate or extent of the semi-conservative replication of telomeric DNA.
Any process that activates or increases the frequency, rate or extent of the semi-conservative replication of telomeric DNA.
Any process that activates or increases the frequency, rate or extent of the semi-conservative replication of telomeric DNA.
Any process that activates or increases the frequency, rate or extent of the semi-conservative replication of telomeric DNA.
Any process that activates or increases the frequency, rate or extent of the semi-conservative replication of telomeric DNA.
Any process that activates or increases the frequency, rate or extent of the semi-conservative replication of telomeric DNA.
Catalysis of the reaction: glucosaminyl-phosphotidylinositol + fatty acyl-CoA = glucosaminyl-acyl-phosphotidylinositol + CoA.
Enables the transfer of riboflavin from one side of a membrane to the other. Riboflavin (vitamin B2) is a water-soluble B-complex vitamin, converted in the cell to FMN and FAD, cofactors required for the function of flavoproteins.
The directed movement of riboflavin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Riboflavin (vitamin B2) is a water-soluble B-complex vitamin, converted in the cell to FMN and FAD, cofactors required for the function of flavoproteins.
The chemical reactions and pathways resulting in the breakdown of macromolecules forming part of a cell wall that contribute to cytogamy.
The joining of two or more lipid bilayer membranes that surround cells, that contributes to cytogamy.
The joining of two or more lipid bilayer membranes that surround cells, that contributes to cytogamy.
The joining of two or more lipid bilayer membranes that surround cells, that contributes to cytogamy.
A eukaryotically conserved histone deacetylase complex which deacetylates histones preferentially in promoter regions. Composed of a catalytic histone deacetylase subunit, a chromodomain protein, a SIN3 family co-repressor, and a WD repeat protein (Clr6p, Alp13p, Pst2p, and Prw1p respectively in Schizosaccharomyces; Rpd3p, Sin3p, Ume1p, Rco1p and Eaf3 in Saccharomyces; homologs thereof in other species).
A eukaryotically conserved histone deacetylase complex which deacetylates histones preferentially in promoter regions. Composed of a catalytic histone deacetylase subunit, a chromodomain protein, a SIN3 family co-repressor, and a WD repeat protein (Clr6p, Alp13p, Pst2p, and Prw1p respectively in Schizosaccharomyces; Rpd3p, Sin3p, Ume1p, Rco1p and Eaf3 in Saccharomyces; homologs thereof in other species).
A eukaryotically conserved histone deacetylase complex which deacetylates histones preferentially in promoter regions. Composed of a catalytic histone deacetylase subunit, a chromodomain protein, a SIN3 family co-repressor, and a WD repeat protein (Clr6p, Alp13p, Pst2p, and Prw1p respectively in Schizosaccharomyces; Rpd3p, Sin3p, Ume1p, Rco1p and Eaf3 in Saccharomyces; homologs thereof in other species).
A eukaryotically conserved histone deacetylase complex which deacetylates histones preferentially in promoter regions. Composed of a catalytic histone deacetylase subunit, a chromodomain protein, a SIN3 family co-repressor, and a WD repeat protein (Clr6p, Alp13p, Pst2p, and Prw1p respectively in Schizosaccharomyces; Rpd3p, Sin3p, Ume1p, Rco1p and Eaf3 in Saccharomyces; homologs thereof in other species).
Any process that modulates the frequency, rate or extent of cholinergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter acetylcholine.
Any process that stops, prevents, or reduces the frequency, rate or extent of cholinergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter acetylcholine.
Any process that stops, prevents, or reduces the frequency, rate or extent of cholinergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter acetylcholine.
Any process that stops, prevents, or reduces the frequency, rate or extent of cholinergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter acetylcholine.
Any process that stops, prevents, or reduces the frequency, rate or extent of cholinergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter acetylcholine.
Any process that activates, maintains or increases the frequency, rate or extent of cholinergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter acetylcholine.
Any process that activates, maintains or increases the frequency, rate or extent of cholinergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter acetylcholine.
Any process that activates, maintains or increases the frequency, rate or extent of cholinergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter acetylcholine.
Any process that activates, maintains or increases the frequency, rate or extent of cholinergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter acetylcholine.
Any process that activates, maintains or increases the frequency, rate or extent of cholinergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter acetylcholine.
Any process that modulates the frequency, rate or extent of dopaminergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter dopamine.
Any process that activates, maintains or increases the frequency, rate or extent of dopaminergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter dopamine.
Any process that activates, maintains or increases the frequency, rate or extent of dopaminergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter dopamine.
Any process that activates, maintains or increases the frequency, rate or extent of dopaminergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter dopamine.
Any process that activates, maintains or increases the frequency, rate or extent of dopaminergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter dopamine.
Any process that activates, maintains or increases the frequency, rate or extent of dopaminergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter dopamine.
Any process that stops, prevents, or reduces the frequency, rate or extent of dopaminergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter dopamine.
Any process that stops, prevents, or reduces the frequency, rate or extent of dopaminergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter dopamine.
Any process that stops, prevents, or reduces the frequency, rate or extent of dopaminergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter dopamine.
Any process that stops, prevents, or reduces the frequency, rate or extent of dopaminergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter dopamine.
Any process that modulates the frequency, rate or extent of GABAergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter gamma-aminobutyric acid (GABA).
Any process that stops, prevents, or reduces the frequency, rate or extent of GABAergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter gamma-aminobutyric acid (GABA).
Any process that stops, prevents, or reduces the frequency, rate or extent of GABAergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter gamma-aminobutyric acid (GABA).
Any process that stops, prevents, or reduces the frequency, rate or extent of GABAergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter gamma-aminobutyric acid (GABA).
Any process that stops, prevents, or reduces the frequency, rate or extent of GABAergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter gamma-aminobutyric acid (GABA).
Any process that activates, maintains or increases the frequency, rate or extent of GABAergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter gamma-aminobutyric acid (GABA).
Any process that activates, maintains or increases the frequency, rate or extent of GABAergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter gamma-aminobutyric acid (GABA).
Any process that activates, maintains or increases the frequency, rate or extent of GABAergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter gamma-aminobutyric acid (GABA).
Any process that activates, maintains or increases the frequency, rate or extent of GABAergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter gamma-aminobutyric acid (GABA).
Any process that activates, maintains or increases the frequency, rate or extent of GABAergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter gamma-aminobutyric acid (GABA).
Any process that modulates the frequency, rate or extent of the assembly of actin filament bundles.
Any process that modulates the frequency, rate or extent of the assembly of actin filament bundles.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of actin filament bundles.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of actin filament bundles.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of actin filament bundles.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of actin filament bundles.
Any process that activates or increases the frequency, rate or extent of the assembly of actin filament bundles.
Any process that activates or increases the frequency, rate or extent of the assembly of actin filament bundles.
Any process that activates or increases the frequency, rate or extent of the assembly of actin filament bundles.
Any process that activates or increases the frequency, rate or extent of the assembly of actin filament bundles.
Any process that activates or increases the frequency, rate or extent of the assembly of actin filament bundles.
A process that initiates the activity of an inactive store-operated calcium channel.
The directed movement of adenosine, adenine 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 nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of nucleobases, nucleosides, nucleotides and nucleic acids, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.