The invasion by a symbiont of a cell of its host organism, forming a vacuole in which the parasite resides. The vacuole membrane is formed from lipids and proteins derived from both host and symbiont. Begins when the symbiont attaches on to the host cell membrane which invaginates and deepens as the symbiont enters, and ends when the host cell membrane closes behind the newly-formed vacuole.
The process in which a host organism maintains the structure and function of a symbiont-containing vacuole. The symbiont-containing vacuole is a membrane-bounded vacuole within a host cell in which a symbiont organism resides, and can serve to reduce pathogenicity of invading symbionts by restricting them to the vacuolar compartment.
The process in which a host organism maintains the structure and function of a symbiont-containing vacuole. The symbiont-containing vacuole is a membrane-bounded vacuole within a host cell in which a symbiont organism resides, and can serve to reduce pathogenicity of invading symbionts by restricting them to the vacuolar compartment.
The process in which a host organism maintains the structure and function of a symbiont-containing vacuole. The symbiont-containing vacuole is a membrane-bounded vacuole within a host cell in which a symbiont organism resides, and can serve to reduce pathogenicity of invading symbionts by restricting them to the vacuolar compartment.
The assembly of a symbiont-induced complex organelle that comprises of multiple protein and lipid domains for the purpose of obtaining nutrients from its host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 6 of the ubiquitin monomers, is added to a protein. K6-linked ubiquitination is involved in DNA repair.
The process in which an organism effects a change in the structure or function of its host organism, mediated by a substance secreted by a type I secretion system in the organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The process in which an organism effects a change in the structure or function of its host organism, mediated by a substance secreted by a type VI secretion system in the organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The process in which an organism effects a change in the structure or function of its host organism, mediated by a substance secreted by a type VII secretion system in the organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The process in which an organism (symbiont) effects a change in the structure or function of its host organism, mediated by a substance secreted by the Sec complex in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The process in which an organism (symbiont) effects a change in the structure or function of its host organism, mediated by a substance secreted by the Tat complex in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
A complex, symbiont-induced host-derived organelle that is comprised of multiple protein and lipid domains.
A complex, symbiont-induced host-derived organelle that is comprised of multiple protein and lipid domains.
Penetration by symbiont of a host anatomical structure which provides a barrier to symbiont entry, mediated by symbiont degradative enzymes.
Penetration by symbiont of host physical barriers, mediated by symbiont degradative enzymes.
The aggregation, arrangement and bonding together of the extracellular matrix.
A process carried out by symbiont gene products that enables a symbiotic interaction with a host organism, that is beneficial to the host organism.
Any process in which an organism modulates the frequency, rate or extent of host NF-kappaB-mediated signal transduction pathways during the host defense response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process that activates or increases the frequency, rate or extent of host NF-kappaB-mediated signal transduction pathways during the host defense response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process that activates or increases the frequency, rate or extent of host NF-kappaB-mediated signal transduction pathways during the host defense response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process that activates or increases the frequency, rate or extent of host NF-kappaB-mediated signal transduction pathways during the host defense response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process that activates or increases the frequency, rate or extent of host NF-kappaB-mediated signal transduction pathways during the host defense response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process that activates or increases the frequency, rate or extent of host NF-kappaB-mediated signal transduction pathways during the host defense response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process that activates or increases the frequency, rate or extent of host NF-kappaB-mediated signal transduction pathways during the host defense response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process that activates or increases the frequency, rate or extent of host NF-kappaB-mediated signal transduction pathways during the host defense response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process that activates or increases the frequency, rate or extent of host NF-kappaB-mediated signal transduction pathways during the host defense response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
Any process that stops, prevents, or reduces the frequency, rate or extent of host NF-kappaB-mediated signal transduction pathways during the host defense response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
A projection from a cell or tissue that penetrates the host's cell wall and invaginates the host cell membrane.
The space between the symbiont plasma membrane and the extrahaustorial membrane of the host.
The membrane surrounding the symbiont haustorium during symbiosis, derived from the host plasma membrane.
A host-derived membrane surrounding the symbiont invasive hypha during symbiosis.
The space between the symbiont plasma membrane and the extra-invasive hyphal membrane.
Highly branched symbiont haustoria within host root cortex cells, responsible for nutrient exchange.
A host-derived membrane surrounding the symbiont arbuscule during symbiosis.
The process in which a symbiont organism effects a breakdown of the host organism cuticle. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The process in which a symbiont organism effects a breakdown of the host organism cuticle. The host is defined as the larger of the organisms involved in a symbiotic interaction.
An action potential that occurs in a cardiac muscle cell.
An action potential that occurs in a cardiac muscle cell and is involved in its contraction.
The actin filament-based process in which cytoplasmic actin filaments slide past one another resulting in contraction of a cardiac muscle cell.
Any process that modulates the frequency, rate or extent of cardiac muscle cell contraction.
An action potential that occurs in a ventricular cardiac muscle cell.
Enables the transmembrane transfer of a sodium ion by a voltage-gated channel through the plasma membrane of a cardiac muscle cell contributing to the depolarization phase of an action potential. 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 calcium ion by a voltage-gated channel across the plasma membrane of a cardiac muscle cell that contributes to the depolarization phase of an action potential. 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 potassium ion by a voltage-gated channel through the plasma membrane of a cardiac muscle cell contributing to the repolarization phase of an action potential. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
The process in which ions are transported across a membrane such that the membrane potential changes in the repolarizing direction, toward the steady state potential. For example, the repolarization during an action potential is from a positive membrane potential towards a negative resting potential.
The process in which membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which ions are transported across a membrane such that the membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which ions are transported across a membrane such that the cardiac muscle cell plasma membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
An action potential that occurs in an atrial cardiac muscle cell.
An action potential that occurs in a sinoatrial node cardiac muscle cell.
An action potential that occurs in a sinoatrial node cardiac muscle cell.
An action potential that occurs in a sinoatrial node cardiac muscle cell.
An action potential that occurs in a sinoatrial node cardiac muscle cell.
An action potential that occurs in a Purkinje myocyte.
Any process that mediates the transfer of information from an SA node cardiomyocyte to an atrial cardiomyocyte.
Any process that mediates the transfer of information from an SA node cardiomyocyte to an atrial cardiomyocyte.
Any process that mediates the transfer of information from an SA node cardiomyocyte to an atrial cardiomyocyte.
Any process that mediates the transfer of information from an SA node cardiomyocyte to an atrial cardiomyocyte.
Any process that mediates the transfer of information from an SA node cardiomyocyte to an atrial cardiomyocyte.
Any process that mediates the transfer of information from one cell to another and contributes to the heart process that regulates cardiac muscle contraction; beginning with the generation of an action potential in the sinoatrial node and ending with regulation of contraction of the myocardium.
A wide pore channel activity that enables a direct cytoplasmic connection from an SA node cell to an atrial cardiomyocyte. The gap junction passes electrical signals between the cells contributing to cardiac conduction.
A wide pore channel activity that enables a direct cytoplasmic connection from an SA node cell to an atrial cardiomyocyte. The gap junction passes electrical signals between the cells contributing to cardiac conduction.
A wide pore channel activity that enables a direct cytoplasmic connection from an SA node cell to an atrial cardiomyocyte. The gap junction passes electrical signals between the cells contributing to cardiac conduction.
A wide pore channel activity that enables a direct cytoplasmic connection from an SA node cell to an atrial cardiomyocyte. The gap junction passes electrical signals between the cells contributing to cardiac conduction.
The process that mediates signaling interactions between an SA node cardiomyocyte and an atrial cardiomyocyte by transfer of current between their adjacent cytoplasms via intercellular protein channels.
The process that mediates signaling interactions between an SA node cardiomyocyte and an atrial cardiomyocyte by transfer of current between their adjacent cytoplasms via intercellular protein channels.
The process that mediates signaling interactions between an SA node cardiomyocyte and an atrial cardiomyocyte by transfer of current between their adjacent cytoplasms via intercellular protein channels.
The process that mediates signaling interactions between an SA node cardiomyocyte and an atrial cardiomyocyte by transfer of current between their adjacent cytoplasms via intercellular protein channels.
The process that mediates signaling interactions between an SA node cardiomyocyte and an atrial cardiomyocyte by transfer of current between their adjacent cytoplasms via intercellular protein channels.
The attachment of SA node cardiomyocyte to an atrial cardiomyocyte via adhesion molecules that results in the cells being juxtaposed so that they can communicate.
The attachment of SA node cardiomyocyte to an atrial cardiomyocyte via adhesion molecules that results in the cells being juxtaposed so that they can communicate.
The attachment of SA node cardiomyocyte to an atrial cardiomyocyte via adhesion molecules that results in the cells being juxtaposed so that they can communicate.
The attachment of SA node cardiomyocyte to an atrial cardiomyocyte via adhesion molecules that results in the cells being juxtaposed so that they can communicate.
The attachment of SA node cardiomyocyte to an atrial cardiomyocyte via adhesion molecules that results in the cells being juxtaposed so that they can communicate.
A series of molecular signals beginning with a G protein-coupled adrenergic cell surface receptor combining with epinephrine or norepinephrine, to activate adenylate cyclase, which contributes to a circulatory system process carried out by the heart.
A series of molecular signals beginning with a G protein-coupled adrenergic cell surface receptor combining with epinephrine or norepinephrine, to activate adenylate cyclase, which contributes to a circulatory system process carried out by the heart.
A series of molecular signals beginning with a G protein-coupled adrenergic cell surface receptor combining with epinephrine or norepinephrine, to activate adenylate cyclase, which contributes to a circulatory system process carried out by the heart.
An adrenergic receptor signaling pathway that contributes to an increase in frequency or rate of heart contraction. Binding of adrenalin or noradrenalin to a beta-adrenergic receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gs protein. Gs activates adenylate cyclase to increase intracellular cyclic-AMP (cAMP) levels. cAMP binds directly to F-channels to allow an inward flow of sodium (known as funny current, or If current). The funny current is responsible for membrane depolarization and an increase in heart rate.
An adrenergic receptor signaling pathway that contributes to an increase in frequency or rate of heart contraction. Binding of adrenalin or noradrenalin to a beta-adrenergic receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gs protein. Gs activates adenylate cyclase to increase intracellular cyclic-AMP (cAMP) levels. cAMP binds directly to F-channels to allow an inward flow of sodium (known as funny current, or If current). The funny current is responsible for membrane depolarization and an increase in heart rate.
An adrenergic receptor signaling pathway that contributes to an increase in frequency or rate of heart contraction. Binding of adrenalin or noradrenalin to a beta-adrenergic receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gs protein. Gs activates adenylate cyclase to increase intracellular cyclic-AMP (cAMP) levels. cAMP binds directly to F-channels to allow an inward flow of sodium (known as funny current, or If current). The funny current is responsible for membrane depolarization and an increase in heart rate.
An adrenergic receptor signaling pathway that contributes to an increase in frequency or rate of heart contraction. Binding of adrenalin or noradrenalin to a beta-adrenergic receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gs protein. Gs activates adenylate cyclase to increase intracellular cyclic-AMP (cAMP) levels. cAMP binds directly to F-channels to allow an inward flow of sodium (known as funny current, or If current). The funny current is responsible for membrane depolarization and an increase in heart rate.
An adrenergic receptor signaling pathway that contributes to an increase in frequency or rate of heart contraction. Binding of adrenalin or noradrenalin to a beta-adrenergic receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gs protein. Gs activates adenylate cyclase to increase intracellular cyclic-AMP (cAMP) levels. cAMP binds directly to F-channels to allow an inward flow of sodium (known as funny current, or If current). The funny current is responsible for membrane depolarization and an increase in heart rate.
An adrenergic receptor signaling pathway that contributes to an increase in frequency or rate of heart contraction. Binding of adrenalin or noradrenalin to a beta-adrenergic receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gs protein. Gs activates adenylate cyclase to increase intracellular cyclic-AMP (cAMP) levels. cAMP binds directly to F-channels to allow an inward flow of sodium (known as funny current, or If current). The funny current is responsible for membrane depolarization and an increase in heart rate.
An adrenergic receptor signaling pathway that contributes to an increase in frequency or rate of heart contraction. Binding of adrenalin or noradrenalin to a beta-adrenergic receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gs protein. Gs activates adenylate cyclase to increase intracellular cyclic-AMP (cAMP) levels. cAMP binds directly to F-channels to allow an inward flow of sodium (known as funny current, or If current). The funny current is responsible for membrane depolarization and an increase in heart rate.
Any process that mediates the transfer of information from an atrial cardiomyocyte to an AV node cell.
Any process that mediates the transfer of information from an atrial cardiomyocyte to an AV node cell.
Any process that mediates the transfer of information from an atrial cardiomyocyte to an AV node cell.
Any process that mediates the transfer of information from an AV node cardiac muscle cell to a bundle of His cardiomyocyte.
Any process that mediates the transfer of information from an AV node cardiac muscle cell to a bundle of His cardiomyocyte.
Any process that mediates the transfer of information from a bundle of His cardiomyocyte to a Purkinje myocyte.
Any process that mediates the transfer of information from a bundle of His cardiomyocyte to a Purkinje myocyte.
Any process that mediates the transfer of information from a Purkinje myocyte to a ventricular cardiac muscle cell.
An adrenergic receptor signaling pathway that contributes to a reduction in cardiac muscle contraction. Beta-adrenergic receptor-induced cardiac relaxation is achieved by a GPCR-activated adenylate cyclase generating cAMP; cAMP then activates the cAMP-dependent protein kinase A (PKA), which phosphorylates the sarcoplasmic reticulum (SR) membrane protein PLB. In its non-phosphorylated state, PLB acts as an inhibitor of the ATPase Ca(2+) pump of the cardiac SR (SERCA2a); inhibition of the pump is relieved upon phosphorylation. The pump removes Ca(2+) from the cytoplasm, thereby preventing cytosolic Ca(2+)-dependent activation of contractile proteins, leading to enhanced muscle relaxation.
An adrenergic receptor signaling pathway that contributes to a reduction in cardiac muscle contraction. Beta-adrenergic receptor-induced cardiac relaxation is achieved by a GPCR-activated adenylate cyclase generating cAMP; cAMP then activates the cAMP-dependent protein kinase A (PKA), which phosphorylates the sarcoplasmic reticulum (SR) membrane protein PLB. In its non-phosphorylated state, PLB acts as an inhibitor of the ATPase Ca(2+) pump of the cardiac SR (SERCA2a); inhibition of the pump is relieved upon phosphorylation. The pump removes Ca(2+) from the cytoplasm, thereby preventing cytosolic Ca(2+)-dependent activation of contractile proteins, leading to enhanced muscle relaxation.
An adrenergic receptor signaling pathway that contributes to a reduction in cardiac muscle contraction. Beta-adrenergic receptor-induced cardiac relaxation is achieved by a GPCR-activated adenylate cyclase generating cAMP; cAMP then activates the cAMP-dependent protein kinase A (PKA), which phosphorylates the sarcoplasmic reticulum (SR) membrane protein PLB. In its non-phosphorylated state, PLB acts as an inhibitor of the ATPase Ca(2+) pump of the cardiac SR (SERCA2a); inhibition of the pump is relieved upon phosphorylation. The pump removes Ca(2+) from the cytoplasm, thereby preventing cytosolic Ca(2+)-dependent activation of contractile proteins, leading to enhanced muscle relaxation.
An adrenergic receptor signaling pathway that contributes to a reduction in cardiac muscle contraction. Beta-adrenergic receptor-induced cardiac relaxation is achieved by a GPCR-activated adenylate cyclase generating cAMP; cAMP then activates the cAMP-dependent protein kinase A (PKA), which phosphorylates the sarcoplasmic reticulum (SR) membrane protein PLB. In its non-phosphorylated state, PLB acts as an inhibitor of the ATPase Ca(2+) pump of the cardiac SR (SERCA2a); inhibition of the pump is relieved upon phosphorylation. The pump removes Ca(2+) from the cytoplasm, thereby preventing cytosolic Ca(2+)-dependent activation of contractile proteins, leading to enhanced muscle relaxation.
An adrenergic receptor signaling pathway that contributes to a reduction in cardiac muscle contraction. Beta-adrenergic receptor-induced cardiac relaxation is achieved by a GPCR-activated adenylate cyclase generating cAMP; cAMP then activates the cAMP-dependent protein kinase A (PKA), which phosphorylates the sarcoplasmic reticulum (SR) membrane protein PLB. In its non-phosphorylated state, PLB acts as an inhibitor of the ATPase Ca(2+) pump of the cardiac SR (SERCA2a); inhibition of the pump is relieved upon phosphorylation. The pump removes Ca(2+) from the cytoplasm, thereby preventing cytosolic Ca(2+)-dependent activation of contractile proteins, leading to enhanced muscle relaxation.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to a decrease in frequency or rate of heart contraction. Binding of acetylcholine to a G protein-coupled (muscarinic) receptor on the surface of the signal-receiving cell results in the alpha subunit of a coupled G-protein binding to GTP. This results in the separation of the beta-gamma complex from the alpha subunit. Both the alpha subunit, and the beta-gamma complex can continue to signal to bring about membrane hyperpolarization and a reduction in heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to a decrease in frequency or rate of heart contraction. Binding of acetylcholine to a G protein-coupled (muscarinic) receptor on the surface of the signal-receiving cell results in the alpha subunit of a coupled G-protein binding to GTP. This results in the separation of the beta-gamma complex from the alpha subunit. Both the alpha subunit, and the beta-gamma complex can continue to signal to bring about membrane hyperpolarization and a reduction in heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to a decrease in frequency or rate of heart contraction. Binding of acetylcholine to a G protein-coupled (muscarinic) receptor on the surface of the signal-receiving cell results in the alpha subunit of a coupled G-protein binding to GTP. This results in the separation of the beta-gamma complex from the alpha subunit. Both the alpha subunit, and the beta-gamma complex can continue to signal to bring about membrane hyperpolarization and a reduction in heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to a decrease in frequency or rate of heart contraction. Binding of acetylcholine to a G protein-coupled (muscarinic) receptor on the surface of the signal-receiving cell results in the alpha subunit of a coupled G-protein binding to GTP. This results in the separation of the beta-gamma complex from the alpha subunit. Both the alpha subunit, and the beta-gamma complex can continue to signal to bring about membrane hyperpolarization and a reduction in heart rate.
Any process that modulates the establishment or extent of a membrane potential in a cardiac muscle cell (a cardiomyocyte). A membrane potential is 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.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) + K+(out) = ADP + phosphate + Na+(out) + K+(in), that contributes to regulating the membrane potential of a cardiac muscle cell.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: Ca2+(in) + Na+(out) = Ca2+(out) + Na+(in), which contributes to regulating the membrane potential of a cardiac muscle cell.
Enables the transfer of a solute or solutes from one side of a cardiac muscle cell plasma membrane to the other according to the reaction: ATP + H2O + Ca2+(cis) = ADP + phosphate + Ca2+(trans). The transfer contributes to the regulation of the plasma membrane potential.
Enables the transfer of a solute or solutes from one side of a cardiac muscle cell membrane to the other according to the reaction: Na+(out) + H+(in) = Na+(in) + H+(out). This transfer contributes to the regulation of the cardiac muscle cell plasma membrane potential.
Enables the transmembrane transfer of a potassium ion by a voltage-gated channel through the plasma membrane of an SA node cardiac muscle cell contributing to the depolarization phase of an action potential. 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 potassium ion by a voltage-gated channel through the plasma membrane of an SA node cardiac muscle cell contributing to the depolarization phase of an action potential. 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 potassium ion by a voltage-gated channel through the plasma membrane of an SA node cardiac muscle cell contributing to the depolarization phase of an action potential. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
The attachment of one cardiomyocyte to another cardiomyocyte via adhesion molecules.
An action potential that occurs in a bundle of His cell.
The process that mediates signaling interactions between an atrial cardiomyocyte and an AV node cell by transfer of current between their adjacent cytoplasms via intercellular protein channels.
The process that mediates signaling interactions between an atrial cardiomyocyte and an AV node cell by transfer of current between their adjacent cytoplasms via intercellular protein channels.
The process in which AV node cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which AV node cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which SA node cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which SA node cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which SA node cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which SA node cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which Purkinje myocyte membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which bundle of His cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which ions are transported across a membrane such that the AV node cardiac muscle cell membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which ions are transported across a membrane such that the AV node cardiac muscle cell membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which ions are transported across a membrane such that the bundle of His cardiac muscle cell membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which ions are transported across a membrane such that the Purkinje myocyte membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which an SA node cardiac muscle cell membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which an SA node cardiac muscle cell membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which an SA node cardiac muscle cell membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which an SA node cardiac muscle cell membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process that mediates signaling interactions between an AV node cardiomyocyte and a bundle of His cardiac muscle cell by transfer of current between their adjacent cytoplasms via intercellular protein channels.
The process that mediates signaling interactions between a bundle of His cardiac muscle cell and a Purkinje myocyte by transfer of current between their adjacent cytoplasms via intercellular protein channels.
The process that mediates signaling interactions between a Purkinje myocyte and a ventricular cardiac muscle cell by transfer of current between their adjacent cytoplasms via intercellular protein channels.
Enables the transmembrane transfer of a calcium ion by a voltage-gated channel across the plasma membrane of an AV node cardiac muscle cell that contributes to the depolarization phase of an action potential. 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 calcium ion by a voltage-gated channel across the plasma membrane of an AV node cardiac muscle cell that contributes to the depolarization phase of an action potential. 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 calcium ion by a voltage-gated channel across the plasma membrane of a bundle of His cardiac muscle cell that contributes to the depolarization phase of an action potential. 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 calcium ion by a voltage-gated channel across the plasma membrane of an Purkinje myocyte cell that contributes to the depolarization phase of an action potential. 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 calcium ion by a voltage-gated channel across the plasma membrane of an SA node cardiac muscle cell that contributes to the depolarization phase of an action potential. 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 calcium ion by a voltage-gated channel across the plasma membrane of an SA node cardiac muscle cell that contributes to the depolarization phase of an action potential. 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 calcium ion by a voltage-gated channel across the plasma membrane of an SA node cardiac muscle cell that contributes to the depolarization phase of an action potential. 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 calcium ion by a voltage-gated channel across the plasma membrane of an SA node cardiac muscle cell that contributes to the depolarization phase of an action potential. 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 sodium ion by a voltage-gated channel through the plasma membrane of an AV node cardiac muscle cell contributing to the depolarization phase of an action potential. 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 sodium ion by a voltage-gated channel through the plasma membrane of an AV node cardiac muscle cell contributing to the depolarization phase of an action potential. 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 sodium ion by a voltage-gated channel through the plasma membrane of a bundle of His cardiac muscle cell contributing to the depolarization phase of an action potential. 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 sodium ion by a voltage-gated channel through the plasma membrane of a Purkinje myocyte contributing to the depolarization phase of an action potential. 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 sodium ion by a voltage-gated channel through the plasma membrane of an SA node cardiac muscle cell contributing to the depolarization phase of an action potential. 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 sodium ion by a voltage-gated channel through the plasma membrane of an SA node cardiac muscle cell contributing to the depolarization phase of an action potential. 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 sodium ion by a voltage-gated channel through the plasma membrane of an SA node cardiac muscle cell contributing to the depolarization phase of an action potential. 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 sodium ion by a voltage-gated channel through the plasma membrane of an SA node cardiac muscle cell contributing to the depolarization phase of an action potential. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
The process that mediates signaling interactions between one cell and another cell by transfer of current between their adjacent cytoplasms via intercellular protein channels and contributes to the process of cardiac conduction.
Any process that mediates interactions between a cell and its surroundings that contributes to the process of cardiac conduction. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The process that mediates interactions between an atrial cardiomyocyte and its surroundings that contributes to the process of the atrial cardiomyocyte communicating with an AV node cell in cardiac conduction. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The process that mediates interactions between an atrial cardiomyocyte and its surroundings that contributes to the process of the atrial cardiomyocyte communicating with an AV node cell in cardiac conduction. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The process that mediates interactions between an AV node cell and its surroundings that contributes to the process of the AV node cell communicating with a bundle of His cell in cardiac conduction. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The process that mediates interactions between a Purkinje myocyte and its surroundings that contributes to the process of the Purkinje myocyte communicating with a ventricular cardiac muscle cell in cardiac conduction. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The process that mediates interactions between a bundle of His cell and its surroundings that contributes to the process of the bundle of His cell communicating with a Purkinje myocyte in cardiac conduction. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The process that mediates interactions between an SA node cardiomyocyte and its surroundings that contributes to the process of the SA node cardiomyocyte communicating with an atrial cardiomyocyte in cardiac conduction. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The process that mediates interactions between an SA node cardiomyocyte and its surroundings that contributes to the process of the SA node cardiomyocyte communicating with an atrial cardiomyocyte in cardiac conduction. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The process that mediates interactions between an SA node cardiomyocyte and its surroundings that contributes to the process of the SA node cardiomyocyte communicating with an atrial cardiomyocyte in cardiac conduction. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The process that mediates interactions between an SA node cardiomyocyte and its surroundings that contributes to the process of the SA node cardiomyocyte communicating with an atrial cardiomyocyte in cardiac conduction. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The process that mediates interactions between an SA node cardiomyocyte and its surroundings that contributes to the process of the SA node cardiomyocyte communicating with an atrial cardiomyocyte in cardiac conduction. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment.
The attachment of an atrial cardiomyocyte to an AV node cell via adhesion molecules that results in the cells being juxtaposed so that they can communicate.
The attachment of an atrial cardiomyocyte to an AV node cell via adhesion molecules that results in the cells being juxtaposed so that they can communicate.
The attachment of an AV node cell to an bundle of His cell via adhesion molecules that results in the cells being juxtaposed so that they can communicate.
The attachment of a bundle of His cell to a Purkinje myocyte via adhesion molecules that results in the cells being juxtaposed so that they can communicate.
The attachment of an Purkinje myocyte to a ventricular cardiac muscle cell via adhesion molecules that results in the cells being juxtaposed so that they can communicate.
A wide pore channel activity that enables a direct cytoplasmic connection from one cardiomyocyte to an adjacent cardiomyocyte. The gap junction passes electrical signals between the cells contributing to cardiac conduction.
A wide pore channel activity that enables a direct cytoplasmic connection from an atrial cardiomyocyte to an AV node cell. The gap junction passes electrical signals between the cells contributing to cardiac conduction.
A wide pore channel activity that enables a direct cytoplasmic connection from an atrial cardiomyocyte to an AV node cell. The gap junction passes electrical signals between the cells contributing to cardiac conduction.
A wide pore channel activity that enables a direct cytoplasmic connection from an AV node cell to a bundle of His cell. The gap junction passes electrical signals between the cells contributing to cardiac conduction.
A wide pore channel activity that enables a direct cytoplasmic connection from a bundle of His cell to a Purkinje myocyte. The gap junction passes electrical signals between the cells contributing to cardiac conduction.
A wide pore channel activity that enables a direct cytoplasmic connection from a Purkinje myocyte to a ventricular cardiac muscle cell. The gap junction passes electrical signals between the cells contributing to cardiac conduction.
Interacting selectively and non-covalently with any protein or protein complex contributing to the adhesion of two different types of cells.
Interacting selectively and non-covalently with any protein or protein complex that results in the connection of an atrial cardiomyocyte with an AV node cell and contributes to the communication between the two cells.
Interacting selectively and non-covalently with any protein or protein complex that results in the connection of an atrial cardiomyocyte with an AV node cell and contributes to the communication between the two cells.
Interacting selectively and non-covalently with any protein or protein complex that results in the connection of an AV node cell with a bundle of His cell and contributes to the communication between the two cells.
Interacting selectively and non-covalently with any protein or protein complex that results in the connection of a bundle of His cell with a Purkinje myocyte and contributes to the communication between the two cells.
Interacting selectively and non-covalently with any protein or protein complex that results in the connection of a Purkinje myocyte with an ventricular cardiac muscle cell and contributes to the communication between the two cells.
Interacting selectively and non-covalently with any protein or protein complex that results in the connection of an SA cardiomyocyte with an atrial cardiomyocyte and contributes to the communication between the two cells.
Catalysis of the transmembrane transfer of a potassium ion by a voltage-gated channel through the plasma membrane of an AV node cardiac muscle cell contributing to the repolarization phase of an action potential. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Catalysis of the transmembrane transfer of a potassium ion by a voltage-gated channel through the plasma membrane of an AV node cardiac muscle cell contributing to the repolarization phase of an action potential. 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 potassium ion by a voltage-gated channel through the plasma membrane of a bundle of His cell contributing to the repolarization phase of an action potential. 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 potassium ion by a voltage-gated channel through the plasma membrane of a Purkinje myocyte contributing to the repolarization phase of an action potential. 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 potassium ion by a voltage-gated channel through the plasma membrane of an atrial cardiomyocyte contributing to the repolarization phase of an action potential. 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 potassium ion by a voltage-gated channel through the plasma membrane of an SA node cell contributing to the repolarization phase of an action potential. 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 potassium ion by a voltage-gated channel through the plasma membrane of an SA node cell contributing to the repolarization phase of an action potential. 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 potassium ion by a voltage-gated channel through the plasma membrane of an SA node cell contributing to the repolarization phase of an action potential. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
A cardiac conduction process that modulates the frequency or rate of heart contraction.
A cardiac conduction process that modulates the extent of heart contraction, changing the force with which blood is propelled.
A G protein-coupled acetylcholine receptor signaling pathway, which contributes to a circulatory system process carried out by the heart.
A G protein-coupled acetylcholine receptor signaling pathway, which contributes to a circulatory system process carried out by the heart.
A G protein-coupled acetylcholine receptor signaling pathway, which contributes to a circulatory system process carried out by the heart.
A G protein-coupled acetylcholine receptor signaling pathway, which contributes to a circulatory system process carried out by the heart.
An adrenergic receptor signaling pathway that contributes to an increase in frequency or rate of cardiac muscle contraction through phosphorylation and enhancement of the ryanodine receptor, a calcium-activated calcium-release channel found in the membrane of the sarcoplasmic reticulum. An adrenergic receptor-activated adenylate cyclase generates cAMP. cAMP then activates the cAMP-dependent protein kinase A (PKA), which phosphorylates the ryanodine receptor (RyR). PKA-phosphorylation of RyR enhances channel activity by sensitizing the channel to cytosolic calcium. Cytosolic calcium stimulates contractile proteins to promote muscle contraction.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to a decrease in frequency or rate of heart contraction through activation of the IKACh potassium channel. Binding of acetylcholine to a G protein-coupled acetylcholine receptor (muscarinic receptor) on the surface of the signal-receiving cell results in liberation of the G-beta/gamma complex from the alpha subunit. The G-beta/gamma complex binds directly to the inward-rectifying potassium channel IKACh. Once the ion channel is activated, potassium ions (K+) flow out of the cell and cause it to hyperpolarize. In its hyperpolarized state, action potentials cannot be fired as quickly as possible, which slows the heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to a decrease in frequency or rate of heart contraction through activation of the IKACh potassium channel. Binding of acetylcholine to a G protein-coupled acetylcholine receptor (muscarinic receptor) on the surface of the signal-receiving cell results in liberation of the G-beta/gamma complex from the alpha subunit. The G-beta/gamma complex binds directly to the inward-rectifying potassium channel IKACh. Once the ion channel is activated, potassium ions (K+) flow out of the cell and cause it to hyperpolarize. In its hyperpolarized state, action potentials cannot be fired as quickly as possible, which slows the heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to a decrease in frequency or rate of heart contraction through activation of the IKACh potassium channel. Binding of acetylcholine to a G protein-coupled acetylcholine receptor (muscarinic receptor) on the surface of the signal-receiving cell results in liberation of the G-beta/gamma complex from the alpha subunit. The G-beta/gamma complex binds directly to the inward-rectifying potassium channel IKACh. Once the ion channel is activated, potassium ions (K+) flow out of the cell and cause it to hyperpolarize. In its hyperpolarized state, action potentials cannot be fired as quickly as possible, which slows the heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to a decrease in frequency or rate of heart contraction through activation of the IKACh potassium channel. Binding of acetylcholine to a G protein-coupled acetylcholine receptor (muscarinic receptor) on the surface of the signal-receiving cell results in liberation of the G-beta/gamma complex from the alpha subunit. The G-beta/gamma complex binds directly to the inward-rectifying potassium channel IKACh. Once the ion channel is activated, potassium ions (K+) flow out of the cell and cause it to hyperpolarize. In its hyperpolarized state, action potentials cannot be fired as quickly as possible, which slows the heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to a decrease in frequency or rate of heart contraction through activation of the IKACh potassium channel. Binding of acetylcholine to a G protein-coupled acetylcholine receptor (muscarinic receptor) on the surface of the signal-receiving cell results in liberation of the G-beta/gamma complex from the alpha subunit. The G-beta/gamma complex binds directly to the inward-rectifying potassium channel IKACh. Once the ion channel is activated, potassium ions (K+) flow out of the cell and cause it to hyperpolarize. In its hyperpolarized state, action potentials cannot be fired as quickly as possible, which slows the heart rate.
An adrenergic receptor signaling pathway which contributes to a circulatory system process carried out by the heart, where the activated adrenergic receptor transmits the signal by Gi-mediated inhibition of adenylate cyclase activity.
An adrenergic receptor signaling pathway which contributes to a circulatory system process carried out by the heart, where the activated adrenergic receptor transmits the signal by Gi-mediated inhibition of adenylate cyclase activity.
An adrenergic receptor signaling pathway which contributes to a circulatory system process carried out by the heart, where the activated adrenergic receptor transmits the signal by Gi-mediated inhibition of adenylate cyclase activity.
An adrenergic receptor signaling pathway which contributes to a circulatory system process carried out by the heart, where the activated adrenergic receptor transmits the signal by Gi-mediated inhibition of adenylate cyclase activity.
An angiotensin-mediated signaling pathway where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
An angiotensin-mediated signaling pathway where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
An angiotensin-mediated signaling pathway where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
An angiotensin-mediated signaling pathway where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
An angiotensin-mediated signaling pathway where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
An angiotensin receptor signaling pathway which contributes to a circulatory system process carried out by the heart.
An angiotensin receptor signaling pathway which contributes to a circulatory system process carried out by the heart.
An angiotensin receptor signaling pathway which contributes to a circulatory system process carried out by the heart.
An angiotensin-mediated signaling pathway that contributes to a circulatory system process carried out by the heart, where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
An angiotensin-mediated signaling pathway that contributes to a circulatory system process carried out by the heart, where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
An angiotensin-mediated signaling pathway that contributes to a circulatory system process carried out by the heart, where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
An angiotensin-mediated signaling pathway that contributes to a circulatory system process carried out by the heart, where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
An angiotensin-mediated signaling pathway that contributes to a circulatory system process carried out by the heart, where the activated receptor transmits the signal via Gq-mediated activation of phospholipase C (PLC). PLC hydrolyses phosphatidylinositol 4,5-bisphosphate (PIP2) into the second messengers inositol-1,4,5,-triphosphate (IP3) and diacylglycerol (DAG). DAG activates protein kinase C (PKC), whilst IP3 binds intracellular receptors to induce the release of Ca2+ from intracellular stores.
A series of molecular signals initiated by an endothelin receptor binding to one of its physiological ligands, and proceeding with the activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. Ends with regulation of a downstream cellular process, e.g. transcription.
An endothelin receptor signaling pathway which contributes to a circulatory system process carried out by the heart.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to an decrease in frequency or rate of heart contraction through inhibition of adenylate cyclase (AC) activity. Binding of acetylcholine to a G protein-coupled (muscarinic) receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gi/o protein. Gi/o inhibits adenylate cyclase to decrease cyclic-AMP (cAMP) levels. Since cAMP binds directly to F-channels to allow an inward flow of sodium (funny current, If current), a reduction in cAMP reduces the funny current to bring about membrane hyperpolarization and a decrease in heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to an decrease in frequency or rate of heart contraction through inhibition of adenylate cyclase (AC) activity. Binding of acetylcholine to a G protein-coupled (muscarinic) receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gi/o protein. Gi/o inhibits adenylate cyclase to decrease cyclic-AMP (cAMP) levels. Since cAMP binds directly to F-channels to allow an inward flow of sodium (funny current, If current), a reduction in cAMP reduces the funny current to bring about membrane hyperpolarization and a decrease in heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to an decrease in frequency or rate of heart contraction through inhibition of adenylate cyclase (AC) activity. Binding of acetylcholine to a G protein-coupled (muscarinic) receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gi/o protein. Gi/o inhibits adenylate cyclase to decrease cyclic-AMP (cAMP) levels. Since cAMP binds directly to F-channels to allow an inward flow of sodium (funny current, If current), a reduction in cAMP reduces the funny current to bring about membrane hyperpolarization and a decrease in heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to an decrease in frequency or rate of heart contraction through inhibition of adenylate cyclase (AC) activity. Binding of acetylcholine to a G protein-coupled (muscarinic) receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gi/o protein. Gi/o inhibits adenylate cyclase to decrease cyclic-AMP (cAMP) levels. Since cAMP binds directly to F-channels to allow an inward flow of sodium (funny current, If current), a reduction in cAMP reduces the funny current to bring about membrane hyperpolarization and a decrease in heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to an decrease in frequency or rate of heart contraction through inhibition of adenylate cyclase (AC) activity. Binding of acetylcholine to a G protein-coupled (muscarinic) receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gi/o protein. Gi/o inhibits adenylate cyclase to decrease cyclic-AMP (cAMP) levels. Since cAMP binds directly to F-channels to allow an inward flow of sodium (funny current, If current), a reduction in cAMP reduces the funny current to bring about membrane hyperpolarization and a decrease in heart rate.
A G protein-coupled acetylcholine receptor signaling pathway that contributes to an decrease in frequency or rate of heart contraction through inhibition of adenylate cyclase (AC) activity. Binding of acetylcholine to a G protein-coupled (muscarinic) receptor on the surface of the signal-receiving cell results in the activation of an intracellular Gi/o protein. Gi/o inhibits adenylate cyclase to decrease cyclic-AMP (cAMP) levels. Since cAMP binds directly to F-channels to allow an inward flow of sodium (funny current, If current), a reduction in cAMP reduces the funny current to bring about membrane hyperpolarization and a decrease in heart rate.
An G protein-coupled receptor signaling pathway which contributes to a circulatory system process carried out by the heart.
An G protein-coupled receptor signaling pathway which contributes to a circulatory system process carried out by the heart.
An G protein-coupled receptor signaling pathway which contributes to a circulatory system process carried out by the heart.
An G protein-coupled receptor signaling pathway which contributes to a circulatory system process carried out by the heart.
A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase D, which occurs as a result of a single trigger reaction or compound.
A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase D, which occurs as a result of a single trigger reaction or compound.
A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase D, which occurs as a result of a single trigger reaction or compound.
A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase D, which occurs as a result of a single trigger reaction or compound.
A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase D, which occurs as a result of a single trigger reaction or compound.
A heterodimeric protein complex consisting of conserved large and small U2AF subunits that contributes to spliceosomal RNA splicing by binding to consensus sequences at the 3' splice site. U2AF is required to stabilize the association of the U2 snRNP with the branch point.
Catalysis of the reaction: UDP-glucose + ditrans,octacis-undecaprenyl phosphate = UMP + alpha-D-glucopyranosyl-diphospho-ditrans,octacis-undecaprenol.
The directed movement of L-aspartate out of the vacuole, across the vacuolar membrane.
The directed movement of L-glutamate out of the vacuole, across the vacuolar membrane.
A process in which a protein is transported to, or maintained in, a specific location the cell outer membrane.
The directed movement of L-ornithine out of the vacuole, across the vacuolar membrane.
The directed movement of L-lysine out of the vacuole, across the vacuolar membrane.
The directed movement of L-histidine out of the vacuole, across the vacuolar membrane.
The directed movement of L-histidine across a membrane.
Interacting selectively and non-covalently with a endocytic signal sequence, a specific peptide sequence, of 4-6 amino acids with an essential tyrosine (Y), found on cytoplasmic tails of some cell surface membrane proteins, which directs internalization by clathrin-coated pits.
A heteromeric complex consisting of Cbf1 and basic leucine zipper (bZIP) containing transcriptional activators, Met4 and Met28, that forms over the sequence TCACGTG in the upstream activating sequence (UAS) of genes involved in sulfur amino acid metabolism, resulting in their transcriptional activation.
Catalysis of the reaction: UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O = UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA containing N6-threonylcarbamoyladenosine = S-adenosyl-L-homocysteine + tRNA containing N6-methylthreonylcarbamoyladenosine.
A heterodimeric complex consisting of Zn(2)Cys(6) containing transcription factors Pip2 and Oaf1. It binds to the oleate response element (ORE), found in the promoters of fatty acid-inducible genes in Saccharomyces where, in the presence of oleate this bound complex activates the transcription of genes encoding peroxisomal proteins.
The component of a membrane consisting of gene products and protein complexes that have some part that spans both leaflets of the membrane.
The directed movement of an amino acid from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of an amino acid from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of an amino acid from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of an amino acid from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of an amino acid from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of an amino acid from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of an amino acid from outside of a cell, across the plasma membrane and into the cytosol.
Interacting selectively and non-covalently with an RHG (reaper/hid/grimm) domain/motif (AKA iap binding motif).
Interacting selectively and non-covalently with an RHG (reaper/hid/grimm) domain/motif (AKA iap binding motif).
Interacting selectively and non-covalently with an RHG (reaper/hid/grimm) domain/motif (AKA iap binding motif).
Interacting selectively and non-covalently with an RHG (reaper/hid/grimm) domain/motif (AKA iap binding motif).
Interacting selectively and non-covalently with a caspase family protein.
Enables the transfer of a phosphoenolpyruvate from one side of a membrane to the other.
The directed movement of phosphoenolpytuvate across a membrane.
A process that impedes the progress of the DNA replication fork at natural replication fork pausing sites within the eukaryotic tRNA transcription unit.
Any process that modulates the rate, frequency or extent of linear element assembly. Linear element assembly is 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.
The process whose specific outcome is the progression of the hypoblast over time, from its formation to the mature structure. The hypoblast is a tissue formed from the inner cell mass that lies beneath the epiblast.
The developmental process pertaining to the initial formation of the primitive streak from unspecified parts. The primitive streak is a ridge of cells running along the midline of the embryo where the mesoderm ingresses. It defines the anterior-posterior axis.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, which contributes to the formation of the primitive streak.
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, which contributes to the formation of the primitive streak.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in transcription of target genes that contribute to the formation of the primitive streak.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in transcription of target genes that contribute to the formation of the primitive streak.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in transcription of target genes that contribute to the formation of the primitive streak.
Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway that contributes to the formation of the primitive streak.
Any process that modulates the frequency, rate or extent of any TGF-beta receptor signaling pathway that contributes to the formation of the primitive streak.
The developmental process pertaining to the initial formation of a leaflet from unspecified parts. A leaflet is one of the ultimate segments of a compound leaf.
Any process that increases the frequency, rate or extent of leaflet formation as a result of the series of molecular signals generated in response to detection of auxin.
Any process that modulates the frequency, rate or extent of leaflet formation.
The formation of anterior end of the flat, thickened layer of ectodermal cells known as the neural plate.
The formation of posterior end of the flat, thickened layer of ectodermal cells known as the neural plate.
Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter contributing to the formation of the anterior neural plate.
Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter contributing to the formation of the posterior neural plate.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell and increasing the rate or extent of posterior neural plate formation.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell and increasing the rate or extent of posterior neural plate formation.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell and increasing the rate or extent of posterior neural plate formation.
Any process that modulates the frequency, rate, or extent of neutrophil chemotaxis. Neutrophil chemotaxis is 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.
Any process that increases the frequency, rate, or extent of neutrophil chemotaxis. Neutrophil chemotaxis is 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.
Any process that decreases the frequency, rate, or extent of neutrophil chemotaxis. Neutrophil chemotaxis is 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.
Any process that modulates the frequency, rate, or extent of monocyte chemotaxis.
Any process that increases the frequency, rate, or extent of monocyte chemotaxis.
Any process that decreases the frequency, rate, or extent of monocyte chemotaxis.
Any process that increases the frequency, rate or extent of pheromone-dependent signal transduction during conjugation with cellular fusion, a signal transduction process resulting in the relay, amplification or dampening of a signal generated in response to pheromone exposure in organisms that undergo conjugation with cellular fusion.
Any process that decreases the frequency, rate or extent of pheromone-dependent signal transduction during conjugation with cellular fusion, a signal transduction process resulting in the relay, amplification or dampening of a signal generated in response to pheromone exposure in organisms that undergo conjugation with cellular fusion.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of steroid hormones,compounds with a 1, 2, cyclopentanoperhydrophenanthrene nucleus that act as hormones.
Any process that increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of steroid hormones,compounds with a 1, 2, cyclopentanoperhydrophenanthrene nucleus that act as hormones.
Any process that decreases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of steroid hormones,compounds with a 1, 2, cyclopentanoperhydrophenanthrene nucleus that act as hormones.
Any process that increases the frequency, rate or extent of the process in which a multicellular organism or a group of unicellular organisms grow in a threadlike, filamentous shape.
Any process that modulates the frequency, rate, or extent of chaperone-mediated protein complex assembly. Chaperone-mediated protein complex assembly is the aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
Any process that increases the frequency, rate, or extent of chaperone-mediated protein complex assembly. Chaperone-mediated protein complex assembly is the aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
Any process that modulates the frequency, rate, or extent of a series of reactions, mediated by the intracellular serine/threonine kinase protein kinase C, which occurs as a result of a single trigger reaction or compound.
Any process that modulates the frequency, rate, or extent of a series of reactions, mediated by the intracellular serine/threonine kinase protein kinase C, which occurs as a result of a single trigger reaction or compound.
Any process that increases the frequency, rate, or extent of a series of reactions, mediated by the intracellular serine/threonine kinase protein kinase C, which occurs as a result of a single trigger reaction or compound.
Any process that increases the frequency, rate, or extent of a series of reactions, mediated by the intracellular serine/threonine kinase protein kinase C, which occurs as a result of a single trigger reaction or compound.
Any process that decreases the frequency, rate, or extent of a series of reactions, mediated by the intracellular serine/threonine kinase protein kinase C, which occurs as a result of a single trigger reaction or compound.
Any process that decreases the frequency, rate, or extent of a series of reactions, mediated by the intracellular serine/threonine kinase protein kinase C, which occurs as a result of a single trigger reaction or compound.
The removal of an acetyl group from tubulin. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid.
Any process that modulates the frequency, rate or extent of tubulin deacetylation. Tubulin deacetylation is the removal of an acetyl group from a protein amino acid.
Any process that increases the frequency, rate or extent of tubulin deacetylation. Tubulin deacetylation is the removal of an acetyl group from a protein amino acid.
Any process that activates or increases the frequency, rate or extent of deacetylase activity, the catalysis of the hydrolysis of an acetyl group or groups from a substrate molecule.
Any process that modulates the frequency, rate or extent of cell migration involved in sprouting angiogenesis. Cell migration involved in sprouting angiogenesis is the orderly movement of endothelial cells into the extracellular matrix in order to form new blood vessels contributing to the process of sprouting angiogenesis.
Any process that increases the frequency, rate or extent of cell migration involved in sprouting angiogenesis. Cell migration involved in sprouting angiogenesis is the orderly movement of endothelial cells into the extracellular matrix in order to form new blood vessels contributing to the process of sprouting angiogenesis.
Any process that decreases the frequency, rate or extent of cell migration involved in sprouting angiogenesis. Cell migration involved in sprouting angiogenesis is the orderly movement of endothelial cells into the extracellular matrix in order to form new blood vessels contributing to the process of sprouting angiogenesis.
Any process that modulates the frequency, rate or extent of chromatin silencing at the centromere. Chromatin silencing at the centromere is the repression of transcription of centromeric DNA by altering the structure of chromatin.
Any process that increases the frequency, rate or extent of chromatin silencing at the centromere. Chromatin silencing at the centromere is the repression of transcription of centromeric DNA by altering the structure of chromatin.
Any process that modulates the frequency, rate, or extent of chromatin silencing at silent mating-type cassette. Chromatin silencing at silent mating-type cassette is the repression of transcription at silent mating-type loci by altering the structure of chromatin.
Any process that increases the frequency, rate, or extent of chromatin silencing at silent mating-type cassette. Chromatin silencing at silent mating-type cassette is the repression of transcription at silent mating-type loci by altering the structure of chromatin.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving chlorophyll.
The radial pattern formation process that results in the formation of the different tissues of the root around its radial axis.
The process whose specific outcome is the progression of the metaxylem over time, from its formation to the mature structure. The metaxylem is the part of the primary xylem that differentiates after the protoxylem and before the secondary xylem, if any of the latter is formed.
The process whose specific outcome is the progression of the protoxylem over time, from its formation to the mature structure. The protoxylem comprises the first formed elements of the primary xylem.
Any process that modulates the frequency, rate, or extent of metaxylem development. Metaxylem development is the process whose specific outcome is the progression of the metaxylem over time, from its formation to the mature structure. The metaxylem is the part of the primary xylem that differentiates after the protoxylem and before the secondary xylem, if any of the latter is formed.
Any process that modulates the frequency, rate or extent of trehalose metabolism, the chemical reactions and pathways involving trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.
Any process that increases the rate, frequency or extent of microtubule nucleation. Microtubule nucleation is the 'de novo' formation of a microtubule, in which tubulin heterodimers form metastable oligomeric aggregates, some of which go on to support formation of a complete microtubule. Microtubule nucleation usually occurs from a specific site within a cell.
Any process that starts the inactive process of microtubule nucleation. Microtubule nucleation is the 'de novo' formation of a microtubule, in which tubulin heterodimers form metastable oligomeric aggregates, some of which go on to support formation of a complete microtubule. Microtubule nucleation usually occurs from a specific site within a cell.
Any process that modulates the frequency, rate or extent of the production of siRNA, the cleavage of double-stranded RNA to form small interfering RNA molecules (siRNAs) of 21-23 nucleotides, in the context of RNA interference.
Any process that modulates the size of an anatomical structure.
Any process that modulates the size of the thalamus. The thalamus is a part of the diencephalon that is composed of the dorsal thalamus and the ventral thalamus.
Any process that increases the rate, frequency or extent of a cellular process that is involved in the progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events.
Any process that modulates the rate, frequency or extent of ribosome biogenesis. Ribosome biogenesis is the cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of ribosome subunits.
Any process that increases the rate, frequency or extent of ribosome biogenesis. Ribosome biogenesis is the cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of ribosome subunits.
Any process that decreases the rate, frequency or extent of ribosome biogenesis. Ribosome biogenesis is the cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of ribosome subunits.
Any process that increases the frequency, rate or extent of protein homodimerization, interacting selectively with an identical protein to form a homodimer.
Any process that decreases the frequency, rate or extent of protein homodimerization, interacting selectively with an identical protein to form a homodimer.
A process in which the extent of muscle contraction is reduced. Muscle relaxation can involve a number of processes including the removal of calcium from the cytoplasm to the sarcoplasmic reticulum lumen through the action of Ca2+ ATPases. In some muscles, calcium-independent pathways also play a role in muscle relaxation by decreasing the phosphorylation state of myosin light chain.
A process in which the extent of skeletal muscle tissue contraction is reduced. Muscle relaxation involves the removal of calcium from the cytoplasm to the sarcoplasmic reticulum lumen through the action of Ca2+ ATPases.
The process in which a relatively unspecialized cell acquires the specialized features of a foam cell. A foam cell is a type of cell containing lipids in small vacuoles and typically seen in atherosclerotic lesions, as well as other conditions.
The process in which a smooth muscle cell acquires the specialized features of a foam cell. A foam cell is a type of cell containing lipids in small vacuoles and typically seen in atherosclerotic lesions, as well as other conditions.
Any selective and non-covalent interaction with a nucleic acid involved in the initiation, activation, perpetuation, repression or termination of polypeptide synthesis at the ribosome.
The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands resulting in an increase in the rate or frequency of a MAPKKK cascade.
Any process that modulates the rate, frequency or extent of canonical Wnt signaling pathway that regulates heart induction. Canonical Wnt signaling pathway involved in heart induction is the series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell, followed by relaying of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that modulates the rate, frequency or extent of canonical Wnt signaling pathway that regulates heart induction. Canonical Wnt signaling pathway involved in heart induction is the series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell, followed by relaying of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that modulates the rate, frequency or extent of canonical Wnt signaling pathway that regulates heart induction. Canonical Wnt signaling pathway involved in heart induction is the series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell, followed by relaying of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that decreases the rate, frequency or extent of canonical Wnt signaling pathway that positively regulates heart induction. Canonical Wnt signaling pathway involved in heart induction is the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that decreases the rate, frequency or extent of canonical Wnt signaling pathway that positively regulates heart induction. Canonical Wnt signaling pathway involved in heart induction is the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that decreases the rate, frequency or extent of canonical Wnt signaling pathway that positively regulates heart induction. Canonical Wnt signaling pathway involved in heart induction is the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that modulates the rate, frequency, or extent of inclusion body assembly. Inclusion body assembly is the aggregation, arrangement and bonding together of a set of components to form an inclusion body.
Any process that decreases the rate, frequency, or extent of inclusion body assembly. Inclusion body assembly is the aggregation, arrangement and bonding together of a set of components to form an inclusion body.
Any process that modulates the frequency, rate or extent of protein deubiquitination. Protein deubiquitination is the removal of one or more ubiquitin groups from a protein.
Any process that decreases the frequency, rate or extent of protein deubiquitination. Protein deubiquitination is the removal of one or more ubiquitin groups from a protein.
Any process that modulates the frequency, rate or extent of the directed movement of peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another, 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 oligopeptides into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Oligopeptides are molecules that contain a small number (2 to 20) of amino-acid residues connected by peptide linkages.
Any process that modulates the rate, frequency or extent of dipeptide transport. Dipeptide transport is the directed movement of a dipeptide, a combination of two amino acids by means of a peptide (-CO-NH-) link, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that decreases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that decreases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that decreases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that decreases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that decreases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that decreases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that decreases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that increases the rate, frequency or extent of extracellular matrix disassembly. Extracellular matrix disassembly is a process that results in the breakdown of the extracellular matrix.
Any process that modulates the rate, frequency, or extent of the series of molecular signals generated as a consequence of a transmembrane receptor serine/threonine kinase binding to its physiological ligand.
Any process that modulates the frequency, rate or extent of fungal-type cell wall beta-glucan biosynthesis, the chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of fungal cells.
The multiplication or reproduction of metanephric cap mesenchymal cells, resulting in the expansion of the cell population. A metanephric cap mesenchymal cell is a mesenchymal cell that has condensed with other mesenchymal cells surrounding the ureteric bud tip.
Any process that modulates the frequency, rate, or extent of metanephric cap mesenchymal cell proliferation. Metanephric cap mesenchymal cell proliferation is the multiplication or reproduction of metanephric cap mesenchymal cells, resulting in the expansion of the cell population. A metanephric cap mesenchymal cell is a mesenchymal cell that has condensed with other mesenchymal cells surrounding the ureteric bud tip.
Any process that increases the frequency, rate, or extent of metanephric cap mesenchymal cell proliferation. Metanephric cap mesenchymal cell proliferation is the multiplication or reproduction of metanephric cap mesenchymal cells, resulting in the expansion of the cell population. A metanephric cap mesenchymal cell is a mesenchymal cell that has condensed with other mesenchymal cells surrounding the ureteric bud tip.
Any process that modulates the frequency, rate, or extent of the decapentaplegic signaling pathway. The decapentaplegic signaling pathway is the series of molecular signals generated as a consequence of the signal decapentaplegic binding to one of its physiological receptors.
Any process that modulates the frequency, rate, or extent of the decapentaplegic signaling pathway. The decapentaplegic signaling pathway is the series of molecular signals generated as a consequence of the signal decapentaplegic binding to one of its physiological receptors.
Any process that increases the frequency, rate, or extent of the decapentaplegic signaling pathway. The decapentaplegic signaling pathway is the series of molecular signals generated as a consequence of the signal decapentaplegic binding to one of its physiological receptors.
Any process that increases the frequency, rate, or extent of the decapentaplegic signaling pathway. The decapentaplegic signaling pathway is the series of molecular signals generated as a consequence of the signal decapentaplegic binding to one of its physiological receptors.
Any process that decreases the frequency, rate, or extent of the decapentaplegic signaling pathway. The decapentaplegic signaling pathway is the series of molecular signals generated as a consequence of the signal decapentaplegic binding to one of its physiological receptors.
Any process that decreases the frequency, rate, or extent of the decapentaplegic signaling pathway. The decapentaplegic signaling pathway is the series of molecular signals generated as a consequence of the signal decapentaplegic binding to one of its physiological receptors.
Any process that increases the rate, frequency, or extent of the series of molecular signals generated as a consequence of a transmembrane receptor serine/threonine kinase binding to its physiological ligand.
Any process that decreases the rate, frequency, or extent of the series of molecular signals generated as a consequence of a transmembrane receptor serine/threonine kinase binding to its physiological ligand.
The progression of the cochlea over time from its formation to the mature structure. The cochlea is the snail-shaped portion of the inner ear that is responsible for the detection of sound.
The process in which the cochlea is generated and organized.
The process in which relatively unspecialized cells acquire specialized structural and functional features of a pancreatic epsilon cell. A pancreatic epsilon cell is a cell in the pancreas that secretes ghrelin.
The process whose specific outcome is the progression of a pancreatic E cell over time, from its formation to the mature structure.
The commitment of a cell to a pancreatic E cell fate and its capacity to differentiate into a pancreatic E cell.
Any process that modulates the frequency, rate, or extent of high-density lipoprotein particle assembly. High-density lipoprotein particle assembly is the aggregation and arrangement of proteins and lipids to form a high-density lipoprotein particle.
Any process that increases the frequency, rate, or extent of high-density lipoprotein particle assembly. High-density lipoprotein particle assembly is the aggregation and arrangement of proteins and lipids to form a high-density lipoprotein particle.
Any process that modulates the rate, frequency, or extent of cell-substrate junction assembly. Cell-substrate junction assembly is the aggregation, arrangement and bonding together of a set of components to form a junction between a cell and its substrate.
The formation of a macromolecular complex between the COPII coat proteins and proteins and/or lipoproteins that are going to be transported by the COPII vesicle to the Golgi.
The formation of a macromolecular complex between the COPII coat proteins and proteins and/or lipoproteins that are going to be transported by the COPII vesicle to the Golgi.
The formation of a macromolecular complex between the COPII coat proteins and proteins and/or lipoproteins that are going to be transported by the COPII vesicle to the Golgi.
Any process that modulates the frequency, rate or extent of COPII vesicle uncoating, the process in which COPII vesicle coat proteins are disassembled, and released.
The process in which COPII vesicle coat proteins are disassembled, and released.
The GTP hydrolysis process that modulates the rate, frequency, or extent of ER to Golgi vesicle-mediated transport, the directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles.
The evagination of an endoplasmic reticulum membrane, resulting in formation of a COPII-coated vesicle.
The evagination of an endoplasmic reticulum membrane, resulting in formation of a COPII-coated vesicle.
The evagination of an endoplasmic reticulum membrane, resulting in formation of a COPII-coated vesicle.
The covalent transfer of a methyl group to C-5 of cytosine in a DNA molecule that contributes to chromatin silencing.
The covalent transfer of a methyl group to C-5 of cytosine in a DNA molecule.
The directed movement of low-density lipoprotein particle from endosomes to lysosomes.
A receptor-mediated endocytosis process involved in intracellular cholesterol transport.
A receptor-mediated endocytosis process involved in intracellular cholesterol transport.
A receptor-mediated endocytosis process involved in intracellular cholesterol transport.
A receptor-mediated endocytosis process involved in intracellular cholesterol transport.
The directed movement of cholesterol, cholest-5-en-3-beta-ol, or cholesterol-containing compounds, by membrane-bounded vesicles.
The directed movement of cholesterol, cholest-5-en-3-beta-ol, or cholesterol-containing compounds, from the lysosome to the endoplasmic reticulum.
The disassembly into constituent parts of the low-density lipoprotein particle in the lysosome that contributes to cholesterol transport.
The cholesterol metabolic process in which cholesterol esters are hydrolyzed into free fatty acids and cholesterol in the lysosome that contributes to intracellular cholesterol transport.
The polysaccharide-based coating on the inner side of a lysosomal membrane that protects it from digestion by lysosomal enzymes.
The covalent transfer of a methyl group to N-4 of cytosine in a DNA molecule.
The attachment of the pre-synaptic cell to the post-synaptic cell via adhesion molecules that contributes to synapse maturation.
The aggregation, arrangement and bonding together of a set of components to form a protein complex that contributes to synapse maturation.
Any process that increases the extent of synaptic maturation as a result of the communication from a pre-synaptic cell to a post-synaptic cell across a synapse.
Any process that modulates the extent of synapse maturation, the process that organizes a synapse so that it attains its fully functional state.
Any process that increases the extent of synapse maturation, the process that organizes a synapse so that it attains its fully functional state.
The process in which the population of cells that make up a tissue undergo directed movement.
The process in which the population of cells that make up a mesenchyme undergo directed movement.
The process in which the population of cells that make up an epithelium undergo directed movement.
The process in which the population of cells that make up a mesendoderm undergo directed movement. The mesendoderm is the epithelial tissue that gives rise to both mesoderm and endoderm.
The orderly movement of epithelial cells from one site to another that contributes to the migration of mesendodermal tissue.
The formation of daughter actin filament branches at an angle on the sides of preexisting mother filaments.
The attachment of an epithelial cell to another epithelial cell via adhesion molecules.
The attachment of an epithelial cell to another epithelial cell via adhesion molecules that contributes to epithelium migration.
Any cell-cell adhesion process that modulates the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
Any process in which mitochondrial DNA and associated proteins are formed into a compact, orderly structure.
Any process that modulates the rate, frequency or extent of mitochondrial fission. Mitochondrial fission is the division of a mitochondrion within a cell to form two or more separate mitochondrial compartments.
Any process that increases the rate, frequency or extent of mitochondrial fission. Mitochondrial fission is the division of a mitochondrion within a cell to form two or more separate mitochondrial compartments.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nucleoid. The nucleoid is the region of a bacterial cell, virion, mitochondrion or chloroplast to which the DNA is confined.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the mitochondrial nucleoid. The mitochondrial nucleoid is the region of a mitochondrion to which the DNA is confined.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the mitochondrial nucleoid that contributes to mitochondrial division.
The directed movement of mitochondria to the correct region of the cell that contributes to the process of mitochondrial fission.
The directed movement of mitochondria to the correct region of the cell that contributes to the process of mitochondrial fission.
Any process that modulates the frequency, rate or extent of the directed movement of mitochondria to the correct region of the cell that contributes to the process of mitochondrial fission.
Any process that modulates the frequency, rate or extent of the directed movement of mitochondria to the correct region of the cell that contributes to the process of mitochondrial fission.
A process that is carried out at the cellular level which results in the separation of a single continuous membrane into two membranes.
A process that is carried out at the cellular level which results in the separation of a single continuous mitochondrial membrane into two membranes and contributes to mitochondrial fission.
A process that is carried out at the cellular level which results in the separation of a single continuous mitochondrial membrane into two membranes and contributes to mitochondrial fission.
The directed movement of a protein to a specific location in a membrane.
The directed movement of a protein to a specific location in a membrane.
The directed movement of a protein to a specific location in the mitochondrial membrane.
The directed movement of a protein to a specific location in the mitochondrial membrane.
The directed movement of a protein to a specific location in the mitochondrial membrane that contributes to mitochondrial fission.
The directed movement of a protein to a specific location in the mitochondrial membrane that contributes to mitochondrial fission.
Any process that modulates the rate, frequency or extent of sphingolipid biosynthesis. Sphingolipid biosynthesis is 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).
Any process that increases the rate, frequency or extent of sphingolipid biosynthesis. Sphingolipid biosynthesis is 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).
Any process that decreases the rate, frequency or extent of sphingolipid biosynthesis. Sphingolipid biosynthesis is 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).
Any process that decreases the rate, frequency or extent of sphingolipid biosynthesis. Sphingolipid biosynthesis is 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).
Any biological process involved in the maintenance of an internal steady state of sphingolipids at the level of the cell.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an endoplasmic reticulum membrane.
The chemical reactions and pathways resulting in the formation of sphingolipids that contributes to endoplasmic reticulum membrane organization.
The directed movement of substances from the Golgi to lysosomes.
The formation of a continuous ribbon of interconnected Golgi stacks of flat cisternae.
The specification and formation of anisotropic intracellular organization of an epithelial cell.
The specification and formation of the polarity of an epithelial cell along the plane of the epithelial tissue.
The asymmetric formation of a continuous ribbon of interconnected Golgi stacks of flat cisternae that contributes to the establishment of epithelial cell polarity.
The asymmetric formation of a continuous ribbon of interconnected Golgi stacks of flat cisternae that modulates the controlled release of a substance from a polarized epithelial cell.
A cellular process that results in the breakdown of a Golgi apparatus that contributes to Golgi inheritance.
Any process in which disassembled Golgi vesicles are localized into daughter cells upon cell division.
The reformation of the Golgi following its breakdown and partitioning contributing to Golgi inheritance.
Any process that modulates the rate, frequency or extent of spindle assembly. Spindle assembly is the aggregation, arrangement and bonding together of a set of components to form the spindle, the array of microtubules and associated molecules that serves to move duplicated chromosomes apart.
Any process that modulates the rate, frequency or extent of Golgi inheritance. Golgi inheritance is the partitioning of Golgi apparatus between daughter cells at cell division.
The process in which the structures of a chondrocyte are generated and organized. This process occurs while the initially relatively unspecialized cell is acquiring the specialized features of a chondrocyte.
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 microtubules and their associated proteins that contributes to chromosomal pairing and precedes synapsis.
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 microtubules and their associated proteins that contributes to chromosomal pairing and precedes synapsis.
Any process that modulates the frequency, rate or extent of synaptonemal complex assembly. Synaptonemal complex assembly is the cell cycle process in which the synaptonemal complex, a structure that holds paired chromosomes together during prophase I of meiosis and that promotes genetic recombination, is formed.
The joining of two lipid bilayers to form a single organelle membrane.
Any process that modulates the rate, frequency or extent of the establishment of planar polarity, the coordinated organization of groups of cells in a tissue, such that they all orient to similar coordinates.
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 microtubules and their associated proteins and contributes to the establishment of planar polarity.
Coordinated organization of groups of cells in the plane of an epithelium that contributes to the closure of the neural tube.
Any process that modulates the rate, frequency, or extent of the establishment of planar polarity involved in neural tube closure, the coordinated organization of groups of cells in the plane of an epithelium that contributes to the closure of the neural tube.
The series of molecular signals initiated by binding of a Wnt protein to a receptor on the surface of the target cell where activated receptors signal via downstream effectors that modulates the establishment of planar polarity contributing to neural tube closure.
Any process that increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of thiamine.
Any process that modulates the rate, frequency, or extent of cholesterol metabolism, the chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
Any process that modulates the rate, frequency or extent of secretion of lysosomal enzymes, the controlled release of lysosomal enzymes by a cell.
Any process that modulates the rate, frequency or extent of kidney development. Kidney development is the process whose specific outcome is the progression of the kidney over time, from its formation to the mature structure. The kidney is an organ that filters the blood and excretes the end products of body metabolism in the form of urine.
Any process that increases the rate, frequency or extent of kidney development. Kidney development is the process whose specific outcome is the progression of the kidney over time, from its formation to the mature structure. The kidney is an organ that filters the blood and excretes the end products of body metabolism in the form of urine.
Any process that decreases the rate, frequency or extent of kidney development. Kidney development is the process whose specific outcome is the progression of the kidney over time, from its formation to the mature structure. The kidney is an organ that filters the blood and excretes the end products of body metabolism in the form of urine.
Any process that modulates the rate, frequency or extent of pancreatic juice secretion, the regulated release of pancreatic juice by the exocrine pancreas into the upper part of the intestine.
Any process that increases the rate, frequency or extent of pancreatic juice secretion, the regulated release of pancreatic juice by the exocrine pancreas into the upper part of the intestine.
Any process that decreases the rate, frequency or extent of pancreatic juice secretion, the regulated release of pancreatic juice by the exocrine pancreas into the upper part of the intestine.
Any process that modulates the rate, frequency or extent of branching involved in ureteric bud morphogenesis, the process in which the branching structure of the ureteric bud is generated and organized. The ureteric bud is an epithelial tube that grows out from the metanephric duct. The bud elongates and branches to give rise to the ureter and kidney collecting tubules.
Any process that increases the rate, frequency or extent of branching involved in ureteric bud morphogenesis, the process in which the branching structure of the ureteric bud is generated and organized. The ureteric bud is an epithelial tube that grows out from the metanephric duct. The bud elongates and branches to give rise to the ureter and kidney collecting tubules.
Any process that decreases the rate, frequency or extent of branching involved in ureteric bud morphogenesis, the process in which the branching structure of the ureteric bud is generated and organized. The ureteric bud is an epithelial tube that grows out from the metanephric duct. The bud elongates and branches to give rise to the ureter and kidney collecting tubules.
Any process that modulates the rate, frequency or extent of glomerulus development, the progression of the glomerulus over time from its initial formation until its mature state. The glomerulus is a capillary tuft surrounded by Bowman's capsule in nephrons of the vertebrate kidney.
Any process that increases the rate, frequency or extent of glomerulus development, the progression of the glomerulus over time from its initial formation until its mature state. The glomerulus is a capillary tuft surrounded by Bowman's capsule in nephrons of the vertebrate kidney.
Any process that decreases the rate, frequency or extent of glomerulus development, the progression of the glomerulus over time from its initial formation until its mature state. The glomerulus is a capillary tuft surrounded by Bowman's capsule in nephrons of the vertebrate kidney.
The regulated release of chemokines from a cell.
Any process that modulates the rate, frequency or extent of chemokine secretion, the regulated release of chemokines from a cell.
Any process that increases the rate, frequency or extent of chemokine secretion, the regulated release of chemokines from a cell.
Any process that decreases the rate, frequency or extent of chemokine secretion, the regulated release of chemokines from a cell.
Any process that modulates the rate, frequency or extent of release of cytochrome c from mitochondria, the process in which cytochrome c is enabled to move from the mitochondrial intermembrane space into the cytosol, which is an early step in apoptosis and leads to caspase activation.
Any process that increases the rate, frequency or extent of release of cytochrome c from mitochondria, the process in which cytochrome c is enabled to move from the mitochondrial intermembrane space into the cytosol, which is an early step in apoptosis and leads to caspase activation.
Any process that decreases the rate, frequency or extent of release of cytochrome c from mitochondria, the process in which cytochrome c is enabled to move from the mitochondrial intermembrane space into the cytosol, which is an early step in apoptosis and leads to caspase activation.
The formation and maintenance of DNA loops that juxtapose sequentially separated regions of RNA polymerase II-transcribed genes.
The formation and maintenance of DNA loops that juxtapose the promoter and terminator regions of RNA polymerase II-transcribed genes and activate transcription from an RNA polymerase II promoter.
A process in which a protein is transported to, or maintained in, a nuclear pore.
Any process that increases the rate, frequency, or extent of cholesterol metabolism, the chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
Any process that decreases the rate, frequency, or extent of cholesterol metabolism, the chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving triglyceride, any triester of glycerol.
Any process that increases the frequency, rate or extent of the chemical reactions and pathways involving triglyceride, any triester of glycerol.
Any process that decreases the frequency, rate or extent of the chemical reactions and pathways involving triglyceride, any triester of glycerol.
Any process that modulates the rate, frequency or extent of the establishment of the blood-brain barrier, a selectively permeable structural and functional barrier that exists between the capillaries and the brain.
Any process that increases the rate, frequency or extent of the establishment of the blood-brain barrier, a selectively permeable structural and functional barrier that exists between the capillaries and the brain.
Any process that decreases the rate, frequency or extent of the establishment of the blood-brain barrier, a selectively permeable structural and functional barrier that exists between the capillaries and the brain.
Any process that modulates the rate, frequency or extent of radial pattern formation, the regionalization process that results in defined areas around a point in which specific types of cell differentiation will occur.
The increase in size or mass of the spongiotrophoblast layer of the placenta where the increase in size or mass contributes to the progression of that layer over time from its formation to its mature state.
Any process that modulates the frequency, rate or extent of the catalysis of the reaction: ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Any process that increases the frequency, rate or extent of the catalysis of the reaction: ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Any process that decreases the frequency, rate or extent of the catalysis of the reaction: ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Any process that increases the frequency, rate or extent of lipid kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a simple or complex lipid.
Any process that decreases the frequency, rate or extent of lipid kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a simple or complex lipid.
The directed movement of a chromosome to the nuclear envelope that contributes to homologous chromosome segregation and precedes synapsis.
The 'de novo' formation of a microtubule, in which tubulin heterodimers form metastable oligomeric aggregates from within the mitotic spindle.
The 'de novo' formation of a microtubule, in which tubulin heterodimers form metastable oligomeric aggregates from the centrosome.
The 'de novo' formation of a microtubule, in which tubulin heterodimers form metastable oligomeric aggregates from chromatin.
Any process that modulates the rate, frequency or extent of the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle.
Any process that modulates the number of microtubules in a given region of the spindle.
Any series of molecular signals in which a Ran GTPase relays one or more of the signals resulting in the modulation of the rate, frequency or extent of microtubule nucleation.
Any process that modulates the rate, frequency or extent of the red or far-red signaling pathway, the series of molecular signals initiated upon sensing by photoreceptor molecules of red light or far red light.
Any process that modulates the rate, frequency or extent of the red or far-red signaling pathway, the series of molecular signals initiated upon sensing by photoreceptor molecules of red light or far red light.
Any process that increases the rate, frequency or extent of the red or far-red signaling pathway, the series of molecular signals initiated upon sensing by photoreceptor molecules of red light or far red light.
Any process that increases the rate, frequency or extent of the red or far-red signaling pathway, the series of molecular signals initiated upon sensing by photoreceptor molecules of red light or far red light.
Any process that decreases the rate, frequency or extent of the red or far-red signaling pathway, the series of molecular signals initiated upon sensing by photoreceptor molecules of red light or far red light.
Any process that decreases the rate, frequency or extent of the red or far-red signaling pathway, the series of molecular signals initiated upon sensing by photoreceptor molecules of red light or far red light.
Any process that modulates the rate, frequency, or extent of centromere complex assembly, the aggregation, arrangement and bonding together of proteins and centromeric DNA molecules to form a centromeric protein-DNA complex.
Any process that modulates the rate, frequency, or extent of the spindle checkpoint, a cell cycle checkpoint that delays the metaphase/anaphase transition until the spindle is correctly assembled and oriented, and chromosomes are attached to the spindle.
Any process that increases the rate, frequency, or extent of the spindle checkpoint, a cell cycle checkpoint that delays the metaphase/anaphase transition until the spindle is correctly assembled and oriented, and chromosomes are attached to the spindle.
Any process that decreases the rate, frequency, or extent of the spindle checkpoint, a cell cycle checkpoint that delays the metaphase/anaphase transition until the spindle is correctly assembled and oriented, and chromosomes are attached to the spindle.
Any process that modulates the rate, frequency, or extent of kinetochore assembly, the aggregation, arrangement and bonding together of a set of components to form the kinetochore, a multisubunit complex that is located at the centromeric region of DNA and provides an attachment point for the spindle microtubules.
Any process that modulates the rate, frequency, or extent of metaphase plate congression, the alignment of chromosomes at the metaphase plate, a plane halfway between the poles of the spindle.
Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter that contributes to the formation of mesodermal clusters that are arranged segmentally along the anterior posterior axis of an embryo.
Any process that modulates the rate, frequency, or extent of arachidonic acid secretion, the controlled release of arachidonic acid from a cell or a tissue.
Any process that increases the rate, frequency, or extent of arachidonic acid secretion, the controlled release of arachidonic acid from a cell or a tissue.
Any process that modulates the rate, frequency, or extent of histone H4 acetylation, the modification of histone H4 by the addition of an acetyl group.
Any process that increases the rate, frequency, or extent of histone H4 acetylation, the modification of histone H4 by the addition of an acetyl group.
Any process that decreases the rate, frequency, or extent of histone H4 acetylation, the modification of histone H4 by the addition of an acetyl group.
The series of molecular signals generated as a consequence of a retinoic acid receptor binding to one of its physiological ligands that contributes to somitogenesis.
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 somitogenesis.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in cell state that contributes to somitogenesis.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in cell state that contributes to somitogenesis.
The series of molecular signals initiated by binding of Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in cell state that contributes to somitogenesis.
The developmental growth that results in the elongation of the rostral-caudal axis that contributes to somitogenesis.
The morphogenetic process in which a presomitic mesoderm narrows along the left-right axis and lengthens in the rostral-caudal axis contributing to somitogenesis.
Any process involved in the controlled self-propelled movement of a cell that contributes to somitogenic axis elongation.
The orderly movement of a presomitic mesoderm cell that contributes to somitogenic axis elongation.
Any process that modulates the frequency, rate, or extent of the controlled self-propelled movement of a cell that contributes to somitogenic axis elongation.
The attachment of one cell to another cell via adhesion molecules that contributes to the establishment of planar cell polarity.
Any process in which a protein is transported to, and/or maintained in, a specific location in a cell that contributes to the establishment of planar polarity.
The process in which the population of cells that make up a wing epithelium undergo directed movement and contribute to imaginal disc-derived morphogenesis.
The morphogenetic process in which the wing epithelium narrows along one axis and lengthens in a perpendicular axis that contributes to imaginal disc-derived wing morphogenesis.
The process in which a cell elongates and contributes to imaginal disc-derived wing morphogenesis.
The multiplication or reproduction of cells, resulting in the expansion of a cell population that contributes to imaginal disc-derived wing morphogenesis.
Any process that modulates the frequency, rate, or extent of the multiplication or reproduction of cells, resulting in the expansion of a cell population that contributes to imaginal disc-derived wing morphogenesis.
Any process that modulates the frequency, rate or extent of a muscle system process, a multicellular organismal process carried out by any of the organs or tissues in a muscle system.
Any process that decreases the rate, frequency or extent of mitochondrial fission. Mitochondrial fission is the division of a mitochondrion within a cell to form two or more separate mitochondrial compartments.
Any process that modulates the frequency, rate, or extent of retinal ganglion cell axon guidance, 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.
Any process that decreases the frequency, rate, or extent of retinal ganglion cell axon guidance, 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.
Any process that increases the rate, frequency, or extent of inclusion body assembly. Inclusion body assembly is the aggregation, arrangement and bonding together of a set of components to form an inclusion body.
Any process that modulates the frequency, rate, or extent of the nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway.
Any process that increases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that increases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that increases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that increases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that increases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that increases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that increases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
Any process that modulates the rate, frequency, or extent of the process of immune complex clearance by monocytes or macrophages.
Any process that increases the rate, frequency, or extent of the process of immune complex clearance by monocytes or macrophages.
Any process that modulates the rate, frequency, or extent of the mitotic cell cycle spindle assembly checkpoint, a cell cycle checkpoint that delays the metaphase/anaphase transition of a mitotic nuclear division until the spindle is correctly assembled and chromosomes are attached to the spindle.
Any process that increases the rate, frequency, or extent of the mitotic cell cycle spindle assembly checkpoint, a cell cycle checkpoint that delays the metaphase/anaphase transition of a mitotic nuclear division until the spindle is correctly assembled and chromosomes are attached to the spindle.
Any process that starts the inactive process of a mitotic cell cycle spindle assembly checkpoint.
The appearance of a fibroblast growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
Any process that modulates the rate, frequency or extent of the appearance of a fibroblast growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
Any process that increases the rate, frequency or extent of the appearance of a fibroblast growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
Any process that decreases the rate, frequency or extent of the appearance of a fibroblast growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
Any process that modulates the rate, frequency, extent of the regulated release of somatostatin from secretory granules in the D cells of the pancreas.
Any process that increases the rate, frequency, extent of the regulated release of somatostatin from secretory granules in the D cells of the pancreas.
Any process that decreases the rate, frequency, extent of the regulated release of somatostatin from secretory granules in the D cells of the pancreas.
Any process that modulates the rate, frequency, or extent of the regulated release of a peptide hormone from secretory granules.
Any process that increases the rate, frequency, or extent of the regulated release of a peptide hormone from secretory granules.
Any process that decreases the rate, frequency, or extent of the regulated release of a peptide hormone from secretory granules.
Any process that modulates the rate, frequency, or extent of the directed movement of calcium ions into a cell or organelle.
Any process that increases the rate, frequency, or extent of the directed movement of calcium ions into a cell or organelle.
Any process that decreases the rate, frequency, or extent of the directed movement of calcium ions into a cell or organelle.
Any process that activates or increases the frequency, rate or extent of transcription of target genes that are transcribed as part of the G2/M transition of the mitotic cell cycle.
Any process that activates or increases the frequency, rate or extent of transcription of target genes that are transcribed as part of the G2/M transition of the mitotic cell cycle.
Any process that activates or increases the frequency, rate or extent of transcription of target genes that are transcribed as part of the G2/M transition of the mitotic cell cycle.
Any process that activates or increases the frequency, rate or extent of transcription of target genes that are transcribed as part of the G2/M transition of the mitotic cell cycle.
Any process that activates or increases the frequency, rate or extent of transcription of target genes that are transcribed as part of the G2/M transition of the mitotic cell cycle.
Any process that activates or increases the frequency, rate or extent of transcription of target genes that are transcribed as part of the G2/M transition of the mitotic cell cycle.
Any process that activates or increases the frequency, rate or extent of transcription of target genes that are transcribed as part of the G2/M transition of the mitotic cell cycle.
Any process that activates or increases the frequency, rate or extent of transcription of target genes that are transcribed as part of the G2/M transition of the mitotic cell cycle.
Any process that modulates the rate, frequency, or extent of the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid in any compartment of the Golgi apparatus.
Any process that increases the rate, frequency, or extent of the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid in any compartment of the Golgi apparatus.
Any process that decreases the rate, frequency, or extent of the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid in any compartment of the Golgi apparatus.
The process in which cytoskeletal filaments are directly or indirectly linked to the nuclear membrane.
Any process that modulates the rate, frequency, or extent of a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a growth factor stimulus.
Any process that decreases the rate, frequency, or extent of a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a growth factor stimulus.
Any process that modulates the rate, frequency, or extent of the multiplication or reproduction of osteoclasts, resulting in the expansion of an osteoclast cell population.
Any process that increases the rate, frequency, or extent of the multiplication or reproduction of osteoclasts, resulting in the expansion of an osteoclast cell population.
Any process that decreases the rate, frequency, or extent of the multiplication or reproduction of osteoclasts, resulting in the expansion of an osteoclast cell population.
The process in which the nuclear matrix, the dense fibrillar network lying on the inner side of the nuclear membrane, is directly or indirectly linked to the nuclear membrane.
A transcription regulation process in which the presence of one nitrogen source leads to the modulation of the frequency, rate, or extent of transcription of specific genes involved in the metabolism of other nitrogen sources.
A transcription regulation process in which the presence of one nitrogen source leads to an increase in the frequency, rate, or extent of transcription of specific genes involved in the metabolism of other nitrogen sources.
A transcription regulation process in which the presence of one nitrogen source leads to a decrease in the frequency, rate, or extent of transcription of specific genes involved in the metabolism of other nitrogen sources.
A transcription regulation process in which the presence of one nitrogen source leads to a decrease in the frequency, rate, or extent of transcription of specific genes involved in the metabolism of other nitrogen sources.
Any process that modulates the rate, frequency or extent of the process in which new strands of DNA are synthesized in the mitochondrion.
Any process that increases the rate, frequency or extent of the process in which new strands of DNA are synthesized in the mitochondrion.
Any process that decreases the rate, frequency or extent of the process in which new strands of DNA are synthesized in the mitochondrion.
Any process that modulates the rate, frequency, or extent of neural crest formation. Neural crest formation is the formation of the specialized region of ectoderm between the neural ectoderm (neural plate) and non-neural ectoderm. The neural crest gives rise to the neural crest cells that migrate away from this region as neural tube formation proceeds.
Any process that increases the rate, frequency, or extent of neural crest formation. Neural crest formation is the formation of the specialized region of ectoderm between the neural ectoderm (neural plate) and non-neural ectoderm. The neural crest gives rise to the neural crest cells that migrate away from this region as neural tube formation procedes.
Any process that decreases the rate, frequency, or extent of neural crest formation. Neural crest formation is the formation of the specialized region of ectoderm between the neural ectoderm (neural plate) and non-neural ectoderm. The neural crest gives rise to the neural crest cells that migrate away from this region as neural tube formation procedes.
Any process that increases the rate, frequency, or extent of the series of events that restore integrity to a damaged tissue, following an injury.
Any cellular metabolic process involving nucleic acids.
The nucleic acid metabolic process in which the phosphodiester bonds between nucleotides are cleaved by hydrolysis.
The aggregation, arrangement and bonding together of a set of components to form the spindle that contributes to the process of meiosis.
The aggregation, arrangement and bonding together of a set of components to form the spindle that contributes to the process of mitosis.
Any process that modulates the rate, frequency, or extent of the repression of transcription by methylation of DNA, leading to the formation of heterochromatin.
Any process that increases the rate, frequency, or extent of the repression of transcription by methylation of DNA, leading to the formation of heterochromatin.
Any process that decreases the rate, frequency, or extent of the repression of transcription by methylation of DNA, leading to the formation of heterochromatin.
Any process that modulates the rate, frequency, or extent of protein deacetylation, the removal of an acetyl group from a protein amino acid. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid.
Any process that increases the rate, frequency, or extent of protein deacetylation, the removal of an acetyl group from a protein amino acid. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid.
Any process that modulates the frequency, rate or extent of the process of directing proteins towards a membrane, usually using signals contained within the protein.
Any process that increases the frequency, rate or extent of the process of directing proteins towards a membrane, usually using signals contained within the protein.
Any process that decreases the frequency, rate or extent of the process of directing proteins towards a membrane, usually using signals contained within the protein.
Any process that activates or increases the frequency, rate or extent of the directed movement of proteins within cells.
Any process that decreases the frequency, rate or extent of the directed movement of proteins within cells.
Any process that modulates the rate, frequency, or extent of chylomicron remodeling. Chylomicron remodeling is the acquisition, loss or modification of a protein or lipid within a chylomicron, including the hydrolysis of triglyceride by lipoprotein lipase and the subsequent loss of free fatty acid.
Any process that increases the rate, frequency, or extent of chylomicron remodeling. Chylomicron remodeling is the acquisition, loss or modification of a protein or lipid within a chylomicron, including the hydrolysis of triglyceride by lipoprotein lipase and the subsequent loss of free fatty acid.
Any process that modulates the rate, frequency or extent of chylomicron remnant clearance. Chylomicron clearance is the process in which a chylomicron remnant is removed from the blood via receptor-mediated endocytosis into liver cells and its constituent parts degraded.
Any process that increases the rate, frequency or extent of chylomicron remnant clearance. Chylomicron clearance is the process in which a chylomicron remnant is removed from the blood via receptor-mediated endocytosis into liver cells and its constituent parts degraded.
Any process that modulates the rate, frequency, or extent of superoxide metabolism, the chemical reactions and pathways involving superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species.
The regulated release of a prostaglandin that contributes to the immune response. Prostaglandins are a group of biologically active metabolites which contain a cyclopentane ring.
Any process that decreases the frequency, rate or extent of the chemical reactions and pathways resulting in the phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.
Any process that modulates the frequency, rate, or extent of the 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.
Any process that increases the frequency, rate, or extent of the 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.
Any process that decreases the frequency, rate, or extent of the 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.
Any process that modulates the rate, frequency, or extent of olfactory learning. Olfactory learning is any process in an organism in which a relatively long-lasting adaptive behavioral change occurs in response to (repeated) exposure to an olfactory cue.
Any process that modulates the rate, frequency, or extent of DNA-dependent DNA replication, the process in which new strands of DNA are synthesized, using parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
Any process that modulates the rate, frequency or extent of platelet aggregation. Platelet aggregation is the adhesion of one platelet to one or more other platelets via adhesion molecules.
Any process that decreases the rate, frequency or extent of platelet aggregation. Platelet aggregation is the adhesion of one platelet to one or more other platelets via adhesion molecules.
The process of closing of stomata, pores in the epidermis of leaves and stems bordered by two guard cells and serving in gas exchange.
Any process that modulates the rate, frequency, or extent of stomatal closure. Stomatal closure is the process of closing of stomata, pores in the epidermis of leaves and stems bordered by two guard cells and serving in gas exchange.
Any process that modulates the rate, frequency, or extent of the chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
Any process that modulates the rate, frequency, or extent of the chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds, found in the walls of cells.
Any process that modulates the rate, frequency, or extent of brown fat cell differentiation. Brown fat cell differentiation is the process in which a relatively unspecialized cell acquires specialized features of a brown adipocyte, an animal connective tissue cell involved in adaptive thermogenesis. Brown adipocytes contain multiple small droplets of triglycerides and a high number of mitochondria.
Any process that increases the rate, frequency, or extent of brown fat cell differentiation. Brown fat cell differentiation is the process in which a relatively unspecialized cell acquires specialized features of a brown adipocyte, an animal connective tissue cell involved in adaptive thermogenesis. Brown adipocytes contain multiple small droplets of triglycerides and a high number of mitochondria.
Any process that modulates the rate, frequency, or extent of formin-nucleated actin cable assembly. Formin-nucleated actin cable assembly is the aggregation, arrangement and bonding together of a set of components to form a formin-nucleated actin cable. A formin-nucleated actin cable is an actin filament bundle that consists of short filaments organized into bundles of uniform polarity, and is nucleated by formins.
Any process that increases the rate, frequency, or extent of formin-nucleated actin cable assembly. Formin-nucleated actin cable assembly is the aggregation, arrangement and bonding together of a set of components to form a formin-nucleated actin cable. A formin-nucleated actin cable is an actin filament bundle that consists of short filaments organized into bundles of uniform polarity, and is nucleated by formins.
Any process that decreases the rate, frequency, or extent of formin-nucleated actin cable assembly. Formin-nucleated actin cable assembly is the aggregation, arrangement and bonding together of a set of components to form a formin-nucleated actin cable. A formin-nucleated actin cable is an actin filament bundle that consists of short filaments organized into bundles of uniform polarity, and is nucleated by formins.
Any process that increases the rate, frequency or extent of secretion of lysosomal enzymes, the controlled release of lysosomal enzymes by a cell.
Any process that decreases the rate, frequency or extent of secretion of lysosomal enzymes, the controlled release of lysosomal enzymes by a cell.
Any process that modulates the rate, frequency, or extent of cell aging. Cell aging is the progression of the cell from its inception to the end of its lifespan.
Any process that increases the rate, frequency, or extent of cell aging. Cell aging is the progression of the cell from its inception to the end of its lifespan.
Any process that decreases the rate, frequency, or extent of cell aging. Cell aging is the progression of the cell from its inception to the end of its lifespan.
The chemical reactions and pathways involving organohalogen compounds, as carried out by individual cells.
The chemical reactions and pathways involving organofluorine compounds, as carried out by individual cells.
Any process that modulates the rate, frequency or extent of the chemical reactions and pathways involving organohalogen compounds, as carried out by individual cells.
Any process that modulates the rate, frequency or extent of the chemical reactions and pathways involving organofluorine compounds, as carried out by individual cells.
Any process that decreases the rate, frequency or extent of the chemical reactions and pathways involving organohalogen compounds, as carried out by individual cells.
Any process that decreases the rate, frequency or extent of the chemical reactions and pathways involving organofluorine compounds, as carried out by individual cells.
The process whose specific outcome is the progression of the seedling over time, beginning with seed germination and ending when the first adult leaves emerge.
Any process that modulates the rate, frequency, or extent of the uptake, from the environment, of nitrates, inorganic or organic salts and esters of nitric acid and the subsequent reduction of nitrate ion to other, less highly oxidized, inorganic nitrogenous substances.
Stops, prevents or reduces the activity of a polygalacturonase. Polygalacturonases catalyze the random hydrolysis of 1,4-alpha-D-galactosiduronic linkages in pectate and other galacturonans.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving auxins, plant hormones that regulate aspects of plant growth.
Any process that increases the frequency, rate or extent of the chemical reactions and pathways involving auxins, plant hormones that regulate aspects of plant growth.
Any process that decreases the frequency, rate or extent of the chemical reactions and pathways involving auxins, plant hormones that regulate aspects of plant growth.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid.
Any process that increases the frequency, rate or extent of the chemical reactions and pathways involving tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid.
Any process that decreases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of abscisic acid.
The appearance of any platelet-derived growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
Any process that modulates the rate, frequency, or extent of the appearance of any platelet-derived growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
Any process that increases the rate, frequency, or extent of the appearance of any platelet-derived growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
Any process that modulates the rate, frequency, or extent of the aggregation, arrangement and bonding together of a mature, active 20S proteasome core particle complex that does not contain any regulatory particles.
Any process that modulates the rate, frequency, or extent of the aggregation, arrangement and bonding together of a mature, active proteasome complex.
Any process that modulates the rate, frequency, or extent of the covalent alteration of one or more nucleotides within an mRNA molecule to produce an mRNA molecule with a sequence that differs from that coded genetically.
Any process that increases the rate, frequency, or extent of the covalent alteration of one or more nucleotides within an mRNA molecule to produce an mRNA molecule with a sequence that differs from that coded genetically.
Any process that decreases the rate, frequency, or extent of the covalent alteration of one or more nucleotides within an mRNA molecule to produce an mRNA molecule with a sequence that differs from that coded genetically.
Any process that modulates the rate, frequency, or extent of the chemical reactions and pathways involving ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.
Stops, prevents, or reduces ornithine carbamoyltransferase activity, the catalysis of the reaction: carbamoyl phosphate + L-ornithine = phosphate + L-citrulline.
Any process that decreases the frequency, rate or extent of cholesterol efflux. Cholesterol efflux is the directed movement of cholesterol, cholest-5-en-3-beta-ol, out of a cell or organelle.
Any process that modulates the rate, frequency, or extent of the directed movement of glycerol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that increases the rate, frequency, or extent of the directed movement of glycerol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
Any process that decreases the rate, frequency, or extent of the directed movement of glycerol into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
The process in which an oligopeptide is transported out of the mitochondrial matrix. Oligopeptides are molecules that contain a small number (2 to 20) of amino-acid residues connected by peptide linkages.
Any process that decreases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of deprivation of iron ions.
The process in which a relatively unspecialized epidermal cell acquires the specialized features of a seed trichome. A seed trichome is a trichome that develops from seed coat epidermis and is often long with putative dispersal function.
The process in which a relatively unspecialized epidermal cell acquires the specialized features of a seed trichome. A seed trichome is a trichome that develops from seed coat epidermis and is often long with putative dispersal function.
The process in which a relatively unspecialized epidermal cell acquires the specialized features of a seed trichome. A seed trichome is a trichome that develops from seed coat epidermis and is often long with putative dispersal function.
The process in which the developmental fate of an epidermal cell becomes restricted such that it will develop into a seed trichome, causing a change in the orientation of cell division in the ovule epidermis at or just before anthesis.
The process in which a seed trichome irreversibly increases in size in one [spatial] dimension or along one axis, resulting in the morphogenesis of the cell.
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of inextensible cellulose- and pectin-containing cell walls that are formed between the plasma membrane and primary cell wall of seed trichomes after cell expansion is complete.
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of inextensible cellulose- and pectin-containing cell walls that are formed between the plasma membrane and primary cell wall of seed trichomes after cell expansion is complete.
A developmental process, independent of morphogenetic (shape) change, that is required for a seed trichome to attain its fully functional state.
Any process that modulates the rate, frequency, or extent of heart induction. Heart induction is the close range interaction between mesoderm and endoderm or ectoderm that causes cells to change their fates and specify the development of the heart.
A process that is carried out at the cellular level which results in the arrangement of constituent parts of a phagosome within a cell. Phagosome maturation begins with endocytosis and formation of the early phagosome and ends with the formation of the hybrid organelle, the phagolysosome.
Any process that reduces the pH of the phagosome, measured by the concentration of the hydrogen ion.
The initial attachment of a phagosome membrane to a lysosome membrane. Docking requires only that the proteins come close enough to interact and adhere.
The creation of a phagolysosome from a phagosome and a lysosome.
A process that is carried out at the cellular level which results in the arrangement of constituent parts of a phagosome within a cell and contributes to apoptotic cell clearance. Phagosome maturation begins with endocytosis and formation of the early phagosome and ends with the formation of the hybrid organelle, the phagolysosome.
The process in which a phagosome, a vesicle formed by phagocytosis, fuses with a lysosome as a part of apoptotic cell clearance.
The initial attachment of a phagosome membrane to a lysosome membrane that occurs as a part of apoptotic cell clearance. Docking requires only that the proteins come close enough to interact and adhere.
The creation of a phagolysosome from a phagosome and a lysosome as a part of apoptotic cell clearance.
Any process that reduces the pH of the phagosome, measured by the concentration of the hydrogen ion, and occurs as a part of apoptotic cell clearance.
A process that is carried out at the cellular level which results in the assembly of a granum. A granum is a distinct stack of lamellae seen within chloroplasts.
The process in which a relatively unspecialized cell acquires specialized features of a sepal giant cell. A sepal giant cell is a pavement cell that is part of the sepal epidermis and stretches one fifth the length of the sepal with a chromosome content of 16C.
The process aimed at the progression of a sepal giant cell over time, from initial commitment of the cell to a specific fate, to the fully functional differentiated cell.
Any process that prevents the establishment or decreases the extent of the excitatory postsynaptic potential (EPSP) which is a temporary increase in postsynaptic potential due to the flow of positively charged ions into the postsynaptic cell. The flow of ions that causes an EPSP is an excitatory postsynaptic current (EPSC) and makes it easier for the neuron to fire an action potential.
Any process that prevents the establishment or decreases the extent of the excitatory postsynaptic potential (EPSP) which is a temporary increase in postsynaptic potential due to the flow of positively charged ions into the postsynaptic cell. The flow of ions that causes an EPSP is an excitatory postsynaptic current (EPSC) and makes it easier for the neuron to fire an action potential.
Any process that prevents the establishment or decreases the extent of the excitatory postsynaptic potential (EPSP) which is a temporary increase in postsynaptic potential due to the flow of positively charged ions into the postsynaptic cell. The flow of ions that causes an EPSP is an excitatory postsynaptic current (EPSC) and makes it easier for the neuron to fire an action potential.
A cell projection that is a short, rounded projection from a plant epidermal cell.
A plant cell papilla that is part of a leaf papilla cell.
A plant cell papilla that is part of a stigma papilla cell.
A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest.
A cell aging process associated with the dismantling of a cell as a response to telomere shortening and/or cellular aging.
A cellular senescence process associated with the dismantling of a cell as a response to environmental factors such as hydrogen peroxide or X-rays.
A cellular senescence process associated with the dismantling of a cell as a response to oncogenic stress, such as the activation of the Ras oncogenic family.
A cellular senescence process associated with the dismantling of a cell as a response to oxidative stress, e.g. high levels of reactive oxygen species, such as superoxide anions, hydrogen peroxide, and hydroxyl radicals.
The region at growing end of the pollen tube cell, where polarized growth occurs.
A cell projection part that is a branch of a unicellular trichome.
A tubular cell projection that is part of a pollen tube cell and extends from a pollen grain.
The chemical reactions and pathways resulting in the biosynthesis of deoxyribose phosphate, the phosphorylated sugar 2-deoxy-erythro-pentose.
The process of loading nitrate into the sieve tube or companion cell of the phloem for long distance transport from source to sink.
Catalysis of the reaction: malonate + ATP + coenzyme A = malonyl-CoA + AMP + diphosphate.
The chemical reactions and pathways resulting in the breakdown of malonate, the propanedioate ion.
Interacting selectively and non-covalently with a brassinosteroid.
The directed movement of molybdate ions out of the vacuole.
Catalysis of the reaction: 7-hydroxymethyl chlorophyll a + 2 reduced ferredoxin + 2 H+ chlorophyll a + 2 oxidized ferredoxin + H2O.
Enables the transfer of nicotinate from one side of a membrane to the other.
Enables the transfer of N-methylnicotinate from one side of a membrane to the other.
Any process that inhibits or decreases the frequency, rate or extent of transcription of target genes that are transcribed as part of the G2/M transition of the mitotic cell cycle.
Any process that inhibits or decreases the frequency, rate or extent of transcription of target genes that are transcribed as part of the G2/M transition of the mitotic cell cycle.
The chemical reactions and pathways involving naphthalene-containing compounds.
Initiation of a region of tissue in a plant embryo that is composed of one or more undifferentiated cells capable of undergoing mitosis and differentiation.
Enables the transfer of thiamine pyrophosphate a substance from one side of a membrane to the other.
Enables the transfer of thiamine pyrophosphate a substance from one side of a membrane to the other.
A phytochelatin metabolic process in which a metal is incorporated with phytochelatin to form a complex.
A phytochelatin metabolic process in which a metal is incorporated with phytochelatin to form a complex.
A phytochelatin metabolic process in which a metal and exogenous sulfur are incorporated with phytochelatin to form a complex.
A phytochelatin metabolic process in which a metal and exogenous sulfur are incorporated with phytochelatin to form a complex.
The epithelial cell differentiation process in which a relatively unspecialized cell acquires specialized features of an acinar cell, a secretory cell that is grouped together with other cells of the same type to form grape-shaped clusters known as acini.
A process of actin filament bundle distribution that results in the compaction of actin filaments.
Any process that starts the inactive process of meiosis.
The process whose specific outcome is the progression of the perianth over time, from its formation to the mature structure. The perianth is a collective phyllome structure composed of two or more petals, sepals, or tepals.
The series of events in which an endogenous biotic stimulus is received by a cell and converted into a molecular signal.
Catalysis of the reaction: caffeoyl-CoA + a saturated primary alcohol = an alkyl caffeate + CoA.
The chemical reactions and pathways resulting in the formation of ester derivatives of alkyl caffeate.
The chemical reactions and pathways resulting in the formation of ester derivatives of alkyl caffeate.
The chemical reactions and pathways resulting in the formation of ester derivatives of alkyl caffeate.
The chemical reactions and pathways resulting in the formation of ester derivatives of alkyl caffeate.
Catalysis of the reaction: ATP + myristic acid + CoA = AMP + diphosphate + myristoyl-CoA.
Catalysis of the reaction: ATP + palmitic acid + CoA = AMP + diphosphate + palmitoyl-CoA.
Catalysis of the reaction: ATP + oleic acid + CoA = AMP + diphosphate + oleoyl-CoA.
A process in which a protein is transported to, or maintained at, a location within a nuclear envelope.
The process whose specific outcome is the progression of an leaf pavement cell over time, from its formation to the mature structure. Cell development does not include the steps involved in committing a cell to a leaf pavement cell fate.
The process in which a relatively unspecialized cell acquires specialized features of a socket cell, a shoot epidermal cell that surrounds a trichome and provides its support.
Catalyzes the reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = camelliol C.
Catalyzes the reaction: a hydroxyacyl-CoA + 3 malonyl-CoA + 2 H+ = a hydroxylated tetraketide alpha-pyrone + 3 CO2 + 4 coenzyme A .
Enables the transfer of abscisic acid from one side of a membrane to the other.
The chemical reactions and pathways resulting in the formation of trehalose that occur as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
The chemical reactions and pathways resulting in the degradation of trehalose that occur as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
A conserved protein phosphatase type 2A complex which contains a protein phosphatase type 2A, a protein phosphatase regulatory subunit, a striatin, an FHA domain protein and other subunits (at least six proteins). In fission yeast this complex negatively regulate the septation initiation network at the spindle pole body.
A conserved protein phosphatase type 2A complex which contains a protein phosphatase type 2A, a protein phosphatase regulatory subunit, a striatin, an FHA domain protein and other subunits (at least six proteins). In fission yeast this complex negatively regulate the septation initiation network at the spindle pole body.
A conserved protein phosphatase type 2A complex which contains a protein phosphatase type 2A, a protein phosphatase regulatory subunit, a striatin, an FHA domain protein and other subunits (at least six proteins). In fission yeast this complex negatively regulate the septation initiation network at the spindle pole body.
A conserved protein phosphatase type 2A complex which contains a protein phosphatase type 2A, a protein phosphatase regulatory subunit, a striatin, an FHA domain protein and other subunits (at least six proteins). In fission yeast this complex negatively regulate the septation initiation network at the spindle pole body.
Any process that modulates the consistent predetermined time point at which a nematode larva progresses from an initial condition to a later condition and the rate at which this time point is reached.
Any process that modulates the consistent predetermined time point at which a nematode larva progresses from an initial condition to a later condition and increases the rate at which this time point is reached.
Any process that modulates the consistent predetermined time point at which a nematode larva progresses from an initial condition to a later condition and decreases the rate at which this time point is reached.
Catalysis of the reaction: an acyl-CoA + sn-glycerol 3-phosphate = CoA + a 2-acyl-sn-glycerol 3-phosphate.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: glucosinolate(out) + H+(out) = glucosinolate(in) + H+(in).
The process of loading glucosinolates into the sieve tube or companion cell of the phloem for long distance transport from source to sink.
The process in which boundaries between a cotyledon and the surrounding tissue are established and maintained.
The directed movement of lithium ions across a membrane.
The directed movement of lithium ions across a membrane.
The directed movement of aspartate into the vacuole across the vacuolar membrane.
The directed movement of glutamate into the vacuole across the vacuolar membrane.
The directed movement of ornithine into the vacuole across the vacuolar membrane.
Any process involved in the maintenance of an internal steady state of aspartate within an organism or cell.
Any process involved in the maintenance of an internal steady state of threonine within an organism or cell.
Any process involved in the maintenance of an internal steady state of glutamate within an organism or cell.
Any process involved in the maintenance of an internal steady state of ornithine within an organism or cell.
Any process involved in the maintenance of an internal steady state of lysine within an organism or cell.
Any process involved in the maintenance of an internal steady state of histidine within an organism or cell.
Any process involved in the maintenance of an internal steady state of arginine within an organism or cell.
The process in which the basal boundary between the stem and both vegetative and reproductive organs are established and maintained.
Catalysis of the reaction: 9,15,9'-tricis-zeta-carotene = 9,9'-dicis-zeta-carotene.
Any protein processing achieved by the cleavage of a peptide bond after two basic amino acids within a protein.
Any protein processing achieved by the cleavage of a peptide bond after a lysine-arginine amino acid residue combination within a protein.
Any protein processing achieved by the cleavage of a peptide bond after two consecutive arginine amino acid residues within a protein.
Any protein processing achieved by the cleavage of a peptide bond after two consecutive lysine amino acid residues within a protein.
The process in which a purine nucleotide-sugar is transported across a membrane.nPurine nucleotide-sugars are purine nucleotides in glycosidic linkage with a monosaccharide or monosaccharide derivative.
The process in which a purine nucleotide-sugar is transported across a membrane.nPurine nucleotide-sugars are purine nucleotides in glycosidic linkage with a monosaccharide or monosaccharide derivative.
The process in which a purine nucleotide-sugar is transported across a membrane.nPurine nucleotide-sugars are purine nucleotides in glycosidic linkage with a monosaccharide or monosaccharide derivative.
The process in which a pyrimidine nucleotide-sugar is transported across a membrane.nPyrimidine nucleotide-sugars are pyrimidine nucleotides in glycosidic linkage with a monosaccharide or monosaccharide derivative.
The process in which a pyrimidine nucleotide-sugar is transported across a membrane.nPyrimidine nucleotide-sugars are pyrimidine nucleotides in glycosidic linkage with a monosaccharide or monosaccharide derivative.
The process in which a pyrimidine nucleotide-sugar is transported across a membrane.nPyrimidine nucleotide-sugars are pyrimidine nucleotides in glycosidic linkage with a monosaccharide or monosaccharide derivative.
Catalysis of the reaction: phosphatidylglycerol + phosphatidylethanolamine = cardiolipin + ethanolamine.
Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to the oxygen atom of a nucleoside residue in a small RNA molecule. Reaction: S-adenosyl-L-methionine + small RNA <=> S-adenosyl-L-homocysteine + small RNA containing a 3'-terminal 2'-O-methylnucleotide.
The chemical reactions and pathways resulting in the breakdown of secondary metabolites, the compounds that are not necessarily required for growth and maintenance of cells, and are often unique to a taxon.
The chemical reactions and pathways resulting in the breakdown of secondary metabolites, the compounds that are not necessarily required for growth and maintenance of cells, and are often unique to a taxon.
The chemical reactions and pathways resulting in the breakdown of secondary metabolites, the compounds that are not necessarily required for growth and maintenance of cells, and are often unique to a taxon.
Interacting selectively and non-covalently with a polo box domain of a protein. The polo box domain is involved in binding substrates of polo kinases.
Catalyzes the multi-step reaction: L-Tryptophan + 2 Oxygen + 2 NADPH + 2 H+ = Indole-3-acetaldehyde oxime + 3 H2O + 2 NADP+ + CO2. The individual reactions are: (1a) L-tryptophan + O2 + NADPH + H+ = N-hydroxy-L-tryptophan + NADP+ + H2O,(1b) N-hydroxy-L-tryptophan + O2 + NADPH + H+ = N,N-dihydroxy-L-tryptophan + NADP+ + H2O, and (1c) N,N-dihydroxy-L-tryptophan = (E)-indol-3-ylacetaldoxime + CO2 + H2O.
Catalyzes the reaction: L-Tryptophan + Oxygen + NADPH + H+ = N-Hydroxy-L-tryptophan + NADP+ + H2O.
Catalyzes the reaction: N-Hydroxy-L-tryptophan + Oxygen + NADPH + H+ = N,N-Dihydroxy-L-tryptophan + NADP+ + H2O.
Catalyzes the reaction: N,N-Dihydroxy-L-tryptophan = Indole-3-acetaldehyde oxime + CO2 + H2O.
The directed movement of catecholamine into a cell.
The directed movement of dopamine into a cell.
The disaggregation of a low-density lipoprotein particle into its constituent components.
The migration of mesenchymal tissue that contributes to the formation of a limb bud.
The orderly movement of a mesenchymal cell from one site to another, often during the development of a multicellular organism.
The component of a Golgi membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
Catalysis of the reaction: pimelyl-[acyl-carrier protein] methyl ester + H2O = pimelyl-[acyl-carrier protein] + methanol.
A transition where an endocardial cushion cell loses apical/basolateral polarity, severs intercellular adhesive junctions, degrades basement membrane components and becomes a migratory mesenchymal cell.
The RNA metabolic process in which the phosphodiester bonds between ribonucleotides are cleaved by hydrolysis.
The chemical reactions and pathways involving the hydrolysis of internal 3',5'-phosphodiester bonds in one or two strands of ribonucleotides.
The chemical reactions and pathways involving the hydrolysis of terminal 3',5'-phosphodiester bonds in one or two strands of ribonucleotides.
The expansion of one cell sheet over other cells or yolk.
The expansion of one cell sheet over other cells involved in wound healing.
A developmental process that results in the initiation of an axillary shoot meristem. An axillary shoot meristem is a shoot meristem formed in the axil of a leaf.
The chemical reactions and pathways involving phenylethylamine that contribute to synaptic transmission.
The chemical reactions and pathways resulting in the formation of phenylethylamine that contribute to synaptic transmission.
A cell division process where the division plane is perpendicular to the surface of the organ. It adds cells to the existing cell layer or cell file.
A cell division process where the division plane is parallel to the surface of the organ. It creates a new cell layer or cell file.
A plasma membrane part that is composed of a furrow-like plasma membrane domain and associated integral transmembrane proteins.
The directed movement of L-histidine into the vacuole across the vacuolar membrane.
The directed movement of L-histidine into the vacuole across the vacuolar membrane.
The directed movement of L-histidine into the vacuole across the vacuolar membrane.
The directed movement of L-tyrosine into the vacuole across the vacuolar membrane.
The directed movement of L-glutamate into the vacuole across the vacuolar membrane.
The directed movement of L-serine into the vacuole across the vacuolar membrane.
The directed movement of L-lysine into the vacuole across the vacuolar membrane.
The directed movement of L-lysine into the vacuole across the vacuolar membrane.
The directed movement of L-lysine into the vacuole across the vacuolar membrane.
The directed movement of L-arginine into the vacuole across the vacuolar membrane.
The directed movement of L-arginine into the vacuole across the vacuolar membrane.
The directed movement of L-arginine into the vacuole across the vacuolar membrane.
Any process in which an organism or cell protects itself from anoxia, which may also result in resistance to repeated exposure to anoxia.
A series of molecular signals mediated by a sphingolipid.
A series of molecular signals mediated by a sphingolipid.
A series of molecular signals mediated by a sphingolipid.
A series of molecular signals mediated by a sphingolipid.
A series of molecular signals mediated by a sphingolipid.
A series of molecular signals mediated by a sphingolipid.
The orderly movement of a podocyte from one site to another, often during the development of a multicellular organism or multicellular structure. A podocyte is a specialized kidney epithelial cell.
The initial, indirect interaction between a secretory vesicle membrane and a site of exocytosis in the plasma membrane. This interaction is mediated by tethering factors (or complexes), which interact with both membranes. Interaction can occur via direct binding  to membrane phospholipids or membrane proteins, or via binding to vesicle coat proteins. This process is distinct from and prior to docking and fusion.
Catalysis of the reaction: NADPH + H+ + 2 ferricytochrome b(5) = NADP+ + 2 ferrocytochrome b(5).
Catalysis of the reaction: NADH + H+ + 2 ferricytochrome b(5) = NAD+ + 2 ferrocytochrome b(5).
A process that is carried out at the cellular level which results in dynamic structural changes to the arrangement of actin filaments.
The assembly of a smooth septate junction, a septate junction that lacks the regular arrays of electron-dense septae found in pleated septate junctions.
The assembly and arrangement of a cellular component that is composed of peptidoglycan and often chitin in addition to other materials and usually forms perpendicular to the long axis of a cell or hypha. It 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.
The assembly and arrangement of a cellular component that is composed of peptidoglycan and often chitin in addition to other materials and usually forms perpendicular to the long axis of a cell or hypha. It 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.
The chemical reactions and pathways resulting in the formation of L-ascorbic acid via the intermediate GDP-alpha-D-mannose.
The chemical reactions and pathways resulting in the formation of L-ascorbic acid via the intermediate GDP-alpha-D-mannose.
The chemical reactions and pathways resulting in the formation of L-ascorbic acid via the intermediate UDP-alpha-D-glucuronate.
Protein complex that carries out the reaction: ATP + H2O + cation(out) = ADP + phosphate + cation(in).
Protein complex that carries out the reaction: ATP + H2O + Ca2+(out) = ADP + phosphate + Ca2+(in).
An ISWI complex that contains an ATPase subunit of the ISWI family (specifically SNF2H in mammals, which contain two ISWI homologs) and WSTF (Williams Syndrome Transcription Factor). WICH plays roles in regulation of RNAP I and III transcription and in DNA replication and repair.
An ISWI complex that contains an ATPase subunit of the ISWI family (specifically SNF2H in mammals, which contain two ISWI homologs) and a Tip5 homolog. In mammals, NoRC is involved in regulation of transcription from RNAP I and RNA polymerase III promoters.
An ISWI complex that contains an ATPase subunit of the ISWI family (specifically SNF2L in mammals, which contain two ISWI homologs) and a CECR2 homolog. In mammals, CERF is involved in regulation of transcription from RNA polymerase II promoters.
The regulated release of a peptide pheromone from a cell.
The directed movement of a peptide pheromone across a membrane and out of a cell.
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, as it occurs in certain types of bacteria, mainly Acetobacter, Sarcina ventriculi and Agrobacteria.
Interacting selectively and non-covalently with the MIT domain of a protein. The MIT domain is found in vacuolar sorting proteins, spastin (probable ATPase involved in the assembly or function of nuclear protein complexes), and a sorting nexin, which may play a role in intracellular trafficking.
Interacting selectively and non-covalently with the ELYC domain of a protein. The ELYC domain is an approximately 150 amino acid sequence which contains a highly conserved tetrapeptide sequence, ELYC.
A cell part that is the central region of the midbody characterized by a gap in alpha-tubulin staining. It is a dense structure of antiparallel microtubules from the central spindle in the middle of the intercellular bridge.
A SWI/SNF-type complex that contains a subunit from the CHD(Chromodomain helicase DNA-binding) family. The CHD family is characterized by two signature sequence motifs: tandem chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein structure.
The process by which excess light energy absorbed by chlorophyll and not used to drive photosynthesis is re-emitted as light.
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 low humidity stimulus, reduced moisture in the atmosphere.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of nitrate.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of a carbon source.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of molybdenum.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of manganese.
A cell projection part that is the apical most portion of a unicellular trichome.
A cell projection part that is the apical most portion of a unicellular trichome apex.
Catalysis of the movement of phosphatidylcholine from one membrane bilayer leaflet to the other, driven by the hydrolysis of ATP.
Catalysis of the movement of phosphatidylethanolamine from one membrane bilayer leaflet to the other, driven by the hydrolysis of ATP.
Catalysis of the movement of phosphatidylserine from one membrane bilayer leaflet to the other, driven by the hydrolysis of ATP.
The establishment of a barrier between endothelial cell layers of the intestine to exert specific and selective control over the passage of water and solutes, thus allowing formation and maintenance of compartments that differ in fluid and solute composition.
The process whose specific outcome is the progression of the plant epidermis over time, from its formation to the mature structure.
Any process that modulates the frequency, rate or extent of the passage or uptake of molecules by a membrane.
Catalysis of the reaction S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] = S-methyl-5-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2].
The dynein-driven microtubule based nuclear migration, whereby daughter nuclei are positioned away from the cell division site prior to cytokinesis.
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,N'-diacetylchitobiose(out) = protein histidine + N,N'-diacetylchitobiose phosphate(in).
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein S-phosphocysteine + sugar(out) = protein cysteine + sugar 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 S-phosphocysteine + glucose(out) = protein cysteine + 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 S-phosphocysteine + mannitol(out) = protein cysteine + 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 S-phosphocysteine + N,N'-diacetylchitobiose(out) = protein cysteine + N,N'-diacetylchitobiose phosphate(in).
The process whose specific outcome is the progression of a reproductive shoot system over time, from its formation to the mature structure.
A protein complex, located in the nucleus, that possesses activity that prevents or downregulates transcription.
A protein complex, located in the cytoplasm, that possesses activity that prevents or downregulates transcription.
A protein complex, located in the nucleus, that possesses activity that prevents or downregulates transcription from a RNA polymerase I promoter.
A protein complex, located in the nucleus, that possesses activity that prevents or downregulates transcription from a RNA polymerase II promoter.
A protein complex, located in the nucleus, that possesses activity that prevents or downregulates transcription from a RNA polymerase III promoter.
A protein complex, located in the nucleus, that possesses activity that prevents or downregulates transcription from a RNA polymerase IV promoter.
A protein complex, located in the nucleus, that possesses activity that prevents or downregulates transcription from a RNA polymerase V promoter.
A transcription factor complex that acts at a regulatory region of a gene transcribed by RNA polymerase II.
A transcription factor complex that acts at a regulatory region of a gene transcribed by RNA polymerase III.
A transcription factor complex that acts at a regulatory region of a gene transcribed by RNA polymerase IV.
A transcription factor complex that acts at a regulatory region of a gene transcribed by RNA polymerase V.
The formation and maintenance of DNA loops that juxtapose separated regions on the same dsDNA molecule.
The formation and maintenance of DNA loops that juxtapose separated regions on the same dsDNA molecule.
Catalysis of the hydrolytic removal of phosphoglycolate from the 3'-terminus of a 3'-phosphoglycolate-terminated DNA strand.
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein S-phosphocysteine + mannosylglycerate(out) = protein cysteine + mannosylglycerate phosphate(in).
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein S-phosphocysteine + D-fructose(out) = protein cysteine + D-fructose-1-phosphate(in).
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein S-phosphocysteine + D-sorbitol(out) = protein cysteine + D-sorbitol-1-phosphate(in).
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein S-phosphocysteine + galactitol(out) = protein cysteine + galactitol-6-phosphate(in).
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein S-phosphocysteine + L-ascorbate(out) = protein cysteine + L-ascorbate-6-phosphate(in).
: Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein S-phosphocysteine + N-acetylglucosamine (out) = protein cysteine + N-acetylglucosamine-6-phosphate (in).
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein S-phosphocysteine + glucosamine (out) = protein cysteine + glucosamine-6-phosphate (in).
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein S-phosphocysteine + N-acetylmuramate (out) = protein cysteine + N-acetylmuramate-6-phosphate (in).
Catalysis of the PEP-dependent, phosphoryl transfer-driven transport of substances across a membrane. The transport happens by catalysis of the reaction: protein S-phosphocysteine + trehalose (out) = protein cysteine + trehalose-6-phosphate (in).
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 + D-glucosamine(out) = protein histidine + glucosamine-6-phosphate(in).
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-acetyl-mannosamine(out) = protein histidine +N-acetyl- mannosamine-6-phosphate(in).
Synthesis of DNA that is a part of the process of duplicating one or more molecules of DNA.
The phosphorylation by a protein of one or more of its own histidine residues, or a histidine residue on an identical protein.
The immediate defensive reaction by vertebrate tissue to injury caused by chemical or physical agents.
Catalysis of the reaction: L-lysine + acetyl-CoA = N6-acetyl-L-lysine + CoA + H(+).
Morphogenesis of a sensory organ. A sensory organ is defined as a tissue or set of tissues that work together to receive and transmit signals from external or internal stimuli. Morphogenesis is the process in which anatomical structures are generated and organized. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that work together to perform a specific function or functions.
The process in which the anatomical structures of the nematode male tail mating organ are generated and organized. The male tail is a sensory organ required for mating and, in C. elegans, consists of ray sensilla, an acellular cuticular fan, a sensory hook, and protracting, copulatory spicules.
The processes by which anatomical structures that are only present in the male organism are generated and organized.
Catalysis of the hydrolysis of terminal, non-reducing alpha-linked alpha-D-glucose residue with release of alpha-D-glucose.
Catalysis of the hydrolysis of terminal, non-reducing alpha-(1->3)-linked alpha-D-glucose residues with release of alpha-D-glucose.
The process in which nucleated precursor cells lose their nucleus.
The process in which nucleated precursor cells lose their nucleus as part of sieve element differentiation. The nuclear contents are released and degraded in the cytoplasm at the same time as other organelles are rearranged and the cytosol is degraded.
The process whereby a relatively unspecialized cell acquires specialized features of a sieve element.
A process in which planktonically growing microorganisms grow at the surface of a liquid-air interface and produce extracellular polymers that facilitate matrix formation, resulting in a change in the organisms' growth rate and gene transcription.
A process in which planktonically growing microorganisms aggregate and grow on solid substrates under the flow of a liquid and produce extracellular polymers that facilitate attachment and matrix formation, resulting in a change in the organisms' growth rate and gene transcription.
A process in which microorganisms produce an extracellular matrix and form multicellular aggregates at an air-liquid interface.
A process in which microorganisms produce an extracellular matrix and form multicellular aggregates at an air-liquid interface.
A process in which planktonically growing microorganisms of different species grow at the surface of a liquid-air interface and produce extracellular polymers that facilitate matrix formation, resulting in a change in the organisms' growth rate and gene transcription.
A process in which planktonically growing microorganisms of different species aggregate and grow on solid substrates under the flow of a liquid and produce extracellular polymers that facilitate attachment and matrix formation, resulting in a change in the organisms' growth rate and gene transcription.
A process in which planktonically growing microorganisms of the same species aggregate and grow on solid substrates under the flow of a liquid and produce extracellular polymers that facilitate attachment and matrix formation, resulting in a change in the organisms' growth rate and gene transcription.
The process in which a cell becomes capable of differentiating autonomously into a bundle sheath cell in an environment that is neutral with respect to the developmental pathway; upon specification, the cell fate can be reversed.
The chemical reactions and pathways resulting in the breakdown of a protein or peptide, via the multivesicular body (MVB) sorting pathway; proteins are sorted into MVBs, and delivered to a lysosome/vacuole for degradation.  This process is independent of ubiquitination.
Catalysis of the reaction: cyclic adenosine monophosphate + H2O = cyclic inosine monophosphate + NH3.
Catalysis of the reaction: 5'deoxyadenosine + H2O = 5'deoxyinosine + NH3.
Catalysis of the reaction: 5'methyl thioadenosine + H2O = 5'methyl thioinosine + NH3.
Steps involved in processing precursor RNAs arising from transcription of operons in the mitochondrial genome into mature mRNAs.
Any process involved in forming the mature 3' end of an mRNA molecule that derives from the mitochondrial genome.
Any process involved in forming the mature 5' end of an mRNA molecule that derives from the mitochondrial genome.
The process of removing the PCNA complex from DNA when Okazaki fragments are completed or the replication fork terminates.
Either of the ends of a meiotic spindle, a spindle that forms as part of meiosis, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.
Catalysis of the endonucleolytic cleavage of the mRNA in a double-stranded RNA molecule formed by the base pairing of an mRNA with an miRNA.
The process in which small interfering RNAs (siRNAs) direct the cleavage of target mRNAs. Once incorporated into a RNA-induced silencing complex (RISC), a siRNA will typically direct cleavage by base pairing with perfect or near-perfect complementarity to the target mRNA.
The process in which the anatomical structures of the plant epidermis are generated and organized.
The process in which a relatively unspecialized cell acquires specialized features of a plant epidermal cell.
The process in which a cell becomes capable of differentiating autonomously into a plant epidermal 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 synthesis of DNA from a template strand in a net 3' to 5' direction is started.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
Catalysis of the reaction: CTP + Neu5Gc = diphosphate + CMP-Neu5Gc.
Catalysis of the reaction: CTP + KDN = diphosphate + CMP-KDN.
Catalysis of the reaction: CTP + KDN = diphosphate + CMP-KDN.
The directed killing of a target cell by a microglial cell.
The desmosomal part containing the desmosomal cadherins, desmogleins and desmocollins, that establish contact and adhere to neighboring cells in a Ca2+-dependent manner.
The desmosomal part containing plakoglobins, plakophilins, the N-termini of desmoplakins,  as well as the cytoplasmic tails of the desmosomal cadherins, which together attach the plaque to the plasma membrane.
The desmosomal part containing the C-termini of desmoplakins which interact with the keratin intermediate filaments, serving to tether the intermediate filaments to the plasma membrane.
The phosphatidylcholine biosynthetic process that depends on direct conversion of the phosphatidyl-base phosphatidylethanolamine to phosphatidylcholine by successive methylations.
The phosphatidylcholine biosynthetic process that involves a one-step direct condensation of choline with CDP-diacylglycerol to form phosphatidylcholine.
The phosphatidylcholine biosynthetic process that involves the two-step acylation of sn-glycero-3-phosphocholine to a phosphatidylcholine.
The middle layer in a microsporidian spore wall that lies under the exospore and outside the plasma membrane, containing chitin and proteins.
The dense, protein rich outermost layer of a microsporidian spore wall that lies above the endospore.
The radial pattern formation process that results in the formation of flowers around a central axis in an inflorescence meristem.
An innate immune response that is positively correlated with host plant development. As a plant develops, its innate resistance to pathogenic infections increases. The mechanisms involved in age-related resistance differ in nature or in aspects of regulation from the hypersensitive response (HR), systemic acquired resistance (SAR), or induced systemic resistance (ISR).
An innate immune response that is positively correlated with host plant development. As a plant develops, its innate resistance to pathogenic infections increases. The mechanisms involved in age-related resistance differ in nature or in aspects of regulation from the hypersensitive response (HR), systemic acquired resistance (SAR), or induced systemic resistance (ISR).
An innate immune response that is positively correlated with host plant development. As a plant develops, its innate resistance to pathogenic infections increases. The mechanisms involved in age-related resistance differ in nature or in aspects of regulation from the hypersensitive response (HR), systemic acquired resistance (SAR), or induced systemic resistance (ISR).
An innate immune response that is positively correlated with host plant development. As a plant develops, its innate resistance to pathogenic infections increases. The mechanisms involved in age-related resistance differ in nature or in aspects of regulation from the hypersensitive response (HR), systemic acquired resistance (SAR), or induced systemic resistance (ISR).
An innate immune response that is positively correlated with host plant development. As a plant develops, its innate resistance to pathogenic infections increases. The mechanisms involved in age-related resistance differ in nature or in aspects of regulation from the hypersensitive response (HR), systemic acquired resistance (SAR), or induced systemic resistance (ISR).
An innate immune response that is positively correlated with host plant development. As a plant develops, its innate resistance to pathogenic infections increases. The mechanisms involved in age-related resistance differ in nature or in aspects of regulation from the hypersensitive response (HR), systemic acquired resistance (SAR), or induced systemic resistance (ISR).
An innate immune response that is positively correlated with host plant development. As a plant develops, its innate resistance to pathogenic infections increases. The mechanisms involved in age-related resistance differ in nature or in aspects of regulation from the hypersensitive response (HR), systemic acquired resistance (SAR), or induced systemic resistance (ISR).
The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group,  in the mitochondrion.
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 the provision of a combination of complex inanimate and social stimulations in the organism's housing environment.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of the deprivation of oxygen and glucose.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of the deprivation of oxygen and glucose.
The region of the cytoplasm located at the apical side of the cell. Used in reference to animal polarized epithelial cells.
The region of the cytoplasm located at the basolateral side of the cell. Used in reference to animal polarized epithelial cells.
Tubulo-vesicular structure located in the apical cytoplasm that participates in apical cargo recycling in polarized epithelial cells.
Tubulo-vesicular structure located in the basolateral cytoplasm that participates in basolateral cargo recycling in polarized epithelial cells.
Interacting selectively and non-covalently with the junction formed at the point where double-stranded telomeric DNA becomes a single-stranded G-rich telomeric DNA 3' overhang.
A telomere maintenance process that results in the formation of a telomeric circle, or t-circle. A t-circle is an extrachromosomal duplex or single-stranded circular DNA molecule composed of t-arrays. T-circles are involved in the control of telomere length via alternative-lengthening of telomeres (ALT) pathway and telomere rapid deletion (TRD).
The telomere maintenance process in which telomeric loops are disassembled to permit efficient telomere replication.
The telomere maintenance process in which telomeric loops are disassembled to permit efficient telomere replication.
A biochemically and structurally distinct domain of the retinal interphotoreceptor matrix that is specifically associated with cone photoreceptor cell inner and outer segments.
The behavior of an organism relating to the progression of that organism along the ground by the process of lifting and setting down each leg.
The neurological system process driven by motile cilia on ependymal cells of the brain by which cerebrospinal fluid circulates from the sites of secretion to the sites of absorption. In ventricular cavities, the flow is unidirectional and rostrocaudal, in subarachnoid spaces, the flow is multi-directional.
The neurological system process driven by motile cilia on ependymal cells of the brain by which cerebrospinal fluid circulates from the sites of secretion to the sites of absorption. In ventricular cavities, the flow is unidirectional and rostrocaudal, in subarachnoid spaces, the flow is multi-directional.
The neurological system process driven by motile cilia on ependymal cells of the brain by which cerebrospinal fluid circulates from the sites of secretion to the sites of absorption. In ventricular cavities, the flow is unidirectional and rostrocaudal, in subarachnoid spaces, the flow is multi-directional.
A box H/ACA ribonucleoprotein complex that contains the RNA component of vertebrate telomerase, the enzyme essential for the replication of chromosome termini in most eukaryotes. This ribonucleoprotein complex is a structural box H/ACA RNP, which does not have the catalytic pseudouridylation function shared by the majority of H/ACA RNPs present in the cell.
The transport of molecules across a membrane and against an electrochemical gradient, using energy from ATP hydrolysis.
The series of molecular signals generated as a consequence of the peptide neurotransmitter galanin binding to a cell surface receptor.
The series of molecular signals generated as a consequence of the peptide neurotransmitter galanin binding to a cell surface receptor.
The series of molecular signals generated as a consequence of the peptide neurotransmitter galanin binding to a cell surface receptor.
Any process that results in a change in state or activity of a cell or a multicellular organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a higher than normal number of multicellular organisms living per unit area.
A protein complex containing at least one glycosylated protein, may be held together by both covalent and noncovalent bonds.
A process in which a small Cajal body-specific RNA is transported to, or maintained in, a Cajal body.
The directed movement of a motile cell in response to the presence of vascular endothelial growth factor (VEGF).
The directed movement of an endothelial cell in response to the presence of vascular endothelial growth factor (VEGF).
Prevention of degradation of telomerase RNA (TERC) molecules.
A process in which an RNA is transported to, or maintained in, a Cajal body.
A process in which telomerase RNA (TERC) is transported to, or maintained in, a Cajal body.
Any process in which telomerase RNA is transported to, or maintained in, a specific location.
The binding of an endothelial cell to the extracellular matrix via adhesion molecules.
The binding of an endothelial cell to the extracellular matrix via fibronectin.
The biological adhesion process by which adjacent microvilli attach to each other through Ca(2+)-dependent adhesion links made of protocadherin-24 and mucin-like protocadherin.
A process in which a calcium ion is transported from one side of a membrane to the other by means of a low voltage-gated calcium channel.
A phenotypic switching process where a cell reversibly differentiates and dedifferentiates from one cell type into another.
A cell dedifferentiation process that is a part of a reversible switch of a cell from one cell type or form to another, at a frequency above the expected frequency for somatic mutations.
A cell differentiation process that is a part of a reversible switch of a cell from one cell type or form to another, at a frequency above the expected frequency for somatic mutations.
A process by which a virus has a negative effect on the functioning of a host outer membrane.
A G protein-coupled receptor activity that is responsible for the sense of taste.
A G protein-coupled receptor activity that is responsible for the sense of taste.
A G protein-coupled receptor activity that is responsible for the sense of bitter taste.
A G protein-coupled receptor activity that is responsible for the sense of bitter taste.
A G protein-coupled receptor activity that is responsible for the sense of sweet taste.
A non-GPCR transmembrane signaling receptor activity that is responsible for contact chemoreception.
A macromolecular localization process in which RNA is transported to and maintained in a location within the nucleus.
Enables the transmembrane transfer of a monovalent cation by a channel that opens when glycine betaine has been bound by the channel complex or one of its constituent parts.
Any process that starts the inactive process of a meiosis I cell cycle spindle assembly checkpoint.
The part of the cleavage furrow closest to the cell surface.
The 'trough' of the cleavage furrow. This is the part of the cleavage furrow closest to the contractile ring.
The regionalization process that specifies plant organ primordium boundaries resulting in a restriction of organogenesis to a limited spatial domain and keeping the organ separate from surrounding tissues.
The site on the mitochondrial membrane where the separation of a single continuous mitochondrial membrane into two membranes occurs as a final step in mitochondrial fission.
The process that occurs in a plant organ near the end of its active life that is associated with the dismantling of cell components and membranes, and an overall decline in metabolism.
A eukaryotically conserved heterodimeric protein complex (comprising adherin and the chromatid cohesion factor MAU2/Scc4/Ssl3) required for the loading of a cohesin, complex onto DNA.
A eukaryotically conserved heterodimeric protein complex (comprising Wings apart-like protein and the Pds5 Armadillo repeat cohesin associated protein) involved in the loading and unloading of a cohesin complex onto DNA.
Development, taking place during the post-embryonic phase of a plant tissue or tissues that work together to perform a specific function or functions. Development pertains to the process whose specific outcome is the progression of a structure over time, from its formation to the mature structure. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that work together to perform a specific function or functions.
Morphogenesis, during the post-embryonic phase, of a plant tissue or tissues that work together to perform a specific function or functions. Morphogenesis pertains to process in which anatomical structures are generated and organized. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that work together to perform a specific function or functions.
The process, occurring after plant embryonic development, by which anatomical structures are generated and organized.
The cell cycle process that corrects the anomalous association of a single chromatid kinetochore with mitotic spindle microtubules emanating from both spindle poles at meiosis I, and would, if uncorrected result in the separation of sister chromatids at meiosis I.
The process in which the identity of a plant organ is maintained. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
The regionalization process in which the identity of a plant organ primordium is specified. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
The process whose specific outcome is the progression of a non-reproductive fruiting body over time, from its formation to the mature structure. A non-reproductive fruiting body is a colonial multicellular structure consisting of co-operating unicellular organisms, some of which are  spores. An example of such a process is found in Dictyostelium discoideum and Myxococcus xanthus colonies.
Catalysis of the reaction: nicotinate + UDP-D-glucose = O-D-glucosylnicotinate + UDP.
A plant cell papilla that is part of a trichome cell.
The regionalization process in which information that determines the correct position at which plant organ primordia are formed is generated and perceived resulting in correct positioning of the new plant organ.
The process that determines the orientation of a plant organ or tissue with reference to an axis.
The process in which the polarity of a plant organ axis is specified.
Any process that modulates the rate, frequency or extent of plant organ formation at a consistent predetermined time point during development.
Catalysis of the reaction: ATP + (R)-mevalonate 5-phosphate = ADP + isopentenyl phosphate + CO2 + phosphate.
Catalysis of the reaction: FMN + H2O = riboflavin + phosphate.
The end of the outer hair cell which receives and transmits neural signals.
Any process of the immune system that can contribute to the formation of immunological memory or an immune response based upon activation of immunological memory.
An immune response mediated by the innate immune system and directed against a previously encountered immunologic stimulus, being quicker and quantitatively better compared with the initial response to that stimulus.
Any immunological memory process that can contribute to the formation of immunological memory.
An immune response directed against a previously encountered antigen, being quicker and quantitatively better compared with the primary response.
An immune response mediated by reactivated memory T cells and B cells and directed against a previously encountered antigen, being quicker and quantitatively better compared with the primary response.
An adaptive immune response that involves one or more immune effector processes and takes place during the effector phase of the adaptive immune response.
An adaptive immune effector response involving T cells and B lineage cells. In the case of B lineage cells, the effector cells are the antibody secreting plasma cells whereas for T cells the effector cells may be helper T cells or cytotoxic T cells.
An adaptive immune response against an antigen not previously encountered by immune system.
An adaptive immune response mediated by naive T or B cells against an antigen not previously encountered by immune system.
The aggregation, arrangement and bonding together of two or more different receptor complexes that individually undergo combination with a hormone, neurotransmitter, drug or intracellular messenger to form a higher level receptor complex. The formation of the higher level complex initiates a change in cell function.
Any constituent part of a growth cone, the migrating motile tip of a growing nerve cell axon or dendrite.
The center of the migrating motile tip of a growing nerve cell axon or dendrite.
The non-central region or periphery of the migrating motile tip of a growing nerve cell axon or dendrite.
A region of the cell cortex that contains a higher concentration of growth polarity factors than the surrounding cortex and that changes position over time. An example is found in fission yeast cells during early mating, in which the GTPase Cdc42 dynamically to discrete zones within the cortex prior to shmoo formation.
Any process that increases brood size. Brood size is the number of progeny that survive embryogenesis and are cared for at one time.
Any process that decreases brood size. Brood size is the number of progeny that survive embryogenesis and are cared for at one time.
A four subunit complex, that comprises all the necessary RNA processing enzymes (endonuclease, polynucleotide kinase, and exonuclease) to mediate 'cistronic rRNA transcript ITS2 (internal transcribed spacer) cleavage' (GO:0000448).
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 very-low-density lipoprotein particle stimulus.
A cellular structure consisting of parallel, hexagonally arranged actin tubules, comprising filamentous actin and disulfide cross-linked cofilin multimers.
A extracellular matrix complex involved in cell adhesion and cell migration. Typically homotrimeric or homohexameric. In mammals, four complexes exist: Tenascin-C, Tenascin-N (also known as Tenascin-W), Tenascin-X and Tenascin-R.
A extracellular matrix complex involved in cell adhesion and cell migration. Typically homotrimeric or homohexameric. In mammals, four complexes exist: Tenascin-C, Tenascin-N (also known as Tenascin-W), Tenascin-X and Tenascin-R.
A extracellular matrix complex involved in cell adhesion and cell migration. Typically homotrimeric or homohexameric. In mammals, four complexes exist: Tenascin-C, Tenascin-N (also known as Tenascin-W), Tenascin-X and Tenascin-R.
A extracellular matrix complex involved in cell adhesion and cell migration. Typically homotrimeric or homohexameric. In mammals, four complexes exist: Tenascin-C, Tenascin-N (also known as Tenascin-W), Tenascin-X and Tenascin-R.
A extracellular matrix complex involved in cell adhesion and cell migration. Typically homotrimeric or homohexameric. In mammals, four complexes exist: Tenascin-C, Tenascin-N (also known as Tenascin-W), Tenascin-X and Tenascin-R.
A region of a chromosome at which DNA damage has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.
The aggregation, arrangement and bonding together of a set of components to form a DNA repair complex.
Interacting selectively and non-covalently with a meprin and TRAF homology (MATH) domain.
A process that contributes to the maintenance of proper telomeric length and structure via the activation of telomere shortening pathways that compensate telomerase-dependent excessive telomere elongation. Telomere attrition is mediated by a mechanism which involves the generation of single-stranded C-rich telomeric DNA, and the formation and removal of double-stranded telomeric circular DNA (T-circles). Telomere trimming is an independent pathway to recombination-mediated telomere elongation and the well-documented gradual telomere attrition that accompanies cellular replication.
The component of the pigment granule 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 membrane that is part of a pigment granule.
The chemical reactions and pathways resulting in the breakdown of a storage polysaccharide into pyruvate through a glucose-1-phosphate intermediate, with the concomitant production of a small amount of ATP and the reduction of NAD to NADH.
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 nematicide stimulus. Nematicides are chemicals used to kill nematodes.
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 nematicide stimulus. Nematicides are chemicals used to kill nematodes.
The series of molecular signals generated as a consequence of an acetylcholine receptor binding to one of its physiological ligands.
Interacting selectively and non-covalently with any ceramide, a class of lipids that is composed of sphingosine linked to a fatty acid. Ceramides are a major component of cell membranes.
The portion of the mitochondrial inner membrane that is not invaginated to form cristae. The inner boundary membrane lies parallel to the outer membrane.
Combining with an adipokinetic hormone to initiate a change in cell activity. Adipokinetic hormones (AKHs) are protein or peptide hormones that are important for sugar and fat homeostasis in metazoa. In insects, they mobilize sugar and lipids from the insect fat body during energy-requiring activities such as flight and locomotion. They also contribute to hemolymph sugar homeostasis.
Interacting selectively and non-covalently with an adipokinetic hormone. Adipokinetic hormones (AKHs) are peptide hormones that are involved in the mobilization of sugar and lipids from the insect fat body during energy-requiring activities such as flight and locomotion. They also contribute to hemolymph sugar homeostasis.
Interacting selectively and non-covalently with an adipokinetic hormone receptor. Adipokinetic hormones (AKHs) are peptide hormones that are involved in the mobilization of sugar and lipids from the insect fat body during energy-requiring activities such as flight and locomotion. They also contribute to hemolymph sugar homeostasis.
Any process involved in the maintenance of internal levels of plasma lipoprotein particles within an organism.
Catalysis of the reaction: (EE)-geranyllinalool + NADPH + O2 = 4,8,12-trimethyl-1,3,7,11-tridecatetraene + NADP+ + 2 H2O. It is unknown whether this reaction proceeds by the direct release of the 4-carbon compound but-1-en-3-one, or whether the substrate is first degraded to C18-farnesylacetone and then cleaved to produce 4,8,12-trimethyl-1,3,7,11-tridecatetraene (TMTT) and acetone.
Catalysis of the reaction: (EE)-geranyllinalool + NADPH + O2 = 4,8,12-trimethyl-1,3,7,11-tridecatetraene + NADP+ + 2 H2O. It is unknown whether this reaction proceeds by the direct release of the 4-carbon compound but-1-en-3-one, or whether the substrate is first degraded to C18-farnesylacetone and then cleaved to produce 4,8,12-trimethyl-1,3,7,11-tridecatetraene (TMTT) and acetone.
Catalysis of the reaction: (E)-nerolidol + NADPH + O2 = (3E)-4,8-dimethylnona-1,3,7-triene + NADP+ + 2 H2O. It is unknown whether this reaction proceeds by the direct release of the 4-carbon compound but-1-en-3-one, or whether the substrate is first degraded to C11-geranylacetone and then cleaved to produce (3E)-4,8-dimethylnona-1,3,7-triene (DMNT) and acetone.
Catalysis of the reaction: (E)-nerolidol + NADPH + O2 = (3E)-4,8-dimethylnona-1,3,7-triene + NADP+ + 2 H2O. It is unknown whether this reaction proceeds by the direct release of the 4-carbon compound but-1-en-3-one, or whether the substrate is first degraded to C11-geranylacetone and then cleaved to produce (3E)-4,8-dimethylnona-1,3,7-triene (DMNT) and acetone.
Any process involved in the balance between food intake (energy input) and energy expenditure.
Any process involved in the balance between food intake (energy input) and energy expenditure.
Any process involved in the balance between food intake (energy input) and energy expenditure.
Any process involved in the balance between food intake (energy input) and energy expenditure.
Any process involved in the balance between food intake (energy input) and energy expenditure.
Any process involved in the balance between food intake (energy input) and energy expenditure.
The aggregation, arrangement and bonding together of a set of components to form the eukaryotic translation initiation factor 4F complex.
The aggregation, arrangement and bonding together of a set of components to form the eukaryotic translation initiation factor 4F complex.
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 granulocyte macrophage colony-stimulating factor stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a granulocyte macrophage colony-stimulating factor stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a granulocyte macrophage colony-stimulating factor stimulus.
The volume enclosed by the membrane of a phagocytic vesicle.
All of the contents of a cilium, excluding the plasma membrane surrounding the cilium.
All of the contents of a cilium, excluding the plasma membrane surrounding the cilium.
All of the contents of a cilium, excluding the plasma membrane surrounding the cilium.
All of the contents of a cilium, excluding the plasma membrane surrounding the cilium.
All of the contents of a cilium, excluding the plasma membrane surrounding the cilium.
All of the contents of a cilium, excluding the plasma membrane surrounding the cilium.
All of the contents of a cilium, excluding the plasma membrane surrounding the cilium.
All of the contents of a cilium, excluding the plasma membrane surrounding the cilium.
Interacting selectively and non-covalently with a L27 domain of a protein. L27 is composed of conserved negatively charged amino acids and a conserved aromatic amino acid. L27 domains can assemble proteins involved in signaling and establishment and maintenance of cell polarity into complexes by interacting in a heterodimeric manner.
A renal system process in which proteins are taken up from the collecting ducts, glomerulus and proximal and distal loops of the nephron. In non-mammalian species, absorption may occur in related structures (e.g. protein absorption is observed in nephrocytes in Drosophila, see PMID:23264686).
A renal system process in which albumin is taken up from the collecting ducts, glomerulus and proximal and distal loops of the nephron.
The chemical reactions and pathways resulting in the breakdown of neurotransmitter receptors.
The chemical reactions and pathways resulting in the breakdown of neurotransmitter receptors.
The chemical reactions and pathways resulting in the breakdown of neurotransmitter receptors.
Bringing together a cargo protein with the COPII coat complex component to allow its uptake by the COPII vesicle.
The movement of a lymphocyte within the lymphatic system into lymphoid organs such as lymph nodes, spleen or Peyer's patches, and its subsequent positioning within defined functional compartments such as sites of cell activation by antigen.
The movement of a lymphocyte within the lymphatic system into a lymph node, and its subsequent positioning within defined functional compartments such as sites of cell activation by antigen.
Catalysis of the reaction: D-fructose-6-phosphate = dihydroxyacetone + D-glyceraldehyde-3-phosphate.
A heterotrimeric protein complex formed by the association of MMP7, DLG1 and either LIN7A or LIN7C; regulates the stability and localization of DLG1 to cell junctions.
Formation of dendrites, branched cellular projections (or cytoplasmic extension) that are extended from the surface of a dendritic immune cell, and which enable the cell to sample luminal pathogens and increase the surface area for antigen presentation to T cells.
Increases the activity of a ubiquitin-protein transferase, an enzyme that catalyzes the covalent attachment of ubiquitin to lysine in a substrate protein.
The process in which a precursor cell type acquires the specialized features of a dendritic cell. A dendritic cell is a leukocyte of dendritic lineage specialized in the uptake, processing, and transport of antigens to lymph nodes for the purpose of stimulating an immune response via T cell activation.
The process in which antigen-activated dendritic cells acquire the specialized features of a mature conventional dendritic cell. Mature conventional dendritic cells upregulate the surface expression of MHC molecules, chemokine receptors and adhesion molecules, and increase the number of dendrites (cytoplasmic protrusions) in preparation for migration to lymphoid organs where they present antigen to T cells.
Interacting selectively and non-covalently with a centromere-specific nucleosome, a form of nucleosome located only at the centromere, in which the histone H3 is replaced by the variant form CENP-A (sometimes known as CenH3).
Interacting selectively and non-covalently with a centromere-specific nucleosome, a form of nucleosome located only at the centromere, in which the histone H3 is replaced by the variant form CENP-A (sometimes known as CenH3).
Any process that modulates the proportions or spatial arrangement of lipids in a cellular membrane.
Any process that modulates the proportions or spatial arrangement of sterols in the plasma membrane.
The directed movement of heme out of a cell or organelle.
The portion of endoplasmic reticulum, the intracellular network of tubules and cisternae, that occurs near the nucleus. The lumen of the perinuclear endoplasmic reticulum is contiguous with the nuclear envelope lumen (also called perinuclear space), the region between the inner and outer nuclear membranes.
A protein ubiquitination process in which a linear polymer of ubiquitin, formed by the amino-terminal methionine (M1) of one ubiquitin molecule and by the carboxy-terminal glycine (G76) of the next, is added to a protein.
The chemical reactions and pathways resulting in the formation of phthiocerol, a lipid-based 1,3-glycol consisting of (3S,4R)-3-methoxy-4-methylnonacosane having (9R)- and (11S)-hydroxy substituents.
The chemical reactions and pathways resulting in the formation of phthiocerol, a lipid-based 1,3-glycol consisting of (3S,4R)-3-methoxy-4-methylnonacosane having (9R)- and (11S)-hydroxy substituents.
The chemical reactions and pathways resulting in the formation of phthiocerol, a lipid-based 1,3-glycol consisting of (3S,4R)-3-methoxy-4-methylnonacosane having (9R)- and (11S)-hydroxy substituents.
The chemical reactions and pathways resulting in the formation of phthiocerol, a lipid-based 1,3-glycol consisting of (3S,4R)-3-methoxy-4-methylnonacosane having (9R)- and (11S)-hydroxy substituents.
The chemical reactions and pathways resulting in the formation of phenolic phthiocerol, a phthiocerol derivative having a 4-hydroxyphenyl substituent at the 29-position.
The chemical reactions and pathways resulting in the formation of phenolic phthiocerol, a phthiocerol derivative having a 4-hydroxyphenyl substituent at the 29-position.
The chemical reactions and pathways resulting in the formation of phenolic phthiocerol, a phthiocerol derivative having a 4-hydroxyphenyl substituent at the 29-position.
The chemical reactions and pathways resulting in the formation of phenolic phthiocerol, a phthiocerol derivative having a 4-hydroxyphenyl substituent at the 29-position.
The chemical reactions and pathways resulting in the formation of phenolic phthiocerol, a phthiocerol derivative having a 4-hydroxyphenyl substituent at the 29-position.
The component of a fungal-type vacuolar 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 modification of histone H3 by the addition of an acetyl group to a lysine residue at position 56 of the histone.
The modification of histone H3 by the addition of an acetyl group to a lysine residue at position 56 of the histone as a result of the detection of DNA damage within a cell.
A phospholipid scrambling process that results in the appearance of phosphatidylserine on the surface of activated blood platelets, and triggers the clotting system.
Regulation of DNA replication by a mechanism that allows a DNA replication fork to progress beyond a termination site, which is a region containing fork pausing elements that influence the progression and merging of DNA replication forks.
A chromosomal region that contains fork pausing elements influencing the progression and merging of DNA replication forks.
Any apoptotic process in a dendritic cell, a cell of hematopoietic origin, typically resident in particular tissues, specialized in the uptake, processing, and transport of antigens to lymph nodes for the purpose of stimulating an immune response via T cell activation.
Any apoptotic process in a motor neuron, an efferent neuron that passes from the central nervous system or a ganglion toward or to a muscle and conducts an impulse that causes movement.
Any apoptotic process in a motor neuron, an efferent neuron that passes from the central nervous system or a ganglion toward or to a muscle and conducts an impulse that causes movement.
Any apoptotic process in a type B pancreatic cell, a cell located towards center of the islets of Langerhans that secretes insulin.
Any apoptotic process in a type B pancreatic cell, a cell located towards center of the islets of Langerhans that secretes insulin.
Any apoptotic process in a type B pancreatic cell, a cell located towards center of the islets of Langerhans that secretes insulin.
The directed movement of a protein to a specific location in the endoplasmic reticulum membrane.
The directed movement of a protein to a specific location in the endoplasmic reticulum membrane.
The chemical reactions and pathways involving L-kynurenine, the L-enantiomer of the amino acid kynurenine (3-(2-aminobenzoyl)-alanine).
The chemical reactions and pathways resulting in the breakdown of L-kynurenine, the L-enantiomer of the amino acid kynurenine (3-(2-aminobenzoyl)-alanine).
The chemical reactions and pathways resulting in the breakdown of L-kynurenine, the L-enantiomer of the amino acid kynurenine (3-(2-aminobenzoyl)-alanine).
The chemical reactions and pathways resulting in the breakdown of L-kynurenine, the L-enantiomer of the amino acid kynurenine (3-(2-aminobenzoyl)-alanine).
The chemical reactions and pathways resulting in the formation of L-glutamate, the L enantiomer anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of L-glutamate, the L enantiomer anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of L-glutamate, the L enantiomer anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of L-glutamate, the L enantiomer anion of 2-aminopentanedioic acid.
The chemical reactions and pathways resulting in the formation of agmatine ((4-aminobutyl)guanidine, NH2-CH2-CH2-CH2-CH2-NH-C(-NH2)(=NH)). Agmatine is the decarboxylation product of the amino acid arginine and is an intermediate in polyamine biosynthesis. It is synthesized in the brain, stored in synaptic vesicles, accumulated by uptake, released by membrane depolarization, and inactivated by agmatinase.
The chemical reactions and pathways resulting in the formation of agmatine ((4-aminobutyl)guanidine, NH2-CH2-CH2-CH2-CH2-NH-C(-NH2)(=NH)). Agmatine is the decarboxylation product of the amino acid arginine and is an intermediate in polyamine biosynthesis. It is synthesized in the brain, stored in synaptic vesicles, accumulated by uptake, released by membrane depolarization, and inactivated by agmatinase.
The chemical reactions and pathways resulting in the formation of agmatine ((4-aminobutyl)guanidine, NH2-CH2-CH2-CH2-CH2-NH-C(-NH2)(=NH)). Agmatine is the decarboxylation product of the amino acid arginine and is an intermediate in polyamine biosynthesis. It is synthesized in the brain, stored in synaptic vesicles, accumulated by uptake, released by membrane depolarization, and inactivated by agmatinase.
The chemical reactions and pathways resulting in the formation of agmatine ((4-aminobutyl)guanidine, NH2-CH2-CH2-CH2-CH2-NH-C(-NH2)(=NH)). Agmatine is the decarboxylation product of the amino acid arginine and is an intermediate in polyamine biosynthesis. It is synthesized in the brain, stored in synaptic vesicles, accumulated by uptake, released by membrane depolarization, and inactivated by agmatinase.
The chemical reactions and pathways resulting in the formation of selenocysteinyl-tRNA(Sec). This process occurs through the following steps: a unique serine-tRNA with a UGA recognizing anticodon is first aminoacylated with serine; this is then phosphorylated by phosphoseryl-tRNA[Ser]Sec kinase; lastly, selenium is swapped for the phosphate on the serine.
The chemical reactions and pathways resulting in the formation of selenocysteinyl-tRNA(Sec). This process occurs through the following steps: a unique serine-tRNA with a UGA recognizing anticodon is first aminoacylated with serine; this is then phosphorylated by phosphoseryl-tRNA[Ser]Sec kinase; lastly, selenium is swapped for the phosphate on the serine.
The chemical reactions and pathways resulting in the formation of selenocysteinyl-tRNA(Sec). This process occurs through the following steps: a unique serine-tRNA with a UGA recognizing anticodon is first aminoacylated with serine; this is then phosphorylated by phosphoseryl-tRNA[Ser]Sec kinase; lastly, selenium is swapped for the phosphate on the serine.
The chemical reactions and pathways resulting in the formation of selenocysteinyl-tRNA(Sec). This process occurs through the following steps: a unique serine-tRNA with a UGA recognizing anticodon is first aminoacylated with serine; this is then phosphorylated by phosphoseryl-tRNA[Ser]Sec kinase; lastly, selenium is swapped for the phosphate on the serine.
A protein complex comprising tumor necrosis factor (TNF) receptor-associated factor 2 (TRAF2) and glutathione S-transferase pi 1 (GSTP1). This complex is thought to disrupt the TNF signaling cascade, thus down-regulating inflammatory responses.
A heterodimeric protein complex that is composed of cardiotrophin-like cytokine factor 1 (product of the CLCF1 gene) and cytokine receptor-like factor 1 (product of the CRLF gene) and is secreted into the extracellular space. The CRLF-CLCF1 complex is a ligand for the ciliary neurotrophic factor (CNTF) receptor complex.
A protein complex that is composed of two soluble ciliary neurotrophic factor receptor alpha subunits (product of the CNTFR gene) and two molecules of cardiotrophin-like cytokine factor 1 (product of the CLCF1 gene). The complex is secreted into the extracellular space.
A specialized area of membrane on either the presynaptic or the postsynaptic side of a synapse, the junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a dendritic spine. A dendritic spine is a specialized protrusion from a neuronal dendrite and is involved in synaptic transmission.
The organization process that preserves a dendritic spine in a stable functional or structural state. A dendritic spine is a specialized protrusion from a neuronal dendrite and is involved in synaptic transmission.
Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of cadmium (Cd++).
The directed movement of a non-coding RNA transcript (ncRNA) from the nucleus to the cytoplasm.
The process whose specific outcome is the progression of the anterior part of the head over time, from its formation to the mature structure.
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 thyroid hormone stimulus.
A change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a thyroid hormone stimulus.
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 thyroxine stimulus.
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 thyroxine stimulus.
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 thyroxine stimulus.
A change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a thyroxine stimulus.
The morphogenesis process in which the ductus arteriosus changes to no longer permit blood flow after birth. The ductus arteriosus is the shunt between the aorta and the pulmonary artery which allows blood to bypass the fetus' lungs.
A protein complex that consists of two interferon regulatory proteins (IRFs); may be homodimeric or heterodimeric. The activation of a latent closed conformation of IRF in the cytoplasm is triggered by phosphorylation of Ser/Thr residues in a C-terminal region. Phosphorylation stimulates the C-terminal autoinhibitory domain to attain a highly extended conformation triggering dimerization through extensive contacts to a second subunit.
An interferon regulatory factor complex that consists of a homodimer of interferon regulatory factor 3.
An interferon regulatory factor complex that consists of a homodimer of interferon regulatory factor 5.
An interferon regulatory factor complex that consists of a homodimer of interferon regulatory factor 7.
An interferon regulatory factor complex that consists of a heterodimer of interferon regulatory factor 3 and interferon regulatory factor 7.
A protein complex that possesses protein kinase activity and activates the I-kappa B kinase complex (IKK) and mitogen-activated protein (MAP) kinases in response to TRAF6 signaling. It comprises the catalytic subunit TAK1 complexed to the regulatory subunits, termed TABs (TAK1-binding subunits).
Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of copper(I) (Cu+).
A protein complex involved in the 18S rRNA biogenesis. In S. cerevisiae this complex consists of Fal1p and Sgd1p and in humans this complex consists of NOM1 and eIF4AIII subunits.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: selenite(out) + H+(out) = selenite(in) + H+(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: selenite(out) + H+(out) = selenite(in) + H+(in).
The directed movement of inorganic selenite (HSeO3-1 at physiological pH) across a plasma membrane.
The commitment of cells to a vascular smooth muscle cell fate and their capacity to differentiate into vascular smooth muscle cells. A vascular smooth muscle cell is a non-striated, elongated, spindle-shaped cell found lining the blood vessels.
The process in which a cell becomes capable of differentiating autonomously into a vascular smooth muscle cell in an environment that is neutral with respect to the developmental pathway. Upon specification, the cell fate can be reversed. A vascular smooth muscle cell is a non-striated, elongated, spindle-shaped cell found lining the blood vessels.
The process in which a cell becomes capable of differentiating autonomously into a vascular smooth muscle cell regardless of its environment; upon determination, the cell fate cannot be reversed. A vascular smooth muscle cell is a non-striated, elongated, spindle-shaped cell found lining the blood vessels.
The process aimed at the progression of a vascular smooth muscle cell over time, from initial commitment of the cell to a specific fate, to the fully functional differentiated cell. A vascular smooth muscle cell is a non-striated, elongated, spindle-shaped cell found lining the blood vessels.
An interferon regulatory factor complex that consists of a heterodimer of interferon regulatory factor 3 and interferon regulatory factor 5.
The process whereby a relatively unspecialized cell acquires specialized features of an amniotic stem cell. An amniotic stem cell is a mesenchymal stem cell extracted from amniotic fluid. Amniotic stem cells are able to differentiate into various tissue types such as skin, cartilage, cardiac tissue, nerves, muscle, and bone.
The appearance of interleukin-17A due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of interleukin-17F due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The chemical reactions and pathways involving methyl-branched fatty acids, aliphatic monocarboxylic acids with methyl branches on the main chain.
A process which results in the assembly, arrangement of constituent parts, or disassembly of a presynaptic membrane, including any proteins associated with the membrane, but excluding other cellular components. A presynaptic membrane is a specialized area of membrane of the axon terminal that faces the plasma membrane of the neuron or muscle fiber with which the axon terminal establishes a synaptic junction.
A process which results in the assembly, arrangement of constituent parts, or disassembly of a presynaptic membrane, including any proteins associated with the membrane, but excluding other cellular components. A presynaptic membrane is a specialized area of membrane of the axon terminal that faces the plasma membrane of the neuron or muscle fiber with which the axon terminal establishes a synaptic junction.
The process that results in grouping synaptic vesicles in presynaptic structures.
The chemical reactions and pathways involving polyacyltrehalose, a pentaacylated, trehalose-based glycolipid.
The chemical reactions and pathways resulting in the formation of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid.
The chemical reactions and pathways resulting in the formation of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid.
The chemical reactions and pathways resulting in the formation of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid.
The chemical reactions and pathways resulting in the formation of polyacyltrehalose, a pentaacylated, trehalose-based glycolipid.
The process in which any suture between cranial and/or facial bones is generated and organized.
The process in which the frontonasal suture, between frontal and nasal bones, is generated and organized.
The process in which any suture between facial bones is generated and organized.
The process in which the nasal suture is generated and organized.
Facilitates the base-pairing of single-stranded RNA to double-stranded DNA resulting in the formation of R-loops.
The action of a molecule that contributes to the structural integrity of albumen (also called egg white). Albumen is the clear liquid contained within an egg and consists of water and proteins, among which are ovomucin and ovomucoid. It protects the egg yolk and provides additional nutrition for the growth of the embryo.
Interacting selectively and non-covalently with supercoiled DNA. For example, during replication and transcription, template DNA is negatively supercoiled in the receding downstream DNA and positively supercoiled in the approaching downstream DNA.
The process involved in the specification of identity of a blood vessel endothelial cell. Once specification has taken place, a cell will be committed to differentiate down a specific pathway if left in its normal environment. A blood vessel endothelial cell is an endothelial cell of the vascular tree, which includes blood vessels and lymphatic vessels.
The process involved in the specification of identity of an endothelial tip cell. Once specification has taken place, a cell will be committed to differentiate down a specific pathway if left in its normal environment. An endothelial tip cell is a specialized endothelial cell localized to the leading edge of an angiogenic sprout that senses extracellular signals and guides the directed growth of blood vessels.
The process involved in the specification of identity of an endothelial stalk cell. Once specification has taken place, a cell will be committed to differentiate down a specific pathway if left in its normal environment. An endothelial stalk cell is a specialized endothelial cell which follows behind the tip cell of an angiogenic sprout.
The aggregation, arrangement and bonding together of a set of components to form a postsynaptic membrane, a specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft).
The aggregation, arrangement and bonding together of a set of components to form a presynaptic membrane, including any proteins associated with the membrane, but excluding other cellular components. A presynaptic membrane is a  specialized area of membrane of the axon terminal that faces the plasma membrane of the neuron or muscle fiber with which the axon terminal establishes a synaptic junction.
A process that results in the assembly, arrangement of constituent parts, or disassembly of a postsynaptic density, a region that lies adjacent to the cytoplasmic face of the postsynaptic membrane at excitatory synapse.
A process that results in the assembly, arrangement of constituent parts, or disassembly of a postsynaptic density, a region that lies adjacent to the cytoplasmic face of the postsynaptic membrane at excitatory synapse.
A process that results in the assembly, arrangement of constituent parts, or disassembly of a postsynaptic density, a region that lies adjacent to the cytoplasmic face of the postsynaptic membrane at excitatory synapse.
A process that results in the assembly, arrangement of constituent parts, or disassembly of a postsynaptic density, a region that lies adjacent to the cytoplasmic face of the postsynaptic membrane at excitatory synapse.
The aggregation, arrangement and bonding together of a set of components to form a postsynaptic density, a region that lies adjacent to the cytoplasmic face of the postsynaptic membrane at excitatory synapse.
The aggregation, arrangement and bonding together of a set of components to form a postsynaptic density, a region that lies adjacent to the cytoplasmic face of the postsynaptic membrane at excitatory synapse.
The aggregation, arrangement and bonding together of a set of components to form a postsynaptic density, a region that lies adjacent to the cytoplasmic face of the postsynaptic membrane at excitatory synapse.
Interacting selectively and non-covalently with a member of the hedgehog protein family, signaling proteins involved in development.
Interacting selectively and non-covalently with a member of the neuroligin protein family, neuronal cell surface proteins that mediate synapse formation.
Interacting selectively and non-covalently with a scaffold protein. Scaffold proteins are crucial regulators of many key signaling pathways. Although not strictly defined in function, they are known to interact and/or bind with multiple members of a signaling pathway, tethering them into complexes.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum (ER)-Golgi intermediate compartment.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum (ER)-Golgi intermediate compartment.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum (ER)-Golgi intermediate compartment.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum (ER)-Golgi intermediate compartment.
The receptor clustering process in which gamma-aminobutyric acid (GABA) receptors are localized to distinct domains in the cell membrane.
The glutamate receptor clustering process in which alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors are localized to distinct domains in the cell membrane.
The glutamate receptor clustering process in which alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors are localized to distinct domains in the cell membrane.
The receptor clustering process in which N-methyl-D-aspartate (NMDA) receptors are localized to distinct domains in the cell membrane.
The receptor clustering process in which N-methyl-D-aspartate (NMDA) receptors are localized to distinct domains in the cell membrane.
The receptor clustering process involved in assembly of the presynaptic membrane in which neurexins are localized to distinct domains in the cell membrane. Neurexins are synaptic cell surface proteins which act as cell recognition molecules at nerve terminals.
The receptor clustering process involved in assembly of the presynaptic membrane in which neurexins are localized to distinct domains in the cell membrane. Neurexins are synaptic cell surface proteins which act as cell recognition molecules at nerve terminals.
The receptor clustering process involved in assembly of the presynaptic membrane in which neurexins are localized to distinct domains in the cell membrane. Neurexins are synaptic cell surface proteins which act as cell recognition molecules at nerve terminals.
The clustering process in which gephyrin molecules are localized to distinct domains in the postsynaptic density as part of postsynaptic density assembly. Gephyrin is a component of the postsynaptic protein network of inhibitory synapses.
The clustering process in which guanylate kinase-associated proteins (GKAPs) are localized to distinct domains in the cell membrane. GKAP facilitates assembly of the post synaptic density of neurons.
The receptor clustering process involved in assembly of the postsynaptic membrane in which neuroligins are localized to distinct domains in the cell membrane. Neuroligins are neuronal cell surface proteins on the postsynaptic membrane that mediate synapse formation between neurons.
The receptor clustering process involved in assembly of the postsynaptic membrane in which neuroligins are localized to distinct domains in the cell membrane. Neuroligins are neuronal cell surface proteins on the postsynaptic membrane that mediate synapse formation between neurons.
The receptor clustering process involved in assembly of the postsynaptic membrane in which neuroligins are localized to distinct domains in the cell membrane. Neuroligins are neuronal cell surface proteins on the postsynaptic membrane that mediate synapse formation between neurons.
The clustering process in which postsynaptic density protein 95 (PSD-95) molecules are localized to distinct domains in the cell membrane. PSD-95 is mostly located in the post synaptic density of neurons, and is involved in anchoring synaptic proteins.
The clustering process in which postsynaptic density protein 95 (PSD-95) molecules are localized to distinct domains in the cell membrane. PSD-95 is mostly located in the post synaptic density of neurons, and is involved in anchoring synaptic proteins.
The clustering process in which postsynaptic density protein 95 (PSD-95) molecules are localized to distinct domains in the cell membrane. PSD-95 is mostly located in the post synaptic density of neurons, and is involved in anchoring synaptic proteins.
Any process in which a receptor is transported to, and/or maintained at the synapse, the junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell.
A protein complex consisting of cyclin A1 and cyclin-dependent kinase 1 (CDK1). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin A2 and cyclin-dependent kinase 1 (CDK1). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin A1 and cyclin-dependent kinase 2 (CDK2). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin A2 and cyclin-dependent kinase 2 (CDK2). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin B1 and cyclin-dependent kinase 1 (CDK1). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin B2 and cyclin-dependent kinase 1 (CDK1). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin B3 and cyclin-dependent kinase 2 (CDK2). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin D1 and cyclin-dependent kinase 4 (CDK4). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin D2 and cyclin-dependent kinase 4 (CDK4). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin D3 and cyclin-dependent kinase 4 (CDK4). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin D1 and cyclin-dependent kinase 6 (CDK6). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin D2 and cyclin-dependent kinase 6 (CDK6). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin D3 and cyclin-dependent kinase 6 (CDK6). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin E1 and cyclin-dependent kinase 2 (CDK2). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex consisting of cyclin E2 and cyclin-dependent kinase 2 (CDK2). Cyclins are characterized by periodicity in protein abundance throughout the cell cycle. Cyclin-dependent kinases represent a family of serine/threonine protein kinases that become active upon binding to a cyclin regulatory partner.
A protein complex that consists of members of the Bcl-2 family of anti- and proapoptotic regulators. Bcl-2 proteins respond to cues from various forms of intracellular stress, such as DNA damage or cytokine deprivation, and interact with opposing family members to determine whether or not the caspase proteolytic cascade should be unleashed.
A heterodimeric protein complex consisting of BAD and BCL-xl, members of the Bcl-2 family of anti- and proapoptotic regulators.
A heterodimeric protein complex consisting of BAD and BCL-2, members of the Bcl-2 family of anti- and proapoptotic regulators.
A heterodimeric protein complex consisting of BID and BCL-2, members of the Bcl-2 family of anti- and proapoptotic regulators.
A heterodimeric protein complex consisting of BIM and BCL-xl, members of the Bcl-2 family of anti- and proapoptotic regulators.
A heterodimeric protein complex consisting of BIM and BCL-2, members of the Bcl-2 family of anti- and proapoptotic regulators.
A heterodimeric protein complex consisting of PUMA and BCL-2, members of the Bcl-2 family of anti- and proapoptotic regulators.
A heterodimeric protein complex consisting of PUMA and BCL-xl, members of the Bcl-2 family of anti- and proapoptotic regulators.
An oligomeric protein complex consisting of BAX, a member of the Bcl-2 family of anti- and proapoptotic regulators.
An oligomeric protein complex consisting of BAK, a member of the Bcl-2 family of anti- and proapoptotic regulators.
A heterodimeric protein complex consisting of NOXA and BCL-xl, members of the Bcl-2 family of anti- and proapoptotic regulators.
A heterodimeric protein complex consisting of NOXA and BCL-2, members of the Bcl-2 family of anti- and proapoptotic regulators.
A homodimeric protein complex consisting of BCL-2, a member of the Bcl-2 family of anti- and proapoptotic regulators.
A heterotetrameric protein complex playing a key role in the formation of the central spindle in mitosis. Made up of two molecules each of a mitotic kinesin (ZEN-4 in Caenorhabditis elegans or MKLP1 in mammals) and of two molecules each of a GTPase activating protein (GAP) factor (CYK-4 in Caenorhabditis elegans or MgcRacGAP in mammals).
Any process in by an organism or tissue maintains a population of neuronal stem cells.
Any process that activates or increases the frequency, rate or extent of inhibitory postsynaptic potential (IPSP). IPSP is a temporary decrease in postsynaptic membrane potential due to the flow of negatively charged ions into the postsynaptic cell. The flow of ions that causes an IPSP is an inhibitory postsynaptic current (IPSC) and makes it more difficult for the neuron to fire an action potential.
Any process that activates or increases the frequency, rate or extent of inhibitory postsynaptic potential (IPSP). IPSP is a temporary decrease in postsynaptic membrane potential due to the flow of negatively charged ions into the postsynaptic cell. The flow of ions that causes an IPSP is an inhibitory postsynaptic current (IPSC) and makes it more difficult for the neuron to fire an action potential.
Any apoptotic process in a mesenchymal cell. A mesenchymal cell is a loosely associated cell that is part of the connective tissue in an organism. Mesenchymal cells give rise to more mature connective tissue cell types.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile, and contributing to the apoptotic process.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile, and contributing to the apoptotic process.
The process in which a neuroblast acquires the specialized structural and functional features of a GABAergic neuron.
The collection of sensory neuron axons into a bundle of rods, known as a fascicle.
The collection of motor neuron axons into a bundle of rods, known as a fascicle.
Interacting selectively and non-covalently with an intronic sequence of a pre-messenger RNA (pre-mRNA).
Interacting selectively and non-covalently with a pyrimidine-rich (CU-rich) intronic sequence of a pre-messenger RNA (pre-mRNA).
Interacting selectively and non-covalently with an organic cyclic compound, any molecular entity that contains carbon arranged in a cyclic molecular structure.
Interacting selectively and non-covalently with a polychlorinated biphenyl (PCB), a biphenyl compound containing between 2 and 10 chlorine atoms attached to the two benzene rings.
Interacting selectively and non-covalently with a polychlorinated biphenyl (PCB), a biphenyl compound containing between 2 and 10 chlorine atoms attached to the two benzene rings.
Interacting selectively and non-covalently with a DH (Dbl homology) domain of a protein. The DH domain contains three structurally conserved regions separated by more variable regions. It is composed of 11 alpha helices that are folded into a flattened, elongated alpha-helix bundle in which two of the three conserved regions, conserved region 1 (CR1) and conserved region 3 (CR3), are exposed near the centre of one surface. CR1 and CR3, together with a part of alpha-6 and the DH/PH (pleckstrin homology) junction site, constitute the Rho GTPase interacting pocket.
Interacting selectively and non-covalently with a MADS box domain, a protein domain that encodes the DNA-binding MADS domain. The MADS domain binds to DNA sequences of high similarity to the motif CC[A/T]6GG termed the CArG-box. MADS-domain proteins are generally transcription factors. The length of the MADS-box is in the range of 168 to 180 base pairs.
Covalently binding to sulfur and delivering it to an acceptor molecule.
The chemical reactions and pathways involving the ammonium ion.
The chemical reactions and pathways involving the ammonium ion.
A dense aggregation in the nucleus composed of proteins and RNAs that appear when the cell is under stress.
The multiplication or reproduction of lens epithelial cells, resulting in the expansion of a cell population. Lens epithelial cells make up the lens epithelium, which is located in the anterior portion of the lens between the lens capsule and the lens fibers and is a simple cuboidal epithelium. The epithelial cells of the lens regulate most of the homeostatic functions of the lens such as osmolarity and liquid volume. The lens epithelial cells also serve as the progenitors for new lens fibers. The lens epithelium constantly lays down fibers in the embryo, fetus, infant, and adult, and continues to lay down fibers for lifelong growth.
Any process that modulates the frequency, rate or extent of mRNA translation with a regularity of approximately 24 hours.
The multiplication or reproduction of mesenchymal stem cells, resulting in the expansion of a stem cell population. A mesenchymal stem cell, or MSC, is a cell that retains the ability to divide and proliferate throughout life to provide progenitor cells that can differentiate into specialized mesenchymal cells.
A protein complex that consists of AIM2, ASC, and caspase-1. AIM2 is a member of the HN-200 protein family that appears to be the sensor of cytosolic double-stranded DNA.
The chemical reactions and pathways involving ADP-L-glycero-beta-D-manno-heptose, an ADP-L-glycero-D-manno-heptose having beta-configuration at the anomeric centre of the heptose. ADP-L-glycero-beta-D-manno-heptose (also called ADP-L-beta-D-heptose or ADP-L-glycero-D-manno-heptose) is a nucleotide-sugar precursor of the inner core lipopolysaccharide (LPS) from D-glycero-beta-D-manno-heptose 7-phosphate.
The chemical reactions and pathways resulting in the formation of ADP-L-glycero-beta-D-manno-heptose, an ADP-L-glycero-D-manno-heptose having beta-configuration at the anomeric centre of the heptose. ADP-L-glycero-beta-D-manno-heptose (also called ADP-L-beta-D-heptose or ADP-L-glycero-D-manno-heptose) is a nucleotide-sugar precursor of the inner core lipopolysaccharide (LPS) from D-glycero-beta-D-manno-heptose 7-phosphate.
The chemical reactions and pathways resulting in the formation of ADP-L-glycero-beta-D-manno-heptose, an ADP-L-glycero-D-manno-heptose having beta-configuration at the anomeric centre of the heptose. ADP-L-glycero-beta-D-manno-heptose (also called ADP-L-beta-D-heptose or ADP-L-glycero-D-manno-heptose) is a nucleotide-sugar precursor of the inner core lipopolysaccharide (LPS) from D-glycero-beta-D-manno-heptose 7-phosphate.
The chemical reactions and pathways resulting in the formation of ADP-L-glycero-beta-D-manno-heptose, an ADP-L-glycero-D-manno-heptose having beta-configuration at the anomeric centre of the heptose. ADP-L-glycero-beta-D-manno-heptose (also called ADP-L-beta-D-heptose or ADP-L-glycero-D-manno-heptose) is a nucleotide-sugar precursor of the inner core lipopolysaccharide (LPS) from D-glycero-beta-D-manno-heptose 7-phosphate.
The chemical reactions and pathways resulting in the formation of ADP-L-glycero-beta-D-manno-heptose, an ADP-L-glycero-D-manno-heptose having beta-configuration at the anomeric centre of the heptose. ADP-L-glycero-beta-D-manno-heptose (also called ADP-L-beta-D-heptose or ADP-L-glycero-D-manno-heptose) is a nucleotide-sugar precursor of the inner core lipopolysaccharide (LPS) from D-glycero-beta-D-manno-heptose 7-phosphate.
The chemical reactions and pathways involving N-acetylmuramic acid (MurNAc), a monosaccharide derivative of N-acetylglucosamine.
The chemical reactions and pathways involving N-acetylmuramic acid (MurNAc), a monosaccharide derivative of N-acetylglucosamine.
The chemical reactions and pathways involving N-acetylmuramic acid (MurNAc), a monosaccharide derivative of N-acetylglucosamine.
The chemical reactions and pathways resulting in the breakdown of N-acetylmuramic acid (MurNAc), a monosaccharide derivative of N-acetylglucosamine.
The chemical reactions and pathways resulting in the breakdown of N-acetylmuramic acid (MurNAc), a monosaccharide derivative of N-acetylglucosamine.
The chemical reactions and pathways resulting in the breakdown of N-acetylmuramic acid (MurNAc), a monosaccharide derivative of N-acetylglucosamine.
The chemical reactions and pathways resulting in the breakdown of N-acetylmuramic acid (MurNAc), a monosaccharide derivative of N-acetylglucosamine.
The chemical reactions and pathways resulting in the breakdown of N-acetylmuramic acid (MurNAc), a monosaccharide derivative of N-acetylglucosamine.
The chemical reactions and pathways resulting in the breakdown of N-acetylmuramic acid (MurNAc), a monosaccharide derivative of N-acetylglucosamine.
The chemical reactions and pathways resulting in the breakdown of N-acetylmuramic acid (MurNAc), a monosaccharide derivative of N-acetylglucosamine.
The chemical reactions and pathways involving 1,6-anhydro-N-acetyl-beta-muramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways involving 1,6-anhydro-N-acetyl-beta-muramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways involving 1,6-anhydro-N-acetyl-beta-muramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways involving 1,6-anhydro-N-acetyl-beta-muramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways involving 1,6-anhydro-N-acetyl-beta-muramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways resulting in the breakdown of 1,6-anhydro-N-acetylmuramic acid, the 1,6-anhydro-derivative of N-acetyl-beta-muramic acid.
The chemical reactions and pathways involving epoxides, compounds in which an oxygen atom is directly attached to two adjacent or non-adjacent carbon atoms of a carbon chain or ring system; thus cyclic ethers.
Interacting selectively and non-covalently with any part of a mitochondrial ribosome, a ribosome found in the mitochondrion of a eukaryotic cell.
The aggregation, arrangement and bonding together of a set of components to form a ruffle, a projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. The formation of ruffles (also called membrane ruffling) is thought to be controlled by a group of enzymes known as Rho GTPases, specifically RhoA, Rac1 and cdc42.
The aggregation, arrangement and bonding together of a set of components to form a ruffle, a projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. The formation of ruffles (also called membrane ruffling) is thought to be controlled by a group of enzymes known as Rho GTPases, specifically RhoA, Rac1 and cdc42.
A heterodimeric protein complex that contains a protease inhibitor and a protease; formation of the complex inhibits protease activity.
A heterodimeric protein complex that contains a serine protease inhibitor and a protease; formation of the complex inhibits serine protease activity.
A heterodimeric protein complex that contains a serine protease inhibitor and a protease; formation of the complex inhibits serine protease activity.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor V (F5); formation of the complex inhibits the serine protease activity of coagulation factor V.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor V (F5); formation of the complex inhibits the serine protease activity of coagulation factor V.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor V (F5); formation of the complex inhibits the serine protease activity of coagulation factor V.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor V (F5); formation of the complex inhibits the serine protease activity of coagulation factor V.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor V (F5); formation of the complex inhibits the serine protease activity of coagulation factor V.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor Xa (F10); formation of the complex inhibits the serine protease activity of coagulation factor Xa.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor Xa (F10); formation of the complex inhibits the serine protease activity of coagulation factor Xa.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor Xa (F10); formation of the complex inhibits the serine protease activity of coagulation factor Xa.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor Xa (F10); formation of the complex inhibits the serine protease activity of coagulation factor Xa.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor XI (F11); formation of the complex inhibits the serine protease activity of coagulation factor XI.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor XI (F11); formation of the complex inhibits the serine protease activity of coagulation factor XI.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor XI (F11); formation of the complex inhibits the serine protease activity of coagulation factor XI.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor XI (F11); formation of the complex inhibits the serine protease activity of coagulation factor XI.
A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor XI (F11); formation of the complex inhibits the serine protease activity of coagulation factor XI.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an azide stimulus.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an azide stimulus.
The process whose specific outcome is the formation of tooth enamel, occurring in two stages: secretory stage and maturation stage.
The process whose specific outcome is the formation of dentin, the mineralized tissue that constitutes the major bulk of teeth. Dentin may be one of three types: primary dentin, secondary dentin, and tertiary dentin.
The process whose specific outcome is the formation of dentin, the mineralized tissue that constitutes the major bulk of teeth. Dentin may be one of three types: primary dentin, secondary dentin, and tertiary dentin.
The process in which calcium salts are deposited into the calcareous tooth structure known as dentin.
A vesicle containing parts of a dying cell. Apoptotic bodies can be formed during the execution phase of the apoptotic process, when the cell's cytoskeleton breaks up and causes the membrane to bulge outward. These bulges may separate from the cell, taking a portion of cytoplasm with them, to become apoptotic bodies. These are then engulfed by phagocytic cells, and their components recycled. Apoptotic bodies may range in size from 0.8 to 5um.
A vesicle containing parts of a dying cell. Apoptotic bodies can be formed during the execution phase of the apoptotic process, when the cell's cytoskeleton breaks up and causes the membrane to bulge outward. These bulges may separate from the cell, taking a portion of cytoplasm with them, to become apoptotic bodies. These are then engulfed by phagocytic cells, and their components recycled. Apoptotic bodies may range in size from 0.8 to 5um.
A series of molecular signals which triggers the apoptotic death of a cell. The pathway starts with reception of a signal, and ends when the execution phase of apoptosis is triggered.
A series of molecular signals which triggers the apoptotic death of a cell. The pathway starts with reception of a signal, and ends when the execution phase of apoptosis is triggered.
A series of molecular signals which triggers the apoptotic death of a cell. The pathway starts with reception of a signal, and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with either a ligand binding to a cell surface receptor, or a ligand being withdrawn from a cell surface receptor (e.g. in the case of signaling by dependence receptors), and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with either a ligand binding to a cell surface receptor, or a ligand being withdrawn from a cell surface receptor (e.g. in the case of signaling by dependence receptors), and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with either a ligand binding to a cell surface receptor, or a ligand being withdrawn from a cell surface receptor (e.g. in the case of signaling by dependence receptors), and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with either a ligand binding to a cell surface receptor, or a ligand being withdrawn from a cell surface receptor (e.g. in the case of signaling by dependence receptors), and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with either a ligand binding to a cell surface receptor, or a ligand being withdrawn from a cell surface receptor (e.g. in the case of signaling by dependence receptors), and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with withdrawal of a ligand from a cell surface receptor, and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with withdrawal of a ligand from a cell surface receptor, and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with withdrawal of a ligand from a cell surface receptor, and ends when the execution phase of apoptosis is triggered.
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway starts with reception of an intracellular signal (e.g. DNA damage, endoplasmic reticulum stress, oxidative stress etc.), and ends when the execution phase of apoptosis is triggered. The intrinsic apoptotic signaling pathway is crucially regulated by permeabilization of the mitochondrial outer membrane (MOMP).
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway starts with reception of an intracellular signal (e.g. DNA damage, endoplasmic reticulum stress, oxidative stress etc.), and ends when the execution phase of apoptosis is triggered. The intrinsic apoptotic signaling pathway is crucially regulated by permeabilization of the mitochondrial outer membrane (MOMP).
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway starts with reception of an intracellular signal (e.g. DNA damage, endoplasmic reticulum stress, oxidative stress etc.), and ends when the execution phase of apoptosis is triggered. The intrinsic apoptotic signaling pathway is crucially regulated by permeabilization of the mitochondrial outer membrane (MOMP).
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway starts with reception of an intracellular signal (e.g. DNA damage, endoplasmic reticulum stress, oxidative stress etc.), and ends when the execution phase of apoptosis is triggered. The intrinsic apoptotic signaling pathway is crucially regulated by permeabilization of the mitochondrial outer membrane (MOMP).
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway starts with reception of an intracellular signal (e.g. DNA damage, endoplasmic reticulum stress, oxidative stress etc.), and ends when the execution phase of apoptosis is triggered. The intrinsic apoptotic signaling pathway is crucially regulated by permeabilization of the mitochondrial outer membrane (MOMP).
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway starts with reception of an intracellular signal (e.g. DNA damage, endoplasmic reticulum stress, oxidative stress etc.), and ends when the execution phase of apoptosis is triggered. The intrinsic apoptotic signaling pathway is crucially regulated by permeabilization of the mitochondrial outer membrane (MOMP).
A stage of the apoptotic process that starts with the controlled breakdown of the cell through the action of effector caspases or other effector molecules (e.g. cathepsins, calpains etc.). Key steps of the execution phase are rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
A stage of the apoptotic process that starts with the controlled breakdown of the cell through the action of effector caspases or other effector molecules (e.g. cathepsins, calpains etc.). Key steps of the execution phase are rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
The reflex process in which the arrectores pilorum (hair follicle) muscles contract and cause the hair to stand erect.
The reflex process in which the arrectores pilorum (hair follicle) muscles contract and cause the hair to stand erect.
The reflex process in which the arrectores pilorum (hair follicle) muscles contract and cause the hair to stand erect.
A protein complex involved in error-free DNA post-replication repair (PRR). In Saccharomyces cerevisiae the complex contains Csm2p, Psy3p, Shu1p, and Shu2p.
A pre-organized unit composed either of adhesion molecules (mainly integrins and members of the Ig superfamily), signaling receptors and/or enzyme-enriched plasma membrane domains that compartmentalizes cellular processes. Tetraspanin-enriched microdomains might be specially suited for the regulation of avidity of adhesion receptors and the compartmentalization of enzymatic activities.
A pre-organized unit composed either of adhesion molecules (mainly integrins and members of the Ig superfamily), signaling receptors and/or enzyme-enriched plasma membrane domains that compartmentalizes cellular processes. Tetraspanin-enriched microdomains might be specially suited for the regulation of avidity of adhesion receptors and the compartmentalization of enzymatic activities.
The modification of histone H3 by addition of three methyl groups to lysine at position 36 of the histone.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile, and contributing to the apoptotic signaling pathway.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile, and contributing to the apoptotic signaling pathway.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile, and contributing to the apoptotic signaling pathway.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile, and contributing to the apoptotic signaling pathway.
Any process that decreases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a stimulus indicating the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase.
Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase.
The tip or margin of the progressing circular lamella that engulfs a particle during phagocytosis. When the two lips of the cup fuse it is converted into a phagosome.
The older part of the phagocytic cup where the actin cytoskeleton disassembles, allowing early incoming and outgoing vesicular trafficking.
A renal system process in which fluid circulating through the body is filtered through a barrier system.
The process by which hemolymph is filtered based on size and charge through a nephrocyte filtration barrier formed by the basement membrane and nephrocyte diaphragm.
A dormancy process in which dormancy (sometimes called a dormant state) is induced, maintained or broken in a bud. Bud dormancy is a suspension of most physiological activity and growth that can be reactivated. It may be a response to environmental conditions such as seasonality or extreme heat, drought, or cold. The exit from bud dormancy is marked by the resumed growth of the bud.
A specialized secretory organelle found in type II pneumocytes and involved in the synthesis, secretion, and reutilization of pulmonary surfactant.
A specialized secretory organelle found in keratinocytes and involved in the formation of an impermeable, lipid-containing membrane that serves as a water barrier and is required for correct skin barrier function.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gonadotropin-releasing hormone stimulus. Gonadotropin-releasing hormone (GnRH) is a peptide hormone responsible for the release of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) from the anterior pituitary. GnRH is synthesized and released by the hypothalamus.
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 gonadotropin-releasing hormone stimulus. Gonadotropin-releasing hormone (GnRH) is a peptide hormone responsible for the release of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) from the anterior pituitary. GnRH is synthesized and released by the hypothalamus.
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 gonadotropin-releasing hormone stimulus. Gonadotropin-releasing hormone (GnRH) is a peptide hormone responsible for the release of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) from the anterior pituitary. GnRH is synthesized and released by the hypothalamus.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lysosomal membrane. A lysosomal membrane is the lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lysosomal membrane. A lysosomal membrane is the lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
Any process that modulates the frequency, rate or extent of the passage or uptake of molecules by the lysosomal membrane.
Any process that increases the frequency, rate or extent of the passage or uptake of molecules by the lysosomal membrane.
Any process that decreases the frequency, rate or extent of the passage or uptake of molecules by the lysosomal membrane.
Interacting selectively and non-covalently with guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions.
A pit-like area in the cell wall of a sieve element; contains pores lined with callose and occupied by strands of protoplasmic material that interconnect the protoplasts of contiguous sieve elements.
A part of the cell wall of a sieve tube member that bears one or more highly specialized sieve areas.
A sieve plate that contains several specialized sieve areas in either a scalariform or reticulate arrangement.
A sieve plate that contains a single specialized sieve area.
A protein complex that contains a MADS-box protein and two forkhead domain proteins, and binds to and regulates transcription from promoters of genes transcribed during the M/G1 transition of the cell cycle. In Schizosaccharomyces pombe, the complex contains the MADS-box protein Mbx1 and two forkhead proteins, Sep1 and Fkh2.
A protein complex that contains a MADS-box protein and two forkhead domain proteins, and binds to and regulates transcription from promoters of genes transcribed during the M/G1 transition of the cell cycle. In Schizosaccharomyces pombe, the complex contains the MADS-box protein Mbx1 and two forkhead proteins, Sep1 and Fkh2.
A protein complex that contains a MADS-box protein and two forkhead domain proteins, and binds to and regulates transcription from promoters of genes transcribed during the M/G1 transition of the cell cycle. In Schizosaccharomyces pombe, the complex contains the MADS-box protein Mbx1 and two forkhead proteins, Sep1 and Fkh2.
A protein complex that contains a MADS-box protein and two forkhead domain proteins, and binds to and regulates transcription from promoters of genes transcribed during the M/G1 transition of the cell cycle. In Schizosaccharomyces pombe, the complex contains the MADS-box protein Mbx1 and two forkhead proteins, Sep1 and Fkh2.
The enzymatic addition of a sequence of 40-60 adenylyl residues at the 3' end of a eukaryotic mitochondrial mRNA primary transcript. Mitochondria contain both stabilizing and destabilizing poly(A) tails.
Any constituent part of a sperm, a mature male germ cell that develops from a spermatid.
The segment of the sperm flagellum that attaches to the implantation fossa of the nucleus in the sperm head; from the remnant of the centriole at this point, the axoneme extends throughout the length of the flagellum.
The highly organized segment of the sperm flagellum which begins at the connecting piece and is characterized by the presence of 9 outer dense fibers (ODFs) that lie outside each of the 9 outer axonemal microtubule doublets and by a sheath of mitochondria that encloses the ODFs and the axoneme; the midpiece terminates about one-fourth of the way down the sperm flagellum at the annulus, which marks the beginning of the principal piece.
The tightly packed helical sheath of ATP-producing mitochondria restricted to the midpiece of the sperm flagellum.
The ring-like, filamentous structure located at the distal end of the midpiece of the sperm flagellum; the annulus is thought to form a diffusion barrier between the midpiece and the principal piece and serve as a stabilizing structure for tail rigidity.
The segment of the sperm flagellum where the mitochondrial sheath ends, and the outer dense fibers (ODFs) associated with outer axonemal doublets 3 and 8 are replaced by the 2 longitudinal columns of the fibrous sheath (FS) which run the length of the principal piece and are stabilized by circumferential ribs. The principal piece makes up ~2/3 of the length of the sperm flagellum and is defined by the presence of the FS and of only 7 (rather than 9) ODFs which taper and then terminate near the distal end of the principal piece.
The short tip of the sperm flagellum, adjacent to the sperm principal piece and furthest from the sperm head, which contains only the axoneme surrounded by the plasma membrane.
Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another as a result of a potassium ion stimulus.
Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another as a result of a potassium ion stimulus.
Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another as a result of a calcium ion stimulus.
Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another as a result of a calcium ion stimulus.
The lipid bilayer surrounding a lamellar body. A lamellar body is a membrane-bounded organelle, specialized for the storage and secretion of various substances (surfactant phospholipids, glycoproteins and acid phosphates) which are arranged in the form of tightly packed, concentric, membrane sheets or lamellae. Has some similar properties to, but is distinct from, a lysosome.
The lipid bilayer surrounding an alveolar lamellar body, a specialized secretory organelle found in type II pneumocytes and involved in the synthesis, secretion, and reutilization of pulmonary surfactant.
The lipid bilayer surrounding an epidermal lamellar body, a specialized secretory organelle found in keratinocytes and involved in the formation of an impermeable, lipid-containing membrane that serves as a water barrier and is required for correct skin barrier function.
Any process that activates or increases the frequency, rate or extent of fatty acid beta-oxidation by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of deprivation of zinc ions.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a toxic 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 methylglyoxal stimulus. Methylglyoxal is a 2-oxoaldehyde derived from propanal.
Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter in response to a methylglyoxal stimulus.
The process in which chromatin is anchored to the nuclear envelope.
The orderly movement of a hematopoietic stem cell into the bone marrow, and its subsequent positioning within defined functional compartments in that microenvironment. A hematopoietic stem cell is a cell from which all cells of the lymphoid and myeloid lineages develop, including blood cells and cells of the immune system.
The orderly movement of a hematopoietic stem cell into the bone marrow, and its subsequent positioning within defined functional compartments in that microenvironment. A hematopoietic stem cell is a cell from which all cells of the lymphoid and myeloid lineages develop, including blood cells and cells of the immune system.
The orderly movement of a hematopoietic stem cell into the bone marrow, and its subsequent positioning within defined functional compartments in that microenvironment. A hematopoietic stem cell is a cell from which all cells of the lymphoid and myeloid lineages develop, including blood cells and cells of the immune system.
The process in which amyloid-beta is removed from extracellular brain regions by mechanisms involving cell surface receptors.
Interacting selectively and non-covalently with a flavonoid, a compound containing two or more aromatic rings, each bearing at least one aromatic hydroxyl and connected with a carbon bridge.
Interacting selectively and non-covalently with a flavonol, a flavonoid that contains a 3-hydroxy-2-phenylchromen-4-one backbone.
Interacting selectively and non-covalently with a flavanol.
Interacting selectively and non-covalently with a catechin, a polyphenolic antioxidant plant metabolite with a flavonoid or flavan-3-ol structure.
Interacting selectively and non-covalently with epigallocatechin 3-gallate, a compound that is a gallic acid ester of a catechin.
Interacting selectively and non-covalently with epigallocatechin 3-gallate, a compound that is a gallic acid ester of a catechin.
A process in which a protein or protein complex is maintained in a specific location in the cell cortex of a cell tip, and is prevented from moving elsewhere. The cell cortex of a cell tip is the region directly beneath the plasma membrane at either end of the longest axis of a cylindrical or elongated cell.
A set of respiratory enzyme complexes of the mitochondrial inner membrane (including, for example, Complex II, Complex III, Complex IV, or F1-F0 ATPase) arranged to form a large supercomplex.
A set of respiratory enzyme complexes of the mitochondrial inner membrane (including, for example, Complex II, Complex III, Complex IV, or F1-F0 ATPase) arranged to form a large supercomplex.
The aggregation, arrangement and bonding together of a set of respiratory enzyme complexes of the mitochondrial inner membrane (including, for example, Complex II, Complex III, Complex IV, or F1-F0 ATPase) to form a large supercomplex.
The aggregation, arrangement and bonding together of a set of respiratory enzyme complexes of the mitochondrial inner membrane (including, for example, Complex II, Complex III, Complex IV, or F1-F0 ATPase) to form a large supercomplex.
The chemical reactions and pathways resulting in the formation of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways resulting in the formation of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways resulting in the formation of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways resulting in the formation of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways resulting in the formation of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways resulting in the formation of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways resulting in the formation of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
The chemical reactions and pathways resulting in the formation of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents.
Any apoptotic process in an oligodendrocyte. Oligodendrocytes belong to a class of large neuroglial (macroglial) cells in the central nervous system, where they form the insulating myelin sheath of axons.
Enables the transfer of beta-hydroxybutyrate from one side of a membrane to the other. Beta-hydroxybutyrate is the conjugate base of (R)-3-hydroxybutyric acid.
Enables the transfer of beta-hydroxybutyrate from one side of a membrane to the other. Beta-hydroxybutyrate is the conjugate base of (R)-3-hydroxybutyric acid.
Secretion of substances from peritubular capillaries into the renal tubules to be incorporated subsequently into the urine. Substances that are secreted include organic anions, ammonia, potassium and drugs.
A highly conserved protein complex comprised of two ATP-dependent DNA helicases (Rvb1p and Rvb2p in yeast, Pontin52 and Reptin52 in humans), Pih1p in yeast or PIH1D1 in humans, and Tah1 in yeast or RPAP3 in humans. The complex associates with Hsp90 and is thought to have a role in assembly of large protein or protein/nucleic acid complexes. In this role it is involved in multiple processes such as box C/D snoRNP biogenesis, phosphatidylinositol-3 kinase-related protein kinase (PIKK) signaling, RNA polymerase II assembly, and others.
Catalysis of the oxidation of phenyllactate to produce phenylpyruvate.
Catalysis of the reaction: leukotriene B4 + NADP(+) = 12-oxo-leukotriene B4 + NADPH + H(+).
Catalysis of the reaction: 20-hydroxy-leukotriene B4 + O2 + NADPH + H(+) = 20-aldehyde-leukotriene B4 + 2H2O + NADP(+).
Catalysis of the reaction: 20-hydroxy-leukotriene B4 + O2 + NADPH + H(+) = 20-aldehyde-leukotriene B4 + 2H2O + NADP(+).
Catalysis of the reaction: 20-aldehyde-leukotriene B4 + O2 + NADPH + H(+) = 20-carboxy-leukotriene B4 + H2O + NADP(+).
Catalysis of the reaction: leukotriene A4 = eoxin A4.
Catalysis of the reaction: eoxin A4 + glutathione = eoxin C4.
Catalysis of the reaction: eoxin C4 = eoxin D4 + 5-L-glutamyl amino acid.
Catalysis of the reaction: eoxin D4 + H20 = eoxin E4 + glycine.
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their own peptide bonds.
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their own peptide bonds.
Catalysis of the reaction: 5-HETE + NADP(+) = 5-oxo-ETE + NADPH + H(+).
Catalysis of the reaction: 5-HETE + NADP(+) = 5-oxo-ETE + NADPH + H(+).
Catalysis of the reaction: 5-HETE + NADP(+) = 5-oxo-ETE + NADPH + H(+).
Catalysis of the reaction: phenylacetyl-CoA + H(+) + NADPH + O2 = 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP(+).
Catalysis of the reaction: phenylacetyl-CoA + H(+) + NADPH + O2 = 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP(+).
Catalysis of the reaction: phenylacetyl-CoA + H(+) + NADPH + O2 = 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP(+).
The chemical reactions and pathways by which arachidonic acid is converted to other compounds initially by omega-hydroxylation.
A subcellular filamentary structure where CTP synthase is compartmentalized in a range of organisms including bacteria, yeast, fruit fly, rat and human.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + all-trans-decaprenyl diphosphate.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + all-trans-decaprenyl diphosphate.
The temporary recovery of response to a stimulus when a novel stimulus is added.
A process in which a protein is transported to, or maintained at, a location within a cellular bud neck.
A process in which a protein is transported to, or maintained at, a location within a cellular bud neck.
Any biological process involved in the maintenance of an internal steady state of ammonia.
Any biological process involved in the maintenance of an internal steady state of creatinine.
Any biological process involved in the maintenance of an internal steady state of urea.
Any biological process involved in the maintenance of an internal steady state of ammonia at the level of the cell.
Any biological process involved in the maintenance of an internal steady state of creatinine at the level of the cell.
Any biological process involved in the maintenance of an internal steady state of urea at the level of the cell.
Lysis of a cell resulting from triggering of the complement cascade. An example can be seen with complement activation and subsequent lysis of a bacterial cell as a result of the binding of IgM to the cell surface followed by the binding of complement proteins to that antibody.
Histamine release triggered by the binding of an antigen to an IgE immunoglobulin bound to the cell surface. An example is mast cell histamine degranulation as a result of exposure of mast cell-bound IgE to alder tree pollen.
Histamine release triggered by the binding of an antigen to an IgE immunoglobulin bound to the cell surface. An example is mast cell histamine degranulation as a result of exposure of mast cell-bound IgE to alder tree pollen.
Histamine release triggered by the binding of an antigen to an immunoglobulin bound to the cell surface.
The process that gives rise to an immune complex. Immune complexes are clusters of antibodies bound to antigen, to which complement may also be fixed, and which may precipitate or remain in solution. Examples are the clumping of cells such as bacteria or red blood cells in the presence of an antibody, precipitation of a toxin after an antibody binds to it, and clumping of viral particles as a result of antibody binding to the virus.
The inhibition of an antigen's biological effects by antibody binding to it. An example is neutralization of diphtheria toxin by preventing its entry into human cells via the binding of antibody specific for diphtheria toxin.
Any apoptotic process in a keratinocyte. A keratinocyte is an epidermal cell which synthesizes keratin and undergoes a characteristic change as it moves upward from the basal layers of the epidermis to the cornified (horny) layer of the skin.
Any apoptotic process in a hepatocyte, the main structural component of the liver.
The directed movement of iron ions into a cell or organelle.
The chemical reactions and pathways involving the Q nucleoside precursor 7-cyano-7-deazaguanine, also known as 2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile or preQo.
The chemical reactions and pathways resulting in the formation of the Q nucleoside precursor 7-cyano-7-deazaguanine, also known as 2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile or preQo.
The chemical reactions and pathways resulting in the formation of the Q nucleoside precursor 7-cyano-7-deazaguanine, also known as 2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile or preQo.
The chemical reactions and pathways resulting in the formation of the Q nucleoside precursor 7-cyano-7-deazaguanine, also known as 2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile or preQo.
The chemical reactions and pathways resulting in the formation of the Q nucleoside precursor 7-cyano-7-deazaguanine, also known as 2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile or preQo.
The chemical reactions and pathways involving alpha-ribazole, the benzimidazole nucleoside in adenosyl cobalamin (vitamin B12).
The chemical reactions and pathways resulting in the formation of alpha-ribazole, the benzimidazole nucleoside in adenosyl cobalamin (vitamin B12).
The chemical reactions and pathways resulting in the formation of alpha-ribazole, the benzimidazole nucleoside in adenosyl cobalamin (vitamin B12).
The chemical reactions and pathways resulting in the formation of alpha-ribazole, the benzimidazole nucleoside in adenosyl cobalamin (vitamin B12).
The chemical reactions and pathways resulting in the formation of alpha-ribazole, the benzimidazole nucleoside in adenosyl cobalamin (vitamin B12).
A renal system process in which phosphate ions are taken up from the collecting ducts and proximal and distal loops of the nephron. In non-mammalian species, absorption may occur in related structures.
The chemical reactions and pathways involving XMP, xanthosine monophosphate.
The chemical reactions and pathways resulting in the formation of XMP, xanthosine monophosphate.
The chemical reactions and pathways resulting in the formation of XMP, xanthosine monophosphate.
The chemical reactions and pathways resulting in the formation of XMP, xanthosine monophosphate.
The chemical reactions and pathways resulting in the formation of XMP, xanthosine monophosphate.
The chemical reactions and pathways resulting in the formation of XMP, xanthosine monophosphate, from simpler precursors.
The chemical reactions and pathways resulting in the formation of XMP, xanthosine monophosphate, from simpler precursors.
The chemical reactions and pathways resulting in the formation of XMP, xanthosine monophosphate, from simpler precursors.
The chemical reactions and pathways resulting in the formation of XMP, xanthosine monophosphate, from simpler precursors.
The chemical reactions and pathways resulting in the formation of morphine, 17-methyl-7,8-didehydro-4,5alpha-epoxymorphinan-3,6alpha-diol. Morphine is a highly potent opiate analgesic psychoactive drug obtained form the opium poppy, Papaver somniferum.
The chemical reactions and pathways resulting in the formation of morphine, 17-methyl-7,8-didehydro-4,5alpha-epoxymorphinan-3,6alpha-diol. Morphine is a highly potent opiate analgesic psychoactive drug obtained form the opium poppy, Papaver somniferum.
The chemical reactions and pathways resulting in the formation of morphine, 17-methyl-7,8-didehydro-4,5alpha-epoxymorphinan-3,6alpha-diol. Morphine is a highly potent opiate analgesic psychoactive drug obtained form the opium poppy, Papaver somniferum.
The chemical reactions and pathways resulting in the formation of morphine, 17-methyl-7,8-didehydro-4,5alpha-epoxymorphinan-3,6alpha-diol. Morphine is a highly potent opiate analgesic psychoactive drug obtained form the opium poppy, Papaver somniferum.
Any process that initiates the activity of an inactive cysteine-type endopeptidase involved in the apoptotic signaling pathway.
Any process that initiates the activity of an inactive cysteine-type endopeptidase involved in the apoptotic signaling pathway.
Any process that initiates the activity of an inactive cysteine-type endopeptidase involved in the execution phase of apoptosis.
Any process that modulates the size of the nucleus.
Any process that modulates the size of the nucleus.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile, and contributing to plant-type hypersensitive response, the rapid, localized death of plant cells in response to invasion by a pathogen.
A necrotic cell death process that results from the activation of endogenous cellular processes, such as signaling involving death domain receptors or Toll-like receptors.
A necrotic cell death process that results from the activation of endogenous cellular processes, such as signaling involving death domain receptors or Toll-like receptors.
Any process that regulates the internal concentration of potassium ions at the level of a cell by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
Any process that regulates the internal concentration of potassium ions at the level of a cell by activating or increasing the frequency, rate or extent of transcription from an RNA polymerase II promoter.
The chemical reactions and pathways by which diacylglyceryl transfer leads to formation of a water-soluble protein-lipid complex.
The chemical reactions and pathways by which N-acyl transfer leads to formation of a water-soluble protein-lipid complex.
The chemical reactions and pathways by which signal peptide cleavage leads to formation of a water-soluble protein-lipid complex.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an alcohol stimulus.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an alcohol 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 farnesol 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 farnesol stimulus.
Methylation of the ribose of the first nucleotide of a 5'-capped mRNA.
Methylation of the ribose of the first and second nucleotides of a 5'-capped mRNA.
A structure lying external to bacterial cells. A biofilm is an aggregate of surface-associated bacteria, and the biofilm matrix is the envelope of polymeric substances that surrounds the bacteria.
Any constituent part of the biofilm matrix, a structure lying external to bacterial cells. A biofilm is an aggregate of surface-associated bacteria, and the biofilm matrix is the envelope of polymeric substances that surrounds the bacteria.
The external part of the biofilm matrix, a structure lying external to bacterial cells. A biofilm is an aggregate of surface-associated bacteria, and the biofilm matrix is the envelope of polymeric substances that surrounds the bacteria.
The aggregation, arrangement and bonding together of the apoptosome, a multisubunit protein complex involved in the signaling phase of the apoptotic 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 an N-acetyl-D-glucosamine stimulus.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an N-acetyl-D-glucosamine stimulus.
The growth of colonies in filamentous chains of cells as a result of a biotic stimulus. An example of this is Candida albicans forming invasive filaments in agar medium in response to a serum stimulus.
The growth of colonies in filamentous chains of cells as a result of a abiotic stimulus. An example of this process is found in Candida albicans.
A membrane tubulation process occurring in a plasma membrane.
A membrane tubulation process occurring in a plasma membrane.
The process in which a cell switches from growing as a filament (elongated cells attached end-to-end) to growing as a round budding cell. An example of this is observed in Candida albicans.
Interacting selectively and non-covalently with a 7SK small nuclear RNA (7SK snRNA).
The attachment of a B cell to another cell via adhesion molecules.
The orderly movement of melanocytes from one site to another, often during the development of a multicellular organism. A melanocyte is a pigment cell derived from the neural crest. It contains melanin-filled pigment granules, which give a brown to black appearance.
The multiplication or reproduction of melanocytes, resulting in the expansion of a cell population. A melanocyte is a pigment cell derived from the neural crest. It contains melanin-filled pigment granules, which give a brown to black appearance.
The attachment of a melanocyte to another cell via adhesion 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 an antineoplastic agent stimulus. An antineoplastic agent is a substance that inhibits or prevents the proliferation of neoplasms.
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 carboplatin stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antimetabolite stimulus. An antimetabolite is a substance which is structurally similar to a metabolite but which competes with it or replaces it, and so prevents or reduces its normal utilization.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a 5-fluoro-2'-deoxyuridine stimulus. 5-fluoro-2'-deoxyuridine is a pyrimidine 2'-deoxyribonucleoside compound having 5-fluorouracil as the nucleobase; it is used to treat hepatic metastases of gastrointestinal adenocarcinomas and for palliation in malignant neoplasms of the liver and gastrointestinal tract.
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 cytarabine stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antipsychotic drug stimulus. Antipsychotic drugs are agents that control agitated psychotic behaviour, alleviate acute psychotic states, reduce psychotic symptoms, and exert a quieting effect.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an olanzapine 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 perphenazine stimulus. Perphenazine is a phenothiazine derivative having a chloro substituent at the 2-position and a 3-[4-(2-hydroxyethyl)piperazin-1-yl]propyl group at the N-10 position.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a quetiapine 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 risperidone 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 ziprasidone stimulus. Ziprasidone is a piperazine compound having 1,2-benzothiazol-3-yl- and 2-(6-chloro-1,3-dihydro-2-oxindol-5-yl)ethyl substituents attached to the nitrogen atoms.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a clozapine stimulus.
The process in which glycolate is transported across a membrane. Glycolate is the anion of hydroxyethanoic acid (glycolic acid).
Any process that prevents the activation of an inactive cysteine-type endopeptidase.
Any process that prevents the activation of an inactive cysteine-type endopeptidase.
Any process that prevents the activation of an inactive cysteine-type endopeptidase.
Any process that prevents the proteolytic processing of an inactive enzyme to an active form.
A protein complex whose core components are the receptor-interacting serine/threonine-protein kinases RIPK1 and RIPK3 (also called RIP1 and RIP3). Formation of the ripoptosome can induce an extrinsic apoptotic signaling pathway or a necroptotic signaling pathway. The composition of this protein complex may depend on several factors including nature of the signal, cell type and more.
A protein complex whose core components are the receptor-interacting serine/threonine-protein kinases RIPK1 and RIPK3 (also called RIP1 and RIP3). Formation of the ripoptosome can induce an extrinsic apoptotic signaling pathway or a necroptotic signaling pathway. The composition of this protein complex may depend on several factors including nature of the signal, cell type and more.
A protein complex whose core components are the receptor-interacting serine/threonine-protein kinases RIPK1 and RIPK3 (also called RIP1 and RIP3). Formation of the ripoptosome can induce an extrinsic apoptotic signaling pathway or a necroptotic signaling pathway. The composition of this protein complex may depend on several factors including nature of the signal, cell type and more.
The aggregation, arrangement and bonding together of a set of components to form a ripoptosome, a protein complex whose formation can induce an extrinsic apoptotic signaling pathway or a necroptotic signaling pathway. The composition of this protein complex may depend on several factors including nature of the signal, cell type and more.
A protein complex that comprises Rix1p, Ipi1p and Ipi3p, and is required for processing of ITS2 sequences from 35S pre-rRNA. The Rix1 complex has been identified in budding yeast and fission yeast, and members of this complex are conserved in higher eukaryotes.
The process by which the mitochondrial outer membrane becomes permeable to the passing of proteins and other molecules from the intermembrane space to the cytosol as part of the apoptotic signaling pathway.
The process by which the mitochondrial outer membrane becomes permeable to the passing of proteins and other molecules from the intermembrane space to the cytosol as part of the apoptotic signaling pathway.
The process by which the mitochondrial outer membrane becomes permeable to the passing of proteins and other molecules from the intermembrane space to the cytosol as part of the apoptotic signaling pathway.
A chromatin remodeling protein complex initially purified from S. cerevisiae and containing more than 10 subunits, including the SWR1-related complexes. INO80 (inositol requiring 80)-type complexes have diverse functions, including promoting transcriptional activation and DNA repair.
A heterooligomeric protein complex that spans the bacterial periplasm and enables the secretion of adhesin proteins in Gram-negative bacteria. In Citrobacter rodentium, Salmonella enterica and Escherichia coli, the TAM complex consists of an Omp85-family protein, TamA, in the outer membrane and TamB in the inner membrane.
The lipid bilayer surrounding a host cell endocytic vesicle.
The selective elimination of senescent neutrophils from the body by autoregulatory mechanisms.
Interacting selectively and non-covalently with a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.
Removal of PI3P and Atg8/LC3 after the closure of the phagophore and before the fusion with the endosome/lysosome (e.g. mammals and insects) or vacuole (yeast), and that very likely destabilizes other Atg proteins and thus enables their efficient dissociation and recycling.
Removal of PI3P and Atg8/LC3 after the closure of the phagophore and before the fusion with the endosome/lysosome (e.g. mammals and insects) or vacuole (yeast), and that very likely destabilizes other Atg proteins and thus enables their efficient dissociation and recycling.
Removal of PI3P and Atg8/LC3 after the closure of the phagophore and before the fusion with the endosome/lysosome (e.g. mammals and insects) or vacuole (yeast), and that very likely destabilizes other Atg proteins and thus enables their efficient dissociation and recycling.
Removal of PI3P and Atg8/LC3 after the closure of the phagophore and before the fusion with the endosome/lysosome (e.g. mammals and insects) or vacuole (yeast), and that very likely destabilizes other Atg proteins and thus enables their efficient dissociation and recycling.
The regionalization process in which the areas along the centrolateral axis are established that will lead to differences in cell differentiation, or in which cells interpret a specific environment.
The covalent attachment of a prenyl group to a molecule; geranyl, farnesyl, or geranylgeranyl groups may be added.
Any process in which a protein is transported to, or maintained at, a part of a chromosome that is organized into heterochromatin.
The perinucleolar compartment (PNC) is a subnuclear structure associated with, but structurally distinct from, the nucleolus. The PNC contains large amounts of the heterogeneous nuclear ribonucleoprotein complex (hnRNP) called hnRNP 1 (PTB). Many RNA binding proteins as well as RNA polymerase III transcripts are highly enriched in this compartment. PTB and pol III transcripts are required for the integrity of the PNC.
Catalysis of the reaction: D-leucyl-tRNA(Leu) = D-leucine + tRNA(Leu). Hydrolysis of the removal of D-leucine from residues in charged tRNA(Leu).
The covalent attachment of a UDP-glucose residue to a substrate molecule.
The multiplication or reproduction of chorionic trophoblast cells, resulting in the expansion of their population.
The cytosolic iron-sulfur protein assembly (CIA) complex mediates the incorporation of iron-sulfur clusters into apoproteins involved in DNA metabolism and genomic integrity.
A hexameric protein complex composed of MCM8 and MCM9 and involved in homologous recombination repair following DNA interstrand cross-links.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine, or UDP-N-acetyl-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine, or UDP-N-acetyl-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine, or UDP-N-acetyl-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine.
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine, or UDP-N-acetyl-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine.
Enables the transmembrane transfer of a calcium ion by a channel that opens in response to a mechanical stress in the form of stretching, and contributing to the regulation of action potential.
Enables the transmembrane transfer of a calcium ion by a channel that opens in response to a mechanical stress in the form of stretching, and contributing to the regulation of action potential in a cardiac muscle cell.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a bronchodilator stimulus. A bronchodilator is a chemical that causes an increase in the expansion of a bronchus or bronchial tubes.
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 bronchodilator stimulus. A bronchodilator is a chemical that causes an increase in the expansion of a bronchus or bronchial tubes.
Interacting selectively and non-covalently with a carbohydrate derivative.
Establishment of a structure near the basement membrane in adjacent Sertoli cells of the seminiferous epithelium for maintaining spermatogenesis. The structure consists of tight junctions, basal ectoplasmic specializations, and desmosome-like junctions.
Establishment of a structure near the basement membrane in adjacent Sertoli cells of the seminiferous epithelium for maintaining spermatogenesis. The structure consists of tight junctions, basal ectoplasmic specializations, and desmosome-like junctions.
Establishment of a structure near the basement membrane in adjacent Sertoli cells of the seminiferous epithelium for maintaining spermatogenesis. The structure consists of tight junctions, basal ectoplasmic specializations, and desmosome-like junctions.
The glycosylation of a protein by addition of N-acetylglucosamine via the O3 atom of peptidyl-threonine, forming O3-N-acetylglucosamine-L-threonine.
Catalysis of the reaction: histone H3 N6-acetyl-L-lysine (position 18) + H2O = histone H3 L-lysine (position 18) + acetate. This reaction requires the presence of NAD, and represents the removal of an acetyl group from lysine at position 18 of the histone H3 protein.
A protein complex that contains Mcm4, Mcm6, and Mcm7 proteins, and possesses DNA helicase activity. In the heterohexameric MCM complex, the Mcm4/6/7 proteins form a stable core, and Mcm2, Mcm3, and Mcm5 are more peripherally associated.
The process in which the migration of an axon growth cone of a sensory neuron is directed to a specific target site in response to a combination of attractive and repulsive cues. A sensory neuron is an afferent neuron conveying sensory impulses.
The process in which the migration of an axon growth cone of a spinal sensory neuron is directed to a specific target site in response to a combination of attractive and repulsive cues. A spinal sensory neuron is a sensory neuron that project to the spinal cord.
The process in which the migration of an axon growth cone of an interneuron is directed to a specific target site in response to a combination of attractive and repulsive cues. An interneuron is any neuron which is not motor or sensory. Interneurons may also refer to neurons whose axons remain within a particular brain region, as contrasted with projection neurons which have axons projecting to other brain regions.
The process in which the migration of an axon growth cone of a spinal cord interneuron is directed to a specific target site in response to a combination of attractive and repulsive cues. A spinal cord interneuron is a CNS interneuron located in the spinal cord.
The process in which the migration of an axon growth cone of a dorsal spinal cord interneuron is directed to a specific target site in response to a combination of attractive and repulsive cues. A dorsal spinal cord interneuron is an interneuron located in the dorsal part of the spinal cord.
The process in which the migration of an axon growth cone of a dorsal spinal cord interneuron is directed to a specific target site in the posterior direction along the anterior-posterior body axis in response to a combination of attractive and repulsive cues. The anterior-posterior axis is defined by a line that runs from the head or mouth of an organism to the tail or opposite end of the organism.
The process in which the migration of an axon growth cone of a dorsal spinal cord interneuron is directed to a specific target site in the anterior direction along the anterior-posterior body axis in response to a combination of attractive and repulsive cues. The anterior-posterior axis is defined by a line that runs from the head or mouth of an organism to the tail or opposite end of the organism.
Ovally-shaped membranous stack located inside the photoreceptor outer segment, and containing densely packed molecules of the photoreceptor protein rhodopsin that traverse the lipid bilayer. Disc membranes are apparently derived from the plasma membrane in the region of the cilium that connects the photoreceptor outer segment to the inner segment.
Catalysis of the reaction: a deoxynucleoside diphosphate + H2O = a deoxynucleotide + phosphate.
Catalysis of the reaction: dIDP + H2O = dIMP + phosphate.
The chemical reactions and pathways resulting in the formation of lipids, as carried out by individual cells.
The chemical reactions and pathways resulting in the formation of lipids, as carried out by individual cells.
The chemical reactions and pathways resulting in the formation of lipids, as carried out by individual cells.
The chemical reactions and pathways resulting in the formation of lipids, as carried out by individual cells.
A programmed necrotic cell death occurring as a result of a starvation stimulus (deprivation of nourishment).
A prolongation or process extending from a glial cell.
A prolongation or process extending from a glial cell.
Simple or compound process of epithelial glial cells with a spherical head that inserts into photoreceptor axons. Capitate projections have only been observed in Brachycera (flies).
The appearance of chemokine (C-C motif) ligand 19 (CCL19) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-C motif) ligand 19 (CCL19) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-C motif) ligand 19 (CCL19) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-C motif) ligand 19 (CCL19) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-C motif) ligand 19 (CCL19) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-C motif) ligand 21 (CCL21) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-X-C motif) ligand 12 (CXCL12) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-X-C motif) ligand 13 (CXCL13) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The appearance of chemokine (C-X-C motif) ligand 16 (CXCL16) due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.
The synthesis of telomeric repeat-containing RNA from a DNA template. A telomere is a complex of DNA and proteins that seals the end of a chromosome.
The synthesis of telomeric repeat-containing RNA from a DNA template by RNA polymerase II (Pol II), originating at a Pol II promoter.
The synthesis of telomeric repeat-containing RNA from a DNA template by RNA polymerase II (Pol II), originating at a Pol II promoter.
The synthesis of telomeric repeat-containing RNA from a DNA template by RNA polymerase II (Pol II), originating at a Pol II promoter.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-32 stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-17 stimulus.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-32 stimulus.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-17 stimulus.
A series of molecular signals initiated by the binding of interleukin-32 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of interleukin-32 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of interleukin-32 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of interleukin-17 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of interleukin-17 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by the binding of interleukin-17 to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
The acidification of the synaptic vesicle lumen via transport of protons into the vesicle. The resulting electrochemical gradient powers neurotransmitter loading.
The acidification of the synaptic vesicle lumen via transport of protons into the vesicle. The resulting electrochemical gradient powers neurotransmitter loading.
The orderly movement of a neuroblast from one site to another, often during the development of a multicellular organism or multicellular structure. A neuroblast is any cell that will divide and give rise to a neuron.
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 raffinose stimulus.
Small granular inclusions (about 1-3 microns in diameter) found in the anterior horn cells, and appearing either singly or in a group. Sometimes they are arranged in small beaded chains. Bunina bodies express cystatin C and consist of electron-dense amorphous material that contains tubules or vesicular structures. The amorphous material frequently includes a cytoplasmic island containing neurofilaments and other micro-organelles.
Cellular inclusion consisting of circular areas filled with fine slender filaments about 10 nanometers in diameter, delimited by a wall of varying complexity (either a single continuous membrane or a tubular network consisting of a fine filamentous material giving the wall a honeycomb appearance). Fibrillary inclusions are found in the cytoplasm of giant cells of Dieters in the lateral vestibular nucleus of the rat; similar structures have been described in the ventral cochlear nucleus, spinal cord, and substantia nigra.
Non-membrane-bound cytoplasmic inclusions composed of 10-40 nm granule-coated fibrils. These inclusions have an abnormal accumulation of alpha-synuclein protein and are found in association with multiple system atrophy.
Non-membrane-bound cytoplasmic inclusions composed of 10-40 nm granule-coated fibrils. These inclusions have an abnormal accumulation of alpha-synuclein protein and are found in association with multiple system atrophy.
The process in which a relatively unspecialized cell acquires specialized features of a hippocampal interneuron.
A series of molecular signals mediated by hypoxia-inducible factor (HIF1) in response to lowered oxygen levels (hypoxia). Under hypoxic conditions, the oxygen-sensitive alpha-subunit of hypoxia-inducible factor (HIF)-1 dimerizes with a HIF1-beta subunit (also called ARNT or aryl-hydrocarbon-receptor nuclear translocator), translocates to the nucleus and activates transcription of genes whose products participate in responding to hypoxia.
A series of molecular signals mediated by hypoxia-inducible factor (HIF1) in response to lowered oxygen levels (hypoxia). Under hypoxic conditions, the oxygen-sensitive alpha-subunit of hypoxia-inducible factor (HIF)-1 dimerizes with a HIF1-beta subunit (also called ARNT or aryl-hydrocarbon-receptor nuclear translocator), translocates to the nucleus and activates transcription of genes whose products participate in responding to hypoxia.
A series of molecular signals mediated by hypoxia-inducible factor (HIF1) in response to lowered oxygen levels (hypoxia). Under hypoxic conditions, the oxygen-sensitive alpha-subunit of hypoxia-inducible factor (HIF)-1 dimerizes with a HIF1-beta subunit (also called ARNT or aryl-hydrocarbon-receptor nuclear translocator), translocates to the nucleus and activates transcription of genes whose products participate in responding to hypoxia.
A glass-like, pale intracellular inclusion.
Cytoplasmic, spherical inclusion commonly found in damaged neurons, and composed of abnormally phosphorylated, neurofilament proteins aggregated with ubiquitin and alpha-synuclein.
Cytoplasmic inclusion, 5 to 15 micrometers in diameter, with a dense core surrounded by a halo of 10 to 20 nm wide radially oriented alpha-synuclein fibrils.
Cytoplasmic inclusion similar to a classical Lewy body but lacking a halo of protein fibrils.
Cytoplasmic inclusion found in neurons. It consists of filaments and granular materials, exhibits a dense core with a rough peripheral halo and lacks a limiting membrane. The filaments of these inclusions are composed of approximately 15-25 nm granule-coated fibrils in association with normal 10-nm neurofilaments.
Cytoplasmic, ball-like inclusion resembling a nucleolus and consisting of a convoluted network of electron-opaque strands embedded in a less dense matrix. It measures approximately 0.9 microns and lacks a limiting membrane. Its strands (diameter = 400-600 A) appear to be made of an entanglement of tightly packed filaments and particles approximately 25-50 A thick. Cytochemical studies suggest the presence of nonhistone proteins and some RNA. Usually only one such structure is present in a cell, and it appears to occur in most ganglion cells. Although they can be seen anywhere in the cell body, nematosomes are typically located in the perinuclear cytoplasm, where they are often associated with smooth-surfaced and coated vesicles.
Intracellular mass of paired, helically wound protein filaments (also called PHF) lying in the cytoplasm of neuronal cell bodies and neuritic cell processes. Neurofibrillary tangles contain an abnormally phosphorylated form of a microtubule-associated protein, tau. The shape of these inclusions may resemble a flame or a star.
Intracellular mass of paired, helically wound protein filaments (also called PHF) lying in the cytoplasm of neuronal cell bodies and neuritic cell processes. Neurofibrillary tangles contain an abnormally phosphorylated form of a microtubule-associated protein, tau. The shape of these inclusions may resemble a flame or a star.
Cellular inclusion composed of numerous tau fibrils arranged in a disorderly array. Tau protein is a major component, though Pick bodies also contain ubiquitin, alpha-synuclein, and apolipoprotein E.
Intracytoplasmic filamentous structure frequently encountered in preparations immunostained for ubiquitin.
The regrowth of lost or destroyed liver.
A network of fine tubules in the vicinity of the Golgi complex and around the centriole.
An organelle arrangement comprised of the following elements: a mitochondrion positioned near the presynaptic membrane; an electron-dense mitochondrial plaque adjacent to the outer mitochondrial membrane that faces the presynaptic membrane; filament-like elements appearing to link the mitochondrial plaque to a cell-cell junction region (sometimes termed punctum adherens); tubular or vesicular-appearing membrane (also called vesicular chain) interposed among the filaments. Mitochondrion-associated adherens complexes were initially described in the dorsal horn of the spinal cord. They are found in calyces and other large terminals of the auditory brainstem, and in a variety of mammalian species including humans.
An organelle arrangement comprised of the following elements: a mitochondrion positioned near the presynaptic membrane; an electron-dense mitochondrial plaque adjacent to the outer mitochondrial membrane that faces the presynaptic membrane; filament-like elements appearing to link the mitochondrial plaque to a cell-cell junction region (sometimes termed punctum adherens); tubular or vesicular-appearing membrane (also called vesicular chain) interposed among the filaments. Mitochondrion-associated adherens complexes were initially described in the dorsal horn of the spinal cord. They are found in calyces and other large terminals of the auditory brainstem, and in a variety of mammalian species including humans.
Dense particles of heterochromatin, consisting of a loosely twisted strand about 600 Angstrom thick, found associated with the nucleolus.
Any constituent part of the smooth endoplasmic reticulum (also called smooth ER, or SER).
An intermediate filament composed of glial fibrillary acidic protein (GFAP) and found in astrocytes.
An arrangement of closely apposed microtubules running parallel to each other.
The transfer of an assembled iron-sulfur cluster from a scaffold protein to an acceptor protein that contributes to the attainment of the full functional capacity of a protein.
Catalysis of the ligation of an amino acid to another amino acid via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate, carried out by a nonribosomal peptide synthase.
The directed movement of copper ions from outside of a cell, across an ascospore-type prospore membrane and into the cytosol.
The directed movement of copper ions from outside of a cell, across an ascospore-type prospore membrane and into the cytosol.
The directed movement of copper ions from outside of a cell, across an ascospore-type prospore membrane and into the cytosol.
Either of the ends of a mitotic spindle, a spindle that forms as part of mitosis, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.
The process in which a relatively unspecialized cell acquires specialized features of a hippocampal pyramidal neuron, a pyramidal cell of the hippocampus.
An electron dense body which may contain granules.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: succinate(out) + H+(out) = succinate(in) + H+(in).
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.
The dormancy process that results in entry into dormancy. Dormancy (sometimes called a dormant state) is a suspension of most physiological activity and growth that can be reactivated.
The dormancy process that results in an organism remaining in dormancy. Dormancy (sometimes called a dormant state) is a suspension of most physiological activity and growth that can be reactivated.
The dormancy process that results in exit from dormancy. Dormancy (sometimes called a dormant state) is a suspension of most physiological activity and growth that can be reactivated.
The process in which tolerance to severe drying is acquired, before entering into a dry, either dormant or quiescent state.
A dendrite that emerges near the apical pole of a neuron. In bipolar neurons, apical dendrites are located on the opposite side of the soma from the axon.
A dendrite that emerges near the basal pole of a neuron. In bipolar neurons, basal dendrites are either on the same side of the soma as the axon, or project toward the axon.
A dendrite of a hippocampal CA3 pyramidal cell.
A multivesicular body surrounded by and connected with multiple tubular compartments with associated vesicles.
A specialization of the endomembrane system found in some classes of dendritic spines consisting of two or more closely apposed lamellae with interspersed electron dense material.  The endomembrane component is continuous with the smooth endoplasmic reticulum.
Electron dense projection extending from the cytomatrix into the cytoplasm on which synaptic vesicles are tethered.
Electron dense projection extending from the cytomatrix into the cytoplasm on which synaptic vesicles are tethered.
A process in which a protein is transported to, and/or maintained in, a specific location in a eisosome filament (also called linear eisosome), a filamentous cortical structure formed, in S. pombe, by the eisosome component Pil1.
The entire complement of dendrites for a neuron, consisting of each primary dendrite and all its branches.
A configuration of neuron spines found on ciliary ganglion neurons in the embryonic and adult brain consisting of patches of closely spaced spines lying flat against the soma.
A prolongation or process extending from the soma of an astrocyte and wrapping around neurons.
A prolongation or process extending from the soma of an astrocyte and wrapping around neurons.
A prolongation or process extending from the soma of an astrocyte and wrapping around neurons.
Terminal process of astrocyte abutting non-neuronal surfaces in the brain.
Terminal process of astrocyte that extends to the surface of the central nervous system. Together, glial limiting end-feet form the glial limiting membrane or glia limitans.
A protein complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. The complex binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs and suppresses their translation by blocking the recruitment of the 43S ribosomal complex to m7G cap-bound eIF4G. In humans it includes RPL13A, EPRS, SYNCRIP and GAPDH; mouse complexes lack SYNCRIP.
A protein complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. The complex binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs and suppresses their translation by blocking the recruitment of the 43S ribosomal complex to m7G cap-bound eIF4G. In humans it includes RPL13A, EPRS, SYNCRIP and GAPDH; mouse complexes lack SYNCRIP.
Portion of the ensheathing process (either myelin or non-myelin) where the enveloping lips of the ensheathing cell come together so that their apposed plasma membranes run parallel to each other, separated by a cleft 12 nm wide.
Small finger-like extension of a Schwann cell that contacts the nodal membrane.
Paranodal terminations of Schwann cells that do not directly contact the paranodal axon membrane. Usually found in thicker myelin.
Portion of myelin-forming Schwann cell consisting of terminal cytoplasmic extensions adhered to the axon at the beginning and end of the myelin sheath.
Axon of dentate gyrus granule cell projecting to hippocampal area CA3, characterized by expansions (mossy fiber expansions) giving the fibers a mossy appearance. These unmyelinated axons were first described by Ramon y Cajal.
Any constituent part of a neuron, the basic cellular unit of nervous tissue. A typical neuron consists of a cell body (often called the soma), an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the nervous system.
Elongated neuronal process, often with side branches and more than one branching point, described in brains of patients with Parkinson's disease. Lewy neurites stain positively for ubiquitin in brainstem and forebrain regions affected in Parkinson's disease.
Spine-like process found on some neurons, e.g., periglomerular cells of olfactory cortex.
Large complex spine protruding from a dendrite. Each excrescence is formed by a cluster of spine heads.
Spine emanating from the cell soma of a neuron.
An ERAD pathway whereby endoplasmic reticulum (ER)-resident glycoproteins are targeted for degradation. Includes differential processing of the glycoprotein sugar chains, retrotranslocation to the cytosol and degradation by the ubiquitin-proteasome pathway. A glycoprotein is a compound in which a carbohydrate component is covalently bound to a protein component.
An ERAD pathway whereby endoplasmic reticulum (ER)-resident glycoproteins are targeted for degradation. Includes differential processing of the glycoprotein sugar chains, retrotranslocation to the cytosol and degradation by the ubiquitin-proteasome pathway. A glycoprotein is a compound in which a carbohydrate component is covalently bound to a protein component.
An ERAD pathway whereby endoplasmic reticulum (ER)-resident glycoproteins are targeted for degradation. Includes differential processing of the glycoprotein sugar chains, retrotranslocation to the cytosol and degradation by the ubiquitin-proteasome pathway. A glycoprotein is a compound in which a carbohydrate component is covalently bound to a protein component.
An ERAD pathway whereby endoplasmic reticulum (ER)-resident glycoproteins are targeted for degradation. Includes differential processing of the glycoprotein sugar chains, retrotranslocation to the cytosol and degradation by the ubiquitin-proteasome pathway. A glycoprotein is a compound in which a carbohydrate component is covalently bound to a protein component.
Terminal inflated portion of the axon of a non-glutamatergic neuron, containing the specialized apparatus necessary to release neurotransmitters at a regulatory synapse. The axon terminus is considered to be the whole region of thickening and the terminal bouton is a specialized region of it. Type III terminal boutons are larger than type II ones.
Cell death resulting from activation of endogenous cellular processes and occurring as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
Cell death resulting from activation of endogenous cellular processes and occurring as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
Cell death resulting from activation of endogenous cellular processes and occurring as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
Cell death resulting from activation of endogenous cellular processes and occurring as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
Cell death resulting from activation of endogenous cellular processes and occurring as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
Type of synapse characterized by an electron-dense ribbon, lamella (bar) or spherical body in the presynaptic process cytoplasm.
A synapse of a mossy fiber onto the dendrite of a granule cell; each mossy fiber can have up to 50 rosettes.
Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. This reaction requires the binding of a regulatory cyclin subunit and full activity requires stimulatory phosphorylation by a CDK-activating kinase (CAK).
Any apoptotic process in a retinal rod cell, one of the two photoreceptor cell types of the vertebrate retina.
Any apoptotic process in a retinal cone cell, one of the two photoreceptor cell types of the vertebrate retina.
The orderly movement of a motor neuron from one site to another. A motor neuron is an efferent neuron that passes from the central nervous system or a ganglion toward or to a muscle and conducts an impulse that causes movement.
The orderly movement of a spinal cord motor neuron from one site to another. A spinal cord motor neuron is a motor neuron that passes from the spinal cord toward or to a muscle and conducts an impulse that causes movement.
The orderly movement of a lateral motor column neuron from one site to another. A lateral motor column neuron is a motor neuron that is generated only on limb levels and send axons into the limb mesenchyme.
Any of the two layers of lipid molecules that constitute a membrane.
Any process in which a synaptic vesicle or vesicles are transported to, and/or maintained in, a specific location.
Any process in which a synaptic vesicle or vesicles are transported to, and/or maintained in, a specific location.
Any process in which a synaptic vesicle or vesicles are transported to, and/or maintained in, a specific location.
The directed movement of a synaptic vesicle or vesicles to a specific location.
A postsynaptic specialization that is part of a neuromuscular junction.
A postsynaptic specialization that is part of a neuromuscular junction.
Long distance growth of a single dendrite involved in cellular development.
The process in which the migration of a neuron projection is directed to a specific target site in response to a combination of attractive and repulsive cues.
The process in which the migration of a neuron projection is directed to a specific target site in response to a combination of attractive and repulsive cues.
The process in which the migration of a neuron projection is directed to a specific target site in response to a combination of attractive and repulsive cues.
The process in which the migration of a neuron projection is directed to a specific target site in response to a combination of attractive and repulsive cues.
The volume enclosed by the outermost membrane of a multivesicular body.
A membrane-bounded vesicle wholly contained within a multivesicular body.
The lipid bilayer surrounding a multivesicular body internal vesicle.
The volume enclosed by the membrane of the multivesicular body internal vesicle.
Long distance growth of a single sympathetic neuron projection involved in cellular development. A neuron projection is a prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
Long distance growth of a single sympathetic neuron projection involved in cellular development. A neuron projection is a prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
Long distance growth of a single sympathetic neuron projection involved in cellular development. A neuron projection is a prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
Long distance growth of a single sympathetic neuron projection involved in cellular development. A neuron projection is a prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
The process in which the migration of a sympathetic neuron projection is directed to a specific target site in response to a combination of attractive and repulsive cues.
The process in which the migration of a sympathetic neuron projection is directed to a specific target site in response to a combination of attractive and repulsive cues.
The process in which the migration of a sympathetic neuron projection is directed to a specific target site in response to a combination of attractive and repulsive cues.
The process in which the migration of a sympathetic neuron projection is directed to a specific target site in response to a combination of attractive and repulsive cues.
The chemotaxis process that directs the migration of a sympathetic neuron axon growth cone to a specific target site in response to a combination of attractive and repulsive cues.
The chemotaxis process that directs the migration of a sympathetic neuron axon growth cone to a specific target site in response to a combination of attractive and repulsive cues.
The chemotaxis process that directs the migration of a sympathetic neuron axon growth cone to a specific target site in response to a combination of attractive and repulsive cues.
The action of a molecule that contributes to the structural integrity of a complex or assembly within or outside a cell, providing elasticity and recoiling.
Any process that modulates the size of a vesicle.
A trimeric protein complex made up of an H-NS homodimer and an Hha monomer. In Enterobacteriaceae, this complex negatively regulates transcription of a range of genes.
A blood vessel lumenization process that occurs by blood vessel endothelial cells delaminating and aligning along the inner surface of an existing luminal space, extending the open ended lumen, and joining to other blood vessels to form a complete blood vessel.
The process of negative regulation of cell adhesion that results in blood vessel endothelial cells splitting off from an existing endothelial sheet.
Any endothelial tube morphogenesis process by which the tube is increased in length.
A process in which a protein is transported to, or maintained in, a location within a non-motile cilium.
A process in which a receptor is transported to, or maintained in, a location within a non-motile cilium.
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 disturbance in organismal or cellular homeostasis caused by a metal 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 disturbance in organismal or cellular homeostasis caused by a metal 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 disturbance in organismal or cellular homeostasis caused by a metal 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 disturbance in organismal or cellular homeostasis caused by a metal ion stimulus.
The covalent attachment of a mannose residue to a substrate molecule.
The covalent attachment of sialic acid to a substrate molecule.
Nuclear bodies frequently found near or associated with Cajal bodies (also called coiled bodies or CBs). Gemini of coiled bodies, or 'gems', are similar in size and shape to CBs, and often indistinguishable under the microscope. Unlike CBs, gems do not contain small nuclear ribonucleoproteins (snRNPs); they contain a protein called survivor of motor neurons (SMN) whose function relates to snRNP biogenesis. Gems are believed to assist CBs in snRNP biogenesis, and to play a role in the etiology of spinal muscular atrophy (SMA).
A ubiquitin ligase complex found to be involved in post-replicative bypass of UV-damaged DNA and UV mutagenesis. In S. cerevisiae, the complex contains the ubiquitin conjugating enzyme Rad6 and Rad18, a protein containing a RING finger motif and a nucleotide binding motif. The yeast Rad6-Rad18 heterodimer has ubiquitin conjugating activity, binds single-stranded DNA, and possesses single-stranded DNA-dependent ATPase activity.
DNA N-glycosylase activity acting on deaminated bases.
DNA N-glycosylase activity acting on deaminated bases.
DNA N-glycosylase activity acting on deaminated adenine (hypoxanthine).
DNA N-glycosylase activity acting on deaminated guanine (xanthine).
DNA N-glycosylase activity acting on deaminated guanine where the resulting base (oxanine) is generated by NO- or HNO2-induced nitrosative deamination.
A base-excision repair, AP site formation process occurring via excision of a deaminated base.
A branched cellular projection (or cytoplasmic extension) that is extended from the surface of a dendritic immune cell, and which enables the cell to sample luminal pathogens and increase the surface area for antigen presentation to T cells.
A cardiac myofibril is a myofibril specific to cardiac muscle cells.
A bipolar filament composed of myosin II molecules.
A specialized envelope lying outside the cell membrane of a spore derived from a product of meiosis.
A specialized envelope lying outside the cell membrane of a spore derived from an asexual process. Examples of this process are found in bacterial and fungal species.
A parallel bundle of actin filaments at the core of a microvillus.
An actin filament bundle 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.
An actin filament bundle in which the filaments are tightly packed (approximately 10-20 nm apart) and oriented with the same polarity.
A protein-DNA complex consisting of a higher-order oligomer of strand exchange proteins (recombinases) on single-stranded DNA.
A multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage.
A multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage.
A multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage.
A protein-DNA complex formed through interaction of the protein(s) with an interferon-stimulated response element (ISRE) in the DNA.
A protein-DNA-RNA complex composed of RNA polymerase, template DNA, and an RNA transcript.
A plasma membrane that is part of a sperm cell.
A ribonucleoprotein complex involved in formation of the spliceosome and composed of one or more snRNA and multiple protein components.
A spliceosomal snRNP complex containing U4 and U6 (or U4atac and U6atac) snRNAs and U5 snRNAs and associated proteins.
A series of molecular signals which triggers the necroptotic death of a cell. The pathway starts with reception of a signal, is characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3), and ends when the execution phase of necroptosis is triggered.
A series of molecular signals which triggers the necroptotic death of a cell. The pathway starts with reception of a signal, is characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3), and ends when the execution phase of necroptosis is triggered.
A series of molecular signals which triggers the necroptotic death of a cell. The pathway starts with reception of a signal, is characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3), and ends when the execution phase of necroptosis is triggered.
A series of molecular signals which triggers the necroptotic death of a cell. The pathway starts with reception of a signal, is characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3), and ends when the execution phase of necroptosis is triggered.
A stage of the necroptotic process that starts after a necroptotic signal has been relayed to the execution machinery. Key steps of the execution phase are swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. The execution phase ends when the cell has died.
A stage of the necroptotic process that starts after a necroptotic signal has been relayed to the execution machinery. Key steps of the execution phase are swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. The execution phase ends when the cell has died.
A stage of the necroptotic process that starts after a necroptotic signal has been relayed to the execution machinery. Key steps of the execution phase are swelling of organelles, minor ultrastructural modifications of the nucleus (specifically, dilatation of the nuclear membrane and condensation of chromatin into small, irregular, circumscribed patches) and increased cell volume (oncosis), culminating in the disruption of the plasma membrane and subsequent loss of intracellular contents. The execution phase ends when the cell has died.
The movement of a myeloid leukocyte within or between different tissues and organs of the body.
The movement of a granulocyte within or between different tissues and organs of the body.
The movement of a mast cell within or between different tissues and organs of the body.
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 disturbance in organismal or cellular homeostasis caused by the chemical structure of the anion portion of a dissociated acid (rather than the acid acting as a proton donor). The acid chemical may be in gaseous, liquid or solid form.
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 disturbance in organismal or cellular homeostasis caused by the chemical structure of the anion portion of a dissociated acid (rather than the acid acting as a proton donor). The acid chemical may be in gaseous, liquid or solid form.
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 disturbance in cellular homeostasis caused by the chemical structure of the anion portion of a dissociated acid (rather than the acid acting as a proton donor). The acid chemical may be in gaseous, liquid or solid form.
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 disturbance in cellular homeostasis caused by the chemical structure of the anion portion of a dissociated acid (rather than the acid acting as a proton donor). The acid chemical may be in gaseous, liquid or solid form.
The orderly movement of a lymphoid lineage cell from one site to another. A lymphoid lineage cell, also called a lymphoid lineage restricted progenitor cell, is a progenitor cell restricted to the lymphoid lineage.
The movement of a lymphoid lineage cell (also called a lymphoid lineage restricted progenitor cell) into the thymus. Lymphoid lineage cells enter and exit the thymus several times as part of this process.
The process in which the thymus epithelium is generated and organized.
A Y-shaped protein complex in the ciliary transition zone that connects the cilium axoneme to the ciliary necklace. Both protein sorting and protein gating occur at this point in the cilium allowing some, but not all proteins to enter the cilium.
A Y-shaped protein complex in the ciliary transition zone that connects the cilium axoneme to the ciliary necklace. Both protein sorting and protein gating occur at this point in the cilium allowing some, but not all proteins to enter the cilium.
A Y-shaped protein complex in the ciliary transition zone that connects the cilium axoneme to the ciliary necklace. Both protein sorting and protein gating occur at this point in the cilium allowing some, but not all proteins to enter the cilium.
A Y-shaped protein complex in the ciliary transition zone that connects the cilium axoneme to the ciliary necklace. Both protein sorting and protein gating occur at this point in the cilium allowing some, but not all proteins to enter the cilium.
A Y-shaped protein complex in the ciliary transition zone that connects the cilium axoneme to the ciliary necklace. Both protein sorting and protein gating occur at this point in the cilium allowing some, but not all proteins to enter the cilium.
A Y-shaped protein complex in the ciliary transition zone that connects the cilium axoneme to the ciliary necklace. Both protein sorting and protein gating occur at this point in the cilium allowing some, but not all proteins to enter the cilium.
A Y-shaped protein complex in the ciliary transition zone that connects the cilium axoneme to the ciliary necklace. Both protein sorting and protein gating occur at this point in the cilium allowing some, but not all proteins to enter the cilium.
A protein complex located on the cilium membrane in the ciliary transition zone; it is connected to the cilium axoneme via Y-shaped links.
A protein complex located on the cilium membrane in the ciliary transition zone; it is connected to the cilium axoneme via Y-shaped links.
A nine-bladed, propeller-like protein complex that links the distal end of the basal body and the cilium to the plasma membrane. Functions in protein sorting and gating (i.e. active and passive transport of proteins in and out of the cilium).
A nine-bladed, propeller-like protein complex that links the distal end of the basal body and the cilium to the plasma membrane. Functions in protein sorting and gating (i.e. active and passive transport of proteins in and out of the cilium).
A nine-bladed, propeller-like protein complex that links the distal end of the basal body and the cilium to the plasma membrane. Functions in protein sorting and gating (i.e. active and passive transport of proteins in and out of the cilium).
A nine-bladed, propeller-like protein complex that links the distal end of the basal body and the cilium to the plasma membrane. Functions in protein sorting and gating (i.e. active and passive transport of proteins in and out of the cilium).
A nine-bladed, propeller-like protein complex that links the distal end of the basal body and the cilium to the plasma membrane. Functions in protein sorting and gating (i.e. active and passive transport of proteins in and out of the cilium).
A nine-bladed, propeller-like protein complex that links the distal end of the basal body and the cilium to the plasma membrane. Functions in protein sorting and gating (i.e. active and passive transport of proteins in and out of the cilium).
A nine-bladed, propeller-like protein complex that links the distal end of the basal body and the cilium to the plasma membrane. Functions in protein sorting and gating (i.e. active and passive transport of proteins in and out of the cilium).
A nine-bladed, propeller-like protein complex that links the distal end of the basal body and the cilium to the plasma membrane. Functions in protein sorting and gating (i.e. active and passive transport of proteins in and out of the cilium).
A nine-bladed, propeller-like protein complex that links the distal end of the basal body and the cilium to the plasma membrane. Functions in protein sorting and gating (i.e. active and passive transport of proteins in and out of the cilium).
A nine-bladed, propeller-like protein complex that links the distal end of the basal body and the cilium to the plasma membrane. Functions in protein sorting and gating (i.e. active and passive transport of proteins in and out of the cilium).
A nine-bladed, propeller-like protein complex that links the distal end of the basal body and the cilium to the plasma membrane. Functions in protein sorting and gating (i.e. active and passive transport of proteins in and out of the cilium).
Part of the axoneme consisting of the inner two microtubule doublets of the 9+2 axoneme occurring in most motile cilia.
Part of the axoneme consisting of the inner two microtubule doublets of the 9+2 axoneme occurring in most motile cilia.
Part of the axoneme consisting of the inner two microtubule doublets of the 9+2 axoneme occurring in most motile cilia.
Part of the axoneme consisting of the inner two microtubule doublets of the 9+2 axoneme occurring in most motile cilia.
Part of the axoneme consisting of the inner two microtubule doublets of the 9+2 axoneme occurring in most motile cilia.
Part of the axoneme consisting of a highly electron-dense region at the distal end of the ciliary transition zone within the axonemal lumen at which the axonemal central pair of microtubules is connected to the rest of the axonemal structure.
Part of the axoneme consisting of a highly electron-dense region at the distal end of the ciliary transition zone within the axonemal lumen at which the axonemal central pair of microtubules is connected to the rest of the axonemal structure.
Part of the cilium where the axoneme ends. The ciliary tip has been implicated in ciliary assembly and disassembly, as well as signal transduction.
Part of the cilium where the axoneme ends. The ciliary tip has been implicated in ciliary assembly and disassembly, as well as signal transduction.
Part of the cilium where the axoneme ends. The ciliary tip has been implicated in ciliary assembly and disassembly, as well as signal transduction.
Part of the cilium where the axoneme ends. The ciliary tip has been implicated in ciliary assembly and disassembly, as well as signal transduction.
Proximal part of the ciliary shaft to which the inversin protein (also called Inv) specifically localizes. The inversin compartment appears to have a different protein composition than the rest of the cilium, although there is no structure that separates it form the distal part of the cilium.
Proximal part of the ciliary shaft to which the inversin protein (also called Inv) specifically localizes. The inversin compartment appears to have a different protein composition than the rest of the cilium, although there is no structure that separates it form the distal part of the cilium.
Proximal part of the ciliary shaft to which the inversin protein (also called Inv) specifically localizes. The inversin compartment appears to have a different protein composition than the rest of the cilium, although there is no structure that separates it form the distal part of the cilium.
Proximal part of the ciliary shaft to which the inversin protein (also called Inv) specifically localizes. The inversin compartment appears to have a different protein composition than the rest of the cilium, although there is no structure that separates it form the distal part of the cilium.
Proximal part of the ciliary shaft to which the inversin protein (also called Inv) specifically localizes. The inversin compartment appears to have a different protein composition than the rest of the cilium, although there is no structure that separates it form the distal part of the cilium.
Proximal part of the ciliary shaft to which the inversin protein (also called Inv) specifically localizes. The inversin compartment appears to have a different protein composition than the rest of the cilium, although there is no structure that separates it form the distal part of the cilium.
The mid part of a cilium between the ciliary base and ciliary tip that extends into the extracellular space.
The mid part of a cilium between the ciliary base and ciliary tip that extends into the extracellular space.
The mid part of a cilium between the ciliary base and ciliary tip that extends into the extracellular space.
The mid part of a cilium between the ciliary base and ciliary tip that extends into the extracellular space.
Part of an axoneme consisting in a doublet microtubule. Nine of these outer doublets form the 9+0 axoneme, while the 9+2 axoneme also contains a central pair. Dynein arms attached to the doublets provide the mechanism of movement of the cilium.
Part of an axoneme consisting in a doublet microtubule. Nine of these outer doublets form the 9+0 axoneme, while the 9+2 axoneme also contains a central pair. Dynein arms attached to the doublets provide the mechanism of movement of the cilium.
Part of an axoneme consisting in a doublet microtubule. Nine of these outer doublets form the 9+0 axoneme, while the 9+2 axoneme also contains a central pair. Dynein arms attached to the doublets provide the mechanism of movement of the cilium.
Area of the cilium (also called flagellum) where the basal body and the axoneme are anchored to the plasma membrane. The ciliary base encompasses the distal part of the basal body, transition fibers and transition zone and is structurally and functionally very distinct from the rest of the cilium. In this area proteins are sorted and filtered before entering the cilium, and many ciliary proteins localize specifically to this area.
Area of the cilium (also called flagellum) where the basal body and the axoneme are anchored to the plasma membrane. The ciliary base encompasses the distal part of the basal body, transition fibers and transition zone and is structurally and functionally very distinct from the rest of the cilium. In this area proteins are sorted and filtered before entering the cilium, and many ciliary proteins localize specifically to this area.
Area of the cilium (also called flagellum) where the basal body and the axoneme are anchored to the plasma membrane. The ciliary base encompasses the distal part of the basal body, transition fibers and transition zone and is structurally and functionally very distinct from the rest of the cilium. In this area proteins are sorted and filtered before entering the cilium, and many ciliary proteins localize specifically to this area.
Area of the cilium (also called flagellum) where the basal body and the axoneme are anchored to the plasma membrane. The ciliary base encompasses the distal part of the basal body, transition fibers and transition zone and is structurally and functionally very distinct from the rest of the cilium. In this area proteins are sorted and filtered before entering the cilium, and many ciliary proteins localize specifically to this area.
A cytoplasmic vesicle composed of both tubulovesicular and clear core vesicles that transport synaptic vesicle-associated proteins. Proteins carried by synaptic vesicle protein transport vesicles (STVs) include synaptophysin, synapsin Ia, synaptotagmin and synaptobrevin/vesicle-associated membrane protein 2 (VAMP2). STVs are packaged via the trans-Golgi network before being transported through the axon.
The controlled shedding of a seed.
Any process that stops, prevents, or reduces the frequency, rate or extent of transcription by chromatin organization.
A protein-DNA complex composed of proteins binding promoter DNA to form the transcriptional preinitiation complex (PIC), the formation of which is a prerequisite for transcription.
A protein-DNA complex composed of proteins binding promoter DNA to form the transcriptional preinitiation complex (PIC), the formation of which is a prerequisite for transcription.
A protein-DNA complex composed of proteins binding promoter DNA to form the transcriptional preinitiation complex (PIC), the formation of which is a prerequisite for transcription.
A protein-DNA complex composed of proteins binding promoter DNA to form the transcriptional preinitiation complex (PIC), the formation of which is a prerequisite for transcription.
A protein-DNA complex composed of proteins binding promoter DNA to form the transcriptional preinitiation complex (PIC), the formation of which is a prerequisite for transcription.
The repair of double-strand breaks in mitochondrial DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
The repair of a double-strand break in mitochondrial DNA in which the broken DNA molecule is repaired using homologous sequences.
A process in which a calcium ion is transported from one side of a membrane to the other into the cytosol by means of some agent such as a transporter or pore.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It originates at the left anterior basal body, extends laterally through the cytoplasm, crosses the right anterior axoneme, and exits as a membrane-bound flagellum on the anterior left side of the cell.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It originates at the right anterior basal body, extends laterally through the cytoplasm, crosses the left anterior axoneme, and exits as a membrane-bound flagellum on the anterior right side of the cell.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It is nucleated by the left posteriolateral basal body and extends cytoplasmically toward the cell posterior, marking the left anterior boundary of the lateral shield and the left lateral region of the funis before exiting at the left lateral region of the cell body.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It is nucleated by the left posteriolateral basal body and extends cytoplasmically toward the cell posterior, marking the left anterior boundary of the lateral shield and the left lateral region of the funis before exiting at the left lateral region of the cell body.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It is nucleated by the left posteriolateral basal body and extends cytoplasmically toward the cell posterior, marking the left anterior boundary of the lateral shield and the left lateral region of the funis before exiting at the left lateral region of the cell body.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It is nucleated by the right posteriolateral basal body and extends cytoplasmically toward the cell posterior, marking the right anterior boundary of the lateral shield and the right lateral region of the funis before exiting at the right lateral region of the cell body.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It is nucleated by the right posteriolateral basal body and extends cytoplasmically toward the cell posterior, marking the right anterior boundary of the lateral shield and the right lateral region of the funis before exiting at the right lateral region of the cell body.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It is nucleated by the right posteriolateral basal body and extends cytoplasmically toward the cell posterior, marking the right anterior boundary of the lateral shield and the right lateral region of the funis before exiting at the right lateral region of the cell body.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It is nucleated by the left ventral basal body and exits the cell body proximally and dorsal to the ventral disc.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It is nucleated by the right ventral basal body and exits the cell body proximally and dorsal to the ventral disc.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It is nucleated by the left caudal basal body, extending cytoplasmically and exiting at the posterior end of the cell body.
A cilium (also called flagellum) found in Giardia species (trophozoite stage). It is nucleated by the right caudal basal body, extending cytoplasmically and exiting at the posterior end of the cell body.
Set of two basal bodies found in Giardia species (trophozoite stage). It comprises the anterior and ventral basal bodies located to the right of the left nucleus of the trophozoite when viewed dorsally.
Set of two basal bodies found in Giardia species (trophozoite stage). It comprises the caudal and posteriolateral basal bodies located to the right of the left nucleus of the trophozoite when viewed dorsally.
Set of two basal bodies found in Giardia species (trophozoite stage). It comprises the anterior and ventral basal bodies located to the left of the right nucleus of the trophozoite when viewed dorsally.
Set of two basal bodies found in Giardia species (trophozoite stage). It comprises the caudal and posteriolateral basal bodies located to the left of the right nucleus of the trophozoite when viewed dorsally.
Set of four basal bodies found in Giardia species (trophozoite stage). It comprises the left lateral basal body pair and the left middle basal body pair (i.e. the anterior, ventral, caudal and posteriolateral basal bodies located to the right of the left nucleus of the trophozoite when viewed dorsally).
Set of four basal bodies found in Giardia species (trophozoite stage). It comprises the right lateral basal body pair and the right middle basal body pair (i.e. the anterior, ventral, caudal and posteriolateral basal bodies located to the left of the right nucleus of the trophozoite when viewed dorsally).
A non-membrane bound, semi-organized microtubule array of unknown function found in Giardia species (trophozoite stage). It is located on the dorsal side of the trophozoite, slightly posterior to the ventral disc.
Region of the ventral side of the cell body found in Giardia species (trophozoite stage). It is located posterior on either side of the ventral groove; the upper boundary is the ventral disc, and the lower boundary is marked by the posteriolateral flagella.
The specialized envelope lying outside the cell membrane of a cyst. A cyst is a resting or dormant stage of a microorganism, usually a bacterium or a protist or rarely an invertebrate animal, that helps the organism to survive in unfavorable environmental conditions. In protists such as protozoan parasites alternating cystic- and non-cystic stages, the cyst wall is usually composed of carbohydrates and proteins.
One of the two nuclei found in Giardia species (trophozoite stage). It is located on the left side of the cell when viewed from the dorsal side.
One of the two nuclei found in Giardia species (trophozoite stage). It is located on the right side of the cell when viewed from the dorsal side.
Catalysis of the reaction: protein-S-S-glutathione + glutathione-SH = protein-SH + glutathione-S-S-glutathione.
The region of a polarized cell other than its tips or ends (in some cell types, one end may be called the apex and the other the base). For example, in a polarized epithelial cell, the lateral part includes the cell sides which interface adjacent cells.
The region directly beneath the plasma membrane of the lateral portion of the cell.
Merging of two or more vacuoles, or of vacuoles and vesicles within a cell to form a single larger vacuole.
The process of binding or confining iron ions such that they are separated from other components of a biological system.
The process of binding or confining iron ions such that they are separated from other components of a biological system.
The process of binding or confining iron ions such that they are separated from other components of a biological system.
The process of binding or confining iron ions such that they are separated from other components of a biological system.
The process of binding or confining iron ions such that they are separated from other components of a biological system.
The process of binding or confining iron ions such that they are separated from other components of a biological system.
The process of binding or confining iron ions such that they are separated from other components of a biological system.
The process of binding or confining copper ions such that they are separated from other components of a biological system.
The process of binding or confining copper ions such that they are separated from other components of a biological system.
The process of binding or confining copper ions such that they are separated from other components of a biological system.
The process of binding or confining copper ions such that they are separated from other components of a biological system.
The process of binding or confining copper ions such that they are separated from other components of a biological system.
The process of binding or confining copper ions such that they are separated from other components of a biological system.
The process of binding or confining copper ions such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an extracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an intracellular area such that they are separated from other components of a biological system.
The process of binding or confining copper ions in an intracellular area such that they are separated from other components of a biological system.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lamellipodium. A lamellipodium is a thin sheetlike process extended by the leading edge of a crawling fibroblast; contains a dense meshwork of actin filaments.
A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt1p-Pmt2p.
A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt1p-Pmt3p.
A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt5p-Pmt2p.
A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt5p-Pmt3p.
A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt4p.
A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt4p.
A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt4p.
A heterodimer involved in the recognition of base-base and small insertion/deletion mismatches. In S. cerevisiae the complex consists of two subunits, Mlh1 and Mlh3.
Cell motility due to movement of bacterial- or archaeal-type flagella.
A non-membrane-bounded organelle superficially similar to a bacterial-type flagellum; they both consist of filaments extending outside the cell, and rotate to propel the cell, but the archaeal flagella (also called archaella) have a unique structure which lacks a central channel. Similar to bacterial type IV pilins, the archaeal flagellins (archaellins) are made with class 3 signal peptides and they are processed by a type IV prepilin peptidase-like enzyme. The archaellins are typically modified by the addition of N-linked glycans which are necessary for proper assembly and/or function.
A non-membrane-bounded organelle superficially similar to a bacterial-type flagellum; they both consist of filaments extending outside the cell, and rotate to propel the cell, but the archaeal flagella (also called archaella) have a unique structure which lacks a central channel. Similar to bacterial type IV pilins, the archaeal flagellins (archaellins) are made with class 3 signal peptides and they are processed by a type IV prepilin peptidase-like enzyme. The archaellins are typically modified by the addition of N-linked glycans which are necessary for proper assembly and/or function.
A non-membrane-bounded organelle superficially similar to a bacterial-type flagellum; they both consist of filaments extending outside the cell, and rotate to propel the cell, but the archaeal flagella (also called archaella) have a unique structure which lacks a central channel. Similar to bacterial type IV pilins, the archaeal flagellins (archaellins) are made with class 3 signal peptides and they are processed by a type IV prepilin peptidase-like enzyme. The archaellins are typically modified by the addition of N-linked glycans which are necessary for proper assembly and/or function.
Cell motility due to the motion of one or more archaeal-type flagella. An archaeal-type flagellum (also called archaellum) is a non-membrane-bounded organelle superficially similar to a bacterial-type flagellum, but having a different molecular structure and lacking a central channel.
Fibrillar repetitive structure surrounding the ventral disc edge in Giardia species (trophozoite stage). The composition of the lateral crest is not fully known yet.
Fibrillar repetitive structure surrounding the ventral disc edge in Giardia species (trophozoite stage). The composition of the lateral crest is not fully known yet.
A region of the ventral disc of Giardia species (trophozoite stage) where two portions of the same array of microtubules overlap (the microtubule array makes a complete circle and overlaps on itself).
A region of the ventral disc of Giardia species (trophozoite stage) where two portions of the same array of microtubules overlap (the microtubule array makes a complete circle and overlaps on itself).
A part of the ventral disc of Giardia species (trophozoite stage) consisting of a spiral array of microtubules linked to the ventral membrane. These microtubules form the base of the ventral disc dorsal microribbons that extend nearly perpendicular from the membrane.
A part of the ventral disc of Giardia species (trophozoite stage) consisting of a spiral array of microtubules linked to the ventral membrane. These microtubules form the base of the ventral disc dorsal microribbons that extend nearly perpendicular from the membrane.
A part of the ventral disc of Giardia species (trophozoite stage) consisting of a spiral array of microtubules linked to the ventral membrane. These microtubules form the base of the ventral disc dorsal microribbons that extend nearly perpendicular from the membrane.
Trilaminar structure extending perpendicularly into the cytoplasm along the length of ventral disc microtubules in Giardia species (trophozoite stage). Constituents of dorsal microribbons (also called dorsal ribbons or microribbons) include alpha-coiled-helix proteins approximately 29 to 38 kDa in size. These proteins line the edges of the microribbons but are not found in microtubules. Tubulins are not found in microribbons.
Trilaminar structure extending perpendicularly into the cytoplasm along the length of ventral disc microtubules in Giardia species (trophozoite stage). Constituents of dorsal microribbons (also called dorsal ribbons or microribbons) include alpha-coiled-helix proteins approximately 29 to 38 kDa in size. These proteins line the edges of the microribbons but are not found in microtubules. Tubulins are not found in microribbons.
Trilaminar structure extending perpendicularly into the cytoplasm along the length of ventral disc microtubules in Giardia species (trophozoite stage). Constituents of dorsal microribbons (also called dorsal ribbons or microribbons) include alpha-coiled-helix proteins approximately 29 to 38 kDa in size. These proteins line the edges of the microribbons but are not found in microtubules. Tubulins are not found in microribbons.
Trilaminar structure extending perpendicularly into the cytoplasm along the length of ventral disc microtubules in Giardia species (trophozoite stage). Constituents of dorsal microribbons (also called dorsal ribbons or microribbons) include alpha-coiled-helix proteins approximately 29 to 38 kDa in size. These proteins line the edges of the microribbons but are not found in microtubules. Tubulins are not found in microribbons.
Structure horizontally linking adjacent microribbons of the ventral disc in Giardia species (trophozoite stage). The composition of crossbridges is not fully known yet.
Structure horizontally linking adjacent microribbons of the ventral disc in Giardia species (trophozoite stage). The composition of crossbridges is not fully known yet.
A partial left-handed spiral array of microtubules that lies generally dorsal to the main ventral disc microtubule array in Giardia species (trophozoite stage).
A partial left-handed spiral array of microtubules that lies generally dorsal to the main ventral disc microtubule array in Giardia species (trophozoite stage).
Specialized organelle found in Giardia species (trophozoite stage) and characterized by a spiral array of microtubules and microtubule-associated structures including dorsal microribbons and crossbridges. The edge of the ventral disc narrows into a lateral crest. The ventral disk mediates mechanical attachment of the trophozoite to the host's intestinal wall, and contains the contractile proteins actinin, alpha-actinin, myosin, and tropomyosin working towards contraction of the disk involved in adherence.
Specialized organelle found in Giardia species (trophozoite stage) and characterized by a spiral array of microtubules and microtubule-associated structures including dorsal microribbons and crossbridges. The edge of the ventral disc narrows into a lateral crest. The ventral disk mediates mechanical attachment of the trophozoite to the host's intestinal wall, and contains the contractile proteins actinin, alpha-actinin, myosin, and tropomyosin working towards contraction of the disk involved in adherence.
Specialized organelle found in Giardia species (trophozoite stage) and characterized by a spiral array of microtubules and microtubule-associated structures including dorsal microribbons and crossbridges. The edge of the ventral disc narrows into a lateral crest. The ventral disk mediates mechanical attachment of the trophozoite to the host's intestinal wall, and contains the contractile proteins actinin, alpha-actinin, myosin, and tropomyosin working towards contraction of the disk involved in adherence.
A small amount of cytoplasm surrounded by a cell membrane that is generally retained in spermatozoa after spermiogenesis, when the majority of the cytoplasm is phagocytosed by Sertoli cells to produce "residual bodies". Initially, the droplet is located at the neck just behind the head of an elongated spermatid. During epididymal transit, the cytoplasmic droplet migrates caudally to the annulus at the end of the midpiece; the exact position and time varies by species. The cytoplasmic droplet consists of lipids, lipoproteins, RNAs, a variety of hydrolytic enzymes, receptors, ion channels, and Golgi-derived vesicles. The droplet may be involved in regulatory volume loss (RVD) at ejaculation, and in most species, though not in humans, the cytoplasmic droplet is lost at ejaculation. Note that the cytoplasmic droplet is distinct from "excessive residual cytoplasm" that sometimes remains in epididymal spermatozoa, particularly when spermiogenesis has been disrupted.
Catalysis of the hydrolysis of xylans, homopolysaccharides composed of xylose residues.
A xylanase activity that acts on one of the ends of a xylan polymer which does not contain side chains.
A retina homeostatic process preventing the degeneration of a retina blood vessel.
A retina homeostatic process preventing the degeneration of a retina blood vessel.
A retina homeostatic process preventing the degeneration of a retina blood vessel.
Interacting selectively and non-covalently with any member of the cullin family, hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3).
Enables the transmembrane transfer of an ion by a channel that opens in response to a temperature stimulus (e.g. exposure to a temperature range different than the optimal temperature for that organism).
Enables the transmembrane transfer of an ion by a channel that opens in response to a temperature stimulus (e.g. exposure to a temperature range different than the optimal temperature for that organism).
Enables the transmembrane transfer of an ion by a channel that opens in response to a temperature stimulus (e.g. exposure to a temperature range different than the optimal temperature for that organism).
Enables the transmembrane transfer of an ion by a channel that opens in response to a temperature stimulus (e.g. exposure to a temperature range different than the optimal temperature for that organism).
Enables the transmembrane transfer of a cation by a channel that opens in response to a temperature stimulus (e.g. exposure to a temperature range different than the optimal temperature for that organism).
Enables the transmembrane transfer of a cation by a channel that opens in response to a temperature stimulus (e.g. exposure to a temperature range different than the optimal temperature for that organism).
Enables the transmembrane transfer of a cation by a channel that opens in response to a temperature stimulus (e.g. exposure to a temperature range different than the optimal temperature for that organism).
Enables the transmembrane transfer of a cation by a channel that opens in response to a temperature stimulus (e.g. exposure to a temperature range different than the optimal temperature for that organism).
A motile cilium found in dinoflagellates. It coils around the cell and provides the forward thrust for motility. It is often contained in a furrow called the cingulum, and emerges from a flagellar pore located in the cingulum.
A motile cilium found in dinoflagellates. It trails the cell and acts as a steering rudder. It is often partially contained in a furrow called the sulcus, and emerges from a flagellar pore located in the sulcus.
A furrow that may be found on the cell surface. Examples include the cingulum and sulcus found in some dinoflagellates.
A furrow that may be found on the cell surface. Examples include the cingulum and sulcus found in some dinoflagellates.
A furrow that may be found on the cell surface. Examples include the cingulum and sulcus found in some dinoflagellates.
A cell surface furrow that wraps around a dinoflagellate cell; the transverse flagellum lies in it.
A cell surface furrow that wraps around a dinoflagellate cell; the transverse flagellum lies in it.
A cell surface furrow that wraps around a dinoflagellate cell; the transverse flagellum lies in it.
A cell surface furrow that occurs on the ventral side of a dinoflagellate cell. It partially houses the longitudinal flagellum. The sulcus intersects with the cingulum on the ventral side of a dinoflagellate cell.
A cell surface furrow that occurs on the ventral side of a dinoflagellate cell. It partially houses the longitudinal flagellum. The sulcus intersects with the cingulum on the ventral side of a dinoflagellate cell.
A cell surface furrow that occurs on the ventral side of a dinoflagellate cell. It partially houses the longitudinal flagellum. The sulcus intersects with the cingulum on the ventral side of a dinoflagellate cell.
The part of a dinoflagellate cell above the cingulum; also referred to as the anterior portion of a dinoflagellate cell. It is separated from the hypocone by the cingulum.
The part of a dinoflagellate cell above the cingulum; also referred to as the anterior portion of a dinoflagellate cell. It is separated from the hypocone by the cingulum.
The part of a dinoflagellate cell above the cingulum; also referred to as the anterior portion of a dinoflagellate cell. It is separated from the hypocone by the cingulum.
The part of a dinoflagellate cell below the cingulum; also referred to as the posterior portion of a dinoflagellate cell. It is separated from the epicone by the cingulum.
The part of a dinoflagellate cell below the cingulum; also referred to as the posterior portion of a dinoflagellate cell. It is separated from the epicone by the cingulum.
The part of a dinoflagellate cell below the cingulum; also referred to as the posterior portion of a dinoflagellate cell. It is separated from the epicone by the cingulum.
The process in which an organism effects a change in the type IV pilus-dependent motility of a symbiont organism (i.e. the controlled movement of a bacterial cell which is dependent on the presence of type IV pili, and which includes social gliding motility and twitching motility). The symbiont is defined as the smaller of the organisms involved in a symbiotic interaction.
Any process in which an organism activates, maintains or increases the frequency, rate or extent of the type IV pilus-dependent motility of a symbiont organism (i.e. the controlled movement of a bacterial cell which is dependent on the presence of type IV pili, and which includes social gliding motility and twitching motility). The symbiont is defined as the smaller of the organisms involved in a symbiotic interaction.
A nucleic acid binding activity that brings together complementary sequences of nucleic acids so that they pair by hydrogen bonds to form a double-stranded polynucleotide.
A dinoflagellate sulcus that extends all the way to the posterior end of the cell (also known as antapex). The presence of a sulcal notch makes the dinoflagellate hypocone appear bilobed.
A dinoflagellate sulcus that extends all the way to the posterior end of the cell (also known as antapex). The presence of a sulcal notch makes the dinoflagellate hypocone appear bilobed.
A protein complex that acts as a protein trafficking machinery and is responsible for the export of proteins across the parasitophorous (symbiont-containing) vacuolar membrane and into the human host cell. The PTEX complex is located in the vacuole membrane. It is ATP-powered, and comprises heat shock protein 101 (HSP101; a ClpA/B-like ATPase from the AAA+ superfamily, of a type commonly associated with protein translocons), a parasite protein termed PTEX150, and exported protein 2 (EXP2). EXP2 is the potential channel, as it is the membrane-associated component of the core PTEX complex. Two other proteins, PTEX88 and thioredoxin 2 (TRX2), were also identified as PTEX components.
Catalysis of the reaction: (R)-2-hydroxy-2-phenylacetate + acceptor = phenylglyoxylate + reduced acceptor.
Catalysis of the reaction: RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2.
The successive addition of amino acid residues to a nascent polypeptide chain, proceeding through regions of multiple repeated proline codons, during protein biosynthesis in the cytoplasm.
The directed movement of potassium ions from inside of a cell, across the plasma membrane and into the extracellular region.
The directed movement of potassium ions from inside of a cell, across the plasma membrane and into the extracellular region.
The directed movement of potassium ions from inside of a cell, across the plasma membrane and into the extracellular region.
The directed movement of UDP-galactose into the Golgi lumen across the Golgi membrane.
Enables the transfer of basic amino acids from one side of a membrane to the other. Basic amino acids have a pH above 7. In low-affinity transport the transporter is able to bind the solute only if it is present at very high concentrations.
Enables the transfer of L-arginine from one side of a membrane to the other. In low-affinity transport the transporter is able to bind the solute only if it is present at very high concentrations.
Enables the transfer of L-ornithine from one side of a membrane to the other. In high-affinity transport the transporter is able to bind the solute even if it is only present at very low concentrations.
The orderly movement of a distal tip cell.
The component of the omegasome 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 omegasome 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 omegasome 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 omegasome 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 omegasome 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 phagophore assembly site 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 phagophore assembly site 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 phagophore assembly site 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 phagophore assembly site 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 phagophore assembly site 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 phagophore assembly site 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 autophagosome 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 autophagosome 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 autophagosome 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 autophagosome 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 autophagosome 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 autophagosome 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 autophagosome 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 autophagosome 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 directed movement of L-arginine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-arginine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-arginine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-arginine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-lysine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-lysine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-ornithine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-ornithine from outside of a cell, across the plasma membrane and into the cytosol.
Catalysis of the reaction: 2-oxoglutarate (alpha-ketoglutarate) + O2 + xanthine = CO2 + succinate + urate.
Catalysis of the reaction: 2-oxoglutarate (alpha-ketoglutarate) + O2 + xanthine = CO2 + succinate + urate.
Catalysis of the reaction: 2-oxoglutarate (alpha-ketoglutarate) + O2 + xanthine = CO2 + succinate + urate.
Combining with any member of the calcitonin family (e.g. adrenomedullin, adrenomedullin 2 (intermedin), amylin, calcitonin and calcitonin gene-related peptides (CGRPs)) to initiate a change in cell activity.
Combining with amylin to initiate a change in cell activity.
Interacting selectively and non-covalently with any member of the calcitonin family (e.g. adrenomedullin, adrenomedullin 2 (intermedin), amylin, calcitonin and calcitonin gene-related peptides (CGRPs)).
Interacting selectively and non-covalently with amylin.
A series of molecular signals initiated by an extracellular member of the calcitonin family (e.g. adrenomedullin, adrenomedullin 2 (intermedin), amylin, calcitonin and calcitonin gene-related peptides (CGRPs)) combining with a calcitonin family receptor on the surface of the target cell. Calcitonin family receptors may form dimers, trimers or tetramers; adrenomedullin and amylin receptors have only been observed as dimers so far.
A series of molecular signals initiated by an extracellular amylin combining with a dimeric amylin receptor on the surface of the target cell.
A protein complex that contains G protein-coupled receptors.
A complete microtubule with 13 protofilaments that fuses with an incomplete microtubule called B tubule (containing 10 protofilaments only) to form an axonemal outer doublet. Inner and outer dynein arms, as well as the radial spoke, are attached to the A tubule.
An incomplete microtubule containing 10 protofilaments that fuses with a complete microtubule called A tubule (containing 13 protofilaments) to form an axonemal outer doublet.
A phosphatidylinositol 3-kinase complex that contains a catalytic and a regulatory subunit of a phosphatidylinositol 3-kinase (PI3K) enzyme, plus one or more adaptor proteins. Class I PI3Ks phosphorylate phosphatidylinositol [PI], phosphatidylinositol-4-phosphate [PI(4)P] and phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2], and are divided into subclasses A and B according to the type of adaptor subunit with which they associate. The class I PI3K subfamily of genes comprises members in vertebrates, worm and fly, but none in yeast.
A phosphatidylinositol 3-kinase complex that contains a catalytic and a regulatory subunit of a phosphatidylinositol 3-kinase (PI3K) enzyme, plus one or more adaptor proteins. Class I PI3Ks phosphorylate phosphatidylinositol [PI], phosphatidylinositol-4-phosphate [PI(4)P] and phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2], and are divided into subclasses A and B according to the type of adaptor subunit with which they associate. The class I PI3K subfamily of genes comprises members in vertebrates, worm and fly, but none in yeast.
A phosphatidylinositol 3-kinase complex that contains a catalytic subunit of a phosphatidylinositol 3-kinase (PI3K) enzyme and one or more adaptor proteins. There is no known obligatory regulatory subunit. The class II PI3K (PI3KC2) subfamily of genes has members in vertebrates, worm and fly, but none in yeast.
A phosphatidylinositol 3-kinase complex that contains a catalytic subunit of a phosphatidylinositol 3-kinase (PI3K) enzyme and one or more adaptor proteins. There is no known obligatory regulatory subunit. The class II PI3K (PI3KC2) subfamily of genes has members in vertebrates, worm and fly, but none in yeast.
The part of a cell encompassing the intracellular environment and the plasma membrane; it excludes any external encapsulating structures.
A SNARE complex that is capable of fusing intracellular vesicles to the plasma membrane of platelets for exocytosis of alpha-granules or dense granules. Contains isoforms of VAMP, SNAP and syntaxin proteins. Ternary SNARE complexes interact in a circular array to form ring complexes or channels around the membrane fusion. A common composition in human is VAMP-8, SNAP-23 and syntaxin-2 or -4.
Interacting selectively and non-covalently with any member of the serpin protein family (serine protease inhibitors or classified inhibitor family I4). Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades. The majority of serpins inhibit serine proteases, but serpins that inhibit caspases and papain-like cysteine proteases have also been identified. Rarely, serpins perform a non-inhibitory function; for example, several human serpins function as hormone transporters and certain serpins function as molecular chaperones or tumor suppressors.
A cell-cell recognition process by which a cell distinguishes between self and non self during cooperative behavior, such as early development.
A cell-cell recognition process by which a cell distinguishes between self and non self during cooperative behavior, such as early development.
A cell-cell recognition process by which a cell distinguishes between self and non self during cooperative behavior, such as early development.
Catalysis of the reaction: 3',5'-nucleotide bisphosphate + H20 = 5'-nucleotide monophosphate + phosphate.
A nuclear ubiquitin ligase multiprotein complex located in the inner nuclear membrane (INM) that recognizes and ubiquitinates misfolded INM proteins and also some proteins involved in sterol biosynthesis, during ER-associated protein degradation (ERAD). In S. cerevisiae, this complex contains the ubiquitin ligases Asi1p and Asi3p.
The cellular synthesis of RNA on a template of nucleic acid (DNA or RNA).
An SCF ubiquitin ligase complex in which the F-box protein is Cdc4 in S. cerevisiae.
An SCF ubiquitin ligase complex in which the F-box protein is Ctf13 in S. cerevisiae.
An SCF ubiquitin ligase complex in which the F-box protein is Das1 in S. cerevisiae.
An SCF ubiquitin ligase complex in which the F-box protein is Dia2 in S. cerevisiae (Pof3 in S. pombe).
An SCF ubiquitin ligase complex in which the F-box protein is Grr1 in S. cerevisiae (Pof2 in S. pombe).
An SCF ubiquitin ligase complex in which the F-box protein is Mdm30 in S. cerevisiae.
An SCF ubiquitin ligase complex in which the F-box protein is Met30 in S. cerevisiae (Pof1 in S pombe).
An SCF ubiquitin ligase complex in which the F-box protein is Rcy1 in S. cerevisiae (Pof6 in S. pombe).
An SCF ubiquitin ligase complex in which the F-box protein is Saf1 in S. cerevisiae (Pof9 in S. pombe).
An SCF ubiquitin ligase complex in which the F-box protein is Skp2 in S. cerevisiae.
An SCF ubiquitin ligase complex in which the F-box protein is Ufo1 in S. cerevisiae (Pof10 in S. pombe).
An SCF ubiquitin ligase complex in which the F-box protein is YDR131C in S. cerevisiae.
An SCF ubiquitin ligase complex in which the F-box protein is Pof5 in S. pombe (YDR306C in S. cerevisiae).
An SCF ubiquitin ligase complex in which the F-box protein is YLR224W in S. cerevisiae.
An SCF ubiquitin ligase complex in which the F-box protein is YLR352W in S. cerevisiae.
An SCF ubiquitin ligase complex in which the F-box protein is Hrt3 in S. cerevisiae (Pof7 in S. pombe).
The modification of histone H3 by addition of two methyl groups to lysine at position 36 of the histone.
Interacting selectively and non-covalently with any member of the signal transducers and activators of transcription (STAT) protein family. STATs are, as the name indicates, both signal transducers and transcription factors. STATs are activated by cytokines and some growth factors and thus control important biological processes including cell growth, cell differentiation, apoptosis and immune responses.
Interacting selectively and non-covalently with any member of the suppressor of cytokine signaling (SOCS) family of proteins. SOCS represent an important mechanism to extinguish cytokine and growth factor receptor signaling. Individual SOCS proteins are typically induced by specific cytokines and growth factors, thereby generating a negative feedback loop. SOCS proteins have important functions in development and homeostasis, and in disease, particularly tumor suppression and anti-inflammatory functions.
The cytoplasm of a secondary organism with which the first organism is interacting.
An instance of double-strand break repair via nonhomologous end joining that requires a number of factors important for V(D)J recombination, including the KU70/80 heterodimer (KU), XRCC4, ligase IV, and DNA-PKcs in mammals. It does not produce translocations (as opposed to the alternative nonhomologous end joining).
An instance of double-strand break repair via nonhomologous end joining that requires a number of factors important for V(D)J recombination, including the KU70/80 heterodimer (KU), XRCC4, ligase IV, and DNA-PKcs in mammals. It does not produce translocations (as opposed to the alternative nonhomologous end joining).
An instance of double-strand break repair via nonhomologous end joining that is independent of factors important for V(D)J recombination (as opposed to classical nonhomologous end joining). It often results in a deletion with microhomology (i.e. 5-25bp homology) at the repair junction. Among different subclasses of nonhomologous end joining (NHEJ), alternative NHEJ appears to play a significant role in the etiology of mutations that arise during cancer development and treatment.
An instance of double-strand break repair via nonhomologous end joining that is independent of factors important for V(D)J recombination (as opposed to classical nonhomologous end joining). It often results in a deletion with microhomology (i.e. 5-25bp homology) at the repair junction. Among different subclasses of nonhomologous end joining (NHEJ), alternative NHEJ appears to play a significant role in the etiology of mutations that arise during cancer development and treatment.
An instance of double-strand break repair via nonhomologous end joining that is independent of factors important for V(D)J recombination (as opposed to classical nonhomologous end joining). It often results in a deletion with microhomology (i.e. 5-25bp homology) at the repair junction. Among different subclasses of nonhomologous end joining (NHEJ), alternative NHEJ appears to play a significant role in the etiology of mutations that arise during cancer development and treatment.
An instance of double-strand break repair via nonhomologous end joining that is independent of factors important for V(D)J recombination (as opposed to classical nonhomologous end joining). It often results in a deletion with microhomology (i.e. 5-25bp homology) at the repair junction. Among different subclasses of nonhomologous end joining (NHEJ), alternative NHEJ appears to play a significant role in the etiology of mutations that arise during cancer development and treatment.
Enables the transmembrane transfer of cations by a channel that opens when phosphatidylinositol-3,5-bisphosphate has been bound by the channel complex or one of its constituent parts.
The anterior most point of a dinoflagellate epicone.
The anterior most point of a dinoflagellate hypocone.
A cell surface furrow (or groove) found on a dinoflagellate apex. It typically loops around the apex.
A horn-shaped dinoflagellate apex found in thecate species.
A horn-shaped dinoflagellate antapex found in thecate species.
The neurotransmitter-gated ion channel clustering process in which glutamate receptors are localized to distinct domains in the cell membrane.
Enables the facilitated diffusion of an iron ion (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism.
Stops, prevents, or reduces the activity of an iron channel.
Small membrane vesicle (< 1 um) that buds off a prokaryotic cell plasma membrane, able to carry proteins, phospholipids, lipopolysaccharides, nucleic acids, viruses, and more. Important in intercellular communication and pathogenesis; can exist within host cells.
The modification of histone H3 by addition of one methyl group to lysine at position 4 of the histone.
Eye-like subcellular structure found in dinoflagellates (a large group of single-celled eukaryotes). Consists of subcellular analogues to a cornea, lens, iris, and retina. Ocelloids are built from pre-existing organelles, including a cornea-like layer made of mitochondria and a retinal body made of anastomosing plastids.
The directed movement of RNA to a specific location in the telomeric region of a chromosome.
The directed movement of a protein-containing macromolecular complex to a specific location in the telomeric region of a chromosome.
The directed movement of a protein-containing macromolecular complex to a specific location in the telomeric region of a chromosome.
An intracellular signal transduction process in which STAT proteins (Signal Transducers and Activators of Transcription) convey a signal to trigger a change in the activity or state of a cell. The STAT cascade begins with activation of STAT proteins by kinases, proceeds through dimerization and subsequent nuclear translocation of STAT proteins, and ends with regulation of target gene expression by STAT proteins.
An intracellular signal transduction process in which STAT proteins (Signal Transducers and Activators of Transcription) convey a signal to trigger a change in the activity or state of a cell. The STAT cascade begins with activation of STAT proteins by kinases, proceeds through dimerization and subsequent nuclear translocation of STAT proteins, and ends with regulation of target gene expression by STAT proteins.
An intracellular signal transduction process in which STAT proteins (Signal Transducers and Activators of Transcription) convey a signal to trigger a change in the activity or state of a cell. The STAT cascade begins with activation of STAT proteins by kinases, proceeds through dimerization and subsequent nuclear translocation of STAT proteins, and ends with regulation of target gene expression by STAT proteins.
Catalysis of the transfer of a methyl group from S-adenosylmethionine to a 5-carboxymethoxy-modified uridine residue in a tRNA molecule.
A telomere maintenance process that occurs by base-excision repair of telomeric DNA in response to DNA damage. Telomeric sequences are particularly susceptible to oxidative DNA damage, due to their G-rich nature.
Any response to fluid shear stress in a vascular endothelial cell.
Any response to laminar fluid shear stress in a vascular endothelial cell.
Any response to fluid shear stress where the fluid is flowing across a solid surface with periodic variations. For example, the endothelium in straight parts of the artery tree is subjected to pulsatile shear stress with a significant forward direction, which is believed to be an important physiological stimulus enhancing vessel compliance and conferring anti-thrombotic, anti-adhesive, and anti-inflammatory effects.
Any response to fluid shear stress where the fluid is moving across a solid surface with an oscillatory flow. Disturbed flow patterns at the arterial bifurcations and curvatures may cause endothelial dysfunction, which initiates atherosclerosis.
Any response to pulsatile fluid shear stress that occurs at the level of a cell.
Any response to oscillatory fluid shear stress that occurs at the level of a cell.
Any response to pulsatile fluid shear stress that occurs in a vascular endothelial cell.
Any response to oscillatory fluid shear stress that occurs in a vascular endothelial cell.
A programmed cell death characterized morphologically by the presence of smaller than normal mitochondria with condensed mitochondrial membrane densities, reduction or vanishing of mitochondria crista, and outer mitochondrial membrane rupture. Activation of mitochondrial voltage-dependent anion channels and mitogen-activated protein kinases, upregulation of endoplasmic reticulum stress, and inhibition of cystine/glutamate antiporter are involved in the induction of ferroptosis. This process is characterized by the accumulation of lipid peroxidation products and lethal reactive oxygen species (ROS) derived from iron metabolism. Glutathione peroxidase 4 (GPX4), heat shock protein beta-1, and nuclear factor erythroid 2-related factor 2 function as negative regulators of ferroptosis by limiting ROS production and reducing cellular iron uptake, respectively. In contrast, NADPH oxidase and p53 act as positive regulators of ferroptosis by promotion of ROS production and inhibition of expression of SLC7A11 (a specific light-chain subunit of the cystine/glutamate antiporter), respectively. Misregulated ferroptosis has been implicated in multiple physiological and pathological processes.
Any vesicle that is part of the intracellular region.
The series of events leading to growth of connective tissue when loss of tissues that are incapable of regeneration occurs, or when fibrinous exudate cannot be adequately cleared.
The part of the viral terminase complex that acts as a phage DNA-recognition component and regulates the activity of the large subunit. The small subunit usually assembles as a heterooligomer with the large subunit.
The docking of a cytosolic centriole/basal body to the plasma membrane via the ciliary transition fibers. In some species this may happen via an intermediate step, by first docking to the ciliary vesicle via the ciliary transition fibers. The basal body-ciliary vesicle then relocates to the plasma membrane, followed by the ciliary vesicle fusing with the plasma membrane, effectively attaching the basal body to the plasma membrane.
The docking of a cytosolic centriole/basal body to the plasma membrane via the ciliary transition fibers. In some species this may happen via an intermediate step, by first docking to the ciliary vesicle via the ciliary transition fibers. The basal body-ciliary vesicle then relocates to the plasma membrane, followed by the ciliary vesicle fusing with the plasma membrane, effectively attaching the basal body to the plasma membrane.
The process in which vesicles formed at the trans-Golgi network are directed to the plasma membrane surrounding the base of the cilium, including the ciliary pocket, mediated by molecules at the vesicle membrane and target membrane surfaces.
Binds to and modulates the activity of dolichol-phosphate-mannose synthase.
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 viscosity 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 viscosity stimulus.
The directed movement of copper (Cu) ions passing through the blood-brain barrier.
The directed movement of copper (Cu) ions passing through the blood-cerebrospinal fluid barrier.
The directed movement of copper (Cu) ions passing through the blood-cerebrospinal fluid barrier.
Interacting selectively and non-covalently with a disordered domain of a protein.
The regrowth of neural tissue following its loss or destruction.
Any intracellular signal transduction in which the signal is passed on within the cell by activation of a transcription factor as a consequence of dephosphorylation by Ca(2+)-activated calcineurin. The process begins with calcium-dependent activation of the phosphatase calcineurin. Calcineurin is a calcium- and calmodulin-dependent serine/threonine protein phosphatase with a conserved function in eukaryotic species from yeast to humans. In yeast and fungi, calcineurin regulates stress signaling and cell cycle, and sporulation and virulence in pathogenic fungi. In metazoans, calcineurin is involved in cell commitment, organogenesis and organ development and immune function of T-lymphocytes. By a conserved mechanism, calcineurin phosphatase activates fungal Crz1 and mammalian NFATc by dephosphorylation and translocation of these transcription factors to the nucleus to regulate gene expression.
Any intracellular signal transduction in which the signal is passed on within the cell by activation of a transcription factor as a consequence of dephosphorylation by Ca(2+)-activated calcineurin. The process begins with calcium-dependent activation of the phosphatase calcineurin. Calcineurin is a calcium- and calmodulin-dependent serine/threonine protein phosphatase with a conserved function in eukaryotic species from yeast to humans. In yeast and fungi, calcineurin regulates stress signaling and cell cycle, and sporulation and virulence in pathogenic fungi. In metazoans, calcineurin is involved in cell commitment, organogenesis and organ development and immune function of T-lymphocytes. By a conserved mechanism, calcineurin phosphatase activates fungal Crz1 and mammalian NFATc by dephosphorylation and translocation of these transcription factors to the nucleus to regulate gene expression.
A Golgi-derived vesicle to which the ciliary basal body docks via its transitional fibers. Its membrane is compositionally distinct from Golgi membranes, and will become the ciliary membrane once the ciliary vesicle is fused to the plasma membrane. The ciliary vesicle is thought to be formed by multiple smaller vesicles that attach to the transitional fibers and then fuse to form a larger vesicle.
A Golgi-derived vesicle to which the ciliary basal body docks via its transitional fibers. Its membrane is compositionally distinct from Golgi membranes, and will become the ciliary membrane once the ciliary vesicle is fused to the plasma membrane. The ciliary vesicle is thought to be formed by multiple smaller vesicles that attach to the transitional fibers and then fuse to form a larger vesicle.
Any process involved in the controlled movement of a sperm cell.
Any process involved in the controlled movement of an amoeboid sperm cell.
Any process involved in the controlled movement of an amoeboid sperm cell.
Any process involved in the controlled movement of an amoeboid sperm cell.
The directed, self-propelled movement of a sperm flagellum.
The modification of histone H3 by addition of two methyl groups to lysine at position 79 of the histone.
The modification of histone H3 by addition of two methyl groups to lysine at position 79 of the histone.
Interacting selectively and non-covalently with a LEM domain. The LEM domain (for lamina-associated polypeptide, emerin, MAN1 domain) is present in a group of nuclear proteins that bind chromatin through interaction of the LEM motif with the conserved DNA crosslinking protein, barrier-to-autointegration factor (BAF).
Interacting selectively and non-covalently with a LEM domain. The LEM domain (for lamina-associated polypeptide, emerin, MAN1 domain) is present in a group of nuclear proteins that bind chromatin through interaction of the LEM motif with the conserved DNA crosslinking protein, barrier-to-autointegration factor (BAF).
An intracellular non-membrane-bounded organelle found in multi-ciliated sperm cells of some primitive land plants, and consisting of many radially arranged ninefold symmetric cylinders. The blepharoplast is involved in de novo formation of multiple centrioles; it enlarges and then disintegrates into many procentrioles, which elongate and ultimately nucleate cilia on the surface of the sperm cell.
A motile cilium where the axoneme has a ring of nine outer microtubule doublets but no central microtubules (and is therefore called a 9+0 axoneme).
A motile cilium where the axoneme has a ring of nine outer microtubule doublets but no central microtubules (and is therefore called a 9+0 axoneme).
A motile cilium where the axoneme has a ring of nine outer microtubule doublets plus two central microtubules (and is therefore called a 9+2 axoneme).
A motile cilium where the axoneme has a ring of nine outer microtubule doublets plus two central microtubules (and is therefore called a 9+2 axoneme).
A motile cilium where the axoneme has a ring of nine outer microtubule doublets plus two central microtubules (and is therefore called a 9+2 axoneme).
A cilium which may have a variable array of axonemal microtubules but does not contain molecular motors.
A cilium which may have a variable array of axonemal microtubules but does not contain molecular motors.
A cilium which may have a variable array of axonemal microtubules but does not contain molecular motors.
A cilium which may have a variable array of axonemal microtubules but does not contain molecular motors.
A cilium which may have a variable array of axonemal microtubules but does not contain molecular motors.
A cilium which may have a variable array of axonemal microtubules but does not contain molecular motors.
A cilium which may have a variable array of axonemal microtubules but does not contain molecular motors.
A non-motile cilium where the axoneme has a ring of nine outer microtubule doublets but no central microtubules (and is therefore called a 9+0 axoneme).
A non-motile cilium where the axoneme has a ring of nine outer microtubule doublets but no central microtubules (and is therefore called a 9+0 axoneme).
A non-motile cilium where the axoneme has a ring of nine outer microtubule doublets but no central microtubules (and is therefore called a 9+0 axoneme).
A non-motile cilium where the axoneme has a ring of nine outer microtubule doublets plus two central microtubules (and is therefore called a 9+2 axoneme).
A non-motile cilium where the axoneme has a ring of nine outer microtubule doublets plus two central microtubules (and is therefore called a 9+2 axoneme).
A specialised 9+0 non-motile cilium found in photoreceptor cells. A ciliary transition zone called 'photoreceptor connecting cilium' links the photoreceptor outer segment to the inner segment.
The assembly and secretion of an extracellular exosome, a membrane-bounded vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane.
The assembly and secretion of an extracellular exosome, a membrane-bounded vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane.
The assembly and secretion of an extracellular exosome, a membrane-bounded vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane.
The assembly and secretion of an extracellular exosome, a membrane-bounded vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane.
The assembly and secretion of an extracellular exosome, a membrane-bounded vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane.
A section of the Actinobacterium-type cell wall composed of (phenyl)phthiocerol, phthiodiolone, phthiotriol dimycocerosate, diphthioceranate and other compounds.
Any process that stops, prevents or reduces the rate of ferrichrome biosynthetic process in response to an iron stimulus.
A large lattice-like axial structure found in some flagellated protists which extends alongside the axoneme. Protein components of the paraflagellar rod are likely implicated, among other, in adenine nucleotide signalling and metabolism, and in calcium signalling.
A hair-like structure covering the flagella found in some algae (heterokonts and cryptophytes). It is approximately 15 nm in diameter, and usually consist of a tubular shaft that itself terminates in smaller hairs. It is composed of glycoproteins and, likely, carbohydrates. Mastigonemes may assist in locomotion by increasing the surface area of a flagellum.
Centriole assembly in which a centriole arises de novo, rather than by replication from an existing centriole. This process may occur via different mechanisms. Examples include the deuterosome pathway in multicilated epithelial animal cells and formation of centrioles during parthenogenesis in some insects.
Centriole assembly in which a centriole arises de novo, rather than by replication from an existing centriole. This process may occur via different mechanisms. Examples include the deuterosome pathway in multicilated epithelial animal cells and formation of centrioles during parthenogenesis in some insects.
Centriole assembly in which a centriole arises de novo, rather than by replication from an existing centriole. This process may occur via different mechanisms. Examples include the deuterosome pathway in multicilated epithelial animal cells and formation of centrioles during parthenogenesis in some insects.
Centriole assembly in which a centriole arises de novo, rather than by replication from an existing centriole. This process may occur via different mechanisms. Examples include the deuterosome pathway in multicilated epithelial animal cells and formation of centrioles during parthenogenesis in some insects.
Centriole assembly in which a centriole arises de novo, rather than by replication from an existing centriole. This process may occur via different mechanisms. Examples include the deuterosome pathway in multicilated epithelial animal cells and formation of centrioles during parthenogenesis in some insects.
Centriole assembly in which a centriole arises de novo, rather than by replication from an existing centriole. This process may occur via different mechanisms. Examples include the deuterosome pathway in multicilated epithelial animal cells and formation of centrioles during parthenogenesis in some insects.
Centriole assembly in which a centriole arises de novo, rather than by replication from an existing centriole. This process may occur via different mechanisms. Examples include the deuterosome pathway in multicilated epithelial animal cells and formation of centrioles during parthenogenesis in some insects.
Centriole assembly in which a centriole arises de novo, rather than by replication from an existing centriole. This process may occur via different mechanisms. Examples include the deuterosome pathway in multicilated epithelial animal cells and formation of centrioles during parthenogenesis in some insects.
Centriole assembly in which a centriole arises de novo, rather than by replication from an existing centriole. This process may occur via different mechanisms. Examples include the deuterosome pathway in multicilated epithelial animal cells and formation of centrioles during parthenogenesis in some insects.
A de novo centriole assembly process observed in multi-ciliated sperm cells of some primitive land plants, and where centrioles are formed from a blepharoplast, ultimately giving rise to multiple cilia on the sperm surface.
A de novo centriole assembly process observed in multi-ciliated sperm cells of some primitive land plants, and where centrioles are formed from a blepharoplast, ultimately giving rise to multiple cilia on the sperm surface.
The elimination by an organism of urate salt or uric acid.
The process in which the 5' end of a pre-tRNA molecule is converted to that of a mature tRNA in the mitochondrion.
Any process that modulates the diameter of blood vessels.
Any process that modulates the diameter of blood vessels.
Any process that modulates the diameter of blood vessels.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 5'-end.
A membrane organization process resulting in the formation of a tubular projection. This may face inwardly (as in tubular membrane invaginations) or outwardly (as in endosomal tubules).
A membrane tubulation process occurring in an endosome membrane.
The process of generating a spore-bearing structure. A spore-bearing structure is an anatomical structure that produces new spores.
The process of generating a spore-bearing structure. A spore-bearing structure is an anatomical structure that produces new spores.
Any process that modulates the stability of DNA.
A membrane organization process resulting in the bending of a membrane.
A membrane bending process mediated by clathrin.
Any process that decreases the diameter of blood vessels.
Any process that decreases the diameter of blood vessels.
Process by which a bacteriophage, using its tail fibers, spikes or a baseplate component, initially recognizes and binds to its specific receptor on the host cell surface. This process is reversible and allows the release of a bacteriophage without affecting infection.
Process by which a bacteriophage, using its tail fibers, spikes or a baseplate component, initially recognizes and binds to its specific receptor on the host cell surface. This process is reversible and allows the release of a bacteriophage without affecting infection.
The processes by which a bacteriophage initially commits to infection by binding the host receptor irreversibly. Disruption of the phage:cell complex at this step results in the loss of infective phage virions since the process is characterized by conformational changes of bacteriophage head and tail proteins and injection of bacteriophage proteins into the infected cell.
The processes by which a bacteriophage initially commits to infection by binding the host receptor irreversibly. Disruption of the phage:cell complex at this step results in the loss of infective phage virions since the process is characterized by conformational changes of bacteriophage head and tail proteins and injection of bacteriophage proteins into the infected cell.
The aggregation, arrangement and bonding together of a set of components to form a virus tail.
The aggregation, arrangement and bonding together of a set of components to form a virus tail.
The aggregation, arrangement and bonding together of a set of components to form a virus tail fiber.
Process by which virus heads and tails are attached to each other.
Process by which virus heads and tails are attached to each other.
The encapsulation of the viral genome within the capsid where DNA is packaged into the capsid until the capsid is full.
The part of the viral terminase complex that contains the translocase and endonuclease activities and allows the translocation of the phage DNA into the procapsid. The large subunit usually assembles as a heterooligomer with the small subunit.
Part of the virion that may be used to recognize, attach and inject the viral genome and accessory proteins into the host cell.
Part of the virion that may be used to recognize, attach and inject the viral genome and accessory proteins into the host cell.
The part of the viral capsid that comprises the most common capsomere type. For example, in a T=3 icosahedral capsid, which is composed of 12 pentameric and 20 hexameric capsomeres, the hexameric capsomeres are major subunits.
The part of the viral capsid that comprises the most common capsomere type. For example, in a T=3 icosahedral capsid, which is composed of 12 pentameric and 20 hexameric capsomeres, the hexameric capsomeres are major subunits.
The part of the viral capsid that comprises the less common capsomere type. For example, in a T=3 icosahedral capsid, which is composed of 12 pentameric and 20 hexameric capsomeres, the pentameric capsomeres are minor subunits.
The part of the viral capsid that comprises the less common capsomere type. For example, in a T=3 icosahedral capsid, which is composed of 12 pentameric and 20 hexameric capsomeres, the pentameric capsomeres are minor subunits.
The part of the viral tail that comprises the most common subunit type.
The part of the viral tail that comprises the least common subunit type.
The part of the viral tail that comprises the least common subunit type.
Component of the virus capsid (head), located on the outer head surface. Involved in the stabilization of the head structure and usually non-essential.
A type of capsid decoration composed of fiber structures.
The basal end of the virus tail, which is used by the virus to attach to the host cell.
The fibrous region of the virus tail used to scan, recognize and attach to the host cell.
Multiprotein component at the distal (head) end of the virus tail to which fibers of tailed viruses may be attached.
Multiprotein component at the distal (head) end of the virus tail to which fibers of tailed viruses may be attached.
Multiprotein component at the distal (head) end of the virus tail to which fibers of tailed viruses may be attached.
The internal tube of the contractile tails of some viruses. The virus tail tube is the channel for DNA ejection into the host cytoplasm.
The external contractile envelope of the tail of some viruses. Its contraction ensures ejection of the virus DNA into the host cytoplasm.
The tube of the non-contractile tails of some viruses.
A short structure attached to an icosahedral virion capsid, and used for attachment to the host cell.
A region of constriction located below the head and above the tail sheath of viruses with contractile tails (Myoviridae).
A small disk located at the base of some icosahedral virus capsids.
A fiber attached to the collar structure of some icosahedral viral capsids.
A fiber attached to the neck at the base of some icosahedral viral capsids.
The encapsulation of the viral DNA genome within the capsid, which proceeds via cleavage of the viral DNA at specific sites by a viral terminase.
The encapsulation of the viral DNA genome within the capsid, which proceeds via cleavage of the viral DNA at specific sites to produce 3' protruding ends.
The encapsulation of the viral DNA genome within the capsid, which proceeds via cleavage of the viral DNA at specific sites to produce 5' protruding ends.
Process by which a transposable element is excised from the donor site and integrated at the target site without replication of the element. Also referred to as cut-and-paste transposition.
Process of transposition in which the existing element is replicated and one of the copies is excised and integrated at a new target site. Also referred to as copy-and-paste transposition.
Process of transposition in which the existing element is replicated and one of the copies is excised and integrated at a new target site. Also referred to as copy-and-paste transposition.
The aggregation, arrangement and bonding together of a set of components to form a virus baseplate.
A complex of proteins that permits the translocation of proteins across the outer membrane via a transmembrane pore, formed by a beta-barrel, into the extracellular milieu or directly into host cells; the secreted proteins contain all the information required for translocation of an effector molecule through the cell envelope. The type V secretion systems includes the autotransporters (type Va), the two-partner secretion system (type Vb) and the Oca family (type Vc).
A complex of proteins that permits the translocation of proteins across the outer membrane via a transmembrane pore, formed by a beta-barrel, into the extracellular milieu or directly into host cells; the secreted proteins contain all the information required for translocation of an effector molecule through the cell envelope. The type V secretion systems includes the autotransporters (type Va), the two-partner secretion system (type Vb) and the Oca family (type Vc).
The region of a virus contained within the capsid shell, and usually containing the viral genome and accessory proteins.
The process of removing one or more phosphate groups from a polynucleotide.
The process of removing one or more phosphate groups from a DNA molecule.
The process of removing a 3' phosphate group from a DNA molecule.
Any 3' DNA dephosphorylation that is involved in the process of DNA repair.
Interacting selectively and non-covalently with G-rich, single-stranded, telomere-associated DNA.
The process of removing one or more phosphate groups from the 3' end of a polynucleotide.
The process of removing one or more phosphate groups from the 5' end of a polynucleotide.
The generation of hematopoietic stem cells from hemogenic endothelial cells by a process that includes tight-junction dissolution and loss of cell polarity followed by delamination from the endothelium.
The series of events required for an organism to detect some level of humidity in its environment, convert this detection into a molecular signal, and recognize and characterize the signal. This is a neurological process.
The series of events required for an organism to detect high environmental humidity, convert this detection into a molecular signal, and recognize and characterize the signal. This is a neurological process.
The series of events required for an organism to detect low environmental humidity, convert this detection into a molecular signal, and recognize and characterize the signal. This is a neurological process.
The series of events in which a humidity stimulus is received and converted into a molecular signal as part of the sensory perception of humidity.
The series of events in which a humidity stimulus is received and converted into a molecular signal.
The series of events in which a high humidity stimulus is detected and converted into a molecular signal as a part of the sensory detection of high humidity.
The series of events in which a low humidity stimulus is detected and converted into a molecular signal as a part of the sensory detection of low humidity.
The series of events in which high humidity is detected and converted into a molecular signal.
The series of events in which low humidity is detected and converted into a molecular signal.
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 post-synaptic potential responsible for muscle contraction.
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 that inhibits muscle contraction.
A neuromuscular junction in which the target muscle cell is a skeletal muscle fiber.
A neuromuscular junction in which the target muscle cell is a myotube.
A neuromuscular junction in which the target muscle cell is a somatic muscle myotube, such as an arthropod somatic muscle cell.
A neuromuscular junction that functions in the excitation of somatic muscle myotubes, such as an arthropod somatic muscle cells.
A neuromuscular junction that functions in the inhibition of somatic muscle myotube contraction. Examples of somatic muscle myotubes include the somatic muscle cells of arthropods.
A neuromuscular junction in which the target muscle cell is a somatic muscle cell, such as those found in nematodes and arthropods.
The process in which a relatively unspecialized cell acquires specialized features of a skeletal muscle fiber cell. Skeletal muscle fiber differentiation starts with myoblast fusion and the appearance of specific cell markers (this is the cell development step). Then individual skeletal muscle fibers fuse to form bigger myotubes and start to contract.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a neuromuscular junction that targets a skeletal muscle fiber.
Any process that increases the rate, frequency or extent of strand invasion. Strand invasion is the process in which the nucleoprotein complex (composed of the broken single-strand DNA and the recombinase) searches and identifies a region of homology in intact duplex DNA. The broken single-strand DNA displaces the like strand and forms Watson-Crick base pairs with its complement, forming a duplex in which each strand is from one of the two recombining DNA molecules.
Any process that increases the rate, frequency or extent of strand invasion. Strand invasion is the process in which the nucleoprotein complex (composed of the broken single-strand DNA and the recombinase) searches and identifies a region of homology in intact duplex DNA. The broken single-strand DNA displaces the like strand and forms Watson-Crick base pairs with its complement, forming a duplex in which each strand is from one of the two recombining DNA molecules.
Any process that increases the rate, frequency or extent of strand invasion. Strand invasion is the process in which the nucleoprotein complex (composed of the broken single-strand DNA and the recombinase) searches and identifies a region of homology in intact duplex DNA. The broken single-strand DNA displaces the like strand and forms Watson-Crick base pairs with its complement, forming a duplex in which each strand is from one of the two recombining DNA molecules.
A DNA-binding transcription factor activity that is directly regulated by binding of a ligand to the protein with this activity.  Examples include the lac and trp repressors in E.coli and many steroid hormone receptors.
The modification of histone H3 by addition of three methyl groups to lysine at position 27 of the histone.
A transmembrane protein complex that functions in ATPase dependent active transport across a membrane.
A cellular process that results in the assembly of one or more centrioles.
Centriole assembly in which a centriole arises de novo by a process involving an electron-dense structure known as a deuterosome, rather than by duplication of an existing centriole, and occurring as part of multi-ciliated epithelial cell differentiation.
Centriole assembly in which a centriole arises de novo by a process involving an electron-dense structure known as a deuterosome, rather than by duplication of an existing centriole, and occurring as part of multi-ciliated epithelial cell differentiation.
Centriole assembly in which a centriole arises de novo by a process involving an electron-dense structure known as a deuterosome, rather than by duplication of an existing centriole, and occurring as part of multi-ciliated epithelial cell differentiation.
Centriole assembly in which a centriole arises de novo by a process involving an electron-dense structure known as a deuterosome, rather than by duplication of an existing centriole, and occurring as part of multi-ciliated epithelial cell differentiation.
Centriole assembly in which a centriole arises de novo by a process involving an electron-dense structure known as a deuterosome, rather than by duplication of an existing centriole, and occurring as part of multi-ciliated epithelial cell differentiation.
Centriole assembly in which a centriole arises de novo by a process involving an electron-dense structure known as a deuterosome, rather than by duplication of an existing centriole, and occurring as part of multi-ciliated epithelial cell differentiation.
Centriole assembly in which a centriole arises de novo by a process involving an electron-dense structure known as a deuterosome, rather than by duplication of an existing centriole, and occurring as part of multi-ciliated epithelial cell differentiation.
Centriole assembly in which a centriole arises de novo by a process involving an electron-dense structure known as a deuterosome, rather than by duplication of an existing centriole, and occurring as part of multi-ciliated epithelial cell differentiation.
A spherical, electron dense, cytoplasmic structure that is involved in de novo assembly of centrioles.
Nucleus with two or more lobes connected by a thin filament that contains no internal chromatin.  Examples include the nuclei of mature basophils, eosinophils and neutrophils in mice and humans.
The side (leaflet) of the transport vesicle membrane that faces the lumen.
The side (leaflet) of the transport vesicle membrane that faces the cytoplasm.
The side (leaflet) of the trans-Golgi network transport vesicle membrane that faces the lumen.
The side (leaflet) of the trans-Golgi network transport vesicle membrane that faces the cytoplasm.
Reactions triggered in response to the presence of another organism that act to protect the cell or organism from damage caused by that organism.
The series of events in which a stimulus from another organism is received and converted into a molecular signal.
Any process in which a protein complex is maintained in a location and prevented from moving elsewhere. These include sequestration, stabilization to prevent transport elsewhere and the active retrieval of protein complexes that move away.
Any process in which a protein complex is maintained in a specific location within the cytoplasm and is prevented from moving elsewhere.
Interacting selectively and non-covalently with c[G(2',5')pA(2',5')p], a cyclic purine dinucleotide that consists of AMP and GMP units cyclized via 2',5' and 3',5' linkages.
The side of the Golgi membrane that faces the lumen.
The side (leaflet) of the Golgi membrane that faces the cytoplasm.
A stable intercellular bridge between somatic cells.  Examples include the intercellular bridges between ovarian follicle cells in insects and between imaginal disc cells in insects.
The side (leaflet) of the early endosome membrane that faces the lumen.
The side (leaflet) of the early endosome membrane that faces the lumen.
The side (leaflet) of the late endosome membrane that faces the lumen.
The side (leaflet) of the late endosome membrane that faces the lumen.
A cellular component consisting of one leaflet of a membrane bilayer and any proteins embedded or anchored in it or attached to its surface.
The side (leaflet) of the plasma membrane that faces the lumen.
The side (leaflet) of the plasma membrane that faces the cytoplasm.
The side (leaflet) of the rough endoplasmic reticulum membrane that faces the lumen.
The side (leaflet) of the rough endoplasmic reticulum membrane that faces the cytoplasm.
The side (leaflet) of the smooth endoplasmic reticulum membrane that faces the cytoplasm.
The side (leaflet) of the smooth endoplasmic reticulum membrane that faces the lumen.
The side (leaflet) of the early endosome membrane that faces the cytoplasm.
The side (leaflet) of the early endosome membrane that faces the cytoplasm.
The side (leaflet) of the late endosome membrane that faces the cytoplasm.
The side (leaflet) of the late endosome membrane that faces the cytoplasm.
A transmembrane protein complex that consists of multiple methyl-accepting chemoreceptor protein subunits, a histidine kinase and a connector protein and which functions in the regulation of flagellar rotary motor activity in response to an external chemical stimulus.
The side of a membrane that faces the cytoplasm.
The component of the synaptic vesicle 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 volume enclosed within the membrane of a trans-Golgi network transport vesicle.
The side (leaflet) of the endosome membrane that faces the lumen.
The side (leaflet) of the endosome membrane that faces the lumen.
The volume enclosed within the membrane of a transport vesicle.
The side (leaflet) of a plasma membrane that faces the periplasm, and all proteins embedded in it or attached to its surface.
The side (leaflet) of the mycolate outer membrane that faces the environment and any proteins embedded in it or loosely bound to its surface.
The side of the mycolate outer membrane that faces the cell wall peptidoglycan. It is rich in long-chain mycolic acids (hydroxylated branched-chain fatty acids) that are covalently linked to the cell wall peptidoglycan via an arabinogalactan network.
The side (leaflet) of the plastid inner membrane that faces the stroma, and any proteins embedded in it or loosely bound to its surface.
The side (leaflet) of the plastid thylakoid membrane that faces the lumen, and any proteins embedded in it or loosely bound to its surface.
The side (leaflet) of the plastid thylakoid membrane that faces the stroma, and any proteins embedded in it or loosely bound to its surface.
The component of the mitochondrial 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 side (leaflet) of the lysosomal membrane that faces the cytoplasm.
The side (leaflet) of the lysosomal membrane that faces the cytoplasm.
The side (leaflet) of the lysosomal membrane that faces the lumen.
The side (leaflet) of the lysosomal membrane that faces the lumen.
Any side (leaflet) of a membrane that faces the lumen of an organelle.
A sex chromosome that has been inactivated.
A condensed form of chromatin that is associated with an inactivated sex chromosome and which is responsible for its inactivation.
A sex chromosome that has not been inactivated.
Chromatin that is part of an active sex chromosome.
The series of events in which an external biotic stimulus is detected and converted into a molecular signal.  An external biotic stimulus is defined as one caused or produced by a living organism other than the one being stimulated.
A vocalisation behavior that is innate, i.e. that does not need to be learned in order to occur.
A vocalization behavior that is the result of learning.
A secretory organelle of a host cell, some 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
The lipid bilayer surrounding a host synaptic vesicle.
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 from a virus.
The lipid bilayer that forms the outer-most layer of an organelle.
A membrane that is a part of a larger membrane.  Examples include the apical region of the plasma membrane of an epithelial cell and the various regions of the endoplasmic reticulum membrane.
A membrane that is a (regional) part of the plasma membrane.
The leaflet the apical region of the plasma membrane that faces away from the cytoplasm and any proteins embedded or anchored in it or attached to its surface.
The side (leaflet) of the apical region of the plasma membrane that faces the cytoplasm.
A cup shaped specialization of the cytoskeleton that forms a thin layer located just below the apical mass of mature mucin secretory granules in the cytoplasm of goblet cells of the intestinal epithelium.  It consists of an orderly network of intermediate filaments and microtubules. Microtubules are arranged vertically, like barrel staves, along the inner aspect of the theta. Intermediate filaments form two networks: an inner, basketlike network and an outer series of circumferential bundles resembling the hoops of a barrel.
A secretory granule that contains mucin.
The space between the membrane of an oocyte and a surrounding membranous structure (zona pellucida or perivitelline membrane).
Learning in which new behaviors are acquired through imitation.
Learning that occurs through observing the behavior of others.
Vocalisation behavior that is the result of learning, or the process by which new vocalizations are learned.
Catalysis of a hydrolase reaction that removes a palmitoyl moiety from some substrate.
Catalysis of the reaction: L-Selenomethionine + H2O => Methaneselenol + Ammonia + 2-oxobutanoic acid.
Catalysis of the reaction: ATP + L-Selenomethionine + H2O => Orthophosphate + Diphosphate + Se-Adenosylselenomethionine.
Catalysis of the reaction: R + Se-Adenosylselenomethionine => CH3-R + Se-Adenosyl-L-selenohomocysteine.
Catalysis of the reaction: Se-Adenosyl-L-selenohomocysteine + H2O => Adenosine + Selenohomocysteine.
Catalysis of the reaction: L-Serine + Selenohomocysteine => L-Selenocystathionine + H2O.
Catalysis of the reaction: L-Selenocystathionine + H2O => L-Selenocysteine + NH3 + 2-Oxobutanoic acid.
Catalysis of the reaction: Se-Methyl-L-selenocysteine + H2O => pyruvic acid + NH3 + Methaneselenol.
Catalysis of the reaction: methylselenol + H2O => H2Se + CH3OH.
The attachment of one cell to another cell via adhesion molecules.
The attachment of one cell to another cell via adhesion molecules.
The attachment of two unicellular organisms to each other.
Cell-cell adhesion between two single-celled organisms, during flocculation, mediated via the binding of cell wall proteins on one cell to galactose residues on the other.
Cell-cell adhesion between two single-celled organisms, during flocculation, mediated via the binding of cell wall proteins on one cell to mannose residues on the other.
Catalysis of the reaction: S-Adenosyl-L-methionine + Methaneselenol => S-Adenosyl-L-homocysteine + Dimethyl selenide.
Catalysis of the reaction: S-Adenosyl-L-methionine + Hydrogen selenide => S-Adenosyl-L-homocysteine + Methaneselenol.
Catalysis of the reaction: S-adenosyl-L-methionine + dimethyl selenide => S-adenosyl-L-homocysteine + trimethylselenonium.
Catalysis of the reaction: ATP + H2SeO4 => Diphosphate + Adenylylselenate.
Catalysis of the reaction: ATP + Adenylylselenate => ADP + 3'-Phosphoadenylylselenate.
Catalysis of the reaction: ATP + L-Selenomethionine + tRNA(Met) => AMP + Diphosphate + Selenomethionyl-tRNA(Met).
Catalysis of the reaction: tRNASec + L-Ser + ATP ---> Ser-tRNASec + AMP + Diphosphate.
Catalysis of the reaction: Ser-tRNA(Sec) + ATP ---> Sep-tRNA(Sec) + ADP
Catalysis of the reaction: O-Phosphoseryl-tRNA(Sec) + Selenophosphoric acid + H2O => L-Selenocysteinyl-tRNA(Sec) + 2 phosphoric acid.
Catalysis of the reaction: H+ + selenodiglutathione + NADPH => gluthathioselenol + glutathione + NADP+.
Catalysis of the reaction: SeO3(2-) + 3NADPH + 5H+ ---> H2Se + 3NADP+ + 3H2O.
Catalysis of the reaction: 3'-Phosphoadenylylselenate + NADPH => Adenosine 3',5'-bisphosphate + Selenite + NADP+ + H+.
Catalysis of the reaction: NADPH + H+ + CH3SeOH => NADP+ + CH3SeH + H2O
Catalysis of the reaction: NADPH + H+ + CH3SeO2H => NADP+ + CH3SeOH + H2O.
Catalysis of the reaction: protein arginine phosphate + H2O = protein arginine + phosphate.
The removal of phosphate residues from peptidyl-N-phospho-arginine to form peptidyl-arginine
A process which results in the assembly, arrangement of constituent parts, or disassembly of a trans-Golgi network membrane.
The clustering together of unicellular organisms in suspension form aggregates.
The binding by a cell-adhesion protein on the cell surface to an extracellular matrix component, to mediate adhesion of the cell to another cell.
The binding by a cell-adhesion protein on the cell surface to an extracellular matrix component, to mediate adhesion of the cell to another cell.
Interacting selectively and non-covalently with a collagen fibril.
The binding by a cell-adhesion protein on the cell surface to an extracellular matrix component, to mediate adhesion of the cell to the extracellular matrix.
The binding by a cell-adhesion protein on the cell surface to an extracellular matrix component, to mediate adhesion of the cell to the extracellular matrix.
Any protein complex that is capable of carrying out some part of the process of cell-cell adhesion.
Any protein complex that is capable of carrying out some part of the process of cell adhesion to the cell matrix or to another cell.
Any protein complex that is capable of carrying out some part of the process of cell adhesion to the cell matrix or to another cell.
Any protein complex that is capable of carrying out some part of the process of cell-matrix adhesion.
Any laminin protein binding that occurs as part of cell-matrix adhesion.
Any collagen binding that occurs as part of cell-matrix adhesion.
Any integrin binding that occurs as part of the process of cell-matrix adhesion.
Any cadherin binding that occurs as part of the process of cell-cell adhesion.
A collagen trimer that forms networks.
A supramolecular assembly of fibrillar collagen complexes in the form of a long fiber (fibril) with transverse striations (bands).
A complex of collagen trimers such as a fibril or collagen network.
A complex of collagen trimers such as a fibril or collagen network.
A protein complex that consists of collagen triple helices associated to form a network.
A protein complex that consists of collagen triple helices associated to form a sheet-like network.
A supramolecular assembly of collagen trimers with a 'beads on a string'-like structure.
A specialised collagen fibril that functions as an anchor, binding to other collagen structures.
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 peptidyl-dipeptidase A inhibitor 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 peptidyl-dipeptidase A inhibitor stimulus.
Interacting selectively and non-covalently with a peptidyl-proline 4-dioxygenase.
Any collagen timer that is part of a basement membrane.
An antiparallel dimer of two collagen VII trimers, one end of which is embedded in the lamina densa while the other end attaches to banded collagen fibrils in the dermis.
The process by which centromeres/kinetochores become localized to clusters.
The process by which centromeres/kinetochores become localized to clusters.
A protein complex that includes Mis16(Yippee family) and/or Mis18 (WD repeat) subunits that is involved in the deposition of centromere specific (CENP-A containing) nucleosomes at the centromere.
The process in which a cation is transported across a membrane.
The process in which an anion is transported across a membrane.
The directed movement of some substance from outside of a cell into the cytoplasmic compartment. This may occur via transport across the plasma membrane or via endocytosis.
The directed movement of inorganic anions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of inorganic cations from outside of a cell, across the plasma membrane and into the cytosol.
The process in which an inorganic ion is transported across a membrane.
The process in which an inorganic ion is transported across a membrane.
The process in which an inorganic anion is transported across a membrane.
The process in which an inorganic anion is transported across a membrane.
A process in which an inorganic cation is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
A process in which an inorganic cation is transported from one side of a membrane to the other by means of some agent such as a transporter or pore.
The series of molecular signals generated as a consequence of a G protein-coupled serotonin receptor binding to one of its physiological ligands.
A protein complex that is capable of serotonin receptor activity.
A protein complex that is capable of serotonin receptor activity.
A protein complex that is capable of serotonin receptor activity.
A protein complex that is capable of G protein-coupled serotonin receptor activity.
The process by which a preexisting viral infection prevents a secondary infection with the same or a closely related virus.  Typically some aspect of viral entry is inhibited, but post entry mechanisms have also been documented.
The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that mediates/triggers viral entry by endocytosis/pinocytosis or by inducing fusion/penetration.
The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface that does not mediate or trigger entry into the host cell. This binding is typically reversible and enhances significantly infectivity by concentrating the virus in the vicinity of its entry receptors, or bringing it to an organ in which its target cells are located.
Any process, either active or passive, by which a virus evades the CRISPR-cas system of its host. Some viruses can directly suppress the CRISPR system.
Any process by which a virus inhibits DNA replication in its host cell.  Some bacteriophages are known to do this, possibly as a way of increasing the pool of nucleotides available for virus replication.
The component of the neuronal dense core vesicle 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 neuronal dense core vesicle 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.
Any process by which a virus modulates the ability of its host to infect and/or damage an organism for which it is a host.  Typically this involves a phage modulating the virulence of a bacterium.  Mechanisms include the expression of factors that modulate a bacterial adhesion to a host cell, spread through host tissues, production exotoxins or provide protection against host immune defenses.
Maturation of a virion after separation from the host cell. Not all viruses mature after separation.  In those that do, maturation typically involves rearangement and/or cleavage of viral proteins, resulting in the virion becoming competent for reinfection.
Maturation of a virion after separation from the host cell. Not all viruses mature after separation.  In those that do, maturation typically involves rearangement and/or cleavage of viral proteins, resulting in the virion becoming competent for reinfection.
A process by which the range of hosts which a virus can bind and infect is changed.  Examples include phages that switch between types of fibers via the action of a virally encoded invertase.
A regulation of transcription from RNA polymerase II promoter that results in regulation of carbohydrate catabloism.
Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the addition of a terminal nucleotide to an RNA molecule in the absence of a nucleic acid template.
A non-membrane bound, electron dense structure associated that extends perpendicular to the presynaptic membrane in ribbon synapses. The ribbon's surface is studded with small particles to which synaptic vesicles tether via fine filaments. The tethered vesicles function as a pool, several fold greater than the docked pool available for fast release, which supports sustained release of vesicles.  Synaptic ribbons may be plate like or spherical.
An electron dense structure that anchors a synaptic ribbon to the presynaptic membrane.
A ribbon synpase of an auditory hair cell of the cochlear. These ribbon synapses contain spherical synaptic ribbons and lack and arciform density.
A ribbon synapse between a retinal photoreceptor cell (rod or cone) and a retinal bipolar cell.  These contain a plate-like synaptic ribbon.
A synapse between the Schaffer collateral axon of a CA3 pyramidal cell and a CA1 pyramidal cell.
One of the giant synapses that form between the mossy fiber axons of dentate gyrus granule cells and the large complex spines of CA3 pyramidal cells. It consists of a giant bouton known as the mossy fiber expansion, synapsed to the complex, multiheaded spine (thorny excresence) of a CA3 pyramidal cell.
Any subdivision of a chromosome along its length.
An excitatory synapse formed by the parallel fibers of granule cells synapsing onto the dendrites of Purkinje cells.
The process by which a virus switches on its replication cycle in an infected cell.   The process is typically controlled by a genetic swtich controlled by environmental factors such as cell type, cell shape, the availability of nutrients, superinfection or exposure of infected cells to UV or various chemical stimuli.
The process by which a virus switches on its replication cycle in an infected cell.   The process is typically controlled by a genetic swtich controlled by environmental factors such as cell type, cell shape, the availability of nutrients, superinfection or exposure of infected cells to UV or various chemical stimuli.
The process by which a virus switches on its replication cycle in an infected cell.   The process is typically controlled by a genetic swtich controlled by environmental factors such as cell type, cell shape, the availability of nutrients, superinfection or exposure of infected cells to UV or various chemical stimuli.
The process by which a virus switches on its replication cycle in an infected cell.   The process is typically controlled by a genetic swtich controlled by environmental factors such as cell type, cell shape, the availability of nutrients, superinfection or exposure of infected cells to UV or various chemical stimuli.
The process by which a virus switches on its replication cycle in an infected cell.   The process is typically controlled by a genetic swtich controlled by environmental factors such as cell type, cell shape, the availability of nutrients, superinfection or exposure of infected cells to UV or various chemical stimuli.
The process by which a virus switches on its replication cycle in an infected cell.   The process is typically controlled by a genetic swtich controlled by environmental factors such as cell type, cell shape, the availability of nutrients, superinfection or exposure of infected cells to UV or various chemical stimuli.
A synapse that uses glycine as a neurotransmitter.
A synapse that uses dopamine as a neurotransmitter.
A synapse that uses noradrenaline as a neurotransmitter.
Any process that modulates the frequency, rate or extent of the synaptic vesicle cycle.
Any process that modulates the frequency, rate or extent of synaptic vesicle budding from presynaptic endocytic zone membrane.
Any inositol 1,4,5-trisphosphate receptor activity that is involved in regulation of postsynaptic cytosolic calcium ion concentration.
Any process that modulates the frequency, rate or extent of neurotransmitter receptor localization to postsynaptic specialization membrane.
Any ryanodine-sensitive calcium-release channel activity that is involved in regulation of postsynaptic cytosolic calcium ion concentration.
The aggregation, arrangement and bonding together of a set of components to form a postsynaptic specialization, a region that lies adjacent to the cytoplasmic face of the postsynaptic membrane.
The action of a molecule that contributes to the structural integrity of a presynaptic actin cytoskeleton.
The active transport of neurotransmitters into a synaptic vesicle.  This import is fuelled by an electrochemical gradient across the vesicle membrane, established by the action of proton pumps.
The active transport of neurotransmitters into a synaptic vesicle.  This import is fuelled by an electrochemical gradient across the vesicle membrane, established by the action of proton pumps.
The active transport of neurotransmitters into a synaptic vesicle.  This import is fuelled by an electrochemical gradient across the vesicle membrane, established by the action of proton pumps.
The directed movement of adenine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of adenine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of calcium ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of calcium ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of calcium ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of a carbohydrate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of a carbohydrate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of copper ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of copper ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of copper ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of copper ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of copper ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of copper ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of copper ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of ferric iron (Fe(III) or Fe3+) ions from outside of a cell, across the cell outer membrane and into the periplasmic space.
The directed movement of ferric iron (Fe(III) or Fe3+) ions from outside of a cell, across the cell outer membrane and into the periplasmic space.
The directed movement of ferric iron (Fe(III) or Fe3+) ions from outside of a cell, across the cell outer membrane and into the periplasmic space.
The directed movement of ferric iron (Fe(III) or Fe3+) ions from outside of a cell, across the cell outer membrane and into the periplasmic space.
The directed movement of ferric iron (Fe(III) or Fe3+) ions from outside of a cell, across the cell outer membrane and into the periplasmic space.
The directed movement of ferric iron (Fe(III) or Fe3+) ions from outside of a cell, across the cell outer membrane and into the periplasmic space.
The directed movement of ferric iron (Fe(III) or Fe3+) ions from outside of a cell, across the cell outer membrane and into the periplasmic space.
The directed movement of ferrous iron ions (Fe(II) or Fe2+) from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of ferrous iron ions (Fe(II) or Fe2+) from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of ferrous iron ions (Fe(II) or Fe2+) from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of glucose from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of glucose from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of glucose from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of glucose from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of glutathione from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of glutathione from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of glutathione from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of guanine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of guanine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of iron ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of iron ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of iron ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-glutamate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-glutamate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-glutamate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-glutamate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of L-glutamate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of leucine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of leucine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of leucine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of malate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of malate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of malonic acid from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of malonic acid from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of malonic acid from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of nickel cations from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of nickel cations from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of pantothenate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of pantothenate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of pantothenate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of pantothenate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of serine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of serine from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of sodium ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of sodium ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of sodium ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of sodium ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of sodium ions from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of succinate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of succinate from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of uracil from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of uracil from outside of a cell, across the plasma membrane and into the cytosol.
Division of a stem cell during which it retains its identity and buds off a daughter cell with a new identity.
A myofibril of a skeletal muscle fiber.
Symmetric division of a stem cell to produce two stem cells of the same type as the parent. Symmetric stem cell division is necessary for amplification of stem cell populations in the absence of sources of stem cells external to an existing population.
Cell division in which both daughter cells are of the same type.
The symmetric division of a skeletal muscle satellite stem cell, resulting in two skeletal muscle satellite stem cells.  This process is involved in amplification of the pool of these cells.
Any process by which the numbers of cells of a particular type or in a tissue are maintained.
The self-renewing division of a germline stem cell, to produce a daughter stem cell and a daughter germ cell which will divide to form one or more gametes.
Division of a germline stem cell to produce two germline stem cells of the same type as the parent.
The symmetric division of a male germline stem cell to produce two male germline stem cells.  An example of this is found in mammalian spermatogonial stem cells, some proportion of which divide symmetrically, so amplifying the population. The choice between asymmetric and symmetric division in this case appears to be internal and stochastic.
Any process by which the number of skeletal muscle satellite stem cells in a skeletal muscle is maintained during skeletal muscle regeneration. There are at least two mechanisms by which this is achieved. Skeletal muscle satellite stem cell asymmetric division ensures satellite stem cell numbers are kept constant. Symmetric division of these cells amplifies the number of skeletal muscle satellite stem cells.
The removal of an acyl group, any group or radical of the form RCO- where R is an organic group, from a macromolecule.
Any protein complex that is part of or has some part in a hemidesmosome.
The removal of palymitoyl groups from a macromolecule.
Any process that increases the force of heart muscle contraction.
Any process that decreases the force of heart muscle contraction.
The process that results in the incorporation of a protein into a plasma membrane.  Incorporation in this context means having some part or covalently attached group that is inserted into the the hydrophobic region of one or both bilayers.
The directed movement of some substance from outside of a cell, across the plasma membrane and into the cytosol.
Cell adhesion that involves cells from multiple organisms or that is mediated by gene products from multiple organisms.
The attachment of two unicellular organisms to each other via interaction between cell-wall components.
The attachment of one cell to another cell via adhesion molecules that are at least partially embedded in the plasma membrane.
The clustering together and adhesion of initially separate cells to form an aggregate.  Examples include the clustering of unicellular organisms or blood cells in suspension and the condensation of mesenchymal cells during cartilage formation.
Binds to and increases the activity of 1-phosphatidylinositol 4-kinase.
A protein complex consisting of a Dcp1 regulatory subunit and a Dcp2 catalytic subunit that has mRNA cap binding activity and is involved in decapping of nuclear-transcribed mRNA.
The fast, initial phase of calcium ion-induced neurotransmitter release, via exocytosis, into the synaptic cleft. This depends on low affinity calcium sensors and typically begins a fraction of a millisecond after Ca2+ influx, and decays rapidly (1-10ms) with a decay constant of around 5-10ms. The underlying molecular mechanisms of this process are distinct from those of the later, slow phase of release.
The slow, second phase of calcium ion-induced neurotransmitter release, via exocytosis, into the synaptic cleft. This depends on high affinity calcium sensors and decays slowly, typically with a decay constant of over 100ms. The underlying molecular mechanisms of this process are distinct from those of the earlier, fast phase of release.
The activity of bridging an endocytic receptor to its substrate (for substrates that do not directly bind the cargo receptor).
The process whose specific outcome is the progression of a cerebellar neuron over time, from initial commitment of the cell to a specific fate, to the fully functional differentiated cell.
Interacting selectively and non-covalently with a FXYD domain.
The process whose specific outcome is the progression of a bone cell over time, from initial commitment of the cell to a specific fate, to the fully functional differentiated cell.
The component of the plasma membrane consisting of the gene products that penetrate only the cytoplasmic side of the membrane.
The component of the plasma membrane consisting of gene products and protein complexes with covalently attached hydrophobic anchors products that penetrate only the cytoplasmic side of the membrane.
Any process that reduces or removes the toxicity of a toxic substance. These may include transport of the toxic substance away from sensitive areas and to compartments or complexes whose purpose is sequestration of the toxic substance.
The process by which seed dormancy is maintained by the presence of absisic acid.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-21 stimulus.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-21 stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-8 stimulus.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-8 stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-7 stimulus.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-7 stimulus.
One of the distinct periods or stages into which the meiotic cell cycle is divided. Each phase is characterized by the occurrence of specific biochemical and morphological events.
One of the distinct periods or stages into which the mitotic cell cycle is divided. Each phase is characterized by the occurrence of specific biochemical and morphological events.
A meiotic cell cycle phase prior to a during which some part of meiosis I nuclear division or the proceeding cytokinesis occurs.
A meiotic cell cycle phase that occurs after meiosis I (the first meiotic nuclear division).
The meiotic cell cycle phase in eukaryotes between meiotic prophase I and meiotic metaphase I. During meiotic prometaphase I, the nuclear envelope breaks down and one kinetochore forms per chromosome. Chromosomes attach to spindle microtubules and begin to move towards the metaphase plate.
Interacting selectively and non-covalently with any member of the Tissue inhibitors of metalloproteinases (TIMPs) family. TIMPs are endogenous protein regulators of the matrix metalloproteinase (MMPs) family
Interacting selectively and non-covalently with any member of the FBXO protein family. Members of this family have an F-box protein motif of approximately 50 amino acids that functions as a site of protein-protein interaction.
Any process involved in the maintenance of an internal steady state of inorganic ions within an organism or cell.
The process whose specific outcome is the progression of the skin epidermis over time, from its formation to the mature structure.
A proteinaceous extracellular fiber, produced by an enteric bacterium, that is involved in surface and cell-cell contacts that promote community behavior and host colonization.
A proteinaceous extracellular fiber, produced by an enteric bacterium, that is involved in surface and cell-cell contacts that promote community behavior and host colonization.
The process of assembly of curli, extracellular fibers produced by enteric bacteria.  This process occurs outside the cell, where it is coupled to secretion across the cell outer membrane via nucleation by elements of the transporter complex.
The directed movement of proteins across the cell outer membrane.
Protein secretion through the outer membrane via the mechanism used for the secretion of curli subunits.
The secretion of soluble curli subunits through the outer membrane, coupled to nucleation of curli fiber formation at the membrane surface.
Any process that activates or increases the frequency, rate or extent of mitophagy in response to mitochondrial depolarization.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) in response to the depolarization of one or more mitochondria.
The transcription of non (protein) coding RNA from a DNA template.
Enables the transmembrane transfer of a potassium ion by a channel that opens in response to a mechanical stress.
The cell cycle process that corrects the anomalous association of a single chromatid kinetochore with mitotic spindle microtubules emanating from both spindle poles (otherwise known as merotelic attachment to the spindle).
A process that results in the assembly, arrangement of constituent parts, or disassembly of a biofilm matrix.
A process that results in the assembly of a biofilm matrix.
A process that results in the disassembly of a biofilm matrix.
Cleavage of an immature mRNA transcript to produce one or more more mature mRNA transcripts, prior to translation into polypeptide.
The terminal swelling of an apical dendrite of a ciliated olfactory receptor neuron. Each knob gives rise to 5 to 20 long delicate nonmotile cilia, which extend into the mucus covering the sensory epithelium.
The targeted, endonucleolytic cleavage of a pre-mRNA,  required for polyadenylation of the 3' end.  This cleavage is directed by binding sites near the 3' end of the mRNA and leaves a 3' hydoxyl end which then becomes a target for adenylation.
The targeted, endonucleolytic cleavage of a pre-mRNA,  required for polyadenylation of the 3' end.  This cleavage is directed by binding sites near the 3' end of the mRNA and leaves a 3' hydoxyl end which then becomes a target for adenylation.
The transcription of non-coding RNA associated with transcriptional start and end sites of protein coding genes. This occurs at some low level for many protein coding genes.
A compartment that consists of a lumen and an enclosing membrane, and is part of the Golgi Apparatus.
The macroautophagy process in which a region of cytoplasm containing an intracellular pathogen or some part of an intracellular pathogen (e.g. viral capsid) is enclosed in a double membrane bound autophagosome, which then fuses with the lysosome leading to degradation of the contents.
The part of a synapse that is part of the presynaptic cell.
The part of a synapse that is part of the post-synaptic cell.
Cleavage of an mRNA occurring as part of the mechanism of gene silencing.
Any protein complex that is part of a membrane.
Any protein complex that is part of the plasma membrane.
A protein complex that is part of a mitochondrion.
Any protein complex that is part of the outer mitochondrial membrane.
Any protein complex that is part of the inner mitochondrial membrane.
Any process that modulates the frequency, rate or extent of a system process, a multicellular organismal process carried out by the renal system.
Any protein complex that is part of the plasma membrane and which functions as a receptor.
Any protein complex that is part of a respiratory chain
The portion of the plasma membrane surrounding a non-motile cilium.
Any lipid bilayer that completely encloses some structure, and all the proteins embedded in it or attached to it.  Examples include the plasma membrane and most organelle membranes.
Shortening of the poly(A) tail of a nuclear-transcribed mRNA following miRNA binding to mRNA, resulting in destabilization of the mRNA and a reduction in the efficiency of its translation.
A protein complex that is part of a chloroplast thylakoid membrane.
Interacting selectively and non-covalently with a 7-methylguanosine (m7G) group or derivative located at the 5' end of an mRNA molecule.
Catalysis of the reaction: nitrite + acceptor = product(s) of nitrate reduction + reduced acceptor.
The directed movement of neurotransmitter molecules from the extrasynaptic space into the presynaptic cytosol.
The enzymatic addition of a sequence of adenylyl residues (polyadenylation) at the 3' end of a rRNA, occurring as part of the process of polyadenylation-dependent rRNA catabolism in the nucleus.
The enzymatic addition of a sequence of adenylyl residues (polyadenylation) at the 3' end of a rRNA, occurring as part of the process of polyadenylation-dependent rRNA catabolism in the nucleus.
The process in which genetic material, in the form of nuclear chromosomes, is organized into specific structures and then physically separated and apportioned to two or more sets. Nuclear chromosome segregation begins with the condensation of chromosomes, includes chromosome separation, and ends when chromosomes have completed movement to the spindle poles.
The low level of synaptic transmission that occurs via spontaneous neurotransmitter release into the synaptic cleft in the absence of a presynaptic action potential.
Any process that modulates the frequency, rate or extent of excitatory postsynaptic potential (EPSP). EPSP is a process that leads to a temporary increase in postsynaptic potential due to the flow of positively charged ions into the postsynaptic cell. The flow of ions that causes an EPSP is an excitatory postsynaptic current (EPSC) and makes it easier for the neuron to fire an action potential.
A process that leads to a temporary increase in postsynaptic potential due to the flow of positively charged ions into the postsynaptic cell, induced by the spontaneous release of a single vesicle of an excitatory neurotransmitter into the synapse.
A process that leads to a temporary increase in postsynaptic potential due to the flow of positively charged ions into the postsynaptic cell induced by the evoked release of many vesicles of excitatory neurotransmitter at the synapse.
A process that hyerpolarizes a postsynaptic membrane relative to its resting potential.  This has an inhibitory effect on the post-synaptic cell, moving the membrane potential away from the firing threshold.
A process that depolarizes a postsynaptic membrane relative to its resting potential.  This has an excitatory effect on the post-synaptic cell, moving the membrane potential towards the firing threshold.
A protein complex that spans the synaptic cleft and has parts in both the pre- and post-synaptic membranes.
Combining with a member of the bone morphogenetic protein (BMP) family, and transmitting a signal across the plasma membrane to initiate a change in cell activity.
The modification of peptidyl-cysteine to form peptidyl-L-cysteine persulfide.
The amidinylation of peptidyl-cysteine to form peptidyl-S-amidino-L-cysteine.
The sulfation of peptidyl-cysteine to form S-sulfo-L-cysteine.
The guanylylation of peptidyl-histidine to form (phospho-5'-guanosine)-L-histidine.
The membrane of the endoplasmic reticulum tubular network.
A distinct  region of the endoplasmic reticulum
Any process that modulates the frequency, rate or extent of inhibitory postsynaptic potential (IPSP). IPSP is a temporary decrease in postsynaptic membrane potential due to the flow of negatively charged ions into the postsynaptic cell. The flow of ions that causes an IPSP is an inhibitory postsynaptic current (IPSC) and makes it more difficult for the neuron to fire an action potential.
Uptake of folic into the blood by absorption from the small intestine.
An endosome present in the presynapse that fuses with endocytic vesicles arising in the presynaptic endocytic zone.  This organelle is believed to be involved in regeneration of synaptic vesicles.
A specialized region below the presynaptic membrane, characterized by electron-dense material, a specialized cytoskeletal matrix and accumulated (associated) synaptic vesicles.
A specialized region below the presynaptic membrane, characterized by electron-dense material, a specialized cytoskeletal matrix and accumulated (associated) synaptic vesicles.
A recycling endosome that is organized around the microtubule organizing center, close to the nucleus. This is the main recycling endosome of most cells. It receives input from the Golgi as well as recycled molecules from early endosomes.
A specialized region of the plasma membrane and underlying cytoplasm which surround the the active zone, into which synaptic vesicle membranes are recycled following exocytosis.  It is especially enriched in endocytic proteins following intense activity.
The cytoplasmic component of the presynaptic endocytic zone.
The region of the presynaptic membrane that is part of the presynaptic endocytic zone - where synaptic vesicles are endocytosed and recycled following release.
The portion of the cytoskeleton that lies within a dendritic spine.  The actin component of this cytoskeleton is involved in spine head remodelling in response to postsynaptic signalling.
A recycling endosome of the postsynapse. In postsynaptic terminals with dendritic spines, it is typically located at the base of a dendritic spine. It is involved in recycling of neurotransmitter receptors to the postsynaptic membrane.  In some cases at least, this recycling is activated by postsynaptic signalling and so can play a role in long term potentiation.
A recycling endosome of the postsynapse. In postsynaptic terminals with dendritic spines, it is typically located at the base of a dendritic spine. It is involved in recycling of neurotransmitter receptors to the postsynaptic membrane.  In some cases at least, this recycling is activated by postsynaptic signalling and so can play a role in long term potentiation.
The process in which a folic acid, or one of its derivatives (dihydrofolate, tetrahydrofolate, methylene-tetrahydrofolate or methyl-tetrahydrofolate) is transported across a membrane.
The process in which a folic acid, or one of its derivatives (dihydrofolate, tetrahydrofolate, methylene-tetrahydrofolate or methyl-tetrahydrofolate) is transported across a membrane.
The membrane component of the postsynaptic density. This is the region of the postsynaptic membrane in which the population of neurotransmitter receptors involved in synaptic transmission are concentrated.
The directed movement of a protein along a microtubule, mediated by motor proteins.
A cellular protein localization process in which a protein is transported to, or maintained at, the site of cell division following cytokinesis.
An early endosome of the postsynapse. It acts as the major sorting station on the endocytic pathway, targeting neurotransmitter receptors for degregation or recycling.
A stably positioned site of clathrin adjacent and physically attached to the postsynaptic specialization, which is the site of endocytosis of post-synaptic proteins.
The region of the postsynaptic membrane that is part of the postsynaptic endocytic zone.  This region of membrane is associated with stable clathrin puncta.
An endosomal compartment that is part of the post-synapse. Only early and recycling endosomes are typically present in the postsynapse.
A cell projection of a podocyte (glomerular visceral epithelial cell) forming a foot-like structure projecting from a podocyte primary projection, that wraps around capillaries of a renal glomerulus. Adjacent feet (pedicels) interdigitate, leaving thin filtration slits between them, which are covered by slit diaphragms.
A cell projection of a podocyte (glomerular visceral epithelial cell) forming a foot-like structure projecting from a podocyte primary projection, that wraps around capillaries of a renal glomerulus. Adjacent feet (pedicels) interdigitate, leaving thin filtration slits between them, which are covered by slit diaphragms.
A cell projection of a podocyte (glomerular visceral epithelial cell) forming a foot-like structure projecting from a podocyte primary projection, that wraps around capillaries of a renal glomerulus. Adjacent feet (pedicels) interdigitate, leaving thin filtration slits between them, which are covered by slit diaphragms.
Interacting selectively and non-covalently with single-stranded DNA of a specific nucleotide composition.
Catalysis of the reaction: alpha-D-ribose 1-methylphosphonate 5-phosphate = alpha-D-ribose 1,2-cyclic phosphate 5-phosphate + methane.
Any process that reduces or removes the toxicity of cadmium cations in a cell. These include transport of cadmium cations away from sensitive areas and to compartments or complexes whose purpose is sequestration.
The component of the synaptic vesicle 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 double-stranded miRNA. double-stranded miRNA is formed by processing of pre-miRNA stem-loop structures.
The lipid bilayer surrounding a lytic vacuole and separating its contents from the cytoplasm of the cell.
A zone of apposition between endoplasmic-reticulum and lytic vacuole membranes, structured by bridging complexes.
A cell projection originating from a renal glomerular podocyte and extending to the renal glomerular podocyte foot.
A cell projection originating from a renal glomerular podocyte and extending to the renal glomerular podocyte foot.
A cell projection originating from a renal glomerular podocyte and extending to the renal glomerular podocyte foot.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
Any process in which lipids are taken up from the contents of the intestine.
A membrane region with a lipid composition that is distinct from that of the membrane regions that surround it.
A cell projection supported by an assembly of actin filaments, and which lacks microtubules.
A bundle of cross-linked actin filaments that is part of an actin-based cell protrusion, in which filaments are oriented such that the plus (barbed) ends are at the tip of the protrusion, capped by a tip complex which stabilizes the filaments.
A bundle of hundreds of cross-linked actin filaments (an actin cable), that is the supporting structure of a stereocilium.  Filaments are oriented such that the the plus (barbed) ends are at the tip of the protrusion and are capped by a tip complex which bridges to the plasma membrane.
A parallel bundle of actin filaments that is part of filopodium. Filaments are oriented such that the plus (barbed) ends are at the tip of the protrusion, capped by a tip complex.
A cell part consisting of multiple, closely packed actin-based cell projections.
The directed movement of the nucleus by pushing forces exerted by polymerization of backward-extending microtubules.
The process in which a symbiont organism effects a change in the structure or function of its host tight junction, a cell-cell junction that seals cells together in an epithelium in a way that prevents even small molecules from leaking from one side of the sheet to the other.
The process in which an organism effects a change in the structure or function of its host bicellular tight junctions, an occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet
The fusion of the membrane of a multivesicular body with the apical plasma membrane, resulting in release of exosomes from the cell.
The increase in size or mass of an intramembranous bone that contributes to the shaping of the bone.
The increase in size or mass of a bone that contributes to the shaping of that bone.
Any process carried out at the cellular level that reduces or removes the toxicity superoxide radicals or hydrogen peroxide.
The propagation of an action potential along the plane of an excitable membrane.  Action potentials typically propagate once triggered because the depolarization of adjacent membrane regions due to an action potential crosses the firing threshold.
The actin cytoskeleton that is part of a postsynapse
A G protein-coupled neurotransmitter receptor activity occurring in the postsynaptic membrane, that is involved in regulating the cytosolic concentration of calcium ions in the postsynapse.
A G protein-coupled neurotransmitter receptor activity occurring in the postsynaptic membrane, that is involved in regulating the cytosolic concentration of calcium ions in the postsynapse.
Propagation of an action potential in a neuron, from its site of initiation (typically the axon hillock) towards the soma.
A series of sequential, propagated action potentials occurring in a single cell.
A series of sequential, propagated action potentials occurring in a single cell.
A series of sequential, propagated action potentials occurring in a single cell.
A microvesicle of the epididymal fluid, from which spermatozoa aquire membrane proteins.
The directed movement of substances to the plasma membrane in transport vesicles that fuse with the plasma membrane by exocytosis.
The directed movement of neurotransmitter receptor to the plasma membrane in transport vesicles.
Any protein complex that is capable of functioning as a neurotransmitter receptor.
The action of a molecule that contributes to the structural integrity of a postsynaptic specialization.
A process which maintains the organization and the arrangement of proteins in the presynaptic specialization.
The exocytic fusion of neurotransmitter receptor containing vesicles with a plasma-membrane resulting in the integration of NT receptors with the plasma-membrane. This process includes tethering and docking steps that prepare vesicles for fusion.
The action of a molecule that contributes to the structural integrity of a presynaptic active zone.
A cellular process that results in the controlled breakdown of synapse. After it starts the process is continuous until the synapse has disappeared.
A cellular process that results in the controlled breakdown of synapse. After it starts the process is continuous until the synapse has disappeared.
A cellular process that results in the controlled breakdown of synapse. After it starts the process is continuous until the synapse has disappeared.
A cellular process that results in the controlled breakdown of synapse. After it starts the process is continuous until the synapse has disappeared.
A receptor-mediated endocytosis process that results in the internalization of a neurotransmitter receptor from the postsynaptic membrane endocytic zone into an endocytic vesicle.
Any process that modifies the structure of a postsynaptic actin cytoskeleton.
Any process that modifies the structure of a dendritic spine.
The directed movement of neurotransmitter receptor from the postsynaptic endosome to the postsynaptic membrane in transport vesicles.
The component of the presynaptic 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 presynaptic 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 postsynaptic 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 presynaptic active zone 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 postsynaptic specialization 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 postsynaptic endocytic zone 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 presynaptic endocytic zone 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 lipid bilayer surrounding a postsynaptic endosome.
The lipid bilayer surrounding a postsynaptic early endosome.
The lipid bilayer surrounding the spine apparatus.
The volume enclosed by the dense core granule membrane.
The volume enclosed by the spine apparatus membrane.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in a cardiac muscle cell. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the rate, frequency or extent of membrane depolarization during an action potential. Membrane depolarization is the process in which membrane potential changes in the depolarizing direction from the resting potential.
Any process that modulates the rate, frequency or extent of membrane repolarization during an action potential. Membrane repolarization is the process in which membrane potential changes in the repolarizing direction, towards the resting potential.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in an atrioventricular node myocyte. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in an atrioventricular node myocyte. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in a cardiac muscle cell of the bundle of His. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in a Purkinje myocyte. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in an SA node cardiac myocyte. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in an SA node cardiac myocyte. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in an SA node cardiac myocyte. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in an SA node cardiac myocyte. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in a neuron. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in a cardiac muscle cell contributing to the regulation of its contraction.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in an atrial cardiac muscle cell contributing to the regulation of its contraction. This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
Any process that modulates the frequency, rate or extent of action potential creation, propagation or termination in a ventricular cardiac muscle cell contributing to the regulation of its contraction.  This typically occurs via modulation of the activity or expression of voltage-gated ion channels.
The process in which atrial cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which atrial cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which atrial cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which ventricular cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which ventricular cardiac muscle cell membrane potential changes in the depolarizing direction from the negative resting potential towards the positive membrane potential that will be the peak of the action potential.
The process in which ions are transported across a membrane such that the atrial cardiomyocyte membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which ions are transported across a membrane such that the atrial cardiomyocyte membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which ions are transported across a membrane such that the ventricular cardiomyocyte membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which ions are transported across a membrane such that the ventricular cardiomyocyte membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
The process in which ions are transported across a membrane such that the ventricular cardiomyocyte membrane potential changes in the direction from the positive membrane potential at the peak of the action potential towards the negative resting potential.
Cell-cell signaling from pre to post-synapse, across the synaptic cleft
Cell-cell signaling from post to pre-synapse, across the synaptic cleft
The action of a molecule that contributes to the structural integrity of a synapse.
The action of a molecule that contributes to the structural integrity of a postsynaptic density.
Cell-cell signaling from postsynapse to presynapse, across the synaptic cleft, mediated by a lipid ligand.
Cell-cell signaling from postsynapse to presynapse, across the synaptic cleft, mediated by an  endocannabinoid ligand.
The component of the dense core granule membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
Cell-cell signaling from postsynapse to presynapse, across the synaptic cleft, mediated by an soluble gas ligand.
Cell-cell signaling from postsynapse to presynapse, across the synaptic cleft, mediated by nitric oxide.
Modulation of synaptic transmission by cell-cell signaling from postsynapse to presynapse, across the synaptic cleft, mediated by nitric oxide.
Signal transduction in which the initial step occurs in a postsynapse.
A cellular transport process in which transported substances are moved in membrane-bounded vesicles between endosomal compartments, e.g, between early endosome and sorting endosome.
Signal transduction in which the initial step occurs in a presynapse.
The component of the spine apparatus 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 directed movement of organelles or molecules along microtubules in axons.
The directed movement of organelles or molecules along microtubules in axons.
The process by which a virion attaches to a the host cell flagellum. Some DNA bacterial viruses use flagella to attach to the host cell. This contact with the flagellum facilitates concentration of phage particles around the entry receptor on the bacterial cell surface.
A process carried out by a virus that breaks down peptidoglycans in the cell wall of its host during viral entry.
A process carried out by a virus that breaks down peptidoglycans in the cell wall of its host during viral entry.
A process carried out by a virus that breaks down peptidoglycans in the cell wall of its host during viral entry.
A process carried out by a virus that breaks down peptidoglycans in the cell wall of its host during viral entry.
The process by which a symbiont breaks down the cell wall of its host. The host is defined as the larger of the organisms involved in a symbiotic interaction.
The directed movement of organelles or molecules along microtubules in a dendrite from the postsynapse towards the cell body.
The directed movement of organelles or molecules along microtubules in dendrites.
The component of the postsynaptic 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 directed movement of organelles or molecules along microtubules from the cell body toward the postsynapse in dendrites.
The actin cytoskeleton that is part of a dendritic spine.
The directed movement of mitochondria along microtubules in nerve cell dendrites.
Cell-cell signaling from presynapse to postynapse, across the synaptic cleft, mediated by nitric oxide.
Cell-cell signaling from presynapse to postynapse, across the synaptic cleft, mediated by a trans-synaptic protein complex.
Cell-cell signaling from postsynapse to presynapse, across the synaptic cleft, mediated by trans-synaptic protein complex.
The directed movement of neurotransmitter receptor from the postsynaptic endosome in tranpsort vesicles to the lysosome for degradation.
The lipid bilayer surrounding a postsynaptic recycling endosome.
The component of the presynaptic active zone 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 presynaptic endocytic zone 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 postsynaptic endocytic zone 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 postsynaptic specialization 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 postsynaptic 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 postsynaptic early 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 postsynaptic recycling 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 spine apparatus 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 process by which a membrane receptor, diffusing freely within the plasma membeane, becomes trapped in some plasma membrane region.  This can happen when a receptor bind, directly or indirectly, to some component of the underlying matrix.
The lipid bilayer surrounding a presynaptic endosome.
The component of the presynaptic 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 dense core granule 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 directed movement of mitochondria along microtubules in axons away from the cell body and towards the presynapse.
The directed movement of mitochondria along microtubules in axons towards the cell body and away from the presynapse.
The directed movement of mitochondria along microtubules in dendrites towards the cell body and away from the postsynapse.
Neurotransmitter receptor activity occuring in the postsynaptic membrane during synaptic transmission.
The directed movement of a ribonucleoprotein complex along microtubules in nerve cell dendrites.
Any process that modulates the frequency, rate or extent of neurotransmitter receptor activity involved in synaptic transmission. Modulation may be via an effect on ligand affinity, or effector funtion such as ion selectivity or pore opening/closing in ionotropic receptors.
The directed movement of a messenger ribonucleoprotein complex along microtubules in nerve cell dendrites.
The directed movement of a messenger ribonucleoprotein complex along microtubules in nerve cell dendrites towards the postsynapse.
The portion of the extracellular matrix that lies within the synaptic cleft.
The portion of the extracellular matrix that lies within the synaptic cleft.
The portion of the extracellular matrix that lies within the perisynaptic space.
The portion of the extracellular matrix that lies within the perisynaptic space.
The exocytic fusion of neurotransmitter receptor containing vesicles with the postsynaptic membrane resulting in the integration of NT receptors, enabling them to participate in neurotransmitter reception.  This process includes tethering and docking steps that prepare vesicles for fusion.
Vesicle-mediated transport of a neurotransmitter receptor complex from the postsynaptic membrane to the postsynaptic early endosome.
The directed movement of neurotransmitter receptor to the postsynaptic membrane in transport vesicles.
The process by which diffusing neurotransmitter receptor becomes trapped at the postsynaptic specialization membrane. This is typically due to interaction with components of the post-synaptic specialization.
The directed movement of a neurotransmitter receptor complex along microtubules in nerve cell dendrites towards the postsynapse.
The directed movement of mitochondria along microtubules in dendrites towards the postsynapse and away from the cell body.
The action of a molecule that contributes to the structural integrity of a postsynaptic actin cytoskeleton.
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 actin filaments and their associated proteins in the postsynaptic actin cytoskeleton.
The postsynapse of a neuromuscular junction. In vertebrate muscles this includes the motor end-plate, consisting of postjunctional folds of the sarcolemma.
Synaptic transmission that results in an excitatory postsynaptic potential.
Synaptic transmission that results in an inhibitory postsynaptic potential.
A synapse that uses glutamate as a neurotransmitter.
A synapse consisting of a single presynapse and multiple postsynapses.  These postsynapses may come from the same cell of from different cells. Polyadic synapses are common in arthropod and nematode central nervous systems.
An electron dense specialization of the presynaptic active zone cytoskeleton.
A synapse that uses acetylcholine as a neurotransmitter.
A synapse that uses GABA as a neurotransmitter.  These synapses are typically inhibitory.
A neuron to neuron synapse that lacks an electron dense postsynaptic specialization, uses GABA as a neurotransmitter and whose activity results in inhibitory postsynaptic potentials.
A synapse in which pre and post-synaptic cells are neurons.
A neuron to neuron synapse with a postsynaptic density, that uses glutamate as a neurotransmitter and whose activity results in excitatory postsynaptic potentials.
A T-shaped presynpatic density.  These are common in arhropod central nervous systems.
Any process that regulates the modification of synaptic structure and as a result regulates synaptic transmission.
Combining with glutamate and transmitting a signal from one side of the membrane to the other by activating an associated G-protein, initiating a change in cell activity.
A series of molecular signals initiated by glutamate binding to an NMDA-selective glutamate receptor on the surface of the target cell, followed by the movement of ions through a channel in the receptor complex. Ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by glutamate binding to an AMPA-selective glutamate receptor on the surface of the target cell, followed by the movement of ions through a channel in the receptor complex. Ends with regulation of a downstream cellular process, e.g. transcription.
A series of molecular signals initiated by glutamate binding to an kainate-selective glutamate receptor on the surface of the target cell, followed by the movement of ions through a channel in the receptor complex. Ends with regulation of a downstream cellular process, e.g. transcription.
A dense core vesicle (granule) that is part of a neuron.  These vesicles typically contain neuropeptides.  They can be found in all parts of neurons, including the soma, dendrites, axonal swellings (varicosities) and synaptic terminals.
The component of the synaptic vesicle membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The disruption of host cell envelope by viral proteins during virus entry
The breakdown of lipopolysaccharides in a host cell envelope during virus entry into a host cell.  For example a phage entering a gram-negative bacterium may actively break down outer membrane lipopolysaccharides.
The breakdown of lipopolysaccharides in a host cell envelope during virus entry into a host cell.  For example a phage entering a gram-negative bacterium may actively break down outer membrane lipopolysaccharides.
The breakdown of lipopolysaccharides in a host cell envelope during virus entry into a host cell.  For example a phage entering a gram-negative bacterium may actively break down outer membrane lipopolysaccharides.
The disruption of host cell glycocalyx by viral proteins during virus entry
The disruption of host cell glycocalyx by viral proteins during virus entry
The disruption of host cell glycocalyx by viral proteins during virus entry
The disruption of host cell glycocalyx by viral proteins during virus entry
Fusion of a viral membrane with the host cell outer membrane during viral entry.
Fusion of a viral membrane with the host cell outer membrane during viral entry.
Fusion of a viral membrane with the host cell outer membrane during viral entry.
Fusion of a viral membrane with the host cell outer membrane during viral entry.
Fusion of a viral membrane with the host cell outer membrane during viral entry.
The component of the postsynaptic early 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 the postsynaptic 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.
Ejection by a non-enveloped prokaryotic virus of its genome into the host cytoplasm via a contractile tail ejection system consisting of a baseplate, a central tube and an external contractile sheath.   Upon binding to the host cell surface, the baseplate changes its conformation and triggers sheath contraction, driving the rigid internal tail tube through the cell envelope.
Ejection by a non-enveloped prokaryotic virus of its genome into the host cytoplasm via a long, flexible tail ejection system consisting a baseplate, a central tube and a terminator complex which attaches the tail to the phage capsid.  Upon binding to the host cell surface, the baseplate changes its conformation and triggers genome ejection into the host cell cytoplasm.
Ejection by a non-enveloped prokaryotic virus of its genome into the host cytoplasm via a short tail ejection system consisting a central tube, the connector which attaches the tail to the phage capsid and releases inner core proteins.  Upon binding to the host cell surface, the phage displays a tube-like extension of its short tail that penetrates both host membranes. This tail extension comes from the release of viral core proteins with channel forming properties.
Any vesicle-mediated transport that occurs in a synapse
Any signal transduction pathway involving calmodulin dependent kinase activity.
The component of the postsynaptic recycling 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 entry of a non-enveloped virus into a host eukaryotic cell, following endocytosis, via permeabilization of the endosomal membrane by membrane penetration protein(s) associated with the viral capsid.  In some cases, viral membrane-penetration protein require first to be activated to display its membrane penetrating activity. Activation can be due to receptor binding or the acidic pH of the endosomal lumen.
The component of the presynaptic 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 entry of a non-enveloped virus into the cytoplasm of a host prokaryotic cell, following fusion with the outer membrane, via permeabilization of the plasma (inner) membrane.  In the case of some double stranded RNA viruses of prokaryotes this occurs via interaction of a membrane-interacting component of the capsid, leading to depolarization an permeabilization of the plasma membrane.
The circularization of a viral genome following infection of a host cell. This is common amongst bacterial viruses to protect the viral genome ends from nucleases, to convert the linear genome to an integrative precursor or to give rise to the replicative form of the genome. It can be mediated by covalent closure of the DNA sticky ends, recombinaison between redundant terminal sequences or via the binding of a protein at the viral DNA extremities
Any process that modifies the structure of a postsynapse.
The secretion of molecules (e.g. neuropeptides, insulin-related peptides or neuromodulators such as serotonin and dopamine) contained within a neuronal dense core vesicle by fusion of the granule with the plasma membrane of a neuron in response to increased cytosolic calcium levels.
The lipid bilayer surrounding a neuronal dense core vesicle.
The volume enclosed by a neuronal dense core vesicle membrane.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a neuronal dense core vesicle.
The catabolic breakdown of the DNA of a host chromosome by a virus.  This occurs during infection of bacteria by some phages.  It frees up a large pool of nucleoside 5'-triphophates for use in viral DNA synthesis.
Any process, either active or passive, by which a virus evades and ends degradation of its DNA when free viral-DNA ends are exposed as part of its life-cycle.  For example, some bacteriophages encode proteins that bind to free viral DNA ends, protecting them from degradation by host exonucleases.
Any process in which localization of a protein is maintained at the cell tip.
Any process, either active or passive, by which a virus evades the DNA restriction modification system of its host. Some viruses encode their own methyltransferase in order to protect their genome from host restriction enzymes. Others directly inhibit restruction enzymes while some use unusual bases in their genome to avoid restriction.
Any process in which localization of a protein is maintained at the growing cell tip.
The volume enclosed by the membranes of the perinuclear endoplasmic reticulum.
The volume enclosed by the membranes of the cortical endoplasmic reticulum.
The initial, indirect interaction between a vesicle membrane and a membrane to which it is targeted for fusion. This interaction is mediated by tethering factors (or complexes), which interact with both membranes.  Interaction can occur via direct binding  to membrane phospholipids or membrane proteins, or via binding to vesicle coat proteins. This process is distinct from and prior to interaction between factors involved in fusion.
Any protein complex that plays a role in vesicle tethering.
An infolding of the plasma membrane.
The component of the postsynaptic membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the presynaptic membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the presynaptic endocytic zone membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the postynaptic endocytic zone membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the presynaptic active zone membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the postsynaptic specialization membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the postsynaptic density membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the postsynaptic early endosome membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the postsynaptic recycling endosome membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the postsynaptic endosome membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the spine apparatus membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the neuronal dense core vesicle membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
The component of the presynaptic endosome membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
Catalysis of the movement of ceramide from one membrane bilayer leaflet to the other, driven by the hydrolysis of ATP.
The movement of a sphingolipid molecule from one leaflet of a membrane bilayer to the opposite leaflet.
The movement of a ceramide molecule from one leaflet of a membrane bilayer to the opposite leaflet.
The initial, indirect interaction between a transport vesicle membrane and the membrane of the Golgi. This interaction is mediated by tethering factors (or complexes), which interact with both membranes.  Interaction can occur via direct binding  to membrane phospholipids or membrane proteins, or via binding to vesicle coat proteins. This process is distinct from and prior fusion.
The first step in clathrin-dependent endocytosis: invagination of the plasma membrane to form a pit.
Formation of a macromolecular complex during clathrin-dependent endocytosis that connects the assembling clathrin coat to the proteins and/or lipoproteins to be transported in an endocytic vesicle. This complex includes a receptor and an adaptor protein that links the receptor to the clathrin coat.
The initial, indirect interaction between a transport vesicle membrane and the membrane of the endoplasmic reticulum. This interaction is mediated by tethering factors (or complexes), which interact with both membranes.  Interaction can occur via direct binding  to membrane phospholipids or membrane proteins, or via binding to vesicle coat proteins. This process is distinct from and prior fusion.
The process whereby a filamentous phage particle is released from a bacterial host cell via a concerted mechanism of assembly and secretion. Neosynthesized virions are coordinately exported as they are assembled at the cell surface in a secretory process that leaves the host cell fully viable.  Non-capsid proteins form structures that facilitate translocation through the inner membrane and outer membranes. A viral single-stranded DNA binding protein coats progeny viral DNA molecules to generate the intracellular precursor for assembly of phage particles as they are extruded through the membranes of the bacterial host. The structural proteins of the virus are anchored in the inner membrane before their incorporation into the phage particle. As assembly proceeds, the phage genome traverses the inner and outer membranes until the entire DNA molecule has been coated and extruded.
A defense process that protects an organism from invading foreign DNA or RNA.
A defense process that protects an organism from invading foreign RNA.
An adaptive immune response of bacteria that serves to clear host cells of foreign DNA and RNA. It has three distinct stage: acquisition of foreign DNA by integration into CRISPR loci in the host chromosome, CRISPR RNA (crRNA) biogenesis, and target interference. CISPR stands for Clustered Regularly Interspaced Short Palindromic Repeat, which describes the nature of the loci.
The process that results in the assembly of clathrin triskelia into a clathrin cage during endocytosis. Clathrin is recruited to the plasma membrane via interaction with scaffolding proteins that bridge between clathtin and cell surface receptors. Clathrin coat formation is concomittant with coated pit formation leading to endocytic vesicle formation.
The membrane scission process that is the final step in the formation of a vesicle, leading to separation from its parent membrane. Vesicle scission involves the constriction of a neck-forming protein complex, consisting e.g. of dynamin, around the budded membrane, leading to vesicle closure during its separation from the parent membrane.
The membrane scission process that is the final step in the formation of an endocytic vesicle: separation from the plasma membrane.
The membrane scission process that is the final step in the formation of a clathrin-coated endocytic vesicle: separation from the plasma membrane.
A protein complex that contains TRIP4 (ASC1) and acts a transcriptional coactivator by interacting with transcription factors such as NF-kappa B.  In humans this complex has 4 subunits: TRIP4 + ASCC1-3.
The aggregation, arrangement and bonding together of a set of components to form a presynapse.
The aggregation, arrangement and bonding together of a set of components to form a presynapse.
The component of the postsynaptic 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 presynaptic 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 presynaptic endocytic zone 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 postsynaptic endocytic zone 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 presynaptic active zone 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 postsynaptic specialization 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 postsynaptic density 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 postsynaptic early endosome 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 postsynaptic recycling endosome 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 postsynaptic endosome 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 spine apparatus 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 neuronal dense core 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.
The component of the presynaptic endosome 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 aggregation, arrangement and bonding together of a set of components to form a postsynapse.
The initial, indirect interaction between a synaptic vesicle membrane and a the preseynaptic membrane active zone. This interaction is mediated by tethering factors (or complexes), which interact with both membranes. This process is distinct from and prior to synaptic vesicle priming and fusion.
A microtubule bundle that has a constant length, and in which microtubule sliding does not take place.
A microtubule bundle that has a constant length, and in which microtubule sliding does not take place.
A microtubule bundle that has a constant length, and in which microtubule sliding does not take place.
A microtubule bundle that undergoes changes in length, and in which microtubule sliding takes place.
Any process that regulates the the local concentration of neurotransmitter receptor at the postsynaptic membrane.
A vesicle derived via budding from a mitochondrion.  These vesicles often contain inner membrane and, much more rarely, cristae.
Transport from the mitochondrion to the lysosome, mediated by mitochondrion-derived vesicles
Transport from the mitochondrion, mediated by mitochondrion derived vesicles.
Transport from the mitochondrion to the peroxisome, mediated by mitochondrion-derived vesicles.
DNA-binding activity that is dependent on binding to a histone.
A protein complex that is invovled in positioning of the lysosome within the cytoplasm and which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN. The BORC complex recruits ARL8 at the cytosolic face of lysosomes and couples them to microtubule plus-end-directed kinesin motors.
An amorphous cytoskeletal structure consisting of aggregated actin filaments and associated proteins (including fibrin and capping protein) in which there is little or no actin filament turnover.  In yeast (S. pombe and S. cerevisiae) these are found only in quiescent cells and are thought to serve as a reserve store of actin.
A cellular component that consists of an indeterminate number of proteins or macromolecular complexes, organized into a regular, higher-order structure such as a polymer, sheet, network or a fiber.
A polymeric supramolecular structure.
Cell-cell signaling from postsynapse to presynapse, across the synaptic cleft, mediated by a neuropeptide.
Modulation of synaptic transmittion by cell-cell signaling across the synaptic cleft from postsynapse to presynapse, mediated by a neuropeptide.
A process that results in the assembly, arrangement of constituent parts, or disassembly of a postsynaptic specialization, a structure that lies adjacent to the cytoplasmic face of the postsynaptic membrane.
A process that results in the assembly, arrangement of constituent parts, or disassembly of a postsynaptic specialization, a structure that lies adjacent to the cytoplasmic face of the postsynaptic membrane.
A process that results in the assembly, arrangement of constituent parts, or disassembly of a postsynaptic specialization, a structure that lies adjacent to the cytoplasmic face of the postsynaptic membrane.
Catalysis of the reaction: 1-[(3,5-dichloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one => 1-[(3-chloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one + Cl-
Catalysis of the reaction: 1-[(3,5-dichloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one => 1-[(3-chloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one + Cl-
Catalysis of the reaction: 1-[(3,5-dichloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one => 1-[(3-chloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one + Cl-
Catalysis of the reaction: 1-[(3,5-dichloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one => 1-[(3-chloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one + Cl-
Catalysis of the reaction: 1-[(3,5-dichloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one => 1-[(3-chloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one + Cl-
Catalysis of the reaction: 1-[(3,5-dichloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one => 1-[(3-chloro-2,6-dihydroxy-4-methoxy)phenyl]hexan-1-one + Cl-
A proteinaceous scaffold found between homologous chromosomes during meiosis.
The directed movement of a messenger ribonucleoprotein complex along microtubules in axons, towards the presynapse.
The directed movement of a messenger ribonucleoprotein complex along microtubules in axons.
The directed movement of endoplasmic reticulum into a postsynaptic compartment such as a dendritic spine.
A network of proteins adjacent to the postsynaptic membrane. Its major components include the proteins that spatially and functionally organize neurotransmitter receptors in the adjacent membrane, such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
A network of proteins adjacent to the postsynaptic membrane forming an electron dense disc. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize neurotransmitter receptors in the adjacent membrane, such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
A process in which a calcium ion (Ca2+) is transported out of the mitochondrial matrix, and into the cytosol.
A process in which a calcium ion (Ca2+) is transported out of the mitochondrial matrix, and into the cytosol.
A process in which a calcium ion (Ca2+) is transported out of the mitochondrial matrix, and into the cytosol.
Enables the transmembrane transfer of an inorganic cation 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 an inorganic anion by a channel that opens when a specific ligand has been bound by the channel complex or one of its constituent parts.
The giant, cup-shaped axon terminal of a vestibular afferent neuron, serving as a post-synaptic contact to a type I hair cell.
A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a prospore membrane.
The movement of a cellular component as a result of microtubule polymerization.
An ion channel activity that is gated by binding of a G-protein beta-gamma dimer.
A cation channel activity that is gated by binding of a G-protein beta-gamma dimer.
A potassium channel activity that is gated by binding of a G-protein beta-gamma dimer.
Any G-protein gated potassium channel activity that is involved regulation of postsynaptic membrane potential.
Direct interaction with a channel (binding or modification), resulting in its opening. A channel catalyzes energy-independent facilitated diffusion, mediated by passage of a solute through a transmembrane aqueous pore or channel.
Direct interaction with a potassium channel (binding or modification), resulting in its opening.
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds through activation or inhibition of an ion channel.
Modulates the activity of a channel via direct interaction with it. A channel catalyzes energy-independent facilitated diffusion, mediated by passage of a solute through a transmembrane aqueous pore or channel.
Modulation of the activity of an ion channel via direct interaction with it as part of G protein-coupled receptor signaling.
Activation potassium ion channel activity via direct interaction with a potassium ion channel during G protein-coupled receptor signaling.
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds activation of a potassium ion channel.
The transport of a protein to the cortex of the cell tip, driven by polymerization of a microtubule to which the protein is attached.
A microtubule-based process that results in the transport of organelles, other microtubules, or other cellular components.  Examples include motor-driven movement along microtubules and movement driven by polymerization or depolymerization of microtubules.
The transport of a protein driven by polymerization of a microtubule to which it is attached.
Any process that decreases the concentration of calcium ions in the presynaptic cytosol.
Repression of transcription of subtelomeric DNA by altering the structure of chromatin.
Repression of transcription of subtelomeric DNA by altering the structure of chromatin.
Repression of transcription of subtelomeric DNA by altering the structure of chromatin.
A heterochromatic region of the chromosome, adjacent to the telomere (on the centromeric side) that contains repetitive DNA and sometimes genes.
The process in which the 5' end of a pre-tRNA molecule is converted to that of a mature tRNA.
The movement of a protein along a microtubule to the cell-tip, mediated by motor proteins.
A microtubule-based process that results in the transport of proteins.
Catalysis of the reaction: S-adenosyl-L-methionine + 3-demethylubiquinone-8 = S-adenosyl-L-homocysteine + ubiquinone-8.
Development a structure consisting of multiple co-operating unicellular organisms of the same species.  Examples include sorocarp development in Dictystelia and co-operative colonial structures formed by Myxococcus xanthus for the purpose of predation and fruiting body formation.
Development a structure consisting of multiple co-operating unicellular organisms of the same species.  Examples include sorocarp development in Dictystelia and co-operative colonial structures formed by Myxococcus xanthus for the purpose of predation and fruiting body formation.
The process whose specific outcome is the progression of a fungal sorus over time, from its formation to the mature structure. A fungal sorus is a spore containing structure.
Interacting selectively and non-covalently with the C-terminal domain (CTD) of the largest subunit of RNA polymerase II. The CTD is comprised of repeats of a heptapeptide with the consensus sequence YSPTSPS. The number of repeats varies with the species and a minimum number of repeats is required for RNAP II function.
The regulated release of dopamine from the somatodendritic compartment (cell body or dendrites) of a neuron.
The regulated release of dopamine from the somatodendritic compartment (cell body or dendrites) of a neuron.
The regulated release of dopamine from the somatodendritic compartment (cell body or dendrites) of a neuron.
The regulated release of dopamine from an axon.
The regulated release of dopamine from an axon.
A protein kinase complex comprising a conserved PAK/GC/Ste20 family kinase, leucine rich repeat protein Sog2 family, which function as part of the cell shape network.
A protein complex acting as ligand of the transforming growth factor beta receptor complex, typically a homodimer of any of the TFGbeta isoforms. The precursor of TGFbeta proteins is cleaved into mature TGFbeta and the latency-associated peptide (LAP), which remains non-covalently linked to mature TGFbeta rendering it inactive. TGFbeta is activated by dimerisation and dissociation of the LAP.
A protein complex acting as ligand of the transforming growth factor beta receptor complex, typically a homodimer of any of the TFGbeta isoforms. The precursor of TGFbeta proteins is cleaved into mature TGFbeta and the latency-associated peptide (LAP), which remains non-covalently linked to mature TGFbeta rendering it inactive. TGFbeta is activated by dimerisation and dissociation of the LAP.
A protein complex acting as ligand of the transforming growth factor beta receptor complex, typically a homodimer of any of the TFGbeta isoforms. The precursor of TGFbeta proteins is cleaved into mature TGFbeta and the latency-associated peptide (LAP), which remains non-covalently linked to mature TGFbeta rendering it inactive. TGFbeta is activated by dimerisation and dissociation of the LAP.
A protein complex acting as ligand of the transforming growth factor beta receptor complex, typically a homodimer of any of the TFGbeta isoforms. The precursor of TGFbeta proteins is cleaved into mature TGFbeta and the latency-associated peptide (LAP), which remains non-covalently linked to mature TGFbeta rendering it inactive. TGFbeta is activated by dimerisation and dissociation of the LAP.
A protein complex acting as ligand of the transforming growth factor beta receptor complex, typically a homodimer of any of the TFGbeta isoforms. The precursor of TGFbeta proteins is cleaved into mature TGFbeta and the latency-associated peptide (LAP), which remains non-covalently linked to mature TGFbeta rendering it inactive. TGFbeta is activated by dimerisation and dissociation of the LAP.
A protein complex acting as ligand of the transforming growth factor beta receptor complex, typically a homodimer of any of the TFGbeta isoforms. The precursor of TGFbeta proteins is cleaved into mature TGFbeta and the latency-associated peptide (LAP), which remains non-covalently linked to mature TGFbeta rendering it inactive. TGFbeta is activated by dimerisation and dissociation of the LAP.
A process that begins with venom being forced into an organism by the bite or sting of another organism, and ends with the activation of the cytosolic argininosuccinate synthase in the bitten organism.
A protein complex consisting of frataxin, cysteine desulfurase, an accessory protein and a Fe-S scaffold protein. In human these genes correspond to FXN, NFS1, ISD11 and ISCU respectively. This complex assembles Fe-S clusters onto the scaffolding protein using the substrates ferrous iron, electrons, and sulfur from l-cysteine.
A rapid, force generating length change of an outer hair cell in response to electical stimulation.  This occurs naturally as during hearing where it serves a source of mechanical amplification.
Interacting selectively and non-covalently with any estrogen.
The transport of an inorganic ion across a membrane and against an electrochemical gradient, using energy from ATP hydrolysis.
The transport of an inorganic cation across a membrane and against an electrochemical gradient, using energy from ATP hydrolysis.
The transport of an inorganic anion across a membrane and against an electrochemical gradient, using energy from ATP hydrolysis.
Development of a sorocarp formed by aggregation of cells with different genotypes.
Development a structure consisting of multiple co-operating unicellular organisms of the same species, involving cells of more that one genotype.
Development of a non-reproductive fruiting body formed by aggregation of cells with different genotypes.
Development of a chimeric, non-reproductive fruiting body in which cells of all genotypes have an equal chance of becoming a spore cell.
Development of a chimeric sorocarp in which cells of all genotypes have an equal chance of becoming a spore cell.
Any process during chimeric sorocarp development that increases by which a cell increases the number of spore cells sharing its genotype at the expense of cells of other genotypes.
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 actin filaments and their associated proteins in the presynaptic actin cytoskeleton.
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 from a protozoan.
Enables the transmembrane transfer of an ion by a channel that opens when ATP has been bound by the channel complex or one of its constituent parts on the intracellular side of the plasma membrane.
The actin cytoskeleton that is part of a presynapse
The component of the synaptic membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
Any process that modulates the frequency, rate or extent of exocytic fusion of neurotransmitter receptor containing vesicles into the postsynaptic membrane.
The component of the postsynaptic density 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 postsynaptic density membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
Any process that modulates the frequency, rate or extent of synaptic vesicle docking.
Any process that modulates the frequency, rate or extent of endocytosis of neurotransmitter receptor at the postsynapse.
Any process that modulates the frequency, rate or extent of postsynaptic specialization assembly, the aggregation, arrangement and bonding together of a set of components to form a postsynaptic specialization.
Any process that modulates the frequency, rate or extent of postsynaptic density assembly, the aggregation, arrangement and bonding together of a set of components to form a postsynaptic density.
Any process that modulates the frequency, rate or extent of the directed movement of neurotransmitter receptor from the postsynaptic endosome to the postsynaptic membrane in transport vesicles.
The vesicular release of  serotonin from a presynapse, across a chemical synapse, the subsequent activation of serotonin receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
A synapse that uses serotonin as a neurotransmitter.
The vesicular release of noradrenaline (norepinephrine) a presynapse, across a chemical synapse, the subsequent activation of noradrenaline receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
Cell-cell signaling in which the ligand is carried between cells by an exosome.
Transynaptic signaling in which the ligand is carried across the synapse by an exosome.
Any process that modulates the frequency, rate or extent of transport or maintenance of location of a postsynaptic recycling endosome within the postsynapse.
Any process that modulates the frequency, rate or extent of modification of postsynaptic structure.
The intermediate filament cytoskeleton that is part of a postsynapse
Any process that modulates the frequency, rate or extent of presynaptic dense core granule exocytosis.
Any process that modulates the frequency, rate or extent of neurotransmitter loading into synaptic vesicles.
Any process that modulates the frequency, rate or extent of neurotransmitter loading into synaptic vesicles.
Cell-cell signaling to or from a synapse, mediated by nitric oxide.
The membrane component of the postsynaptic specialization of a symmetic synapse. This is the region of the postsynaptic membrane in which the population of neurotransmitter receptors involved in synaptic transmission are concentrated.
A network of proteins adjacent to the postsynaptic membrane of a symmetric synapse. Its major components include that spatially and functionally organize neurotransmitter receptors in the adjacent membrane, such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.  This structure is not as thick or electron dense as the postsynaptic density found in asymmetric synapses.
The component of the postsynaptic specialization membrane of a symmetric synapse 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 postsynaptic specialization membrane of a symmetric synapse 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 postsynaptic specialization membrane of a symmetric synapse 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 postsynaptic specialization membrane of a symmetric synapse consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping.
Any process, acting in the postsynapse that results in modulation of chemical synaptic transmission.
Any process, acting in the presynapse that results in modulation of chemical synaptic transmission.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a presynapse.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a presynapse.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a presynapse.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a presynapse.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a postsynapse.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a postsynapse.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a postsynapse.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a postsynapse.
Any process that modulates the physical form of a presynapse.
Any process that modulates the physical form of a presynapse.
Any process that modulates the physical form of a presynapse.
Any process that modulates the physical form of a postsynapse.
Any process that modulates the physical form of a postsynapse.
Any process that modulates the physical form of a postsynapse.
Any process that modulates the frequency, rate or extent of retrograde trans-synaptic signaling by a trans-synaptic complex.
Any process that modulates the frequency, rate or extent of trans-synaptic signaling.
Any process that modulates the frequency, rate or extent of retrograde trans-synaptic signaling by an endocannabinoid.
Any process that modulates the frequency, rate or extent of adhesion between pre- and post-synaptic membranes.
The directed movement of Zn2+ ions from the cytoplasm into the lumen of a cytoplasmic vesicle.
The directed movement of Zn2+ ions from the cytoplasm into the lumen of a cytoplasmic vesicle.
The action of a molecule that contributes to the structural integrity of a presynapse.
The intermediate filament cytoskeleton that is part of a presynapse.
Cell-cell signaling between presynapse and postsynapse, via the vesicular release and reception of brain derived neurotrophic factor (BDNF), that modulates the synaptic transmission properties of the synapse.
The action of a molecule that contributes to the structural integrity of a postsynaptic intermediate filament cytoskeleton.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of  cytoskeletal structures comprised of intermediate filament and their associated proteins in the postsynaptic cytoskeleton.
The action of a molecule that contributes to the structural integrity of a postsynapse.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures and their associated proteins in the presynaptic cytoskeleton.
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 cytoskeletal filaments and their associated proteins in the postsynaptic cytoskeleton.
The portion of the spectrin-associated cytoskeleton contained within the postsynapse.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of spectrin-associated cytoskeleton and associated proteins in the postsynapse.
Cell-cell signaling between presynapse and postsynapse mediated by brain-derived neurotrophic factor (BDNF) crossing the synaptic cleft.
A synapse formed by a cerebellar Golgi cell synapsing on to a cerebellar granule cell.
The component of the synaptic 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 synaptic 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 membrane microdomain that forms a necklace around the bulb (crater) of a caveola.  Intramembrane particles are concentrated in this region and cytoskeletal components, including actin, are highly enriched in the area underlying it.
The region of a caveola that extends into the cytoplasm, excluding the neck (rim).  This region is associated with intracellular caveola proteins.
Development of a plant organ, a multi-tissue plant structure that forms a functional unit.
The process in which the association between sister chromatids of a replicated chromosome along the length of the telomeric region is maintained as chromosomes condense, attach to the spindle in a bipolar orientation, and congress to the metaphase plate during a mitotic cell cycle.
The process in which the association between sister chromatids of a replicated chromosome along the length of the telomeric region is maintained as chromosomes condense, attach to the spindle in a bipolar orientation, and congress to the metaphase plate during a mitotic cell cycle.
The process in which the association between sister chromatids of a replicated chromosome along the length of the telomeric region is maintained as chromosomes condense, attach to the spindle in a bipolar orientation, and congress to the metaphase plate during a mitotic cell cycle.
The cell cycle process in which telomeres of sister chromatids are joined during mitosis.
The cell cycle process in which telomeres of sister chromatids are joined during mitosis.
The cell cycle process in which telomeres of sister chromatids are joined during mitosis.
Fusion of the membrane of a vesicle with the plasma membrane, thereby releasing its contents into the extracellular space.
The lipid bilayer surrounding an exocytic vesicle
The regulatory process by which increased cytosolic calcium levels lead to the the fusion of synaptic vesicles with the presynaptic active zone membrane by bringing primed synaptic vesicle membrane into contact with membrane presynaptic active zone membrane.
A cytoplasmic, membrane bound vesicle that is capable of fusing to the plasma membrane to release its contents into the extracellular space.
A biological process in which synaptic vesicles are loaded with neurotransmitters, move to the active zone, exocytose and are then recycled via endocytosis, ultimately leading to reloading with neurotransmitters.
Any process that modulates the potential difference across a presynaptic membrane.
The directed movement of synaptic vesicles along actin filaments within a cell, powered by molecular motors.
Any ligand-gated ion channel activity, occurring in the presynaptic membrane, that is involved in regulation of presynaptic membrane potential.
Any ligand-gated ion channel activity, occurring in the presynaptic membrane, that is involved in regulation of presynaptic membrane potential.
Any ligand-gated ion channel activity, occurring in the presynaptic membrane, that is involved in regulation of presynaptic membrane potential.
Any ligand-gated ion channel activity, occurring in the presynaptic membrane, that is involved in regulation of presynaptic membrane potential.
Voltage-gated ion channel activity, occurring in the presynaptic membrane, involved in regulation of presynaptic membrane potential. This is a key step in synaptic transmission, following the arrival of an action potential at the synapse.
Voltage-gated ion channel activity, occurring in the presynaptic membrane, involved in regulation of presynaptic membrane potential. This is a key step in synaptic transmission, following the arrival of an action potential at the synapse.
Voltage-gated ion channel activity, occurring in the presynaptic membrane, involved in regulation of presynaptic membrane potential. This is a key step in synaptic transmission, following the arrival of an action potential at the synapse.
Voltage-gated ion channel activity, occurring in the presynaptic membrane, involved in regulation of presynaptic membrane potential. This is a key step in synaptic transmission, following the arrival of an action potential at the synapse.
Any process that regulates the concentration of calcium in the presynaptic cytosol.
The directed change of cytosolic calcium ion concentration in the cytosol via the reversible binding of calcium ions to calcium-binding proteins in the cytosol thereby modulating the spatial and temporal dynamics of changes in cytosolic calcium concentrations.
Regulation of cytosolic calcium ion concentrations via the directed movement of calcium ions across the plasma-membrane into the cytosol via the action of a voltage-gated calcium ion channel.
A polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.
A polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.
A component of the cytoskeleton consisting of a homo or heteropolymeric fiber constructed from an indeterminate number of protein subunits.
The directed movement of synaptic vesicles along cytoskeletal fibers such as microfilaments or microtubules within a cell, powered by molecular motors.
The transport of organelles or other particles from one location in the cell to another along actin filaments.
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ion A(out) + ion B(in) = ion A(in) + ion B(out) where ion A and ion B are different types of ion.
The directed movement of synaptic vesicles along microtubules within a cell, powered by molecular motors.
The directed movement of a vesicle along a cytoskeletal fiber such as a microtubule or and actin filament, mediated by motor proteins.
The directed movement of a vesicle along a cytoskeletal fiber such as a microtubule or and actin filament, mediated by motor proteins.
The directed movement of dense core granules along cytoskeletal fibers, such as microtubules or actin filaments.
The directed movement of dense core granules along cytoskeletal fibers, such as microtubules or actin filaments.
Any ion antiporter activity, occurring in the presynaptic membrane, that is involved in regulation of presynaptic membrane potential
Any ATPase coupled ion transmembrane transporter activity, occurring in the presynaptic membrane, that is involved in regulation of presynaptic membrane potential.
Any ATPase coupled ion transmembrane transporter activity, occurring in the presynaptic membrane, that is involved in regulation of presynaptic membrane potential.
Any (proper) part of the cytosol of a single cell of sufficient size to still be considered cytosol
The region of the cytosol consisting of all cytosol that is part of the presynapse.
The region of the cytosol consisting of all cytosol that is part of the postsynapse.
The secretion of molecules (e.g. neuropeptides and neuromodulators such as serotonin and dopamine) contained within a membrane-bounced dense in response to increased presynaptic cytosolic calcium levels.
A series of molecular signals that conveys information from the presynapse to the nucleus via cytoskeletal transport of a protein from a presynapse to the component to the nucleus where it affects biochemical processes that occur in the nucleus (e.g DNA transcription, mRNA splicing, or DNA/histone modifications).
A series of molecular signals that conveys information from the postsynapse to the nucleus via cytoskeletal transport of a protein from a postsynapse to the component to the nucleus where it affects biochemical processes that occur in the nucleus (e.g DNA transcription, mRNA splicing, or DNA/histone modifications).
Combining with a neurotransmitter 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.
Neurotransmitter receptor activity occurring in the postsynaptic membrane that is involved in regulating postsynaptic membrane potential, either directly (ionotropic receptors) or indirectly (e.g. via GPCR activation of an ion channel.)
A G protein-coupled receptor activity occurring in the postsynaptic membrane that is part of a GPCR signaling pathway that positively regulates ion channel activity in the postsynaptic membrane.
The pathway leading to secretion of a neurotransmitter from the presynapse as part of synaptic transmission.
The process in which synaptic vesicles fuse to the presynaptic endosome followed by sorting of synaptic vesicle components and budding of new synaptic vesicles.
Any process that increases the concentration of calcium ions in the presynaptic cytosol.
The directed change of presynaptic cytosolic free calcium ion concentration in the cytosol via the reversible binding of calcium ions to calcium-binding proteins in the cytosol thereby modulating the spatial and temporal dynamics of changes in presynaptic cytosolic calcium concentrations.
The directed change of presynaptic cytosolic free calcium ion concentration in the cytosol via the reversible binding of calcium ions to calcium-binding proteins in the cytosol thereby modulating the spatial and temporal dynamics of changes in presynaptic cytosolic calcium concentrations.
The directed change of presynaptic cytosolic free calcium ion concentration in the cytosol via the reversible binding of calcium ions to calcium-binding proteins in the cytosol thereby modulating the spatial and temporal dynamics of changes in presynaptic cytosolic calcium concentrations.
The extracellular matrix of the perisynaptic space (the extracellular space adjacent to the synapse) and the synaptic cleft.
Cell-cell signaling to, from or or within a synapse.
Cell-cell signaling in either direction across the synaptic cleft.
Cell-cell signaling to or from a synapse, mediated by a peptide.
The secretion of neuropeptides contained within a dense core vesicle by fusion of the granule with the presynaptic membrane, stimulated by a rise in cytosolic calcium ion concentration.
Cell-cell signaling between presynapse and postsynapse mediated by a peptide ligand crossing the synaptic cleft.
Cell-cell signaling from post to pre-synapse, across the synaptic cleft, mediated by a lipid.
Cell-cell signaling in either direction across the synaptic cleft, mediated by an endocannabinoid ligand.
Cell-cell signaling between presynapse and postsynapse mediated by a soluble gas ligand crossing the synaptic cleft.
The extracellular region immediately adjacent to to a synapse.
Cell-cell signaling between presynapse and postsynapse mediated by a trans-synaptic protein complex.
Any protein degradation process, occurring at a presynapse, that regulates synaptic transmission.
Any process that modulates synaptic transmission by regulating translation occurring at the synapse.
Cell-cell signaling between presynapse and postsynapse mediated by nitric oxide.
Cell-cell signaling between presynapse and postsynapse mediated by carbon monoxide.
Cell-cell signaling between presynapse and postsynapse, across the synaptic cleft, that modulates the synaptic transmission properties of the synapse.
Cell-cell signaling between presynapse and postsynapse, via the vesicular release and reception of neuropeptide molecules, that modulates the synaptic transmission properties of the synapse.
Cell-cell signaling between presynapse and postsynapse, via the release and reception of lipid molecules, that modulates the synaptic transmission properties of the synapse.
Cell-cell signaling between presynapse and postsynapse, via the release and reception of endocannabinoid ligands, that modulates the synaptic transmission properties of the synapse.
Cell-cell signaling between presynapse and postsynapse, via the release and reception of gaseous molecules, that modulates the synaptic transmission properties of the synapse.
Cell-cell signaling between presynapse and postsynapse, via the release and reception of nitric oxide molecules, that modulates the synaptic transmission properties of the synapse.
Cell-cell signaling between presynapse and postsynapse, via the release and reception of carbon monoxide molecules, that modulates the synaptic transmission properties of the synapse.
Cell-cell signaling between presynapse and postsynapse, mediated by transynaptic protein complexes, that modulates the synaptic transmission properties of the synapse.
A process that preserves the structural organistation and orientation of a synaptic cellular component such as the synaptic cytoskeleton and molecular scaffolds.
The process by which alignment between postsynaptic density and presynaptic active zone is maintained.
The attachment of presynaptic membrane to postsynaptic membrane via adhesion molecules that are at least partially embedded in the plasma membrane.
The binding of a synaptic membrane to the extracellular matrix via adhesion molecules.
A process which maintains the organization and the arrangement of proteins in the presynaptic density.
Any process that modifies the structure/morphology of a synapse.
Any process that modulates synaptic transmission via modification of the structure of the synapse.
The part of synaptic transmission occurring in the post-synapse: a signal transduction pathway consisting of neurotransmitter receptor activation and its effects on postsynaptic membrane potential and the ionic composition of the postsynaptic cytosol.
Any process that regulates the concentration of calcium in the postsynaptic cytosol.
The directed change of free calcium ion concentration in the postsynaptic cytosol via the reversible binding of calcium ions to calcium-binding proteins in the cytosol thereby modulating the spatial and temporal dynamics of changes in postsynaptic cytosolic calcium concentrations.
The directed change of free calcium ion concentration in the postsynaptic cytosol via the reversible binding of calcium ions to calcium-binding proteins in the cytosol thereby modulating the spatial and temporal dynamics of changes in postsynaptic cytosolic calcium concentrations.
The directed change of free calcium ion concentration in the postsynaptic cytosol via the reversible binding of calcium ions to calcium-binding proteins in the cytosol thereby modulating the spatial and temporal dynamics of changes in postsynaptic cytosolic calcium concentrations.
Any (proper) part of the cytoplasm of a single cell of sufficient size to still be considered cytoplasm"
The portion of the cytoskeleton contained within the presynapse.
The portion of the cytoskeleton contained within the postsynapse.
A network of proteins within and adjacent to the postsynaptic membrane. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
The post-synaptic specialization of a glutamatergic excitatory synapse.
Any process that modulates synaptic transmission by regulating protein degradation at the synapse.
Any process that modulates synaptic transmission by regulating a catabolic process occurring at a presynapse.
Any process that modulates synaptic transmission by regulating a catabolic process occurring at a postsynapse.
Any process that modulates synaptic transmission by regulating translation occurring at the presynapse.
Any process that modulates synaptic transmission by regulating translation occurring at the postsynapse.
A G protein-coupled neurotransmitter receptor activity, occurring in the postsynaptic membrane, involved in regulation of postsynaptic membrane potential.
Any ion antiporter activity, occurring in the postsynaptic membrane, that is involved in regulation of postsynaptic membrane potential
Any ATPase coupled ion transmembrane transporter activity, occurring in the postsynaptic membrane, that is involved in regulation of postsynaptic membrane potential.
Any ATPase coupled ion transmembrane transporter activity, occurring in the postsynaptic membrane, that is involved in regulation of postsynaptic membrane potential.
Any neurotransmitter receptor activity that is involved in regulating the concentration of calcium in the presynaptic cytosol.
Any neurotransmitter receptor activity that is involved in regulating the concentration of calcium in the postsynaptic cytosol.
The process in which calcium ions sequestered in the endoplasmic reticulum, Golgi apparatus or mitochondria are released into the presynaptic cytosol.
The process in which calcium ions sequestered in the endoplasmic reticulum, Golgi apparatus or mitochondria are released into the postsynaptic cytosol.
The directed movement of inorganic ions from outside of a cell, across the plasma membrane and into the cytosol.
Any process that increases the concentration of calcium ions in the postsynaptic cytosol.
Combining with the biogenic amine serotonin and transmitting a signal across a membrane by activating some effector activity. Serotonin (5-hydroxytryptamine) is a neurotransmitter and hormone found in vertebrates and invertebrates.
A receptor-mediated endocytosis process that results in the internalization of a neurotransmitter receptor.
The process in which endocytosed synaptic vesicles fuse to the presynaptic endosome followed by sorting of synaptic vesicle components and budding of new synaptic vesicles.
Fusion of an endocytosed synaptic vesicle with an endosome.
Any process that modulates the frequency, rate or extent of neurotransmitter receptor activity. Modulation may be via an effect on ligand affinity, or effector funtion such as ion selectivity or pore opening/closing in ionotropic receptors.
A molecular function that directly (via physical interaction or direct modification) activates, inhibits or otherwise modulates the activity of a neurotransmitter receptor. Modulation of activity includes changes in desensitization rate, ligand affinity, ion selectivity and pore-opening/closing.
Enables the transmembrane transfer of a calcium ions by a channel that opens when a specific ligand has been bound by the channel complex or one of its constituent parts.
Any process that regulates the frequency of action potentials in a spike train.
The cell cycle process in which chromosomes that are laterally attached to one or more mitotic spindle microtubules migrate towards the spindle equator via plus-end-directed movement along the microtubules. This process is part of mitotic metaphase plate congression.
The cell cycle process in which sister chromatids become laterally attached to spindle microtubules as part of mitotic metaphase plate congression. Attachment precedes migration along microtubules towards the spindle equator (metaphase plate).
Any process that regulates the temporal pattern of a sequence of action potentials in a neuron.
Interacting selectively and non-covalently with the side of a microtubule.
The initiating cycle of an action potential. In vertebrate neurons this typically occurs at an axon hillock. Not all initiated axon potentials propagate.
The initiating cycle of an action potential. In vertebrate neurons this typically occurs at an axon hillock. Not all initiated axon potentials propagate.
Any process that regulates the potential at which an axon potential is triggered.
A process in which a protein is transported to or maintained in a location within an axon.
The process of directing proteins towards the cell-wall.
A process in which a protein is transported, tethered to or otherwise maintained in a spore cell wall.
Catalysis of the reaction: (R)-2-hydroxyglutarate + pyruvate = alpha-ketoglutarate + D-lactate, with FAD functioning as an intermediate hydrogen acceptor.
Catalysis of the reaction: (R)-2-hydroxyglutarate + pyruvate = alpha-ketoglutarate + D-lactate, with FAD functioning as an intermediate hydrogen acceptor.
The component of the matrix side of the 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."n
The side (leaflet) of the mitochondrial inner membrane that faces the matrix.
Catalytis of the reaction: UDP-glucuronate + NAD+ = UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
Catalysis of the reaction: 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
Catalysis of the reaction: 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
Catalysis of the reaction: 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
Catalysis of the reaction: UDP-4-amino-4-deoxy-beta-L-arabinopyranose + 2-oxoglutarate = UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
Catalysis of the reaction: UDP-4-amino-4-deoxy-beta-L-arabinopyranose + 2-oxoglutarate = UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
Catalysis of the reaction: UDP-4-amino-4-deoxy-beta-L-arabinopyranose + 2-oxoglutarate = UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
Catalysis of the reaction: UDP-4-amino-4-deoxy-beta-L-arabinopyranose + 2-oxoglutarate = UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
Catalysis of the reaction: UDP-4-amino-4-deoxy-beta-L-arabinopyranose + 2-oxoglutarate = UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
Catalysis of the reaction: UDP-4-deoxy-4-formamido-beta-L-arabinopyranose + ditrans,octacis-undecaprenyl phosphate = UDP + 4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate.
Catalysis of the reaction: UDP-4-deoxy-4-formamido-beta-L-arabinopyranose + ditrans,octacis-undecaprenyl phosphate = UDP + 4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate.
Catalysis of the reaction: UDP-4-deoxy-4-formamido-beta-L-arabinopyranose + ditrans,octacis-undecaprenyl phosphate = UDP + 4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate.
Catalysis of the reaction: UDP-4-deoxy-4-formamido-beta-L-arabinopyranose + ditrans,octacis-undecaprenyl phosphate = UDP + 4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate.
The process in which ions are transported across the plasma membrane of a cardiac muscle cell such that the membrane potential changes in the repolarizing direction, toward the steady state potential. For example, the repolarization during an action potential is from a positive membrane potential towards a negative resting potential.
Any process that modulates the establishment or extent of a change in membrane potential in the polarizing direction towards the resting potential in a cardiomyocyte.
Any process that modulates the establishment or extent of a change in membrane potential in the polarizing direction towards the resting potential in a cardiomyocyte.
Any process that modulates the establishment or extent of a change in membrane potential in the polarizing direction towards the resting potential in a cardiomyocyte.
The process in which ions are transported across the plasma membrane of an atrial cardiac muscle cell such that the membrane potential changes in the repolarizing direction, toward the steady state potential. For example, the repolarization during an action potential is from a positive membrane potential towards a negative resting potential.
The process in which ions are transported across the plasma membrane of a ventricular cardiac muscle cell such that the membrane potential changes in the repolarizing direction, toward the steady state potential. For example, the repolarization during an action potential is from a positive membrane potential towards a negative resting potential.
Regulation of presynaptic cytosolic calcium ion concentrations via the action of voltage-gated calcium ion channels.
The process during which neurotransmitter receptors, anchored in some region of the synaptic membrane, are recycled via the endosome.  This cycle includes release from anchoring, diffusion in the synaptic membrane to an endocytic region, endocytosis, transport to the endosome, recycling in the endosome,  transport back the synaptic membrane and subsequent anchoring (trapping).
The process by which diffusing neurotransmitter receptor becomes trapped in region of the plasma membrane.
A network of proteins within and adjacent to the postsynaptic membrane of a symmetric synapse, consisting of anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components that spatially and functionally organize the neurotransmitter receptors at the synapse. This structure is not as thick or electron dense as the postsynaptic densities found in asymmetric synapses.
The process during which neurotransmitter receptors in the postsynaptic specialization membrane are recycled via the endosome. This cycle includes release from anchoring (trapping), diffusion in the synaptic membrane to the postsynaptic endocytic region, endocytosis, transport to the endosome, recycling in the endosome,  transport back the synaptic membrane and subsequent trapping in the postsynaptic specialization membrane.
The cytoplasmic component of the postsynaptic endocytic zone.
A process in which protein is transported from one region of the plasma membrane to another.
A process in which a protein is transported to, or maintained in, a location within the membrane adjacent to a postsynaptic specialization (e.g. post synaptic density).
The membrane component of the postsynaptic specialization. This is the region of the postsynaptic membrane in which the population of neurotransmitter receptors involved in synaptic transmission are concentrated.
Positive regulation of presynaptic cytosolic calcium ion concentrations via the directed movement of calcium ions across the plasma-membrane into the cytosol via the action of voltage-gated calcium ion channels.  This is the first step in synaptic transmission
The directed flow of cytosol (the liquid component of the cytoplasm) and the organelles it contains.
The directed movement of neurotransmitter receptors.
The directed movement of proteins from the endosome to the plasma membrane in transport vesicles.
The directed movement of neurotransmitter receptor from the endosome to the plasma membrane in transport vesicles.
The directed movement of proteins along microtubules in neuron projections.
The directed movement of proteins along microtubules from the cell body toward the cell periphery in nerve cell axons.
The directed movement of proteins along microtubules from the cell periphery toward the cell body in nerve cell axons.
Any signal release from a synapse.
A process in which a protein is transported to, or maintained in, a location within a presynaptic membrane.
A process in which a protein is transported to, or maintained in, a location within a presynaptic membrane.
A process in which a protein is transported to, or maintained in, a location within a presynaptic membrane.
A process in which a neurotransmitter is transported to, or maintained in, a location within the membrane adjacent to a postsynaptic specialization (e.g. postsynaptic density).
Vesicle-mediated transport of a neurotransmitter receptor vesicle from the plasma membrane to the endosome.
The component of the synaptic 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 induction of synaptic vesicle release by any process that leads to a rise in intracellular calcium ion concentration at the presynapse.  This is the first step in synaptic transmission.
The complete extent of cell cortex that underlies some some region of the plasma membrane
Any action potential process that regulates skeletal muscle contraction
Any protein phosphorylation process that negatively_regulates protein kinase activity
Any transcription from RNA polymerase II promoter process that positively_regulates sodium ion transport
Any transcription from RNA polymerase II promoter process that positively_regulates peroxisome organization
Any transcription from RNA polymerase II promoter process that positively_regulates ethanol catabolic process
Any transcription from RNA polymerase II promoter process that positively_regulates sulfite transport
Any transcription from RNA polymerase II promoter process that negatively_regulates ceramide biosynthetic process
Any prostaglandin biosynthetic process process that regulates fever generation
Any prostaglandin secretion process that regulates fever generation
Any prostaglandin biosynthetic process process that positively_regulates fever generation
Any prostaglandin secretion process that positively_regulates fever generation
Any canonical Wnt signaling pathway process that regulates heart induction
Any transcription from RNA polymerase II promoter process that positively_regulates fatty acid beta-oxidation
Any transcription from RNA polymerase II promoter process that positively_regulates mating type switching
Any transcription from RNA polymerase II promoter process that positively_regulates inositol biosynthetic process
Any transcription from RNA polymerase II promoter process that regulates thiamine biosynthetic process
Any transcription from RNA polymerase II promoter process that negatively_regulates single organismal cell-cell adhesion
Any transcription from RNA polymerase II promoter process that regulates glucose import
Any transcription from RNA polymerase II promoter process that regulates transport
Any transcription from RNA polymerase II promoter process that regulates iron ion transport
Any transcription from RNA polymerase II promoter process that regulates iron ion import
Any transcription from RNA polymerase II promoter process that regulates meiotic nuclear division
Any transcription from RNA polymerase II promoter process that regulates carbohydrate metabolic process
Any transcription from RNA polymerase II promoter process that negatively_regulates cellular amino acid biosynthetic process
Any transcription from RNA polymerase II promoter process that positively_regulates DNA repair
Any transcription from RNA polymerase II promoter process that regulates conjugation with cellular fusion
Any transcription from RNA polymerase II promoter process that positively_regulates phospholipid biosynthetic process
Any transcription from RNA polymerase II promoter process that regulates fungal-type cell wall biogenesis
Any transcription from RNA polymerase II promoter process that regulates 4,6-pyruvylated galactose residue biosynthetic process
Any transcription from RNA polymerase II promoter process that positively_regulates purine nucleotide biosynthetic process
Any transcription from RNA polymerase II promoter process that positively_regulates cellular alcohol catabolic process
Any transcription from RNA polymerase II promoter process that regulates cellular response to oxidative stress
Any transcription from RNA polymerase II promoter process that regulates pyrimidine nucleotide biosynthetic process
Any transcription from RNA polymerase II promoter process that negatively_regulates invasive growth in response to glucose limitation
Any transcription from RNA polymerase II promoter process that positively_regulates pseudohyphal growth
Any transcription from RNA polymerase II promoter process that negatively_regulates pseudohyphal growth
Any transcription from RNA polymerase II promoter process that negatively_regulates cellular response to alkaline pH
Any transcription from RNA polymerase II promoter process that negatively_regulates cellular hyperosmotic salinity response
Any transcription from RNA polymerase II promoter process that negatively_regulates arginine catabolic process
Any transcription from RNA polymerase II promoter process that positively_regulates arginine biosynthetic process
Any transcription from RNA polymerase II promoter process that negatively_regulates inositol biosynthetic process
Any transcription from RNA polymerase II promoter process that positively_regulates phosphatidylcholine biosynthetic process
Any transcription from RNA polymerase II promoter process that negatively_regulates phosphatidylcholine biosynthetic process
Any transcription from RNA polymerase II promoter process that negatively_regulates mating type switching
Any transcription from RNA polymerase II promoter process that positively_regulates meiotic nuclear division
Any transcription from RNA polymerase II promoter process that negatively_regulates G1/S transition of mitotic cell cycle
Any transcription from RNA polymerase II promoter process that positively_regulates sulfate assimilation
Any transcription from RNA polymerase II promoter process that positively_regulates flocculation via cell wall protein-carbohydrate interaction
Any transcription from RNA polymerase II promoter process that positively_regulates phosphatidylserine biosynthetic process
Any transcription from RNA polymerase II promoter process that negatively_regulates phosphatidylserine biosynthetic process
Any transcription from RNA polymerase II promoter process that regulates phenotypic switching
Any transcription from RNA polymerase II promoter process that positively_regulates phenotypic switching
Any transcription from RNA polymerase II promoter process that negatively_regulates phenotypic switching
Any transcription from RNA polymerase II promoter process that negatively_regulates filamentous growth of a population of unicellular organisms in response to starvation
Any transcription from RNA polymerase II promoter process that negatively_regulates leucine import
Any transcription from RNA polymerase II promoter process that negatively_regulates induction of conjugation with cellular fusion
Any canonical Wnt signaling pathway process that positively_regulates spinal cord association neuron differentiation
Any transcription from RNA polymerase II promoter process that positively_regulates pyrimidine-containing compound salvage
Any transcription from RNA polymerase II promoter process that negatively_regulates neuron apoptotic process
Any transcription from RNA polymerase II promoter process that regulates fatty acid biosynthetic process
Highly exocytosable gelatinase-poor granules found in neutrophils and rich in ficolin-1.  Ficolin-1 is released from neutrophil granules by stimulation with fMLP or PMA, and the majority becomes associated with the surface membrane of the cells and can be detected by flow cytometry.
Highly exocytosable gelatinase-poor granules found in neutrophils and rich in ficolin-1.  Ficolin-1 is released from neutrophil granules by stimulation with fMLP or PMA, and the majority becomes associated with the surface membrane of the cells and can be detected by flow cytometry.
The lipid bilayer surrounding a ficolin-1-rich granule.
The lipid bilayer surrounding the cytolytic granule.
Catalysis of the hydrolysis of ubiquitin from proteins and other molecules.
Catalysis of the hydrolysis of ubiquitin from proteins and other molecules.
Catalysis of the hydrolysis of ubiquitin from proteins and other molecules.
Catalysis of the reaction: protein histidine phosphate + H2O = protein histidine + phosphate
Catalysis of the reaction: protein histidine phosphate + H2O = protein histidine + phosphate
Any process that decreases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a stimulus indicating the organism is under salt stress. The stress is usually an increase or decrease in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
Any process that decreases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of detection of, or exposure to, an increase in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
The reorganization or renovation of existing pulmonary blood vessels.
Catalysis of the reaction: myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate + H2O = myo-inositol hexakisphosphate + phosphate.
Catalysis of the reaction: myo-inositol 1,5-bisdiphosphate 2,3,4,6-tetrakisphosphate + H2O = myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate + phosphate.
Enables the transmembrane transfer of a sodium ion by a voltage-gated channel whose activity is modulated in response to mechanical stress. Response to mechanical stress and voltage gating  together is different than the sum of individual responses. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
Catalysis of the reaction: [isocitrate dehydrogenase] phosphate + H2O = [isocitrate dehydrogenase] + phosphate.
Interacting selectively and non-covalently with the FMN-binding domain of a protein.
Any process that modulates the frequency, rate or extent of firing from a late origin of replication involved in mitotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of firing from a late origin of replication involved in mitotic DNA replication.
A ribonuclease complex that has 3-prime to 5-prime distributive hydrolytic exoribonuclease activity and in some taxa (e.g. yeast) endoribonuclease activity, producing 5-prime-phosphomonoesters. Participates in a multitude of cellular RNA processing and degradation events preventing nuclear export and/or translation of aberrant RNAs. Restricted to processing linear and circular single-stranded RNAs (ssRNA) only. RNAs with complex secondary structures may have to be unwound or pre-processed by co-factors prior to entering the complex, esp if the 3-prime end is structured.
Catalysis of the reaction: estrogen + donor-H2 + O2 = 16-alpha-hydroxyestrogen + H2O.
Catalysis of the reaction: estrogen + donor-H2 + O2 = 2-hydroxyestrogen + H2O.
The multiplication or reproduction of blood vessel endothelial cells, resulting in the expansion of a cell population.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nuclear inner or outer membrane during mitotic nuclear division.
The process in which a nuclear membrane is synthesized, aggregates, and bonds together.
A process in which the nuclear inner or outer membrane is synthesized, aggregates, and bonds together during mitotic nuclear division.
The regrowth of axons of the optical nerve following their loss or damage.
Any process that activates or increases the surface tension of a liquid.
Any process that prevents or reduces the surface tension of a liquid.
The modification of a tRNA anticodon loop by replacing guanine with queuonine. Reaction is tRNA guanine + queuine = tRNA queuine + guanine.
A protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins.
Catalysis of the reaction: L-isoleucine + 2 O2 + 2 NADPH(4-) + 2 H+ <=> (E)-2-methylbutanal oxime + 2 NADP(3-) + carbon dioxide + 3 H2O.
Catalysis of the reaction: L-valine + 2 O2 + 2 NADPH(4-) + 2 H+ <=> (E)-2-methylpropanal oxime + 2 NADP(3-) + carbon dioxide + 3 H2O.
Catalysis of the reaction: phytosphingosine(1+) + O2 + a reduced electron acceptor <=> 4-hydroxy-trans-8-sphingenine + 2 H2O + an oxidized electron acceptor.
Catalysis of the reaction: 3-(all-trans-octaprenyl)benzene-1,2-diol + S-adenosyl-L-methionine <=> H+ + 2-methoxy-6-(all-trans-octaprenyl)phenol + S-adenosyl-L-homocysteine.
Catalysis of the reaction: 4-methyl-2-oxopentanoate + coenzyme A(4-) + NAD(1-) <=> isovaleryl-CoA(4-) + carbon dioxide + NADH(2-).
Catalysis of the reaction: H2O + an N-acyl-L-homoserine lactone <=> H+ + an N-acyl-L-homoserine.
Catalysis of the reaction: H2O + a dipeptide <=> 2 a standard alpha amino acid that occurs in the cytosol
Catalysis of the reaction: H2O + a dipeptide with proline at the C-terminal <=> L-proline + a standard alpha amino acid.
Catalysis of the reaction: ATP(4-) + L-glutamate(1-) + H2O <=> ADP(3-) + hydrogenphosphate + L-glutamate(1-) + H+.
Catalysis of the reaction: ATP(4-) + beta-D-galactoside + H2O <=> ADP(3-) + hydrogenphosphate + beta-D-galactoside + H+.
Catalysis of the reaction: nickel(2+) (periplam) + ATP + H2O = nickel(2+) (cytosol) + ADP + hydrogenphosphate + H+
Catalysis of the reaction: ATP(4-) + H2O + an alkylphosphonate <=> ADP(3-) + hydrogenphosphate + H+ + an alkylphosphonate.
Catalysis of the reaction: ATP(4-) + H2O + an alkylphosphonate <=> ADP(3-) + hydrogenphosphate + H+ + an alkylphosphonate.
Catalysis of the reaction: ATP(4-) + L-argininium(1+) + H2O <=> ADP(3-) + hydrogenphosphate + L-argininium(1+) + H+.
Catalysis of the reaction: ATP(4-) + cob(I)alamin + H2O <=> ADP(3-) + hydrogenphosphate + cob(I)alamin + H+
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + thiosulfate(out) = ADP + phosphate + thiosulfate(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + thiosulfate(out) = ADP + phosphate + thiosulfate(in).
Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + thiosulfate(out) = ADP + phosphate + thiosulfate(in).
Catalysis of the reaction: ATP + iron(III)  dicitrate + H2O <=> ADP + hydrogenphosphate + iron(III)  dicitrate + H+
Catalysis of the reaction: 2-demethylmenaquinol-8 + S-adenosyl-L-methionine <=> menaquinol-8 + H+ + S-adenosyl-L-homocysteine.
Catalysis of the reaction: L-cysteine + O-phosphonato-L-homoserine = L-cystathionine + hydrogenphosphate
Catalysis of the reaction: (R)-lactate + an ubiquinone = pyruvate + an ubiquinol
Catalysis of the reaction: dTDP-6-deoxy-beta-L-mannose + NAD+ <=> dTDP-4-dehydro-6-deoxy-alpha-D-glucose + NADH + H+
Catalysis of the reaction: dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose + beta-D-ManNAcA-(1->4)-alpha-D-GlcNAc-1-diphospho-ditrans,polycis-undecaprenol <=> H+ + alpha-D-FucNAc4-(1->4)-beta-D-ManNAcA-(1->4)-D-GlcNAc-undecaprenyl diphosphate + dTDP
Catalysis of the reaction: long-chain fatty acid + NADPH + H+ + O2 = an omega-hydroxy-long-chain fatty acid + NADP+ + H2O.
Catalysis of the reaction: H+ + isobutyryl-CoA + FAD <=> methacrylyl-CoA + FADH2
Catalysis of the reaction: a tetrahydrofolate + a [methyl-Co(III) corrinoid Fe-S protein] <=> an N5-methyl-tetrahydrofolate + a [Co(I) corrinoid Fe-S protein]
Catalysis of the reaction: H+ + 4-nitrotoluene + NADH + O2 <=> 4-nitrobenzyl alcohol + NAD+ + H2O
Catalysis of the reaction: 4-nitrobenzyl alcohol + O2 <=> 4-nitrobenzaldehyde + hydrogen peroxide
Catalysis of the reaction: H2O + NAD + an alcohol <=> NADH + H+ + an organic hydroperoxide
Catalysis of the reaction: fumarate + a menaquinol = succinate + a menaquinone
Catalysis of the reaction: 4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate = N-[(7,8-dihydropterin-6-yl)methyl]-4-(beta-D-ribofuranosyl)aniline 5'-phosphate + diphosphoric acid
Catalysis of the reaction: 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonic acid + H2O + NAD = 3-dehydroquinate + ammonium + NADH + H+
Catalysis of the reaction: isopentenyl phosphate(2-) + ATP(4-) <=> isopentenyl diphosphate(3-) + ADP(3-)
Catalysis of the reaction: 3-chlorobenzoate + O2 + a reduced electron acceptor <=> 3-chlorobenzoate-cis-4,5-diol + an oxidized electron acceptor
Catalysis of the reaction: 3-chlorobenzoate + O2 + a reduced electron acceptor <=> 3-chlorobenzoate-cis-3,4-diol + an oxidized electron acceptor
Catalysis of the reaction: 3,4-dichlorobenzoate + O2 + a reduced electron acceptor <=> 3,4-dichlorobenzoate-cis-4,5-diol + an oxidized electron acceptor
Catalysis of the reaction: indole-3-acetate + glycine + ATP(4-) <=> H+ + indole-3-acetyl-glycine + AMP(2-) + diphosphoric acid
Catalysis of the reaction: indole-3-acetate + L-isoleucine + ATP(4-) <=> H+ + indole-3-acetyl-isoleucine + AMP(2-) + diphosphoric acid
Catalysis of the reaction: indole-3-acetate + L-methionine + ATP(4-) <=> H+ + indole-3-acetyl-methionine + AMP(2-) + diphosphoric acid
Catalysis of the reaction: indole-3-acetate + L-tyrosine + ATP(4-) <=> H+ + indole-3-acetyl-tyrosine + AMP(2-) + diphosphoric acid
Catalysis of the reaction: indole-3-acetate + L-tryptophan + ATP(4-) <=> H+ + indole-3-acetyl-tryptophan + AMP(2-) + diphosphoric acid
Catalysis of the reaction: indole-3-acetate + L-proline + ATP(4-) <=> H+ + indole-3-acetyl-proline + AMP(2-) + diphosphoric acid
Catalysis of the reaction: (-)-jasmonate + L-isoleucine  + ATP(4-) <=> H+ + (-)-jasmonoyl-L-isoleucine + AMP(2-) + diphosphoric acid
Catalysis of the reaction: 3-maleylpyruvate(2-) + H2O <=> H+ + maleate(2-) + pyruvate
Catalysis of the reaction: 3'-phosphonato-5'-adenylyl sulfate + a 12-hydroxyjasmonate <=> adenosine 3',5'-bismonophosphate + a 12-hydroxyjasmonate sulfate
Catalysis of the reaction: 3'-phosphonato-5'-adenylyl sulfate + an 11-hydroxyjasmonate <=> adenosine 3',5'-bismonophosphate + H+ + an 11-hydroxyjasmonate sulfate
Catalysis of the reaction: L-valine  + ATP(4-) + a jasmonic acid <=> AMP(2-) + diphosphoric acid + a jasmonoyl-valine
Catalysis of the reaction: L-leucine  + ATP(4-) + a jasmonic acid <=> AMP(2-) + diphosphoric acid + a jasmonoyl-leucine
Catalysis of the reaction: prenyl diphosphate + 2 isopentenyl diphosphate <=> 2 diphosphoric acid + 2-cis,6-cis-farnesyl diphosphate
Catalysis of the reaction: 2-cis,6-cis-farnesyl diphosphate <=> (-)-endo-alpha-bergamotene + diphosphoric acid
Catalysis of the reaction: 2-cis,6-cis-farnesyl diphosphate <=> (+)-endo-beta-bergamotene + diphosphoric acid
Catalysis of the reaction: 2-cis,6-cis-farnesyl diphosphate <=> (+)-alpha-santalene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate(3-) <=> diphosphoric acid + (-)-beta-curcumene
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> gamma-curcumene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> diphosphoric acid + gamma-patchoulene
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = diphosphoric acid + alpha-patchoulene
Catalysis of the reaction: (E)-3,7,11,15-tetramethylhexadec-2-en-1-yl diphosphate + 3 NADP <=> 2-trans,6-trans,10-trans-geranylgeranyl diphosphate + 3 NADPH + 3 H+
Catalysis of the reaction: (1E,4E,8E)-alpha-humulene + NADPH + O2 + H+ <=> 8-hydroxy-alpha-humulene + NADP + H2O
Catalysis of the reaction: 8-hydroxy-alpha-humulene + NAD <=> zerumbone + NADH + H+
Catalysis of the reaction: 18-hydroxyoleate + a lipid hydroperoxide <=> 9,10-epoxy-18-hydroxystearate + a lipid alcohol
Catalysis of the reaction: 9,10-epoxy-18-hydroxystearate + H2O <=> 9,10,18-trihydroxystearate
Catalysis of the reaction: NADP + a 3R-hydroxy cis Delta9-hexadecenoyl-[acp] <=> NADPH + H+ + a 3-oxo-cis-Delta9-hexadecenoyl-[acp]
Catalysis of the reaction: OPC8-3-hydroxyacyl-CoA <=> OPC8-trans-2-enoyl-CoA + H2O
Catalysis of the reaction: OPC6-3-hydroxyacyl-CoA <=> OPC6-trans-2-enoyl-CoA + H2O
Catalysis of the reaction: OPC4-3-hydroxyacyl-CoA <=> OPC4-trans-2-enoyl-CoA + H2O
Catalysis of the reaction: beta-carotene + O2 <=> 10'-apo-beta-carotenal + beta-ionone
Catalysis of the reaction: oleamide + H2O <=> oleate + ammonium
Catalysis of the reaction: S-adenosyl-L-methionine  + a jasmonic acid <=> S-adenosyl-L-homocysteine  + a methyl jasmonate
Catalysis of the reaction: phenylacetyl-CoA + glycine <=> H+ + phenylacetylglycine + coenzyme A
Catalysis of the reaction: homotaurine + 2-oxoglutarate(2-) <=> 3-sulfopropanal + L-glutamate(1-)
Catalysis of the reaction: 4'-demethylrebeccamycin + S-adenosyl-L-methionine  <=> H+ + rebeccamycin + S-adenosyl-L-homocysteine
Catalysis of the reaction: 7,8-dihydromonapterin <=> glycolaldehyde + 2-amino-6-(hydroxymethyl)-7,8-dihydropteridin-4-ol
Catalysis of the reaction: L-dopa + S-adenosyl-L-methionine  <=> 3-O-methyldopa + S-adenosyl-L-homocysteine + H+
Catalysis of the reaction: 4-aminobenzoate + L-glutamate + ATP <=> H+ + p-aminobenzoyl glutamate + AMP + diphosphoric acid
Catalysis of the reaction: vanillate + L-glutamate(1-) + ATP <=> H+ + N-vanillate-L-glutamate + AMP + diphosphoric acid
Catalysis of the reaction: benzoate + L-glutamate + ATP <=> H+ + N-benzoyl-L-glutamate + AMP + diphosphoric acid
Catalysis of the reaction: 4-hydroxybenzoic acid + L-glutamate + ATP <=> H+ + N-(4-hydroxybenzoyl)-L-glutamate + AMP + diphosphoric acid
Catalysis of the reaction: (S)-scoulerine + O2 = dehydroscoulerine + hydrogen peroxide + H+
Catalysis of the reaction: (R)-adrenaline(1+) + S-adenosyl-L-methionine  <=> metanephrine + S-adenosyl-L-homocysteine + H+
Catalysis of the reaction: H2O + a 1-phosphatidyl-1D-myo-inositol 5-phosphate = hydrogenphosphate + an L-1-phosphatidyl-inositol
Catalysis of the reaction: 5-diphospho-1D-myo-inositol pentakisphosphate + ATP = 3,5-bisdiphosphoinositol-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP
Catalysis of the reaction: acryloyl-CoA + H2O <=> acrylate + coenzyme A + H+
Catalysis of the reaction: S-adenosyl-L-methionine  + a demethylmenaquinol <=> S-adenosyl-L-homocysteine  + H+ + a menaquinol
Catalysis of the reaction: dTDP-6-deoxy-beta-L-mannose + N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol <=> dTDP(3-) + alpha-L-Rhap-(1->3)-alpha-D-GlcpNAc-1-diphospho-trans,octacis-decaprenol + H+
Catalysis of the reaction: (5alpha,22S,24R)-22-hydroxyergostan-3-one + O2 + NADPH + H+ <=> 3-dehydro-6-deoxoteasterone + NADP + H2O
Catalysis of the reaction: L-galactonate + NADP = aldehydo-D-galacturonate + NADPH + H+
Catalysis of the reaction: 7,9-dihydro-1H-purine-2,6,8(3H)-trione + NADH + H+ + O2 <=> 5-hydroxyisouric acid + NAD + H2O
Catalysis of the reaction: arsenate + mycothiol <=> mycothiol-arsenate conjugate + H2O
Catalysis of the reaction: 26,27-dehydrozymosterol + S-adenosyl-L-methionine  <=> 24-alkyl sterol 1 + S-adenosyl-L-homocysteine
Catalysis of the reaction: gamma-aminobutyric acid  + L-histidine  + ATP = H+ + homocarnosine + ADP + hydrogenphosphate
Catalysis of the reaction: (4-coumaroyl)acetyl-CoA + 4-coumaryl-CoA + H2O <=> bisdemethoxycurcumin + 2 coenzyme A + carbon dioxide
Catalysis of the reaction: (4-coumaroyl)acetyl-CoA + feruloyl-CoA + H2O <=> demethoxycurcumin + 2 coenzyme A + carbon dioxide
Catalysis of the reaction: feruloylacetyl-CoA + 4-coumaryl-CoA + H2O = demethoxycurcumin + 2 coenzyme A + carbon dioxide
Catalysis of the reaction: feruloylacetyl-CoA + feruloyl-CoA(4-) + H2O <=> curcumin + 2 coenzyme A(4-) + carbon dioxide
Catalysis of the reaction: tricaffeoyl spermidine + 3 S-adenosyl-L-methionine  <=> 3 H+ + triferuloyl spermidine + 3 S-adenosyl-L-homocysteine
Catalysis of the reaction: gibberellin A20 + 2-oxoglutarate + O2 <=> gibberellin A29 + succinate + carbon dioxide
Catalysis of the reaction: 2-oxoglutarate + O2 + a hypoxia inducible factor (HIF) alpha subunit = succinate + carbon dioxide + a (3S)-3-hydroxy-L-asparagine-HIF alpha subunit
Catalysis of the reaction: decanoate + NADPH + O2 + H+ <=> 10-hydroxycaprate + NADP + H2O
Catalysis of the reaction: ditrans,octacis-undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl-L-alanyl-gamma-D-isoglutaminyl-N-(beta-D-asparatyl)-L-lysyl-D-alanyl-D-alanine + ammonium + ATP = H+ + ditrans,octacis-undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl-L-alanyl-gamma-D-isoglutaminyl-N-(beta-D-asparaginyl)-L-lysyl-D-alanyl-D-alanine + AMP + diphosphoric acid
Catalysis of the reaction: dodecanoate + NADPH + O2 + H+ <=> 11-hydroxylaurate + NADP + H2O
Catalysis of the reaction: gibberellin A9 + S-adenosyl-L-methionine  <=> gibberellin A9 methyl ester + S-adenosyl-L-homocysteine
Catalysis of the reaction: gibberellin A4 + S-adenosyl-L-methionine  <=> gibberellin A4 methyl ester + S-adenosyl-L-homocysteine
Catalysis of the reaction: gibberellin A20 + S-adenosyl-L-methionine  <=> gibberellin A20 methyl ester + S-adenosyl-L-homocysteine
Catalysis of the reaction: H2O + a ceramide = a sphingoid base + a fatty acid
Catalysis of the reaction: gibberellin A34 + S-adenosyl-L-methionine  = gibberellin A34 methyl ester + S-adenosyl-L-homocysteine
Catalysis of the reaction: gibberellin A4 + O2 + H+ + NAD(P)H <=> 16alpha,17-epoxy gibberellin A4 + H2O + NAD(P)
Catalysis of the reaction: gibberellin A12 + O2 + H+ + NAD(P)H <=> 16alpha, 17-epoxy gibberellin A12 + H2O + NAD(P)
Catalysis of the reaction: gibberellin A9 + O2 + H+ + NAD(P)H <=> 16alpha, 17-epoxy gibberellin A9 + H2O + NAD(P)
Catalysis of the reaction: H+ + coniferyl aldehyde + NADPH + O2 <=> 5-hydroxy-coniferaldehyde + NADP + H2O
Catalysis of the reaction: H+ + 7,8-dihydro-8-oxoguanine + H2O <=> 7,9-dihydro-1H-purine-2,6,8(3H)-trione + ammonium
Catalysis of the reaction: 4-dihydrocoumaroyl-CoA + 3 malonyl-CoA + 3 H+ = phloretin + 4 coenzyme A + 3 carbon dioxide
Catalysis of the reaction: S-adenosyl-L-methionine  + a malonyl-[acp] = S-adenosyl-L-homocysteine  + a malonyl-[acp] methyl ester
Catalysis of the reaction: NADP + a 3R-hydroxyglutaryl-[acp] methyl ester <=> NADPH + H+ + a 3-oxo-glutaryl-[acp] methyl ester
Catalysis of the reaction: NADP + a 3R-hydroxypimeloyl-[acp] methyl ester <=> NADPH + H+ + a 3-oxo-pimeloyl-[acp] methyl ester.
Catalysis of the reaction: (4R)-limonene + O2 + NADH + H+ <=> (4R)-perillyl alcohol + NAD + H2O.
Catalysis of the reaction: H+ + (22S)-22-hydroxycampesterol + NADPH + O2 <=> (22R,23R)-22,23-dihydroxycampesterol + NADP + H2O.
Catalysis of the reaction: H+ + (22S)-22-hydroxycampest-4-en-3-one + NADPH + O2 <=> (22R,23R)-22,23-dihydroxy-campest-4-en-3-one + NADP + H2O.
Catalysis of the reaction: H+ + 3-epi-6-deoxocathasterone + NADPH + O2 <=> 6-deoxotyphasterol + NADP + H2O.
Catalysis of the reaction: H+ + teasterone + NADPH + O2 <=> 7-oxateasterone + NADP + H2O.
Catalysis of the reaction: H+ + typhasterol + NADPH + O2 <=> 7-oxatyphasterol + NADP + H2O
Catalysis of the reaction: (2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O <=> H+ + anthranilate + (2E)-2-hydroxypenta-2,4-dienoate.
Catalysis of the reaction: H2O + [heparan sulfate]-N-acetyl-alpha-D-glucosamine = acetate + H+ + [heparan sulfate]-alpha-D-glucosamine
Catalysis of the reaction: 3'-phosphonato-5'-adenylyl sulfate + [chondroitin-sulfate]-beta-D-glucuronate = adenosine 3',5'-bismonophosphate + [chondroitin-sulfate]-2-O-sulfo-beta-D-glucuronate
Catalysis of the reaction: 3'-phosphonato-5'-adenylyl sulfate + [dermatan]-alpha-L-iduronate <=> adenosine 3',5'-bismonophosphate + [dermatan-sulfate]-2-O-sulfo-alpha-L-iduronate
Catalysis of the reaction: carboxynorspermidine + NADP + H2O <=> L-aspartic acid 4-semialdehyde betaine + trimethylenediaminium + NADPH + H+
Catalysis of the reaction: carboxyspermidine + H2O + NADP <=> L-aspartic acid 4-semialdehyde betaine + 1,4-butanediammonium + NADPH + H+
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate + H2O <=> (3R,6E)-nerolidol + diphosphoric acid
Catalysis of the reaction: tricetin + S-adenosyl-L-methionine  = H+ + 3'-O-methyltricetin + S-adenosyl-L-homocysteine
Catalysis of the reaction: S-adenosyl-L-methionine  + 3'-O-methyltricetin = H+ + S-adenosyl-L-homocysteine  + 3',5'-di-O-methyltricetin
Catalysis of the reaction: H2O + an N-acetyl-beta-D-galactosalaminyl-[glycan] = N-acetyl-beta-D-galactosamine + a glycan
Catalysis of the reaction: S-[(2E,6E)-farnesyl]-L-cysteine  + O2 + H2O <=> (2-trans,6-trans)-farnesal + L-cysteine  + hydrogen peroxide
Catalysis of the reaction: 3-oxotetradecanoyl-CoA + H2O <=> 3-oxo-myristate + coenzyme A + H+
Catalysis of the reaction: 3-oxo-myristate + H+ <=> 2-tridecanone + carbon dioxide
Catalysis of the reaction: H+ + 1-palmitoyl-2-linoleoyl-phosphatidylcholine + NADPH + O2 <=> 1-palmitoyl-2-vernoloyl-phosphatidylcholine + NADP + H2O
Catalysis of the reaction: 2,4,4',6-tetrahydroxydibenzoylmethane + UDP-alpha-D-glucose <=> 8C-glucosyl-2-hydroxynaringenin + UDP + 2 H+
Catalysis of the reaction: (S)-3-sulfonatolactate + NAD <=> 3-sulfonatopyruvate(2-) + NADH + H+
Catalysis of the reaction: 2,5-dihydroxybenzoate + UDP-alpha-D-glucose <=> 2,5-dihydroxybenzoate 5-O-beta-D-glucoside + UDP + H+
Catalysis of the reaction: (2R)-3-sulfopropanediol(1-) + NAD <=> 2-oxo-3-hydroxy-propane-1-sulfonate + NADH + H+
Catalysis of the reaction: a very-long-chain (3R)-3-hydroxyacyl-CoA = H2O + a very-long-chain trans-2,3-dehydroacyl-CoA
Catalysis of the reaction: UDP-alpha-D-glucuronate + baicalein <=> H+ + UDP + baicalin
Catalysis of the reaction: cyanidin 3-O-beta-D-glucoside betaine + UDP-alpha-D-glucuronate <=> H+ + cyanidin 3-O-beta-(2-O-beta-D-glucuronosyl)-beta-D-glucoside + UDP
Catalysis of the reaction: copal-8-ol diphosphate <=> 2-trans,6-trans,10-trans-geranylgeranyl diphosphate + H2O
Catalysis of the reaction: 8'-apo-beta,psi-caroten-8'-al + O2 <=> all-trans-retinal + 2,6-dimethylocta-2,4,6-trienedial
Catalysis of the reaction: coenzyme A + a (3R)-3-hydroxyacyl-[acyl-carrier protein] = a (3R)-3-hydroxyacyl-CoA + a holo-[acyl-carrier protein]
Catalysis of the reaction: 2-heptyl-4-quinolone + NADH + O2 + H+ <=> 2-heptyl-3-hydroxy-4-quinolone + NAD + H2O
Catalysis of the reaction: acetyl-CoA + (Z)-hex-3-en-1-ol <=> (3Z)-hex-3-en-1-yl acetate + coenzyme A
Catalysis of the reaction: H2O + an N-acetyl-alpha-D-glucosaminyl-L-threonine-[glycoprotein] <=> N-acetyl-alpha-D-glucosaminide + a [protein]-L-threonine
Catalysis of the reaction: H2O + an N-acetyl-alpha-D-glucosaminyl-L-serine-[glycoprotein] <=> N-acetyl-alpha-D-glucosaminide + a [protein]-L-serine
Catalysis of the reaction: phenazine-1-carboxylate + S-adenosyl-L-methionine  <=> 5-methylphenazine-1-carboxylate + S-adenosyl-L-homocysteine
Catalysis of the reaction: 5-methylphenazine-1-carboxylate + NADH + O2 + 2 H+ <=> pyocyanin + NAD + carbon dioxide + H2O
Catalysis of the reaction: (+)-5-epi-aristolochene + 2 NADPH + 2 H+ + 2 O2 <=> capsidiol + 2 NADP + 2 H2O
Catalysis of the reaction: H+ + (3S,6E)-nerolidol + NADPH + O2 <=> (E)-4,8-dimethyl-1,3,7-nonatriene + buten-2-one + NADP + 2 H2O
Catalysis of the reaction: 4alpha-hydroxymethyl,4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + NADH + O2 + H+ <=> 4alpha-formyl,4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + NAD + 2 H2O
Catalysis of the reaction: 24-methylenecycloartanol + NADH + O2 + H+ <=> 4alpha-hydroxymethyl,4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + NAD + H2O
Catalysis of the reaction: 4alpha-formyl,4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + NADH + O2 <=> 4alpha-carboxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + NAD + H2O
Catalysis of the reaction: 4alpha-carboxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + NAD <=> cycloeucalenone + NADH + carbon dioxide
Catalysis of the reaction: cycloeucalenone + NADPH + H+ <=> cycloeucalenol + NADP
Catalysis of the reaction: 24-methylenelophenol + O2 + NADH + H+ <=> 4alpha-hydroxymethyl-ergosta-7,24(241)-dien-3beta-ol + NAD + H2O
Catalysis of the reaction: 4alpha-formyl-ergosta-7,24(241)-dien-3beta-ol + O2 + NADH <=> 4alpha-carboxy-ergosta-7,24(241)-dien-3beta-ol + NAD + H2O
Catalysis of the reaction: 24-ethylidenelophenol + NADH + O2 + H+ <=> 4alpha-hydroxymethyl-stigmasta-7,24(241)-dien-3beta-ol + NAD + H2O
Catalysis of the reaction: 4alpha-hydroxymethyl-stigmasta-7,24(241)-dien-3beta-ol + NADH + O2 + H+ <=> 4alpha-formyl-stigmasta-7,24(241)-dien-3beta-ol + NAD + 2 H2O
Catalysis of the reaction: 4alpha-formyl-stigmasta-7,24(241)-dien-3beta-ol + NADH + O2 <=> 4alpha-carboxy-stigmasta-7,24(241)-dien-3beta-ol + NAD + H2O
Catalysis of the reaction: 4alpha-carboxy-stigmasta-7,24(241)-dien-3beta-ol + NAD <=> avenastenone + NADH + carbon dioxide
Catalysis of the reaction: avenastenone + NADPH + H+ <=> avenasterol + NADP
Catalysis of the reaction: cycloartenol + NADH + O2 + H+ <=> 4alpha-hydroxymethyl,4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3beta-ol + NAD + H2O
Catalysis of the reaction: 4alpha-hydroxymethyl,4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3beta-ol + NADH(2-) + O2 + H+ <=> 4alpha-formyl,4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3beta-ol + NAD(1-) + 2 H2O
Catalysis of the reaction: 4alpha-formyl,4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3beta-ol + NADH(2-) + O2 <=> 4alpha-carboxy,4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3beta-ol + NAD(1-) + H2O
Catalysis of the reaction: 4alpha-carboxy,4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3beta-ol + NAD(1-) <=> 4alpha,14alpha-dimethyl-9beta,19-cyclo-5alpha-cholest-24-en-3-one + NADH(2-) + carbon dioxide
Catalysis of the reaction: 4alpha-methyl-5alpha-cholesta-7,24-dien-3beta-ol + O2 + NADH(2-) + H+ <=> 4alpha-hydroxymethyl-5alpha-cholesta-7,24-dien-3beta-ol + NAD(1-) + H2O
Catalysis of the reaction: 4alpha-hydroxymethyl-5alpha-cholesta-7,24-dien-3beta-ol + O2 + NADH(2-) + H+ <=> 4alpha-formyl-5alpha-cholesta-7,24-dien-3beta-ol + NAD(1-) + 2 H2O
Catalysis of the reaction: 4alpha-formyl-5alpha-cholesta-7,24-dien-3beta-ol + O2 + NADH(2-) <=> 4alpha-carboxy-5alpha-cholesta-7,24-dien-3beta-ol + NAD(1-) + H2O
Catalysis of the reaction: 4alpha-carboxy-5alpha-cholesta-7,24-dien-3beta-ol + NAD(1-) <=> 5alpha-cholesta-7,24-dien-3-one + NADH(2-) + carbon dioxide
Catalysis of the reaction: neryl diphosphate(3-) + isopentenyl diphosphate(3-) <=> diphosphoric acid + 2-cis,6-cis-farnesyl diphosphate(3-)
Catalysis of the reaction: ATP + a [protein]-N6-D-ribulosyl-L-lysine <=> ADP + a [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
Catalysis of the reaction: ATP + a [protein]-N6-D-fructosyl-L-lysine <=> ADP + H+ + a [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
Catalysis of the reaction: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + D-lysinium(1+) + ATP <=> UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-D-lysine + ADP + hydrogenphosphate + H+
Catalysis of the reaction: cortisol + NADP <=> cortisone + NADPH + H+
Catalysis of the reaction: but-3-enoate + H2O <=> allyl alcohol + formate
Catalysis of the reaction: L-idonate + NAD = 5-dehydro-D-gluconate + NADH + H+
Catalysis of the reaction: dinitrogen oxide + H2O + NAD(P) = 2 nitric oxide + H+ + NAD(P)H
Catalysis of the reaction: H2O + an N-acylphosphatidylethanolamine = H+ + an N-acylethanolamine + a 1,2-diacyl-sn-glycerol 3-phosphate
Catalysis of the reaction: 2-cis,6-trans-farnesyl diphosphate <=> (+)-2-epi-prezizaene + diphosphoric acid
Catalysis of the reaction: UDP-alpha-D-glucose + solasodine <=> UDP + solasodine 3-O-beta-D-glucopyranoside + H+
Catalysis of the reaction: UDP-alpha-D-glucose + brassicasterol <=> UDP(3-) + 3-O-beta-D-glucosyl-brassicasterol + H+
Catalysis of the reaction: UDP-alpha-D-glucose + cholesterol = UDP + cholesteryl beta-D-glucoside + H+
Catalysis of the reaction: behenate + NADPH + O2 + H+ = 22-hydroxydocosanoate + NADP + H2O
Catalysis of the reaction: S-adenosyl-L-methionine  + a 3-(all-trans-polyrenyl)benzene-1,2-diol <=> S-adenosyl-L-homocysteine  + H+ + a 2-methoxy-6-(all-trans-polyprenyl)phenol
Catalysis of the reaction: (-)-trans-permethrin + H2O <=> H+ + (3-phenoxyphenyl)methanol + (1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate
Catalysis of the reaction: H2O + a rhamnogalacturonan type I <=> [rhamnogalacturonan I oligosaccharide]-alpha-L-rhamnose + 4-deoxy-4,5-unsaturated D-galactopyranosyluronate-[rhamnogalacturonan I oligosaccharide]
Catalysis of the reaction: 2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose(1-) + H2O <=> (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + alpha-L-rhamnopyranose
Catalysis of the reaction: beta-D-4-deoxy-Delta(4)-GlcpA-(1->3)-beta-D-GalpNAc6S + H2O = 5-dehydro-4-deoxy-D-glucuronate + N-acetyl-beta-D-galactosamine 6-sulfate
Catalysis of the reaction: coenzyme A + ATP + an in-chain hydroxy fatty acid = diphosphoric acid + AMP + a in-chain hydroxyacyl-CoA
Catalysis of the reaction: coenzyme A + ATP + an omega-hydroxy fatty acid = diphosphoric acid + AMP + a omega-hydroxyacyl-CoA
Catalysis of the reaction: thiocyanate + S-adenosyl-L-methionine  <=> methyl thiocyanate + S-adenosyl-L-homocysteine
Catalysis of the reaction: ATP + H2O + a maltodextrin = AMP + hydrogenphosphate + a 6-phosphogluco-maltodextrin
Catalysis of the reaction: n ATP + n H2O + a 6-phosphogluco-maltodextrin = n AMP + n hydrogenphosphate + a poly-6-phosphogluco-maltodextrin
Catalysis of the reaction: n ATP + n H2O + starch = n AMP + n hydrogenphosphate + a 6-phosphogluco-amylopectin
Catalysis of the reaction: n ATP + n H2O + a 6-phosphogluco-amylopectin = n AMP + n hydrogenphosphate + a 6-phosphogluco-3-phosphogluco-amylopectin
Catalysis of the reaction: 2 dihydrogen + NAD + 2 an oxidized ferredoxin = NADH + 3 H+ + 2 a reduced ferredoxin
Catalysis of the reaction: m+q H2O + a 6-phosphogluco-3-phosphogluco-amylopectin <=> m+q hydrogenphosphate + a 6-phosphogluco-3-phosphogluco-amylopectin
Catalysis of the reaction: 4 H+ + 15-cis-4,4'-diapophytoene + 4 FAD <=> 4,4'-diapolycopene + 4 FADH2
Catalysis of the reaction: GDP-2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose + H2O <=> 2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + GDP + H+
Catalysis of the reaction: 4,4'-diaponeurosporene + FAD + H+ <=> 4,4'-diapolycopene + FADH2
Catalysis of the reaction: n H2O + an exposed unphosphorylated, unbranched malto-oligosaccharide tail on amylopectin <=> amylopectin + maltose
Catalysis of the reaction: acrolein + NADPH + H+ <=> propanal + NADP
Catalysis of the reaction: (cis)-crotonaldehyde + NADPH + H+ <=> butanal + NADP.
Catalysis of the reaction: buten-2-one + NADPH + H+ <=> butan-2-one + NADP
Catalysis of the reaction: 1-penten-3-one + NADPH + H+ <=> 1-pentan-3-one + NADP
Catalysis of the reaction: trans-4-hexen-3-one + NADPH + H+ <=> hexan-3-one + NADP
Catalysis of the reaction: (2-trans,6-trans)-farnesol + ATP(4-) <=> H+ + 2-trans,-6-trans-farnesyl monophosphate + ADP(3-)
Catalysis of the reaction: geraniol + ATP = geranyl monophosphate + ADP + H+
Catalysis of the reaction: UDP-D-galactose + soyasapogenol B 3-O-beta-glucuronate <=> H+ + UDP + soyasaponin III
Catalysis of the reaction: UDP-L-rhamnose + soyasaponin III <=> H+ + UDP + soyasaponin I
Catalysis of the reaction: (E,E,E)-geranylgeraniol + ATP = H+ + all-trans-geranyl-geranyl monophosphate + ADP
Catalysis of the reaction: 3-ammoniopropanal + NAD + H2O <=> 2 H+ + beta-alanine  + NADH
Catalysis of the reaction: lupan-3beta,20-diol <=> (S)-2,3-epoxysqualene + H2O
Catalysis of the reaction: aminodeoxyfutalosinate + H2O <=> dehypoxanthine futalosine + adenine.
Catalysis of the reaction: 2 H+ + 2 a malonyl-[acp] <=> 2 carbon dioxide + an acetoacetyl-[acp] + a holo-[acyl-carrier protein]
Catalysis of the reaction: 2 a 1,2-diacyl-sn-glycerol = a triacyl-sn-glycerol + a 2-monoglyceride
Catalysis of the reaction: a phosphatidylcholine + a 1,2-diacyl-sn-glycerol = a 1,2-diacyl-sn-glycerol + a phosphatidylcholine
Catalysis of the reaction: hydrogenphosphate + a linear malto-oligosaccharide = alpha-D-glucose 1-phosphate + a linear malto-oligosaccharide
Catalysis of the reaction: 10'-apo-beta-carotenal + O2 <=> 13-apo-beta-carotenone + 4-methylocta-2,4,6-trienedial
Catalysis of the reaction: n H2O + a cellodextrin = n beta-cellobiose, releasing cellobiose from the reducing ends of the chains.
Catalysis of the reaction: neoagarobiose + H2O <=> 3,6-anhydro-alpha-L-galactopyranose + beta-D-galactoside.
Catalysis of the reaction: neoagarotetraose + H2O <=> 3,6-anhydro-alpha-L-galactopyranose + agarotriose.
Catalysis of the reaction: neo-lambda-carrahexaose + H2O <=> neo-lambda-carratetraose + neo-lambda-carrabiose
Catalysis of the reaction: neoagarohexaose + H2O <=> 3,6-anhydro-alpha-L-galactopyranose + agaropentaose.
Catalysis of the reaction: 1-palmitoyl-2-linoleoyl-phosphatidylcholine + H2O <=> 1-linoleoyl-sn-glycero-3-phosphocholine + hexadecanoate + H+
Catalysis of the reaction: H2O + a 1,3-diglyceride = a monoglyceride + a fatty acid
Catalysis of the reaction: H2O + a 1,2-diacyl-sn-glycerol = a monoglyceride + a fatty acid
Catalysis of the reaction: germacra-1(10),4,11(13)-trien-12-ol + 2 NADP + H2O <=> germacra-1(10),4,11(13)-trien-12-oate + 2 NADPH + 3 H+
Catalysis of the reaction: NADP + a reduced coenzyme F420 <=> NADPH + H+ + an oxidized coenzyme F420
Catalysis of the reaction: a 5,6-dihydrouracil16 in tRNA + NAD(P) <=> H+ + a uracil16 in tRNA + NAD(P)H
Catalysis of the reaction: a 5,6-dihydrouracil17 in tRNA + NAD(P) <=> H+ + a uracil17 in tRNA + NAD(P)H
Catalysis of the reaction: a 5,6-dihydrouracil20 in tRNA + NAD(P) <=> H+ + a uracil20 in tRNA + NAD(P)H
Catalysis of the reaction: a 5,6-dihydrouracil47 in tRNA + NAD(P) <=> H+ + a uracil47 in tRNA + NAD(P)H
Catalysis of the reaction: a 5,6-dihydrouracil20a in tRNA + NAD(P) <=> H+ + a uracil20a in tRNA + NAD(P)H
Catalysis of the reaction: a 5,6-dihydrouracil20b in tRNA + NAD(P) <=> H+ + a uracil20b in tRNA + NAD(P)H
Catalysis of the reaction: glutathionate + a poly gamma-glutamylcysteine-beta-alanine = glycine + a poly gamma-glutamylcysteine-beta-alanine
Catalysis of the reaction: glutathionate + L-gamma-glutamyl-L-cysteinyl-beta-alaninate <=> gamma-Glu-Cys-gamma-Glu-Cys-beta-Ala + glycine
Catalysis of the reaction: H2O + a glutathione-toxin conjugate <=> glycine + a [Glu-Cys]-S-conjugate
Catalysis of the reaction: malonyl-CoA(5-) + an L-cysteine-S-conjugate <=> coenzyme A + H+ + an N-malonyl-L-cysteine-S-conjugate
Catalysis of the reaction: 2-oxoglutarate(2-) + O2 + 2 H+ <=> ethene + 3 carbon dioxide + H2O
Catalysis of the reaction: 2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + H2O = N-acetyl-D-glucosamine + D-glucosamine
Catalysis of the reaction: n H2O + chitin <=> N,N'-diacetylchitobiose
Catalysis of the reaction: an 11-cis retinol-[cellular-retinol-binding-protein] + a phosphatidylcholine <=> a cellular-retinol-binding protein + an 11-cis-retinyl ester + a 1-lysophosphatidylcholine
Catalysis of the reaction: choline + NADP = betaine aldehyde + NADPH + H+
Catalysis of the reaction: formylaminopyrimidine + H2O <=> 4-amino-5-ammoniomethyl-2-methylpyrimidine + formate
Catalysis of the reaction: NAD(1-) + a sphinganine <=> 3-dehydrosphinganinium(1+) + NADH + H+
Catalysis of the reaction: C20 sphinganine(1+) + NADP <=> C20 3-dehydrosphinganine(1+) + NADPH + H+
Catalysis of the reaction: L-threo-sphinganine + NADP <=> H+ + NADPH + 3-dehydrosphinganinium(1+)
Catalysis of the reaction: 1-deoxy-11-oxopentalenate + O2 + NADPH + H+ = pentalenolactone D + H2O + NADP
Catalysis of the reaction: L-ornithinium(1+) = N(5)-acetyl-L-ornithine
Catalysis of the reaction: 4-coumaryl-CoA + 3-oxooctanoyl-CoA + H2O <=> 4-coumaroylhexanoylmethane + 2 coenzyme A + carbon dioxide.
Catalysis of the reaction: beta-amyrin + 2 O2 + 2 NADPH + 2 H+ <=> 11-oxo-beta-amyrin + 3 H2O + 2 NADP.
Catalysis of the reaction: beta-amyrin + O2 + NADPH + H+ <=> 11alpha-hydroxy-beta-amyrin + H2O + NADP
Catalysis of the reaction: 11alpha-hydroxy-beta-amyrin + O2 + NADPH + H+ = 11-oxo-beta-amyrin + 2 H2O + NADP
Catalysis of the reaction: 30-hydroxy-beta-amyrin + O2 + NADPH + H+ <=> 11alpha,30-dihydroxy-beta-amyrin + H2O + NADP.
Catalysis of the reaction: pheophytin b + H2O <=> H+ + pheophorbide b + phytol.
Catalysis of the reaction: cholesterol + NAD = cholest-5-en-3-one + NADH + H+
Catalysis of the reaction: 4-methylumbelliferyl glucoside + malonyl-CoA <=> 4-methylumbelliferone 6'-O-malonylglucoside + coenzyme A.
Catalysis of the reaction: (1E,2Z)-3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate + H2O <=> 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oate + (2Z,4Z)-2-hydroxyhexa-2,4-dienoate + H+.
Catalysis of the reaction: selenic acid + ATP + 2 H+ <=> adenylyl selenate + diphosphoric acid
Catalysis of the reaction: L-selenocysteine  + O-phosphonato-L-homoserine = hydrogenphosphate + L-selenocystathionine
Catalysis of the reaction: alpha-linolenate + O2 <=> (9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate
Catalysis of the reaction: linoleate + O2 = 9(R)-HPODE
Catalysis of the reaction: malonyl-CoA + gamma-linolenoyl-CoA + H+ = (8Z,11Z,14Z)-3-oxoicosa-8,11,14-trienoyl-CoA + coenzyme A + carbon dioxide
Catalysis of the reaction: S-adenosyl-L-methionine  + mycinamicin VI <=> S-adenosyl-L-homocysteine  + mycinamicin III(1+) + H+.
Catalysis of the reaction: 2 S-adenosyl-L-methionine  + trans-resveratrol <=> 2 S-adenosyl-L-homocysteine  + pterostilbene + 2 H+
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate(3-) <=> 7-epi-sesquithujene + diphosphoric acid.
Catalysis of the reaction: 2-cis,6-trans,10-trans-geranylgeranyl diphosphate + H2O <=> (13E)-labda-7,13-dien-15-ol + diphosphoric acid
Catalysis of the reaction: (S)-benzoin + NADP(3-) <=> benzil + NADPH(4-) + H+
Catalysis of the reaction: S-adenosyl-L-methionine  + erythromycin C <=> S-adenosyl-L-homocysteine  + erythromycin A + H+
Catalysis of the reaction: S-adenosyl-L-methionine  + erythromycin D <=> S-adenosyl-L-homocysteine  + erythromycin B + H+
Catalysis of the reaction: dTDP-D-oliose + NADP <=> dTDP-4-dehydro-2,6-dideoxy-D-glucose + NADPH + H+
Catalysis of the reaction: dTDP-4-dehydro-2,6-dideoxy-alpha-D-allose + NAD(P) <=> dTDP-(2R,6S)-6-hydroxy-2-methyl-3-oxo-3,6-dihydro-2H-pyran-4-olate + 2 H+ + NAD(P)H
Catalysis of the reaction: (6E)-8-hydroxygeraniol + 2 NADP <=> (6E)-8-oxogeranial + 2 NADPH + 2 H+
Catalysis of the reaction: 4-coumaryl-CoA + 2-oxoglutarate + O2 <=> 2,4-dihydroxycinnamoyl-CoA + succinate + carbon dioxide
Catalysis of the reaction: geranyl diphosphate(3-) + H2O <=> 1,8-cineole + diphosphoric acid
Catalysis of the reaction: L-dopa  + 0.5 O2 = L-dopaquinone  + H2O
Catalysis of the reaction: 4-(methylamino)butyric acid  + O2 + H2O <=> gamma-aminobutyric acid  + formaldehyde + hydrogen peroxide
Catalysis of the reaction: 2-deoxystreptamine + UDP-alpha-D-glucose <=> 2'-deamino-2'-hydroxyparomamine + UDP(3-) + H+
Catalysis of the reaction: 2-deoxystreptamine(2+) + UDP-N-acetyl-alpha-D-glucosamine <=> H+ + 2'-N-acetylparomamine(2+) + UDP(3-)
Catalysis of the reaction: 1,8-cineole + NADPH + H+ + O2 <=> 2-exo-hydroxy-1,8-cineole + NADP + H2O
Catalysis of the reaction: biphenyl-2,2'-diol + O2 + NADH + H+ <=> biphenyl-2,2',3-triol + H2O + NAD
Catalysis of the reaction: 2-propylphenol + O2 + NADH + H+ = 3-propylcatechol + H2O + NAD
Catalysis of the reaction: 2-isopropylphenol + O2 + NADH + H+ = 3-isopropylcatechol + H2O + NAD
Catalysis of the reaction: 2-hydroxy-6-oxo-nona-2,4-dienoate + H2O = butyrate + 2-oxopent-4-enoate + H+
Catalysis of the reaction: biphenyl-2,2',3-triol + O2 + NADH + H+ <=> 2,2',3,3'-tetrahydroxybiphenyl + NAD + H2O
Catalysis of the reaction: 2-hydroxy-6-oxo-6-(2,3-dihydroxyphenyl)-hexa-2,4-dienoate + H2O <=> 2,3-dihydroxybenzoate + 2-oxopent-4-enoate + H+
Catalysis of the reaction: H2O + a 3-oxoacyl-CoA = H+ + coenzyme A + a 3-oxoacid
Catalysis of the reaction: H+ + a 3-oxoacid = carbon dioxide + a methylketone
Catalysis of the reaction: 16-hydroxy-hentriaconta-3,6,9,12,19,22,25,28-octaene-15-oyl-CoA + NADP <=> hentriaconta-3,6,9,12,19,22,25,28-octaene-16-one-15-oyl-CoA + NADPH + H+.
Catalysis of the reaction: malonyl-CoA + a palmitoyl-[acp] = 1-heptadecene + 2 carbon dioxide + coenzyme A + a holo-[acyl-carrier protein]
Catalysis of the reaction: malonyl-CoA + 3 H+ + a heptodecanoyl-[acp] = octadec-1-ene + 2 carbon dioxide + coenzyme A + a holo-[acyl-carrier protein]
Catalysis of the reaction: malonyl-CoA + H+ + a long-chain acyl-[acp] + a reduced electron acceptor = 2 carbon dioxide + coenzyme A + a terminal olefin + a holo-[acyl-carrier protein] + an oxidized electron acceptor
Catalysis of the reaction: malonyl-CoA + 3 H+ + a stearoyl-[acp] = nonadec-1-ene + 2 carbon dioxide + coenzyme A + a holo-[acyl-carrier protein]
Catalysis of the reaction: ditrans,polycis-undecaprenyl phosphate + UDP-N,N'-diacetylbacillosamine <=> N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tri-trans,hepta-cis-undecaprenol + UMP.
Catalysis of the reaction: N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tri-trans,hepta-cis-undecaprenol + UDP-N-acetyl-D-galactosamine <=> N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tri-trans,hepta-cis-undecaprenol + UDP + H+.
Catalysis of the reaction: stearoyl-CoA(4-) + malonyl-CoA(5-) + H+ <=> 3-oxoicosanoyl-CoA. + carbon dioxide + coenzyme A.
Catalysis of the reaction: tetracosanoyl-CoA(4-) + malonyl-CoA(5-) + H+ <=> 3-oxohexacosanoyl-CoA + carbon dioxide + coenzyme A.
Catalysis of the reaction: behenoyl-CoA(4-) + malonyl-CoA(5-) + H+ <=> 3-oxotetracosanoyl-CoA. + carbon dioxide + coenzyme A.
Catalysis of the reaction: (R)-3-hydroxyicosanoyl-CoA(4-) + NADP(3-) <=> 3-oxoicosanoyl-CoA + NADPH + H+.
Catalysis of the reaction: (R)-3-hydroxybehenoyl-CoA(4-) + NADP(3-) <=> 3-oxodocosanoyl-CoA + NADPH + H+.
Catalysis of the reaction: (R)-3-hydroxylignoceroyl-CoA + NADP <=> 3-oxotetracosanoyl-CoA + NADPH + H+.
Catalysis of the reaction: (R)-3-hydroxycerotoyl-CoA + NADP <=> 3-oxohexacosanoyl-CoA + NADPH + H+
Catalysis of the reaction: (R)-3-hydroxyicosanoyl-CoA <=> trans-2-icosenoyl-CoA + H2O
Catalysis of the reaction: (R)-3-hydroxybehenoyl-CoA <=> trans-2-docosenoyl-CoA + H2O.
Catalysis of the reaction: (R)-3-hydroxylignoceroyl-CoA(4-) <=> trans-2-tetracosenoyl-CoA + H2O.
Catalysis of the reaction: (R)-3-hydroxycerotoyl-CoA(4-) <=> trans-2-hexacosenoyl-CoA(4-) + H2O
Catalysis of the reaction: icosanoyl-CoA(4-) + NADP(3-) <=> trans-2-icosenoyl-CoA(4-) + NADPH(4-) + H+
Catalysis of the reaction: behenoyl-CoA + NADP <=> trans-2-docosenoyl-CoA + NADPH + H+
Catalysis of the reaction: tetracosanoyl-CoA + NADP <=> trans-2-tetracosenoyl-CoA + NADPH + H+
Catalysis of the reaction: hexacosanoyl-CoA(4-) + NADP(3-) <=> trans-2-hexacosenoyl-CoA + NADPH + H+
Catalysis of the reaction: gamma-aminobutyric acid  + 2-oxo monocarboxylic acid anion = 4-oxobutanoate + glycine
Catalysis of the reaction: ATP + a 1,2-diacyl-sn-glycerol 3-phosphate = ADP + a 1,2-diacyl-sn-glycerol 3-diphosphate
Catalysis of the reaction: 5alpha,9alpha,10beta-labda-8(20),13-dien-15-yl diphosphate <=> miltiradiene + diphosphoric acid
Catalysis of the reaction: 11-cis-retinol + NADP = 11-cis-retinal + NADPH + H+
Catalysis of the reaction: 2-oxo-3-(5-oxofuran-2-ylidene)propanoate + H2O <=> 3-maleylpyruvate + H+
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate(3-) <=> diphosphoric acid + (+)-isoitalicene
Catalysis of the reaction: mithramycin + NADP <=> mithramycin DK + NADPH + H+
Catalysis of the reaction: S-adenosyl-L-methionine  + 7,8-dihydroxycoumarin <=> S-adenosyl-L-homocysteine  + 7-hydroxy-8-methoxycoumarin + H+
Catalysis of the reaction: UDP-alpha-D-glucose + 7,8-dihydroxycoumarin <=> UDP + 4-O- beta -D-glucosyl-daphnetin + H+
Catalysis of the reaction: UDP-alpha-D-glucose(2-) + 7,8-dihydroxycoumarin <=> UDP(3-) + 3-O-beta-D-glucosyl-daphnetin + H+
Catalysis of the reaction: esculetin + UDP-alpha-D-glucose <=> 4-O-beta-D-glucosyl-esculetin + UDP + H+
Catalysis of the reaction: esculetin + UDP-alpha-D-glucose <=> 3-O-beta-D-glucosyl-esculetin + UDP + H+
Catalysis of the reaction: isoscopoletin + S-adenosyl-L-methionine  <=> scoparone + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: taxusin + NADPH + O2 + H+ = 2-alpha-hydroxytaxusin + NADP + H2O
Catalysis of the reaction: 7-beta-hydroxytaxusin + NADPH + O2 + H+ = 2alpha, 7-beta-dihydroxytaxusin + NADP + H2O
Catalysis of the reaction: 2alpha-hydroxytaxusin + NADPH + O2 + H+ <=> 2alpha, 7beta-dihydroxytaxusin + NADP + H2O
Catalysis of the reaction: beta-amyrin + NADPH + H+ + O2 <=> 30-hydroxy-beta-amyrin + NADP + H2O
Catalysis of the reaction: 11alpha,30-dihydroxy-beta-amyrin + NADPH + O2 + H+ <=> 30-hydroxy-11-oxo-beta-amyrin + NADP + 2 H2O
Catalysis of the reaction: lupeol + NADPH(4-) + O2 + H+ <=> betulin + NADP(3-) + H2O
Catalysis of the reaction: betulin + NADPH(4-) + H+ + O2 <=> betulinic aldehyde + NADP(3-) + 2 H2O
Catalysis of the reaction: alpha-amyrin + NADPH(4-) + O2 + H+ <=> uvaol + NADP(3-) + H2O
Catalysis of the reaction: uvaol + NADPH + O2 + H+ <=> ursolic aldehyde + NADP + 2 H2O
Catalysis of the reaction: ursolic aldehyde + NADPH + O2 + H+ <=> ursolic acid + NADP + H2O
Catalysis of the reaction: 11-oxo-beta-amyrin + 3 NADPH + 3 O2 + 2 H+ <=> glycyrrhetinic acid + 3 NADP + 4 H2O
Catalysis of the reaction: lupeol + 3 NADPH + 3 O2 + 3 H+ <=> betulinic acid + 3 NADP + 4 H2O
Catalysis of the reaction: steviol + UDP-alpha-D-glucose = steviolmonoside + UDP + H+
Catalysis of the reaction: steviolmonoside + UDP-alpha-D-glucose = rubusoside + UDP + H+
Catalysis of the reaction: steviolbioside + UDP-alpha-D-glucose = stevioside + UDP + H+
Catalysis of the reaction: steviolbioside + UDP-alpha-D-glucose = rebaudioside B + UDP + H+
Catalysis of the reaction: stevioside + UDP-alpha-D-glucose = rebaudioside A + UDP + H+
Catalysis of the reaction: rebaudioside B + UDP-alpha-D-glucose <=> rebaudioside A + UDP + H+
Catalysis of the reaction: steviol + UDP-alpha-D-glucose <=> 19-O-beta-glucopyranosyl-steviol + UDP + H+
Catalysis of the reaction: 19-O-beta-glucopyranosyl-steviol + UDP-alpha-D-glucose <=> rubusoside + UDP + H+
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate(3-) <=> seychellene + diphosphoric acid
Catalysis of the reaction: 2-phenylethanol + NADP = phenylacetaldehyde + NADPH + H+
Catalysis of the reaction: 2-phenylethanol + acetyl-CoA = phenethyl acetate + coenzyme A
Catalysis of the reaction: UDP-N,N'-diacetylbacillosamine + H2O <=> 2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + UDP + H+
Catalysis of the reaction: NADP + a ditrans,polycis-dolichol = NADPH + H+ + a di-trans, poly-cis-polyprenol
Catalysis of the reaction: mycophenolic acid O-acyl-glucuronide(1-) + H2O <=> mycophenolate + H+ + D-glucopyranuronate
Catalysis of the reaction: decanoate + ATP(4-) + coenzyme A(4-) <=> decanoyl-CoA(4-) + AMP(2-) + diphosphoric acid
Catalysis of the reaction: decanoate + ATP(4-) + an HmqF protein <=> AMP(2-) + diphosphoric acid + a decanoyl-HmqF protein
Catalysis of the reaction: FAD + H+ + a decanoyl-HmqF protein <=> FADH2(2-) + a 2,3-dehydro-decanoyl-HmqF
Catalysis of the reaction: (2S,3R,4S)-4-hydroxy-L-isoleucine + NAD <=> (2S,3R)-2-amino-3-methyl-4-ketopentanoate + NADH + H+
Catalysis of the reaction: 9-cis-beta-carotene + O2 <=> 9-cis-10'-apo-beta-carotenal + beta-ionone
Catalysis of the reaction: 9-cis-10'-apo-beta-carotenal + 2 O2 <=> carlactone + (2E,4E,6E)-7-hydroxy-4-methylhepta-2,4,6-trienal
Catalysis of the reaction: S-adenosyl-L-methionine  + dTDP-3-amino-4-dehydro-2,3,6-trideoxy-alpha-D-glucose <=> S-adenosyl-L-homocysteine  + dTDP-3-N-methylamino-4-oxo-2,3,6-trideoxy-alpha-D-glucose + H+
Catalysis of the reaction: S-adenosyl-L-methionine  + dTDP-3-N-methylamino-4-oxo-2,3,6-trideoxy-alpha-D-glucose <=> S-adenosyl-L-homocysteine  + dTDP-3-N,N-dimethylamino-4-oxo-2,3,6-trideoxy-alpha-D-glucose + H+
Catalysis of the reaction: 2 S-adenosyl-L-methionine  + dTDP-3-amino-4-dehydro-2,3,6-trideoxy-alpha-D-glucose <=> 2 S-adenosyl-L-homocysteine  + dTDP-3-N,N-dimethylamino-4-oxo-2,3,6-trideoxy-alpha-D-glucose + 2 H+
Catalysis of the reaction: 2-phenylethyl 6-O-beta-D-xylopyranosyl-beta-D-glucopyranoside + H2O = 2-phenylethanol + 6-O-(beta-D-xylopyranosyl)-beta-D-glucopyranose
Catalysis of the reaction: linalyl 6-O-alpha-L-arabinopyranosyl- beta-D-glucopyranoside + H2O <=> vicianose + linalool
Catalysis of the reaction: (+)-taxifolin(1-) + O2 + NADPH(4-) + H+ <=> (+)-dihydromyricetin + NADP(3-) + H2O
Catalysis of the reaction: sinapoyl-CoA + 16-hydroxypalmitate <=> coenzyme A + 16-sinapoyloxypalmitate
Catalysis of the reaction: C22:0-DCA-CoA + sn-glycerol 3-phosphate <=> coenzyme A + 2-C22:0-DCA-LPA
Catalysis of the reaction: hexadecanedioyl-CoA + sn-glycerol 3-phosphate <=> coenzyme A + sn-2-C16:0-DCA-LPA
Catalysis of the reaction: behenoyl-CoA + sn-glycerol 3-phosphate(2-) <=> coenzyme A + 2-docosanoyl-glycerol 3-phosphate
Catalysis of the reaction: quercetin 4'-O-glucoside + UDP-alpha-D-glucose(2-) <=> quercetin 3,4'-O-diglucoside + UDP(3-)
Catalysis of the reaction: quercetin-3-glucoside + UDP-alpha-D-glucose(2-) <=> quercetin 3,4'-O-diglucoside + UDP(3-)
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate(3-) <=> valerena-4,7(11)-diene + diphosphoric acid
Catalysis of the reaction: 6-O-methyl-N-deacetylisoipecoside + H2O <=> 6-O-methyl-N-deacetylisoipecoside aglycon + beta-D-glucose
Catalysis of the reaction: quercetin-3-glucoside + UDP-alpha-D-glucose(2-) <=> quercetin-3-gentiobioside + UDP
Catalysis of the reaction: quercetin-3-gentiobioside + UDP-alpha-D-glucose <=> quercetin-3-gentiotrioside + UDP + H+
Catalysis of the reaction: quercetin-3-gentiotrioside + UDP-alpha-D-glucose <=> quercetin-3-gentiotetraside + UDP + H+
Catalysis of the reaction: apigenin 7-O-beta-D-glucoside + UDP-alpha-D-glucose <=> apigenin-7-O-gentiobioside + UDP + H+
Catalysis of the reaction: luteolin 7-O-beta-D-glucoside + UDP-alpha-D-glucose = luteolin-7-O-gentiobioside + UDP + H+
Catalysis of the reaction: omega-hydroxy-C22:0-CoA + sn-glycerol 3-phosphate = coenzyme A + 2-omega-hydroxy-C22:0-LPA
Catalysis of the reaction: hexadecanedioyl-CoA + sn-glycerol 3-phosphate = coenzyme A + 1-C16:0-alpha,omega-dicarboxyl-2-lysophosphatidate
Catalysis of the reaction: curcumin 4'-O-beta-D-gentiobioside + UDP-alpha-D-glucose <=> curcumin 4'-O-beta-D-gentiotrioside + UDP + H+
Catalysis of the reaction: curcumin 4'-O-beta-D-gentiotrioside + UDP-alpha-D-glucose <=> curcumin 4'-O-beta-D-gentiotetraside + UDP + H+
Catalysis of the reaction: (+)-sesaminol + UDP-alpha-D-glucose <=> (+)-sesaminol 2-O-beta-D-glucoside + UDP + H+
Catalysis of the reaction: (+)-sesaminol 2-O-beta-D-gentiobioside + UDP-alpha-D-glucose <=> (+)-sesaminol 2-O-beta-D-gentiotrioside + UDP + H+
Catalysis of the reaction: myricetin + UDP-alpha-D-glucose <=> myricetin 3-O-beta-D-glucopyranoside + UDP
Catalysis of the reaction: myricetin 3-O-beta-D-glucopyranoside + UDP-alpha-D-glucose <=> myricetin 3-O-gentiobioside + UDP + H+
Catalysis of the reaction: allocryptopine + NADPH + O2 + H+ <=> 6-hydroxy-allocryptopine + NADP + H2O
Catalysis of the reaction: kaempferol 3-O-glucoside + UDP-alpha-D-glucose <=> kaempferol-3-gentiobioside + UDP
Catalysis of the reaction: genistin + UDP-alpha-D-glucose <=> genistin 7-gentiobioside + UDP + H+
Catalysis of the reaction: alpha-linolenate + O2 + a reduced electron acceptor = coniferonate + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: linoleate + O2 + a reduced electron acceptor = pinolenate + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: quercetin-7-olate + S-adenosyl-L-methionine  <=> rhamnetin + S-adenosyl-L-homocysteine
Catalysis of the reaction: L-phenylalanine  + O2 + an N10-formyl-tetrahydrofolate <=> L-tyrosine  + a 10-formyltetrahydrofolate-4a-carbinolamine
Catalysis of the reaction: a 10-formyltetrahydrofolate-4a-carbinolamine = H2O + a 10-formyldihydrofolate
Catalysis of the reaction: myricetin(1-) + S-adenosyl-L-methionine  <=> 7-O-methylmyricetin + S-adenosyl-L-homocysteine
Catalysis of the reaction: 7-O-methylmyricetin + S-adenosyl-L-methionine  <=> 7,4'-dimethylmyricetin + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: myricetin(1-) + S-adenosyl-L-methionine  <=> 3-O-methylmyricetin + S-adenosyl-L-homocysteine
Catalysis of the reaction: laricitrin(1-) + S-adenosyl-L-methionine  <=> H+ + 3',4'-dimethylmyricetin + S-adenosyl-L-homocysteine
Catalysis of the reaction: 3',4',5'-trimethylmyricetin + S-adenosyl-L-methionine  <=> 7,3',4',5'-tetramethylmyricetin + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: 3',4',5'-trimethylmyricetin + S-adenosyl-L-methionine  <=> 3,3',4',5'-tetramethylmyricetin + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: syringetin(1-) + S-adenosyl-L-methionine  <=> 7,3',5'-trimethylmyricetin + S-adenosyl-L-homocysteine
Catalysis of the reaction: syringetin(1-) + S-adenosyl-L-methionine  <=> 3,3',5'-trimethylmyricetin + S-adenosyl-L-homocysteine
Catalysis of the reaction: NAD(1-) + a (2S)-2-hydroxycarboxylate <=> NADH(2-) + H+ + a 2-oxo carboxylate
Catalysis of the reaction: isorhamnetin + S-adenosyl-L-methionine  <=> 3,3'-dimethylquercetin + S-adenosyl-L-homocysteine
Catalysis of the reaction: 3',4',5-trihydroxy-3-methoxyflavon-7-olate + S-adenosyl-L-methionine  <=> 3,3'-dimethylquercetin + S-adenosyl-L-homocysteine
Catalysis of the reaction: rhamnetin + S-adenosyl-L-methionine  <=> 3',4',5-trihydroxy-3,7-dimethoxyflavone + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: rhamnetin + S-adenosyl-L-methionine  <=> 7,3'-dimethylquercetin + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: rhamnetin + S-adenosyl-L-methionine  <=> ombuin + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: kaempferol oxoanion + S-adenosyl-L-methionine  <=> 3-O-methylkaempferol + S-adenosyl-L-homocysteine
Catalysis of the reaction: kaempferide + S-adenosyl-L-methionine  <=> 7,4'-dimethylkaempferol + S-adenosyl-L-homocysteine
Catalysis of the reaction: kaempferide + S-adenosyl-L-methionine  <=> 3,4'-dimethylkaempferol + S-adenosyl-L-homocysteine
Catalysis of the reaction: 2 4-coumaryl-CoA + malonyl-CoA + H2O + H+ <=> 3 coenzyme A + bisdemethoxycurcumin + 2 carbon dioxide
Catalysis of the reaction: 4-coumaryl-CoA + H+ + an anthocyanidin-3-O-beta-D-glucoside = coenzyme A + H+ + an anthocyanidin-3-O-[6-O-(hydroxycinnamoyl)-beta-D-glucoside]
Catalysis of the reaction: cyanidin + UDP-D-galactose = cyanidin 3-O-beta-D-galactoside betaine + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + an anthocyanidin-3-O-beta-D-glucoside = UDP + H+ + an anthocyanidin 3-O-sophoroside
Catalysis of the reaction: cyanidin 3-O-beta-D-glucoside betaine + 1-O-sinapoyl-beta-D-glucose <=> cyanin betaine + trans-sinapate + H+
Catalysis of the reaction: cyanidin 3-O-beta-D-glucoside betaine + 1-O-vanilloyl-beta-D-glucose <=> H+ + cyanidin 3,7-di-O-beta-D-glucoside betaine + vanillate
Catalysis of the reaction: cyanidin 3-O-beta-D-glucoside betaine + 1-O-vanilloyl-beta-D-glucose <=> cyanin betaine + vanillate + H+
Catalysis of the reaction: 8-oxo-dADP + H2O = 8-oxo-dAMP + hydrogenphosphate + H+
Catalysis of the reaction: kaempferol-3-gentiobioside + UDP-L-rhamnose = H+ + kaempferol-3-O-gentiobioside-7-O-rhamnoside + UDP
Catalysis of the reaction: kaempferol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside + UDP-L-rhamnose <=> kaempferol 3-O-rhamnosyl(1->2)glucoside-7-O-rhamnoside + UDP
Catalysis of the reaction: quercetin 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside + UDP-L-rhamnose <=> quercetin 3-O-rhamnosyl(1->2)glucoside-7-O-rhamnoside + UDP + H+
Catalysis of the reaction: quercetin-3-gentiobioside + UDP-L-rhamnose <=> quercetin 3-O-gentiobioside-7-O-rhamnoside + UDP + H+
Catalysis of the reaction: zeaxanthin + O2 + NADH + H+ <=> caloxanthin + H2O + NAD
Catalysis of the reaction: zeaxanthin + 2 NADH + 2 H+ + 2 O2 <=> nostoxanthin + 2 NAD + 2 H2O
Catalysis of the reaction: beta-carotene + 2 NADH + 2 H+ + 2 O2 = (2R,2'R)-dihydroxy-all-trans-beta-carotene + 2 NAD + 2 H2O
Catalysis of the reaction: UDP-alpha-D-glucuronate + scutellarein <=> UDP( + scutellarin + H+
Catalysis of the reaction: UDP-alpha-D-glucuronate + wogonin <=> UDP + wogonin 7-O-beta-D-glucuronate + H+
Catalysis of the reaction: (S)-naringenin + NADPH + O2 <=> 2-hydroxynaringenin + NADP + H2O
Catalysis of the reaction: 2,4,4',6-tetrahydroxydibenzoylmethane + UDP-alpha-D-glucose <=> 6C-glucosyl-2-hydroxynaringenin + UDP + H+
Catalysis of the reaction: 6C-glucosyl-2-hydroxynaringenin <=> isovitexin-7-olate + H2O
Catalysis of the reaction: eriodictyol + NADPH + O2 + 2 H+ <=> 2-hydroxyeriodictyol + NADP + H2O
Catalysis of the reaction: eriodictyol dibenzoylmethane tautomer + UDP-alpha-D-glucose <=> 8C-beta-D-glucosyl-2-hydroxyeriodictyol + UDP(3-) + H+
Catalysis of the reaction: eriodictyol dibenzoylmethane tautomer + UDP-alpha-D-glucose <=> 6C-beta-D-glucosyl-2-hydroxyeriodictyol + UDP + H+
Catalysis of the reaction: 6C-beta-D-glucosyl-2-hydroxyeriodictyol <=> isoorientin + H2O
Catalysis of the reaction: pinocembrin + NADPH + O2 + H+ <=> 2,5,7-trihydroxyflavanone + NADP + H2O
Catalysis of the reaction: 6C-glucosyl-2,5,7-trihydroxyflavanone <=> H+ + 6C-hexosyl chrysin + H2O
Catalysis of the reaction: beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O = 2 beta-L-arabinofuranose
Catalysis of the reaction: quercetin-7-olate + UDP-D-galactose <=> quercetin 3-O-beta-D-galactopyranoside + UDP(3-) + H+
Catalysis of the reaction: H+ + flucytosine + H2O <=> 5-fluorouracil + ammonium
Catalysis of the reaction: 3D-3,5/4-trihydroxycyclohexane-1,2-dione + H2O <=> 5-deoxy-D-glucuronate + H+
Catalysis of the reaction: 5-deoxy-D-glucuronate = 5-dehydro-2-deoxy-D-gluconate
Catalysis of the reaction: H2O + scopolin <=> beta-D-glucose + scopoletin
Catalysis of the reaction: esculetin + UDP-alpha-D-glucose(2-) <=> esculin + UDP(3-) + H+
Catalysis of the reaction: dATP + 2 H2O = dAMP + 2 hydrogenphosphate + 2 H+
Catalysis of the reaction: dCTP + 2 H2O = dCMP + 2 hydrogenphosphate + 2 H+
Catalysis of the reaction: dUTP + 2 H2O = dUMP + 2 hydrogenphosphate + 2 H+
Catalysis of the reaction: dTTP + 2 H2O = dTMP + 2 hydrogenphosphate + 2 H+
Catalysis of the reaction: GTP + 2 H2O = GMP + 2 hydrogenphosphate + 2 H+
Catalysis of the reaction: 8-oxo-dGTP + 2 H2O <=> 8-oxo-dGMP + 2 hydrogenphosphate + 2 H+
Catalysis of the reaction: dGTP + 2 H2O = dGMP + 2 hydrogenphosphate + 2 H+
Catalysis of the reaction: wogonin + UDP-alpha-D-glucose <=> wogonin 7-O-beta-D-glucoside + UDP + H+
Catalysis of the reaction: gibberellin A20 + O2 + a reduced electron acceptor <=> gibberellin A5 + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: gibberellin A5 + O2 + 2-oxoglutarate <=> gibberellin A3 + succinate + carbon dioxide
Catalysis of the reaction: gibberellin A5 + O2 + 2-oxoglutarate <=> gibberellin A6 + succinate + carbon dioxide
Catalysis of the reaction: scyllo-inositol + NADP <=> 2,4,6/3,5-pentahydroxycyclohexanone + NADPH + H+
Catalysis of the reaction: H2O + maltose = 2 glucose
Catalysis of the reaction: hydrogenphosphate + a plant soluble heteroglycan = alpha-D-glucose 1-phosphate + a plant soluble heteroglycan
Catalysis of the reaction: beta-D-glucose + a plant soluble heteroglycan = a plant soluble heteroglycan + maltose
Catalysis of the reaction: D-mannonate + NADP = NADPH + H+ + D-fructuronate
Catalysis of the reaction: ADP alpha-D-glucoside + n a 1,4-alpha-D-glucan = ADP + n alpha-amylose
Catalysis of the reaction: luteolinidin + UDP-alpha-D-glucose <=> luteolinidin 5-O-glucoside + UDP + 2 H+
Catalysis of the reaction: apigeninidin + UDP-alpha-D-glucose <=> apigeninidin 5-O-glucoside + UDP + H+
Catalysis of the reaction: cyanidin 3-O-beta-D-glucoside betaine + 1-O-feruloyl-beta-D-glucose = cyanin betaine + ferulate + H+
Catalysis of the reaction: cyanidin 3-O-beta-D-glucoside betaine + 1-O-4-hydroxybenzoyl-beta-D-glucose <=> cyanidin 3,7-di-O-beta-D-glucoside betaine + 4-hydroxybenzoic acid + H+
Catalysis of the reaction: cyanidin 3,7-di-O-beta-D-glucoside betaine + H2O <=> cyanidin 3-O-beta-D-glucoside betaine + beta-D-glucose
Catalysis of the reaction: cyanin betaine + H2O <=> cyanidin 3-O-beta-D-glucoside betaine + beta-D-glucose
Catalysis of the reaction: pelargonidin 3-O-beta-D-glucoside + 1-O-vanilloyl-beta-D-glucose <=> anthocyanidin 3,5-di-O-beta-D-glucoside + vanillate + H+
Catalysis of the reaction: pelargonidin 3-O-beta-D-glucoside + 1-O-vanilloyl-beta-D-glucose <=> pelargonidin 3,7-di-O-beta-D-glucoside + vanillate + H+
Catalysis of the reaction: delphinidin 3-O-beta-D-glucoside + 1-O-vanilloyl-beta-D-glucose <=> delphinidin 3-O-beta-D-glucoside-5-O-beta-D-glucoside betaine + vanillate + H+
Catalysis of the reaction: delphinidin 3-O-beta-D-glucoside + 1-O-vanilloyl-beta-D-glucose <=> delphinidin 3,7-di O-beta-D-glucoside + vanillate + H+
Catalysis of the reaction: cyanidin 3-O-beta-D-glucoside betaine + 1-O-feruloyl-beta-D-glucose <=> cyanidin 3,7-di-O-beta-D-glucoside betaine + ferulate + H+
Catalysis of the reaction: pelargonidin 3-O-beta-D-glucoside + 1-O-feruloyl-beta-D-glucose <=> pelargonidin 3,7-di-O-beta-D-glucoside + ferulate + H+
Catalysis of the reaction: delphinidin 3-O-beta-D-glucoside + 1-O-feruloyl-beta-D-glucose <=> delphinidin 3,7-di O-beta-D-glucoside + ferulate + H+
Catalysis of the reaction: oleoyl-CoA + NADH + O2 + H+ = ricinoleyl-CoA + NAD + H2O
Catalysis of the reaction: (11Z)-eicosenoyl-CoA + NADH + O2 + H+ = lesqueroloyl-CoA + NAD + H2O
Catalysis of the reaction: O-phospho-L-threonine + H2O = L-threonine  + hydrogenphosphate
Catalysis of the reaction: pyruvate + S-adenosyl-L-methionine  + N1-methylguanine37 in tRNAPhe = L-methionine  + 5'-deoxyadenosine + carbon dioxide + H2O + 4-demethylwyosine37 in tRNAPhe
Catalysis of the reaction: S-adenosyl-L-methionine  + 4-demethylwyosine37 in tRNAPhe <=> 5'-S-methyl-5'-thioadenosine + H+ + 7-[(3S)-3-amino-3-carboxypropyl]-4-demethylwyosine37 in tRNAPhe
Catalysis of the reaction: (S)-2-chloropropanoate + NADP <=> 2-chloroacrylate + NADPH + H+
Catalysis of the reaction: 2-oxoglutarate + O2 + 7-[(3S)-(3-amino-3-carboxypropyl)]-wyosine37 in tRNAPhe = succinate + carbon dioxide + 7-(2-hydroxy-3-amino-3-carboxypropyl)-wyosine37 in tRNAPhe
Catalysis of the reaction: L-argininium(1+) + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-arginine(1+) + succinate + carbon dioxide
Catalysis of the reaction: S-adenosyl-L-methionine  + 8-desmethylnovobiocic acid <=> S-adenosyl-L-homocysteine  + novobiocic acid + H+
Catalysis of the reaction: 3-amino-4,7-dihydroxycoumarin + 3-dimethylallyl-4-hydroxybenzoate + ATP(4-) <=> H+ + 8-desmethylnovobiocic acid(1-) + AMP(2-) + diphosphoric acid
Catalysis of the reaction: S-adenosyl-L-methionine  + 7,8,4'-trihydroxyflavone <=> H+ + S-adenosyl-L-homocysteine  + 7,4'-dihydroxy, 8-methoxyflavone
Catalysis of the reaction: S-adenosyl-L-methionine  + apigenin-7-olate <=> S-adenosyl-L-homocysteine  + genkwanin
Catalysis of the reaction: aclacinomycin T(1+) + H2O <=> 15-demethylaclacinomycin T  + methanol + H+
Catalysis of the reaction: H2O + an ecdysteroid 22-phosphate <=> hydrogenphosphate + an ecdysteroid
Catalysis of the reaction: genkwanin + O2 + NADPH + H+ <=> scutellarein 7-methyl ether + H2O + NADP
Catalysis of the reaction: genkwanin + S-adenosyl-L-methionine  <=> H+ + apigenin-7,4'-dimethyl ether + S-adenosyl-L-homocysteine
Catalysis of the reaction: apigenin-7,4'-dimethyl ether + O2 + NADPH + H+ <=> ladanein + H2O + NADP
Catalysis of the reaction: ladanein + S-adenosyl-L-methionine  <=> H+ + salvigenin + S-adenosyl-L-homocysteine
Catalysis of the reaction: sakuranetin + O2 + NADPH + H+ <=> carthamidin-7-methyl ether + H2O + NADP
Catalysis of the reaction: ecdysone 22-phosphate + H2O <=> ecdysone + hydrogenphosphate
Catalysis of the reaction: UDP-N-acetyl-alpha-D-quinovosamine + NAD(P) = UDP-2-acetamido-4-dehydro-2,6-dideoxy-beta-D-glucose + H+ + NAD(P)H
Catalysis of the reaction: UDP-N-acetyl-alpha-D-fucosamine + NAD(P) = UDP-2-acetamido-4-dehydro-2,6-dideoxy-beta-D-glucose + H+ + NAD(P)H
Catalysis of the reaction: alpha-D-mannose 6-phosphate = beta-D-mannose 6-phosphate
Catalysis of the reaction: alpha-D-galactose 6-phosphate = beta-D-galactose 6-phosphate
Catalysis of the reaction: aclacinomycin A + H2O <=> 15-demethoxy-aclacinomycin A + methanol + H+
Catalysis of the reaction: epsilon-rhodomycinone + H2O <=> 15-demethoxy-epsilon-rhodomycinone + methanol + H+
Catalysis of the reaction: L-ornithinium(1+) + 2-oxoglutarate + NADPH + H+ <=> ornaline + NADP + H2O
Catalysis of the reaction: 2 H2O + a phosphatidylcholine = sn-glycero-3-phosphocholine + 2 H+ + 2 a carboxylate
Catalysis of the reaction: H2O + 2-(alpha-D-mannosyl)-D-glycerate <=> alpha-D-mannose + D-glycerate
Catalysis of the reaction: H2O + 2-O-(alpha-D-glucopyranosyl)-D-glycerate <=> alpha-D-glucose + D-glycerate
Catalysis of the reaction: 1-18:1-2-16:0-monogalactosyldiacylglycerol + H2O <=> sn-1-lyso-2-16:0-monogalactosyldiacylglycerol + oleate + H+
Catalysis of the reaction: S-adenosyl-L-methionine  + 2-methyl-6-geranylgeranyl-1,4-benzoquinol <=> S-adenosyl-L-homocysteine  + 2,3-dimethyl-6-geranylgeranyl-1,4-benzoquinol + H+
Catalysis of the reaction: 2-trans,6-trans,10-trans-geranylgeranyl diphosphate + homogentisate + H+ <=> diphosphoric acid + 2-methyl-6-geranylgeranyl-1,4-benzoquinol + carbon dioxide
Catalysis of the reaction: 2 S-adenosyl-L-methionine  + a [glycine-cleavage complex H protein] N6-octanoyl-L-lysine + 2 a sulfurated [sulfur carrier] = 2 L-methionine  + 2 5'-deoxyadenosine + a [glycine-cleavage complex H protein] N6-lipoyl-L-lysine + 2 an unsulfurated [sulfur carrier]
Catalysis of the reaction: 2 S-adenosyl-L-methionine  + a [pyruvate dehydrogenase E2 protein] N6-octanoyl-L-lysine + 2 a sulfurated [sulfur carrier] = 2 L-methionine  + 2 5'-deoxyadenosine + 2 H+ + a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + 2 an unsulfurated [sulfur carrier]
Catalysis of the reaction: 2 S-adenosyl-L-methionine  + a [2-oxoglutarate-dehydrogenase E2 protein] N6-octanoyl-L-lysine + 2 a sulfurated [sulfur carrier] = 2 L-methionine  + 2 5'-deoxyadenosine + 2 H+ + a [2-oxoglutarate dehydrogenase E2 protein] N6-lipoyl-L-lysine + 2 an unsulfurated [sulfur carrier]
Catalysis of the reaction: [glycine cleavage system lipoyl-carrier protein]-L-lysine + OCTANOYL-ACP = H+ + a [glycine-cleavage complex H protein] N6-octanoyl-L-lysine + a holo-[acyl-carrier protein]
Catalysis of the reaction: dammarenediol-II + NADPH + H+ + O2 <=> (20S)-protopanaxadiol + NADP + H2O
Catalysis of the reaction: (20S)-protopanaxadiol + O2 + NADPH(4-) + H+ <=> protopanaxatriol + NADP + H2O
Catalysis of the reaction: S-adenosyl-L-methionine  + a [release factor]-L-glutamine = S-adenosyl-L-homocysteine  + H+ + a [release factor]-N5-methyl-L-glutamine
Catalysis of the reaction: 5-phosphonato-alpha-D-ribose cyclic-1,2-phosphate + H2O <=> D-ribofuranose 2,5-bisphosphate + H+
Catalysis of the reaction: H2O + D-ribofuranose 2,5-bisphosphate <=> hydrogenphosphate + D-ribofuranose 5-phosphate
Catalysis of the reaction: UDP-beta-L-arabinofuranose + a [protein]-trans-4-hydroxy-L-proline = UDP + H+ + a protein-O-(beta-L-arabinofuranose)-trans-4-hydroxy-L-proline
Catalysis of the reaction: aurachin C + O2 + H+ + NAD(P)H <=> aurachin C epoxide + H2O + NAD(P)
Catalysis of the reaction: aurachin C epoxide + H+ + NAD(P)H <=> aurachin B + H2O + NAD(P)
Catalysis of the reaction: 1-oleoylglycerone 3-phosphate + NADPH + H+ = 1-oleoyl-sn-glycero-3-phosphate + NADP
Catalysis of the reaction: 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H+
Catalysis of the reaction: 1-18:1-2-18:1-phosphatidylethanolamine + H2O = 1-oleoyl-sn-glycero-3-phosphoethanolamine  + oleate + H+
Catalysis of the reaction: FR-900098 + 2-oxoglutarate(2-) + O2 <=> FR-33289 + succinate(2-) + carbon dioxide
Catalysis of the reaction: keto-phenylpyruvate + L-tyrosine  = L-phenylalanine  + 3-(4-hydroxyphenyl)pyruvate
Catalysis of the reaction: H2O + an N-acetyl-alpha-D-glucosaminyl-[glycoprotein] <=> N-acetyl-alpha-D-glucosaminide + a [glycoprotein]-(L-serine/L-threonine)
Catalysis of the reaction: N5-phenyl-L-glutamine + H2O = L-glutamate + aniline + H+
Catalysis of the reaction: 3-[(1-carboxylatovinyl)oxy]benzoate(2-) + S-adenosyl-L-methionine  + H2O <=> aminodeoxyfutalosinate + L-methionine  + hydrogencarbonate + H+
Catalysis of the reaction: H2O + a 3-oxo-myristoyl-[acp] = 3-oxo-myristate + H+ + a holo-[acyl-carrier protein]
Catalysis of the reaction: H2O + a 3-oxo-dodecanoyl-[acp] = 3-oxododecanoate + H+ + a holo-[acyl-carrier protein]
Catalysis of the reaction: H2O + a 3-oxo-palmitoyl-[acp] = 3-oxopalmitic acid + H+ + a holo-[acyl-carrier protein]
Catalysis of the reaction: 3-oxopalmitic acid + H+ = 2-pentadecanone + carbon dioxide
Catalysis of the reaction: cyanidin 3-O-beta-D-glucoside betaine + UDP-alpha-D-xylose <=> cyanidin 3-O-beta-D-sambubioside + UDP
Catalysis of the reaction: cyanidin 3-O-beta-D-glucoside betaine + 4-coumaryl-CoA + H+ <=> cyanidin 3-O-(6-O-(E)-4-coumaroyl-beta-D-glucoside) + coenzyme A
Catalysis of the reaction: cyanidin 3-O-(6-O-(E)-4-coumaroyl-beta-D-glucoside) + UDP-alpha-D-xylose <=> cyanidin 3-O-[2''-O-xylosyl) 6''-O-(p-coumaroyl) glucoside + UDP + H+.
Catalysis of the reaction: cyanidin 3-O-beta-D-sambubioside + 4-coumaryl-CoA <=> cyanidin 3-O-[2''-O-xylosyl) 6''-O-(p-coumaroyl) glucoside + coenzyme A.
Catalysis of the reaction: cyanidin 3-O-[2''-O-xylosyl) 6''-O-(p-coumaroyl) glucoside + UDP-alpha-D-glucose <=> cyanidin 3-O-[2''-O-(xylosyl)-6''-O-(p-coumaroyl) glucoside] 5-O-glucoside + UDP + H+
Catalysis of the reaction: cyanidin 3-O-[2''-O-(xylosyl)-6''-O-(p-coumaroyl) glucoside] 5-O-glucoside + malonyl-CoA + H+ <=> cyanidin 3-O-[2''-O-(xylosyl)-6''-O-(p-coumaroyl) glucoside] 5-O-malonylglucoside + coenzyme A.
Catalysis of the reaction: cyanidin 3-O-[2''-O-(xylosyl)-6''-O-(p-coumaroyl) glucoside] 5-O-malonylglucoside + 1-O-sinapoyl-beta-D-glucose <=> cyanidin 3-O-[2''-O-(2''-O-(sinapoyl) xylosyl) 6'-O-(p-coumaroyl) glucoside] 5-O-[6''-O-(malonyl) glucoside + beta-D-glucose.
Catalysis of the reaction: cyanidin 3-O-[2''-O-(2'''-O-(sinapoyl) xylosyl) 6''-O-(p-coumaroyl) glucoside] 5-O-[6''-O-(malonyl) glucoside + 1-O-sinapoyl-beta-D-glucose <=> cyanidin 3-O-[6-O-(4-O-beta-D-glucosyl-p-coumaroyl)-2-O-(2-O-sinapoyl-beta-D-xylosyl)-beta-D-glucosyl]-5-O-(6-O-malonyl-beta-D-glucoside) + trans-sinapate + H+.
Catalysis of the reaction: cyanidin 3-O-beta-D-glucoside betaine + malonyl-CoA <=> cyanidin 3-O-(6-O-malonyl-beta-D-glucoside) + coenzyme A.
Catalysis of the reaction: cyanidin 3-O-(6-O-malonyl-beta-D-glucoside) + malonyl-CoA(5-) <=> cyanidin 3-O-(3''', 6''-O-dimalonyl-beta-glucopyranoside) + coenzyme A
Catalysis of the reaction: delphinidin 3-O-rutinoside + 1-O-4-hydroxybenzoyl-beta-D-glucose <=> delphinidin 3-O-rutinoside-7-O-glucoside + 4-hydroxybenzoic acid + H+
Catalysis of the reaction: delphinidin 3-O-rutinoside-7-O-glucoside + 1-O-4-hydroxybenzoyl-beta-D-glucose <=> delphinidin 3-O-rutinoside-7-O-(6-O-(p-hydroxybenzoyl)-glucoside) + beta-D-glucose
Catalysis of the reaction: delphinidin 3-O-rutinoside-7-O-(6-O-(4-O-(glucosyl)-oxybenzoyl)-glucoside) + 1-O-4-hydroxybenzoyl-beta-D-glucose <=> violdelphin + beta-D-glucose
Catalysis of the reaction: N-methylanthranilate + UDP-alpha-D-glucose = N-methylanthraniloyl-beta-D-glucopyranose + UDP
Catalysis of the reaction: cyanidin 3,7-di-O-beta-D-glucoside betaine + 1-O-4-hydroxybenzoyl-beta-D-glucose <=> cyanidin 3-O-glucoside-7-O-(6-O-(p-hydroxybenzoyl)-glucoside) + beta-D-glucose
Catalysis of the reaction: cyanidin 3-O-glucoside-7-O-(6-O-(4-O-(glucosyl)-oxybenzoyl)-glucoside) + 1-O-4-hydroxybenzoyl-beta-D-glucose <=> cyanidin 3-O-glucoside-7-O-(6-O-(4-O-(6-O-(p-hydroxybenzoyl)-glucosyl)-oxybenzoyl)-glucoside) + beta-D-glucose
Catalysis of the reaction: ent-sandaracopimara-8(14),15-diene + NADPH + H+ + O2 <=> ent-sandaracopimaradien-3beta-ol + NADP + H2O
Catalysis of the reaction: ent-sandaracopimaradien-3-beta-ol + NADPH + H+ + O2 <=> oryzalexin E + NADP + H2O
Catalysis of the reaction: ent-sandaracopimaradien-3-beta-ol + NADPH + H+ + O2 <=> oryzalexin D + NADP + H2O
Catalysis of the reaction: beta-amyrin + O2 + H+ + NAD(P)H <=> 12,13beta-epoxy-beta-amyrin + H2O + NAD(P)
Catalysis of the reaction: 12,13beta-epoxy-beta-amyrin + O2 + H+ + NAD(P)H <=> 12,13beta-epoxy-16beta-hydroxy-beta-amyrin + H2O + NAD(P)
Catalysis of the reaction: beta-amyrin + O2 + H+ + NAD(P)H <=> 16beta-hydroxy-beta-amyrin + H2O + NAD(P)
Catalysis of the reaction: 16beta-hydroxy-beta-amyrin + O2 + H+ + NAD(P)H <=> 12,13beta-epoxy-16beta-hydroxy-beta-amyrin + H2O + NAD(P)
Catalysis of the reaction: 12-demethyl-elloramycin + S-adenosyl-L-methionine  <=> elloramycin + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: (S)-naringenin(1-) + O2 + NADPH + H+ <=> 2-hydroxy-2,3-dihydrogenistein-7-olate + NADP + H2O
Catalysis of the reaction: cyclooctat-9-en-5,7-diol + O2 + NADPH + H+ <=> cyclooctatin + H2O + NADP
Catalysis of the reaction: cyclooctat-9-en-7-ol + O2 + NADPH + H+ <=> cyclooctat-9-en-5,7-diol + H2O + NADP
Catalysis of the reaction: 3beta-hydroxy-12,15-cassadiene-11-one + NADPH + O2 + H+ <=> 2beta,3beta-dihydroxy-12,15-cassadiene-11-one + NADP + H2O
Catalysis of the reaction: tetracenomycin B3 + S-adenosyl-L-methionine  <=> tetracenomycin E + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: stemod-13(17)-ene + 3 NADPH + 3 O2 + 3 H+ <=> 9beta-stemod-13(17)-en-19-oate + 3 NADP + 4 H2O
Catalysis of the reaction: (+)-secoisolariciresinol + UDP-alpha-D-glucose <=> (+)-secoisolariciresinol monoglucoside + UDP + H+
Catalysis of the reaction: (+)-secoisolariciresinol monoglucoside + UDP-alpha-D-glucose <=> (+)-secoisolariciresinol diglucoside + UDP + H+
Catalysis of the reaction: 9beta-pimara-7,15-diene + NADPH + O2 + H+ <=> 6beta-hydroxy-syn-pimaradiene + NADP + H2O
Catalysis of the reaction: 1,3,7-trimethyluric acid + O2 + NADH + 3 H+ <=> 1,3,7-trimethyl-5-hydroxyisourate + NAD + H2O
Catalysis of the reaction: germacra-1(10),4,11(13)-trien-12-oate + NADPH + O2 + H+ <=> 8beta-hydroxy-germacra-1(10),4,11(13)-trien-12-oate + NADP + H2O
Catalysis of the reaction: ent-cassa-12,15-diene + NADPH + O2 + H+ <=> 2alpha-hydroxy-ent-cassadiene + NADP + H2O
Catalysis of the reaction: oryzalexin D + NAD(P) <=> oryzalexin A + H+ + NAD(P)H
Catalysis of the reaction: oryzalexin B + NAD(P) <=> oryzalexin C + H+ + NAD(P)H
Catalysis of the reaction: oryzalexin D + NAD(P) <=> oryzalexin B + H+ + NAD(P)H
Catalysis of the reaction: oryzalexin A + NAD(P) <=> oryzalexin C + H+ + NAD(P)H
Catalysis of the reaction: 3-geranylgeranylindole + O2 + NADPH + H+ = 10,11-epoxy-3-geranylgeranylindole + NADP + H2O
Catalysis of the reaction: emindole-SB + O2 + NADPH + H+ <=> 14,15-epoxyemindole-SB + NADP + H2O
Catalysis of the reaction: linuron + H2O <=> N,O-dimethylhydroxylamine + carbon dioxide + 3,4-dichloroaniline
Catalysis of the reaction: scutellarein 7-methyl ether + S-adenosyl-L-methionine  <=> cirsimaritin + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: scutellarein 7-methyl ether + S-adenosyl-L-methionine  <=> ladanein + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: cirsimaritin + S-adenosyl-L-methionine  <=> salvigenin + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: costunolide + NADPH + O2 + H+ <=> parthenolide + NADP(3-) + H2O
Catalysis of the reaction: parthenolide + NADPH + O2 + H+ <=> 3beta-hydroxyparthenolide + NADP + H2O
Catalysis of the reaction: costunolide + NADPH + O2 + H+ <=> 3beta-hydroxycostunolide + NADP + H2O
Catalysis of the reaction: patuletin + S-adenosyl-L-methionine  <=> quercetagetin 3',6-dimethyl ether + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: 3',4',5,7-pentahydroxy-8-methoxyflavon-3-olate + S-adenosyl-L-methionine  <=> gossypetin 3',8-dimethyl ether + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: 1-O-caffeoyl-beta-D-glucose + S-adenosyl-L-methionine  <=> 1-O-feruloyl-beta-D-glucose + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: (S)-scoulerine + NADPH + H+ + O2 <=> (S)-nandinine + NADP + 2 H2O
Catalysis of the reaction: flaviolin-2-olate + NADH + H+ + O2 <=> mompain + NAD + H2O
Catalysis of the reaction: naphthalene-1,3,6,8-tetrol + O2 <=> flaviolin-2-olate + H2O + H+
Catalysis of the reaction: 11-deoxycorticosterone + NADH + H+ <=> 4-pregnen-20,21-diol-3-one + NAD
Catalysis of the reaction: 3-benzyl-3,6 -bis(glutathione)- 6-(hydroxymethyl)-diketopiperazine <=> 3-benzyl-3,6 -bis(cysteinylglycine)- 6-(hydroxymethyl)-diketopiperazine + 2 5-oxo-L-prolinate
Catalysis of the reaction: 5-ammoniolevulinate + coenzyme A + ATP <=> 5-aminolevulinyl-CoA + AMP + diphosphoric acid
Catalysis of the reaction: 4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate + [1-(2-amino-7-methyl-4-oxo-7,8-dihydro-3H-pteridin-6-yl)]ethyl diphosphate = [1-(2-amino-7-methyl-4-oxo-7,8-dihydro-3H-pteridin-6-yl)]ethyl-4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate + diphosphoric acid
Catalysis of the reaction: 13-desoxypaxilline + NADPH + O2 + H+ <=> paspalicine + NADP + 2 H2O
Catalysis of the reaction: paspalicine + O2 + NADPH + H+ <=> paspalinine + NADP + H2O
Catalysis of the reaction: (R)-propane-1,2-diol + NADP <=> (R)-lactaldehyde + NADPH + H+
Catalysis of the reaction: scalarane-17alpha-19-diol <=> all-trans-geranylfarnesol + H2O
Catalysis of the reaction: monocyclic sesterterpenediol <=> all-trans-geranylfarnesol + H2O
Catalysis of the reaction: 17(E)-cheilanthenediol <=> all-trans-geranylfarnesol + H2O
Catalysis of the reaction: 14betaH-scalarane-17alpha-19-diol <=> all-trans-geranylfarnesol + H2O
Catalysis of the reaction: sedoheptulose 7-phosphate + D-ribose 5-phosphate <=> D-glycero-D-altro-octulose 8-phosphate + D-erythrose 4-phosphate
Catalysis of the reaction: D-fructose 6-phosphate + D-ribose 5-phosphate <=> D-glycero-D-altro-octulose 8-phosphate + D-glyceraldehyde 3-phosphate
Catalysis of the reaction: acetyl-CoA + malonyl-CoA + H+ + a holo-[acyl-carrier protein] <=> acetoacetyl-ACP + 2 coenzyme A + carbon dioxide
Catalysis of the reaction: acetoacetyl-ACP + L-tryptophan  + ATP <=> cyclo-acetoacetyl-L-tryptophan + AMP + diphosphoric acid + 2 H+ + a holo-[acyl-carrier protein]
Catalysis of the reaction: gibberellin A9 + 2-oxoglutarate + O2 <=> gibberellin A51 + succinate + carbon dioxide
Catalysis of the reaction: gibberellin A51 + 2-oxoglutarate + O2 <=> H+ + gibberellin A51-catabolite + succinate + carbon dioxide + H2O
Catalysis of the reaction: 1-[(9Z)-octadec-9-enoyl]-2-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol)(1-) + O2 + a reduced electron acceptor <=> 1-18:1-2-trans-16:1-phosphatidylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-trans-16:1-phosphatidylglycerol + O2 + a reduced electron acceptor <=> 1-18:2-2-trans-16:1-phosphatidylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-trans-16:1-phosphatidylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-trans-16:1-phosphatidylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-16:0-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor = 1-18:1-2-16:1-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 5-methylthio-2-oxopentanoate + a standard alpha amino acid <=> L-homomethionine + a 2-oxo carboxylate
Catalysis of the reaction: UDP-alpha-D-glucose + 4-methylthiobutylhydroximate <=> H+ + 3-methylthiopropyl-desulfoglucosinolate + UDP
Catalysis of the reaction: caffeoylshikimate + coenzyme A <=> caffeoyl-CoA + shikimate
Catalysis of the reaction: all-trans-nonaprenyl diphosphate + homogentisate + H+ <=> 2-methyl-6-all-trans-nonaprenyl-1,4-benzoquinone + carbon dioxide + diphosphoric acid
Catalysis of the reaction: 3-oxopropanoate + coenzyme A(4-) + NAD(1-) <=> acetyl-CoA(4-) + carbon dioxide + NADH(2-)
Catalysis of the reaction: gibberellin A34 + 2-oxoglutarate + O2 <=> H+ + gibberellin A34-catabolite + succinate + carbon dioxide + H2O
Catalysis of the reaction: indole-3-acetate + L-leucine  + ATP <=> H+ + indole-3-acetyl-leucine + diphosphoric acid + AMP
Catalysis of the reaction: indole-3-acetate + L-glutamate + ATP <=> H+ + indole-3-acetyl-glutamate + AMP + diphosphoric acid
Catalysis of the reaction: indole-3-acetyl-beta-4-D-glucose + H2O <=> H+ + indole-3-acetate + beta-D-glucose
Catalysis of the reaction: 1-O-(indol-3-ylacetyl)-beta-D-glucose + H2O <=> H+ + indole-3-acetate + beta-D-glucose
Catalysis of the reaction: liquiritigenin + NADPH + O2 + H+ <=> 2,4',7-trihydroxyisoflavanone + NADP(3-) + H2O
Catalysis of the reaction: daidzein 7-O-beta-D-glucoside + H2O <=> daidzein + beta-D-glucose
Catalysis of the reaction: 2,4',7-trihydroxyisoflavanone + S-adenosyl-L-methionine  <=> H+ + 2,7-dihydroxy-4'-methoxyisoflavanone + S-adenosyl-L-homocysteine
Catalysis of the reaction: (+)-6a-hydroxymaackiain + S-adenosyl-L-methionine  <=> H+ + (+)-pisatin + S-adenosyl-L-homocysteine
Catalysis of the reaction: O2 + a 2,3,4-saturated fatty acid <=> a 2(R)-hydroperoxy fatty acid
Catalysis of the reaction: NAD(1-) + H2O + a fatty aldehyde <=> NADH(2-) + 2 H+ + a fatty acid
Catalysis of the reaction: 24-methylenelophenol + a demethylated methyl acceptor <=> 9xi-episterol + a methylated methyl acceptor
Catalysis of the reaction: 24-ethylidenelophenol + a demethylated methyl acceptor <=> avenasterol + a methylated methyl acceptor
Catalysis of the reaction: avenasterol + O2 + NADPH + H+ <=> 5-dehydroavenasterol + 2 H2O + NADP
Catalysis of the reaction: H+ + campesterol + O2 + NADPH <=> (22S)-22-hydroxycampesterol + H2O + NADP
Catalysis of the reaction: (5alpha,22S,24R)-22-hydroxyergostan-3-one + NADP <=> H+ + (22S)-22-hydroxycampest-4-en-3-one + NADPH
Catalysis of the reaction: H+ + (5alpha)-campestan-3-one + O2 + NADPH <=> (5alpha,22S,24R)-22-hydroxyergostan-3-one + H2O + NADP
Catalysis of the reaction: H+ + campest-4-en-3-one + O2 + NADPH <=> (22S)-22-hydroxycampest-4-en-3-one + H2O + NADP
Catalysis of the reaction: n H2O + a glycogen <=> n a maltodextrin
Catalysis of the reaction: N(6)-(dimethylallyl)adenosine 5'-phosphate + H2O <=> N(6)-dimethylallyladenine + D-ribofuranose 5-phosphate
Catalysis of the reaction: L-phenylalanine  + 2 NADPH + 2 O2 + 2 H+ <=> (E)-phenylacetaldehyde oxime + 2 NADP + 3 H2O + carbon dioxide
Catalysis of the reaction: UDP-alpha-D-glucose + trans-zeatin <=> H+ + trans-zeatin-7-N-glucoside + UDP
Catalysis of the reaction: UDP-alpha-D-glucose(2-) + trans-zeatin <=> H+ + 9-(alpha-D-glucosyl)-trans-zeatin + UDP(3-)
Catalysis of the reaction: UDP-alpha-D-glucose + dihydrozeatin <=> H+ + dihydrozeatin-7-N-glucose + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + dihydrozeatin <=> H+ + 9-(alpha-D-glucosyl)dihydrozeatin + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + N(6)-dimethylallyladenine <=> H+ + 7-(alpha-D-glucosyl)-N(6)-isopentenyladenine + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + N(6)-dimethylallyladenine = H+ + 9-(alpha-D-glucosyl)-N(6)-isopentenyladenine + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + N-benzyladenine <=> H+ + benzyladenine-7-N-glucoside + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + N-benzyladenine <=> H+ + N-benzyl-9-(alpha-D-glucosyl)adenine + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + kinetin <=> H+ + kinetin-7-N-glucoside + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + kinetin <=> H+ + 9-(alpha-D-glucosyl)kinetin + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + cis-zeatin <=> H+ + cis-zeatin-7-N-glucoside + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + cis-zeatin = H+ + 9-(alpha-D-glucosyl)-cis-zeatin + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + O-beta-D-glucosyl-trans-zeatin = H+ + trans-zeatin-O-glucoside-7-N-glucoside + UDP
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> (+)-5-epi-aristolochene + diphosphoric acid
Catalysis of the reaction: H+ + 2-methylpropionitrile + O2 + NADPH <=> 2-hydroxy-2-methylpropanenitrile + NADP + H2O
Catalysis of the reaction: geranyl diphosphate(3-) <=> alpha-thujene + diphosphoric acid
Catalysis of the reaction: geranyl diphosphate(3-) <=> tricyclene + diphosphoric acid
Catalysis of the reaction: geranyl diphosphate <=> (+)-2-carene + diphosphoric acid
Catalysis of the reaction: geranyl diphosphate <=> (-)-camphene + diphosphoric acid
Catalysis of the reaction: GDP-alpha-D-mannose(2-) + a (mannosyl)2-(N-acetylglucosaminyl)2-diphosphodolichol <=> H+ + GDP(3-) + a (mannosyl)3-(N-acetylglucosaminyl)2-diphosphodolichol
Catalysis of the reaction: H+ + L-serine  <=> ethanolaminium(1+) + carbon dioxide
Catalysis of the reaction: butein 4'-beta-D-glucoside + O2 = aureusidin 6-O-beta-glucoside + H2O + H+
Catalysis of the reaction: beta-alanine + S-adenosyl-L-methionine  = H+ + N-methyl-beta-alanine + S-adenosyl-L-homocysteine
Catalysis of the reaction: N-methyl-beta-alanine + S-adenosyl-L-methionine  = H+ + N,N-dimethyl-beta-alanine + S-adenosyl-L-homocysteine
Catalysis of the reaction: N,N-dimethyl-beta-alanine + S-adenosyl-L-methionine  = H+ + beta-alanine betaine + S-adenosyl-L-homocysteine
Catalysis of the reaction: UDP-N-acetyl-alpha-D-glucosamine + 1D-myo-inositol 3-phosphate = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside 3-phosphate + UDP + H+
Catalysis of the reaction: gibberellin A25 + 2-oxoglutarate + O2 <=> gibberellin A13 + succinate + carbon dioxide
Catalysis of the reaction: gibberellin A13 + 2-oxoglutarate + O2 <=> gibberellin A43 + succinate + carbon dioxide
Catalysis of the reaction: gibberellin A25 + 2-oxoglutarate(2-) + O2 <=> gibberellin A46 + succinate(2-) + carbon dioxide
Catalysis of the reaction: gibberellin A12 + 2-oxoglutarate + O2 <=> gibberellin A14 + succinate + carbon dioxide
Catalysis of the reaction: gibberellin A17 + 2-oxoglutarate + O2 <=> gibberellin A28 + succinate + carbon dioxide
Catalysis of the reaction: gibberellin A28 + 2-oxoglutarate + O2 <=> (2betaOH)-gibberellin28 + succinate + carbon dioxide
Catalysis of the reaction: DIBOA-beta-D-glucoside + O2 + 2-oxoglutarate <=> TRIBOA-beta-D-glucoside + succinate + carbon dioxide
Catalysis of the reaction: TRIBOA-beta-D-glucoside + S-adenosyl-L-methionine  <=> (2R)-DIMBOA glucoside + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: eugenol + S-adenosyl-L-methionine  = H+ + O-methyleugenol + S-adenosyl-L-homocysteine
Catalysis of the reaction: benzyl alcohol + acetyl-CoA = benzyl acetate + coenzyme A
Catalysis of the reaction: O2 + 2 an ubiquinol = 2 H2O + 2 an ubiquinone
Catalysis of the reaction: 4-hydroxybutyrate + NAD(P) = 4-oxobutanoate + H+ + NAD(P)H
Catalysis of the reaction: UDP-alpha-D-glucose + curcumin = curcumin monoglucoside + UDP + H+
Catalysis of the reaction: UDP-alpha-D-glucose + curcumin monoglucoside = H+ + curcumin diglucoside + UDP
Catalysis of the reaction: H+ + 24-methyldesmosterol + NADPH = campesterol + NADP
Catalysis of the reaction: (2R)-DIMBOA glucoside + H2O = H+ + DIMBOA + beta-D-glucose
Catalysis of the reaction: campest-4-en-3beta-ol + NAD = campest-4-en-3-one + NADH + H+
Catalysis of the reaction: (5alpha)-campestan-3-one + NADP = H+ + campest-4-en-3-one + NADPH
Catalysis of the reaction: H+ + 6-oxocampestanol + O2 + NADPH = cathasterone + H2O + NADP
Catalysis of the reaction: cathasterone + O2 + a reduced electron acceptor <=> teasterone + H2O + an oxidized electron acceptor
Catalysis of the reaction: myo-inositol 1,3,4,6-tetrakisphosphate(8-) + ATP = H+ + 1L-myo-inositol 1,2,3,4,6-pentakisphosphate(10-) + ADP
Catalysis of the reaction: 1L-myo-inositol 1,2,3,4,6-pentakisphosphate(10-) + ATP = H+ + myo-inositol hexakisphosphate(12-) + ADP
Catalysis of the reaction: typhasterol + O2 + a reduced electron acceptor = castasterone + H2O + an oxidized electron acceptor
Catalysis of the reaction: H+ + castasterone + NADPH + O2 <=> brassinolide + NADP + H2O
Catalysis of the reaction: benzoyl-CoA + 3 malonyl-CoA + 3 H+ = 2,4,6-trihydroxybenzophenone + 4 coenzyme A + 3 carbon dioxide
Catalysis of the reaction: 2 H+ + 4-coumaryl-CoA + H2O + 3 malonyl-CoA <=> 4 coenzyme A + 3 carbon dioxide + p-coumaroyltriacetate
Catalysis of the reaction: gibberellin A14 + O2 + 2-oxoglutarate <=> gibberellin A37 + carbon dioxide + succinate
Catalysis of the reaction: gibberellin A36 + O2 + 2-oxoglutarate <=> H+ + gibberellin A4 + succinate + 2 carbon dioxide
Catalysis of the reaction: theobromine + S-adenosyl-L-methionine  <=> H+ + caffeine + S-adenosyl-L-homocysteine
Catalysis of the reaction: 1,7-dimethylxanthine + S-adenosyl-L-methionine  <=> H+ + caffeine + S-adenosyl-L-homocysteine
Catalysis of the reaction: H+ + 3,4-dihydroxyphenylpyruvate + NADPH <=> (2R)-3-(3,4-dihydroxyphenyl)lactate + NADP
Catalysis of the reaction: H+ + eriodictyol + NADPH + O2 <=> 2-(3,4-dihydroxyphenyl)-5-hydroxy-4-oxo-4H-chromen-7-olate luteolin-7-olate(1-) + NADP + 2 H2O
Catalysis of the reaction: H+ + 2-trans,6-trans,10-trans-geranylgeranyl diphosphate + NADPH = dihydrogeranylgeranyl-PP + NADP
Catalysis of the reaction: H+ + dihydrogeranylgeranyl-PP + NADPH = tetrahydrogeranylgeranyl-PP + NADP
Catalysis of the reaction: H+ + tetrahydrogeranylgeranyl-PP + NADPH = (E)-3,7,11,15-tetramethylhexadec-2-en-1-yl diphosphate + NADP
Catalysis of the reaction: H+ + chlorophyllide a(1-) + 2-trans,6-trans,10-trans-geranylgeranyl diphosphate(3-) <=> geranylgeranyl-chlorophyll a + diphosphoric acid
Catalysis of the reaction: H+ + geranylgeranyl-chlorophyll a + NADPH = dihydrogeranylgeranyl-chlorophyll a + NADP
Catalysis of the reaction: H+ + dihydrogeranylgeranyl-chlorophyll a + NADPH = tetrahydrogeranylgeranyl-chlorophyll a + NADP
Catalysis of the reaction: chlorophyll a + NADP = tetrahydrogeranylgeranyl-chlorophyll a + NADPH + H+
Catalysis of the reaction: UDP-alpha-D-glucose + a glucosyl-glycogenin = (1,4-alpha-D-glucosyl)n-glucosyl glucogenin + UDP + H+
Catalysis of the reaction: a glucosylated glycogenin = a glycogen
Catalysis of the reaction: H+ + chlorophyllide b(1-) + 2-trans,6-trans,10-trans-geranylgeranyl diphosphate <=> geranylgeranyl-chlorophyll b + diphosphoric acid
Catalysis of the reaction: H+ + chlorophyllide b + (E)-3,7,11,15-tetramethylhexadec-2-en-1-yl diphosphate <=> chlorophyll b + diphosphoric acid
Catalysis of the reaction: gibberellin A15 (closed lactone form) + O2 + 2-oxoglutarate = gibberellin A37 (closed lactone form) + succinate + carbon dioxide
Catalysis of the reaction: malonyl-CoA + a very-long-chain 2,3,4-saturated fatty acyl CoA = carbon dioxide + coenzyme A + a very-long-chain oxoacyl-CoA
Catalysis of the reaction: NADPH + H2O = NADH + hydrogenphosphate
Catalysis of the reaction: NADP(3-) + a very-long-chain 2,3,4-saturated fatty acyl CoA <=> NADPH(4-) + H+ + a very-long-chain trans-2,3-dehydroacyl-CoA
Catalysis of the reaction: H+ + campestanol + O2 + NADPH <=> 6-deoxycathasterone + H2O + NADP
Catalysis of the reaction: 6-deoxycathasterone + O2 + a reduced electron acceptor <=> 6-deoxoteasterone + H2O + an oxidized electron acceptor
Catalysis of the reaction: eriodictyol + S-adenosyl-L-methionine  <=> H+ + homoeriodictyol + S-adenosyl-L-homocysteine
Catalysis of the reaction: eriodictyol + S-adenosyl-L-methionine  <=> H+ + hesperetin(1-) + S-adenosyl-L-homocysteine
Catalysis of the reaction: phytyl phosphate(2-) + a nucleoside triphosphate <=> (E)-3,7,11,15-tetramethylhexadec-2-en-1-yl diphosphate + a nucleoside diphosphate
Catalysis of the reaction: 6-deoxotyphasterol + O2 + a reduced electron acceptor = 6-deoxocastasterone + H2O + an oxidized electron acceptor
Catalysis of the reaction: H+ + UDP-alpha-D-glucuronate = UDP-alpha-D-apiose + carbon dioxide
Catalysis of the reaction: (S)-naringenin(1-) + S-adenosyl-L-methionine  <=> sakuranetin + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: (S)-naringenin + S-adenosyl-L-methionine  = 2 H+ + ponciretin + S-adenosyl-L-homocysteine
Catalysis of the reaction: flavan-3,3',4,4',5,5',7-heptol + O2 + 2-oxoglutarate = H+ + delphinidin + 2 H2O + carbon dioxide + succinate
Catalysis of the reaction: UDP-alpha-D-glucose + a dihydroceramide = UDP + H+ + a D-glucosyl-N-acylsphinganine
Catalysis of the reaction: an L-1-phosphatidyl-inositol + a dihydroceramide = an inositol phosphodihydroceramide + a 1,2-diacyl-sn-glycerol
Catalysis of the reaction: O2 + NADPH + H+ + a dihydroceramide = NADP + H2O + an alpha hydroxydihydroceramide
Catalysis of the reaction: O2 + H+ + a dihydroceramide + NAD(P)H = H2O + a phytoceramide + NAD(P)
Catalysis of the reaction: ATP + a dihydroceramide = ADP + H+ + a dihydroceramide 1-phosphate
Catalysis of the reaction: 2 H+ + 4-coumaryl-CoA + 3 malonyl-CoA( <=> p-coumaroyltriacetic acid lactone + 4 coenzyme A + 3 carbon dioxide
Catalysis of the reaction: 2 H+ + isovaleryl-CoA + 3 malonyl-CoA = 6-(4-methyl-2-oxopentyl)-4-hydroxy-2-pyrone + 4 coenzyme A + 3 carbon dioxide
Catalysis of the reaction: pelargonidin 3-O-beta-D-glucoside + UDP-alpha-D-glucose <=> anthocyanidin 3,5-di-O-beta-D-glucoside + UDP + H+
Catalysis of the reaction: anthocyanidin 3,5-di-O-beta-D-glucoside + caffeoyl-CoA <=> pelargonidin-3,5-diglucoside-5-O-caffeoylglucoside + coenzyme A(4-)
Catalysis of the reaction: cannabigerolate + O2 <=> Delta(9)-tetrahydrocannabinolic acid + hydrogen peroxide
Catalysis of the reaction: cannabigerolate + O2 <=> cannabidiolate + hydrogen peroxide
Catalysis of the reaction: H+ + sitosterol + O2 + NADPH <=> (22alpha)-hydroxy-sitosterol + H2O + NADP
Catalysis of the reaction: H+ + isofucosterol + O2 + NADPH <=> (22alpha)-hydroxy-isofucosterol + H2O + NADP
Catalysis of the reaction: H+ + epidihydrocholesterin + O2 + NADPH = (22alpha)-hydroxy-cholestanol + H2O + NADP
Catalysis of the reaction: beta-carotene + 2 O2 = 2 beta-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial
Catalysis of the reaction: lutein + 2 O2 = 3-hydroxy-beta-ionone + 3-hydroxy-alpha-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial
Catalysis of the reaction: violaxanthin + 2 O2 = 2 5,6-epoxy-3-hydroxy-9-apo-beta-caroten-9-one + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial
Catalysis of the reaction: O2 + a stearoyl-[acp] + a reduced ferredoxin = 2 H2O + an oleoyl-[acp] + an oxidized ferredoxin
Catalysis of the reaction: pelargonidin 3-O-beta-D-glucoside + caffeoyl-CoA = pelargonidin 3-O-beta-D-caffeoylglucoside + coenzyme A
Catalysis of the reaction: 4-coumaryl-CoA + pelargonidin 3-O-beta-D-glucoside = pelargonidin 3-O-beta-D-p-coumaroylglucoside + coenzyme A
Catalysis of the reaction: UDP-alpha-D-glucose + cyanidin = H+ + cyanidin 5-O-beta-D-glucoside + UDP
Catalysis of the reaction: cyanidin 5-O-beta-D-glucoside + UDP-alpha-D-glucose = cyanin betaine + UDP
Catalysis of the reaction: butein 4'-beta-D-glucoside + O2 + 2 H+ = sulfuretin 6-glucoside + 2 H2O
Catalysis of the reaction: sinapoyl aldehyde + NADP + H2O <=> 2 H+ + trans-sinapate + NADPH
Catalysis of the reaction: UDP-alpha-D-glucuronate + soyasapogenol B <=> H+ + UDP + soyasapogenol B 3-O-beta-glucuronate
Catalysis of the reaction: cinnamaldehyde + O2 + H2O = H+ + trans-cinnamate + hydrogen peroxide
Catalysis of the reaction: 1-naphthaldehyde + O2 + H2O = H+ + 1-naphthoate + hydrogen peroxide
Catalysis of the reaction: 3,4-dihydroxybenzaldehyde + O2 + H2O <=> H+ + 3,4-dihydroxybenzoate + hydrogen peroxide
Catalysis of the reaction: geranial + O2 + H2O = H+ + geranate + hydrogen peroxide
Catalysis of the reaction: heptanal + O2 + H2O = H+ + heptanoate + hydrogen peroxide
Catalysis of the reaction: H2O + a glucosinolate = alpha-D-glucose + a thiohydroximate-O-sulfate.  Glucosinolates are a subclass of thioglucosides.
Catalysis of the reaction: anthocyanidin 3,5-di-O-beta-D-glucoside + caffeoyl-CoA = pelargonidin 3-O-(6-O-caffeoyl-beta-D-glucoside) 5-O-beta-D-glucoside + coenzyme A
Catalysis of the reaction: 4'''-demalonylsalvianin + malonyl-CoA = salvianin + coenzyme A
Catalysis of the reaction: thebaine + 2-oxoglutarate + O2 <=> neopinone + formaldehyde + succinate + carbon dioxide
Catalysis of the reaction: thebaine + 2-oxoglutarate + O2 <=> oripavine + formaldehyde + succinate + carbon dioxide
Catalysis of the reaction: oripavine + 2-oxoglutarate + O2 <=> morphinone + formaldehyde + succinate + carbon dioxide
Catalysis of the reaction: codeine + 2-oxoglutarate + O2 <=> morphine + formaldehyde + succinate + carbon dioxide
Catalysis of the reaction: 4-coumaryl-CoA + cyanin betaine <=> shisonin + coenzyme A
Catalysis of the reaction: UDP-alpha-D-glucose + cyanidin 3-O-beta-D-glucoside betaine <=> cyanidin 3-O-sophoroside + UDP + H+
Catalysis of the reaction: UDP-alpha-D-glucose + pelargonidin 3-O-beta-D-glucoside <=> H+ + pelargonidin 3-O-sophoroside + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + delphinidin 3-O-beta-D-glucoside <=> H+ + delphinidin 3-O-sophoroside + UDP
Catalysis of the reaction: 5-oxopentanoate + NADP + H2O = glutarate + NADPH + 2 H+
Catalysis of the reaction: geraniol + O2 + NADPH + H+ <=> (6E)-8-hydroxygeraniol + NADP + H2O
Catalysis of the reaction: 4-coumaryl-CoA + cyanidin 3-O-beta-D-glucoside betaine <=> cyanidin 3-(p-coumaroyl)-glucoside + coenzyme A
Catalysis of the reaction: UDP-alpha-D-glucose + cyanidin 3-(p-coumaroyl)-glucoside = shisonin + UDP + H+
Catalysis of the reaction: delphinidin 3,3',5-tri-O-beta-D-glucoside betaine + caffeoyl-CoA <=> delphinidin 3-O-glucosyl-5-O-(caffeoylglucoside-3'-O-glucoside) + coenzyme A
Catalysis of the reaction: delphinidin 3-O-beta-D-glucoside-5-O-beta-D-glucoside betaine + caffeoyl-CoA <=> delphinidin 3-O-glucosyl-5-O-caffeoylglucoside + coenzyme A
Catalysis of the reaction: UDP-alpha-D-glucose + delphinidin 3-O-glucosyl-5-O-caffeoylglucoside <=> H+ + delphinidin 3-O-glucosyl-5-O-(caffeoylglucoside-3'-O-glucoside) + UDP
Catalysis of the reaction: delphinidin 3-O-glucosyl-5-O-(caffeoylglucoside-3'-O-glucoside) + caffeoyl-CoA <=> gentiodelphin + coenzyme A
Catalysis of the reaction: lycopene + 2 O2 <=> 2 sulcatone + bixin aldehyde
Catalysis of the reaction: bixin aldehyde + O2 + NAD <=> norbixin + NADH + H+
Catalysis of the reaction: norbixin + S-adenosyl-L-methionine  <=> bixin + S-adenosyl-L-homocysteine
Catalysis of the reaction: bixin + S-adenosyl-L-methionine  <=> bixin dimethyl ester + S-adenosyl-L-homocysteine
Catalysis of the reaction: quercetin-7-olate + S-adenosyl-L-methionine  = H+ + isorhamnetin + S-adenosyl-L-homocysteine
Catalysis of the reaction: UDP-alpha-D-glucose + kaempferol-3-rhamnoside <=> kaempferol 3-O-rhamnoside-7-O-glucoside + UDP
Catalysis of the reaction: quercetin-7-olate + UDP-L-rhamnose <=> H+ + quercetin 3-O-rhamnoside + UDP
Catalysis of the reaction: UDP-alpha-D-glucose(2-) + quercetin 3-O-rhamnoside <=> quercetin 3-O-rhamnoside-7-O-glucoside + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + kaempferol 3-O-glucoside <=> kaempferol 3,7-O-diglucoside + UDP
Catalysis of the reaction: raffinose + D-galactosylononitol = stachyose + 1D-4-O-methyl-myo-inositol
Catalysis of the reaction: stachyose + alpha-D-galactosyl-(1->3)-1D-myo-inositol <=> verbascose + myo-inositol
Catalysis of the reaction: 2 verbascose <=> ajugose + stachyose
Catalysis of the reaction: 2 stachyose <=> verbascose + raffinose
Catalysis of the reaction: 2 raffinose <=> stachyose + sucrose
Catalysis of the reaction: verbascose + alpha-D-galactosyl-(1->3)-1D-myo-inositol <=> ajugose + myo-inositol
Catalysis of the reaction: 1D-5-O-methyl-myo-inositol + alpha-D-galactosyl-(1->3)-1D-myo-inositol <=> D-galactosylononitol + myo-inositol
Catalysis of the reaction: 1-18:1-2-16:0-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:2-2-16:0-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-16:0-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-16:0-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-16:1-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:2-2-16:1-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-16:1-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-16:1-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-16:2-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:2-2-16:2-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-16:2-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-16:2-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-16:3-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-16:3-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-16:1-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:1-2-16:2-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-16:2-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor = 1-18:1-2-16:3-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-16:0-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor = 1-18:2-2-16:1-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-16:1-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor = 1-18:2-2-16:2-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:3-2-16:0-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-16:1-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:3-2-16:1-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-16:2-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:3-2-16:2-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-16:3-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-18:2-digalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-18:2-digalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-18:3-digalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-18:3-digalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-[(9Z)-octadec-9-enoyl]-2-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol)(1-) + O2 + a reduced electron acceptor <=> 1-18:2-2-16:0-phosphatidylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-16:0-phosphatidylglycerol + O2 + a reduced electron acceptor <=> 1-18:2-2-trans-16:1-phosphatidylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:3-2-16:0-phosphatidylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-trans-16:1-phosphatidylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-18:1-sn-glycerol-3-phosphocholine + O2 + a reduced electron acceptor <=> 1-18:2-2-18:1-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-18:1-phosphatidylcholine + O2 + a reduced electron acceptor <=> 1-18:3-2-18:1-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-18:2-phosphatidylcholine + O2 + a reduced electron acceptor <=> 1-18:2-2-18:2-sn-glycerol-3-phosphocholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-18:2-sn-glycerol-3-phosphocholine + O2 + a reduced electron acceptor <=> 1-18:3-2-18:2-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-18:3-phosphatidylcholine + O2 + a reduced electron acceptor <=> 1-18:2-2-18:3-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-18:3-phosphatidylcholine + O2 + a reduced electron acceptor <=> 1-18:3-2-18:3-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-18:2-phosphatidylcholine + O2 + a reduced electron acceptor = 1-18:1-2-18:3-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-18:1-sn-glycerol-3-phosphocholine + O2 + a reduced electron acceptor <=> 1-18:1-2-18:2-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-18:1-phosphatidylcholine + O2 + a reduced electron acceptor = 1-18:2-2-18:2-sn-glycerol-3-phosphocholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-18:2-sn-glycerol-3-phosphocholine + O2 + a reduced electron acceptor = 1-18:2-2-18:3-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:3-2-18:1-phosphatidylcholine + O2 + a reduced electron acceptor <=> 1-18:3-2-18:2-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:3-2-18:2-phosphatidylcholine + O2 + a reduced electron acceptor <=> 1-18:3-2-18:3-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: O2 + a lipid linoleoyl group + a reduced electron acceptor <=> 2 H2O + a lipid gamma-linolenoyl group + an oxidized electron acceptor
Catalysis of the reaction: all-cis-icosa-8,11,14-trienoate + O2 + a reduced electron acceptor <=> arachidonate + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 2 H+ + MoO2-molybdopterin cofactor(2-) + L-cysteine  <=> thio-molybdenum cofactor + L-alanine  + H2O
Catalysis of the reaction: 24-epi-campesterol + NADPH + H+ + O2 <=> brassicasterol + NADP + 2 H2O
Catalysis of the reaction: UDP-alpha-D-glucose + 6-hydroxyflavone <=> 6-O-beta-D-glucosyl-6-hydroxyflavone + UDP + H+
Catalysis of the reaction: UDP-alpha-D-glucose + 7-hydroxyflavone <=> 7-O-beta-D-glucosyl-7-hydroxyflavone + UDP + H+
Catalysis of the reaction: 1-16:0-2-18:1-phosphatidylcholine + O2 + a reduced electron acceptor <=> 1-palmitoyl-2-linoleoyl-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-palmitoyl-2-linoleoyl-phosphatidylcholine + O2 + a reduced electron acceptor <=> 1-16:0-2-18:3-phosphatidylcholine + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:1-2-16:0-digalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:2-2-16:0-digalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-16:0-2-18:2-digalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-16:0-2-18:3-digalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 1-18:2-2-18:2-monogalactosyldiacylglycerol + O2 + a reduced electron acceptor <=> 1-18:3-2-18:2-monogalactosyldiacylglycerol + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: (+)-marmesin + NADPH + H+ + O2 <=> psoralen + NADP + acetone + 2 H2O
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> alpha-copaene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> (+)-alpha-barbatene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> (+)-thujopsene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> isobazzanene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> (+)-beta-barbatene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> beta-acoradiene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> (+)-beta-chamigrene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> zingiberene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> (-)-alpha-cuprenene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> alpha-chamigrene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> beta-sesquiphellandrene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> delta-cuprenene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate <=> beta-elemene + diphosphoric acid
Catalysis of the reaction: UDP-alpha-D-glucose + 2',4,4',6'-tetrahydroxychalcone <=> UDP + 2',4,4',6'-tetrahydroxychalcone 4'-O-beta-D-glucoside + H+
Catalysis of the reaction: UDP-alpha-D-glucose + 2',3,4,4',6'-pentahydroxychalcone <=> H+ + 2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-D-glucoside + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + betanidin <=> H+ + betanin + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + betanidin <=> H+ + gomphrenin I + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + leucodopachrome <=> H+ + cyclo-dopa 5-O-glucoside + UDP
Catalysis of the reaction: 9(S)-HPODE <=> colneleate + H2O
Catalysis of the reaction: (10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate <=> colnelenate + H2O
Catalysis of the reaction: abietal + NADPH + O2 <=> abietate + NADP + H2O
Catalysis of the reaction: H+ + levopimaradienol + NADPH + O2 <=> levopiramadiene-diol + NADP + H2O
Catalysis of the reaction: H+ + dehydroabietadienol + NADPH + O2 <=> dehydroabietadiene-diol + NADP + H2O
Catalysis of the reaction: dehydroabietadienal + NADPH + O2 <=> dehydroabietic acid + NADP + H2O
Catalysis of the reaction: H+ + isopimaradienol + NADPH + O2 <=> isopimaradiene-diol + NADP + H2O
Catalysis of the reaction: isopimaradienal + NADPH + O2 <=> isopimaric acid + NADP + H2O
Catalysis of the reaction: geranyl diphosphate = gamma-terpinene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = germacrene C + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate(3-) <=> (+)-valencene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate(3-) <=> (-)-7-epi-alpha-selinene + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate(3-) <=> diphosphoric acid + sesquisabinene
Catalysis of the reaction: H2O + ATP + a quaternary amine = hydrogenphosphate + ADP + H+ + a quaternary amine
Catalysis of the reaction: NAD + 2-hydroxyglutarate = H+ + 2-oxoglutarate + NADH
Catalysis of the reaction: 2 H+ + 2 coniferol + O2 <=> (+)-pinoresinol + 2 H2O
Catalysis of the reaction: (-)-secoisolariciresinol + NAD <=> H+ + (-)-lactol + NADH
Catalysis of the reaction: (-)-lactol + NAD <=> H+ + (-)-matairesinol + NADH
Catalysis of the reaction: indol-3-ylmethylamine + S-adenosyl-L-methionine  = H+ + N-methyl-3-aminomethylindole + S-adenosyl-L-homocysteine
Catalysis of the reaction: N-methyl-3-aminomethylindole + S-adenosyl-L-methionine  = H+ + gramine + S-adenosyl-L-homocysteine
Catalysis of the reaction: H+ + (+)-pinoresinol + NADPH + O2 <=> (+)-piperitol + NADP + 2 H2O
Catalysis of the reaction: H+ + (+)-piperitol + NADPH + O2 <=> (+)-sesamin + NADP + 2 H2O
Catalysis of the reaction: (S)-reticulinium(1+) + S-adenosyl-L-methionine  <=> H+ + laudanine(1+) + S-adenosyl-L-homocysteine
Catalysis of the reaction: (R)-reticulinium(1+) + S-adenosyl-L-methionine  <=> (R)-laudanine(1+) + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: FMNH2 + O2 <=> 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + dialuric acid
Catalysis of the reaction: octanoyl-CoA + isopenicillin N + H2O <=> H+ + coenzyme A + penicillin K + L-2-aminoadipate
Catalysis of the reaction: GDP-alpha-D-mannose + D-glycerate <=> H+ + 2-(alpha-D-mannosyl)-D-glycerate + GDP
Catalysis of the reaction: baccatin III + (3R)-3-amino-3-phenylpropanoyl-CoA = N-debenzoyl-(3'-RS)-2'-deoxytaxol + coenzyme A
Catalysis of the reaction: 3'-N-debenzoyltaxol + benzoyl-CoA = H+ + paclitaxel + coenzyme A
Catalysis of the reaction: 2 H+ + gibberellin A44 + 2-oxoglutarate + O2 = gibberellin A98 + succinate + carbon dioxide
Catalysis of the reaction: UDP-D-galactose + solanidine = H+ + gamma-solanine + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + solanidine = H+ + gamma-chaconine + UDP
Catalysis of the reaction: beta-chaconine + UDP-L-rhamnose = H+ + alpha-chaconine + UDP
Catalysis of the reaction: beta-solanine + UDP-L-rhamnose = solanine + UDP
Catalysis of the reaction: 1-propenylsulfenate = propanethiol S-oxide
Catalysis of the reaction: geranyl diphosphate + 4-hydroxybenzoic acid = 3-geranyl-4-hydroxybenzoate + diphosphoric acid
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = (Z,E)-alpha-farnesene + diphosphoric acid
Catalysis of the reaction: H+ + (-)-medicarpin + NADPH = (+)-vestitol + NADP
Catalysis of the reaction: GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate = GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
Catalysis of the reaction: germacra-1(10),4,11(13)-trien-12-oate + O2 + NADPH + 2 H+ = costunolide + 2 H2O + NADP
Catalysis of the reaction: UDP-alpha-D-glucose + gypsogenin = gypsogenin-28-beta-D-glucoside + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + gypsogenate = gypsogenate-28-beta-D-glucoside + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + 16-alpha-hydroxygypsogenate = 16-alpha-hydroxygypsogenate-28-beta-D-glucoside + UDP
Catalysis of the reaction: orcinol + S-adenosyl-L-methionine  = H+ + 3-methoxy-5-hydroxytoluene + S-adenosyl-L-homocysteine
Catalysis of the reaction: 3-methoxy-5-hydroxytoluene + S-adenosyl-L-methionine  = H+ + 3,5-dimethoxytoluene + S-adenosyl-L-homocysteine
Catalysis of the reaction: phloroglucinol + S-adenosyl-L-methionine  = H+ + 3,5-dihydroxyanisole + S-adenosyl-L-homocysteine
Catalysis of the reaction: 3,5-dihydroxyanisole + S-adenosyl-L-methionine  = H+ + 3,5-dimethoxyphenol + S-adenosyl-L-homocysteine
Catalysis of the reaction: 3,5-dimethoxyphenol + S-adenosyl-L-methionine  = H+ + 1,3,5-trimethoxybenzene + S-adenosyl-L-homocysteine
Catalysis of the reaction: (2S,3S)-2,3-dihydro-3-hydroxyanthranilic acid  = (1R,6S)-6-ammonio-5-oxocyclohex-2-ene-1-carboxylate
Catalysis of the reaction: UDP-alpha-D-glucose(2-) + medicagenate <=> UDP(3-) + a medicagenate monoglucoside
Catalysis of the reaction: UDP-alpha-D-glucose(2-) + soyasapogenol B <=> UDP(3-) + a soyasapogenol B monoglucoside
Catalysis of the reaction: UDP-alpha-D-glucose + soyasapogenol E <=> UDP + a soyasapogenol E monoglucoside
Catalysis of the reaction: H+ + (+)-delta-cadinene + NADPH + O2 <=> 8-hydroxy-(+)-delta-cadinene + NADP + H2O
Catalysis of the reaction: 2-(3,4-dihydroxyphenyl)-5-hydroxy-4-oxo-4H-chromen-7-olate luteolin-7-olate + a glucosylated glucose acceptor = isoorientin + a non glucosylated glucose acceptor
Catalysis of the reaction: isoorientin + an L-rhamonsylated rhamnosyl acceptor = isoorientin 2''-O-rhamnoside + a non rhamnosylated rhamnosyl acceptor
Catalysis of the reaction: indole-3-acetate + L-valine  + ATP = H+ + indole-3-acetyl-valine + AMP + diphosphoric acid
Catalysis of the reaction: indole-3-acetate + L-phenylalanine  + ATP = H+ + indole-3-acetyl-phenylalanine + AMP + diphosphoric acid
Catalysis of the reaction: UDP-alpha-D-glucose + coniferyl aldehyde = H+ + coniferaldehyde glucoside + UDP
Catalysis of the reaction: glutathionate + hypoglycin A = L-cysteinylglycine + hypoglycin B
Catalysis of the reaction: dalcochinin-8'-O-beta-glucoside + H2O <=> dalcochinin + D-glucopyranose
Catalysis of the reaction: 2-demethylmenaquinol-7 + S-adenosyl-L-methionine  = menaquinol-7 + S-adenosyl-L-homocysteine  + H+
Catalysis of the reaction: UDP-alpha-D-glucose + sinapoyl aldehyde = H+ + sinapaldehyde glucoside + UDP
Catalysis of the reaction: 3beta-hydroxy-9beta-pimara-7,15-diene-19,6beta-olide + NAD(P) = momilactone A + H+ + NAD(P)H
Catalysis of the reaction: all-trans-4,4'-diapophytofluene + FAD + H+ = all-trans-4,4'-diapo-zeta-carotene + FADH2
Catalysis of the reaction: all-trans-4,4'-diapo-zeta-carotene + FAD + H+ = 4,4'-diaponeurosporene + FADH2
Catalysis of the reaction: H+ + (S)-reticulinium(1+) + NADPH + O2 <=> (S)-corytuberine + NADP + 2 H2O
Catalysis of the reaction: (S)-corytuberine + S-adenosyl-L-methionine  <=> H+ + magnoflorine + S-adenosyl-L-homocysteine
Catalysis of the reaction: 2 NADPH + 2 H+ + a long-chain acyl-CoA = coenzyme A + 2 NADP + a long-chain alcohol
Catalysis of the reaction: icosanoyl-CoA + dodecan-1-ol = arachidoyl dodecanoate + coenzyme A
Catalysis of the reaction: (6E)-8-hydroxygeraniol + NADP <=> (6E)-8-hydroxygeranial + NADPH + H+
Catalysis of the reaction: (6E)-8-hydroxygeranial + NADP <=> (6E)-8-oxogeranial + NADPH + H+
Catalysis of the reaction: (6E)-8-oxogeraniol + NADP <=> (6E)-8-oxogeranial + NADPH + H+
Catalysis of the reaction: UDP-alpha-D-glucose + 7-deoxyloganetate <=> H+ + 7-deoxyloganate + UDP
Catalysis of the reaction: acetyl-CoA + phosphinothricin <=> H+ + coenzyme A(4-) + N-acetylphosphinatothricinate
Catalysis of the reaction: gibberellin A12 + 2-oxoglutarate + O2 = gibberellin A110 + succinate + carbon dioxide
Catalysis of the reaction: 7 malonyl-CoA + 5 H+ + a hexanoyl-[acyl-carrier-protein] = norsolorinate anthrone + 7 coenzyme A + 7 carbon dioxide + 2 H2O + a holo-[acyl-carrier protein]
Catalysis of the reaction: versicolorone + NADP = hydroxyversicolorone + NADPH
Catalysis of the reaction: versiconol acetate + NADP <=> versiconal hemiacetal acetate + NADPH
Catalysis of the reaction: versiconol + NADP <=> versiconal hemiacetal + NADPH + H+
Catalysis of the reaction: nitrilotriacetate + O2 + FMNH2 = ammoniodiacetate + 2-oxo monocarboxylic acid anion + H2O + FMN
Catalysis of the reaction: 4-hydroxy-2,5-dimethylfuran-3-one + NADP <=> 4-hydroxy-5-methyl-2-methylenefuran-3-one + NADPH + H+
Catalysis of the reaction: homofuraneol + NADP <=> (2E)-2-ethylidene-4-hydroxy-5-methyl-3(2H)-furanone + NADPH + H+
Catalysis of the reaction: 2-butyl-4-hydroxy-5-methyl-3(2H)-furanone + NADP <=> (2E)-2-butylidene-4-hydroxy-5-methyl-3(2H)-furanone + NADPH + H+
Catalysis of the reaction: 4-hydroxy-5-methyl-2-propyl-3(2H)-furanone + NADP <=> (2E)-4-hydroxy-5-methyl-2-propylidene-3(2H)-furanone + NADPH + H+
Catalysis of the reaction: UDP-alpha-D-glucose + NAD <=> H+ + UDP-3-keto-alpha-D-glucose + NADH
Catalysis of the reaction: UDP-alpha-D-xylose + a homogalacturonan <=> UDP + 4 H+ + a xylogalacturonan
Catalysis of the reaction: sulfonatoacetaldehyde + H2O + NAD <=> sulfonatoacetate + NADH + 2 H+
Catalysis of the reaction: oleoyl-CoA + O2 + a reduced electron acceptor <=> linoleoyl-CoA + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: an NDP-alpha-D-glucose + D-glucopyranose <=> alpha,alpha-trehalose + H+ + a nucleoside diphosphate
Catalysis of the reaction: palmitoleoyl-CoA + O2 + a reduced electron acceptor <=> (9Z,12Z)-hexadecadienoyl-CoA + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: (9Z,12Z)-hexadecadienoyl-CoA + O2 + a reduced electron acceptor <=> 9,12,15-cis-hexadecatrienoyl-CoA + 2 H2O + an oxidized electron acceptor
Catalysis of the reaction: 3 H+ + 9,12,15-cis-hexadecatrienoyl-CoA + 3 malonyl-CoA(5-) <=> 5-(pentadeca-8,11,14-trien-1-yl)resorcinol + 4 coenzyme A + 4 carbon dioxide
Catalysis of the reaction: 5-(pentadeca-8,11,14-trien-1-yl)resorcinol + S-adenosyl-L-methionine  <=> H+ + 5-(pentadeca-8,11,14-trien-1-yl)resorcinol monomethyl ether + S-adenosyl-L-homocysteine
Catalysis of the reaction: myristoyl-CoA + H2O <=> H+ + tetradecanoate + coenzyme A
Catalysis of the reaction: H+ + 2-methylbutyronitrile + NADPH + O2 <=> H2O + NADP + 2-hydroxy-2-methylbutyronitrile
Catalysis of the reaction: O2 + a lipid linoleoyl group + a reduced electron acceptor <=> 2 H2O + a lipid alpha-linolenoyl group + an oxidized electron acceptor
Catalysis of the reaction: columbianetin + NADPH + O2 + H+ <=> angelicin + acetone + NADP + 2 H2O
Catalysis of the reaction: a 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + a beta,beta digalactosyldiacylglycerol <=> a trigalactosyldiacylglycerol + a 1,2-diacyl-sn-glycerol
Catalysis of the reaction: H+ + progesterone + NADPH <=> 5beta-pregnane-3,20-dione + NADP
Catalysis of the reaction: (5-oxo-2-sulfonato-2,5-dihydrofuran-2-yl)acetate + H2O <=> maleylacetate + sulfite + 2 H+
Catalysis of the reaction: UDP-alpha-D-glucose + 2-hydroxylamino-4,6-dinitrotoluene <=> 2-hydroxylamino-4,6-dinitrotoluene-O-glucoside + UDP + H+
Catalysis of the reaction: UDP-alpha-D-glucose + 4-hydroxylamino-2,6-dinitrotoluene <=> 4-hydroxylamino-2,6-dinitrotoluene-O-glucoside + UDP + H+
Catalysis of the reaction: dimethyl sulfoxide + O2 + NADPH + H+ <=> sulfonyldimethane + H2O + NADP
Catalysis of the reaction: 16-hydroxypalmitate + NADP <=> H+ + 16-oxo-palmitate + NADPH
Catalysis of the reaction: oleate + a lipid hydroperoxide <=> 9,10-epoxystearate + a lipid alcohol
Catalysis of the reaction: H+ + 9,10-epoxystearate + O2 + NADPH <=> 9,10-epoxy-18-hydroxystearate + H2O + NADP
Catalysis of the reaction: 9,10-epoxystearate + H2O <=> (9R,10S)-dihydroxystearate
Catalysis of the reaction: H+ + (9R,10S)-dihydroxystearate + O2 + NADPH <=> 9,10,18-trihydroxystearate + H2O + NADP
Catalysis of the reaction: indole-3-acetate + S-adenosyl-L-methionine  <=> methyl (indol-3-yl)acetate + S-adenosyl-L-homocysteine
Catalysis of the reaction: 4-chloro-2-methylphenoxyacetate + 2-oxoglutarate + O2 <=> 4-chloro-2-methylphenol + 2-oxo monocarboxylic acid anion + succinate + carbon dioxide
Catalysis of the reaction: H+ + 3-chlorotoluene + NADH + O2 <=> 3-chlorobenzyl alcohol + NAD + H2O
Catalysis of the reaction: gibberellin A53 + 2-oxoglutarate + O2 = gibberellin A97 + succinate + carbon dioxide
Catalysis of the reaction: GDP-alpha-D-mannose + beta-D-fructofuranose 6-phosphate <=> mannosylfructose-phosphate + GDP
Catalysis of the reaction: 2 H+ + 2 a reduced ferredoxin + an oxidized thioredoxin = 2 an oxidized ferredoxin + a reduced thioredoxin
Catalysis of the reaction: ethyl-(2R)-methyl-(3S)-hydroxybutanoate + NADP = ethyl-2-methylacetoacetate + NADPH + H+
Catalysis of the reaction: (Kdo)2-lipid A + 2 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,poly-cis-undecaprenyl phosphate  = (beta-L-Ara4N)2-(KDO)2-lipid A + 2 ditrans,polycis-undecaprenyl phosphate
Catalysis of the reaction: ATP + H+ + a tRNA uridine34 + a [TusE sulfur carrier protein]-S-sulfanylcysteine = AMP + diphosphoric acid + a tRNA 2-thiouridine34 + a [TusE sulfur carrier protein]-L-cysteine
Catalysis of the reaction: 1-deoxy-D-xylulose + ATP <=> H+ + 1-deoxy-D-xylulose 5-phosphate + ADP
Catalysis of the reaction: ITP + H2O <=> H+ + IDP + hydrogenphosphate
Catalysis of the reaction: XTP + H2O <=> H+ + XDP + monophosphate.
Catalysis of the reaction: n H2O + a 1,4-alpha-D-glucan = alpha-maltohexaose + a 1,4-alpha-D-glucan
Catalysis of the reaction: beta-D-fructofuranose 1-phosphate + H2O <=> beta-D-fructofuranose + hydrogenphosphate
Catalysis of the reaction: FMN + H2O = riboflavin + hydrogenphosphate
Catalysis of the reaction: a peptidoglycan dimer (generic) = a lipid II + GlcNAc-1,6-anhydro-MurNAc-pentapeptide
Catalysis of the reaction: H+ + methylglyoxal + NADH = hydroxyacetone + NAD
Catalysis of the reaction: L-alanyl-D-glutamate = L-alanyl-L-glutamate
Catalysis of the reaction: D-glycerate + NAD <=> H+ + 2-hydroxy-3-oxopropanoate + NADH
Catalysis of the reaction: alpha-lactose = beta-(1->6)-galactobiose
Catalysis of the reaction: 3 H+ + methyl-1,4-benzoquinone + NADPH = methyl-1,4-benzoquinol + NADP
Catalysis of the reaction: 5 H+ + NADH + a menaquinone <=> 4 H+ + NAD + a menaquinol
Catalysis of the reaction: sn-glycerol 3-phosphate + NADP = H+ + L-glyceraldehyde 3-phosphate + NADPH
Catalysis of the reaction: 2 S-adenosyl-L-methionine  + a [ribosomal protein S12] L-aspartate89 + a sulfurated [sulfur carrier] + a reduced electron acceptor = S-adenosyl-L-homocysteine  + L-methionine  + 5'-deoxyadenosine + 2 H+ + a [ribosomal protein S12] 3-methylthio-L-aspartate89 + an unsulfurated [sulfur carrier] + an oxidized electron acceptor
Catalysis of the reaction: H2O + an aldose + an oxidized electron acceptor = H+ + an aldonate + a reduced electron acceptor
Catalysis of the reaction: hydroxidodioxidosulfidosulfate + a reduced thioredoxin = sulfite + hydrogen sulfide + H+ + an oxidized thioredoxin
Catalysis of the reaction: 4-hydroxy-L-threonine <=> glycolaldehyde + glycine
Catalysis of the reaction: 5-phosphonato-alpha-D-ribose cyclic-1,2-phosphate + H2O <=> H+ + alpha-D-ribose 1,5-bisphosphate
Catalysis of the reaction: L-glutamate + ATP + a [protein] C-terminal L-glutamate = ADP + hydrogenphosphate + H+ + a [protein] with C-terminal alpha-L-glutamate-alpha-L-glutamate
Catalysis of the reaction: L-methionine  + acetyl-CoA = N-acetyl-L-methionine + coenzyme A + H+
Catalysis of the reaction: L-alanyl-L-glutamate + H2O <=> L-alanine + L-glutamate
Catalysis of the reaction: methyl beta-D-glucoside 6-phosphate + H2O = beta-D-glucose 6-phosphate + methanol
Catalysis of the reaction: 2 S-adenosyl-L-methionine  + an adenine37 in tRNA <=> S-adenosyl-L-homocysteine  + L-methionine  + 5'-deoxyadenosine + a 2-methyladenine37 in tRNA
Catalysis of the reaction: isobutanol + NADP <=> isobutyraldehyde + NADPH + H+
Catalysis of the reaction: 1-methyladenine + O2 + 2-oxoglutarate <=> adenine + carbon dioxide + formaldehyde + succinate
Catalysis of the reaction: N3-methylcytosine + O2 + 2-oxoglutarate <=> H+ + cytosine + carbon dioxide + formaldehyde + succinate
Catalysis of the reaction: 1-ethyladenine + O2 + 2-oxoglutarate(2-) <=> adenine + carbon dioxide + acetaldehyde + succinate
Catalysis of the reaction: gibberellin A12 + O2 + 2-oxoglutarate <=> gibberellin A15 + carbon dioxide + succinate
Catalysis of the reaction: gibberellin A15 + 2-oxoglutarate + O2 <=> gibberellin A24 + succinate + carbon dioxide + H2O
Catalysis of the reaction: gibberellin A53 + O2 + 2-oxoglutarate <=> gibberellin A44 diacid + carbon dioxide + succinate
Catalysis of the reaction: gibberellin A19 + O2 + 2-oxoglutarate <=> H+ + gibberellin A20 + 2 carbon dioxide + succinate
Catalysis of the reaction: kaempferol 3-O-glucoside + UDP-L-rhamnose <=> kaempferol-3-glucoside-7-rhamnoside + UDP
Catalysis of the reaction: kaempferol oxoanion + UDP-L-rhamnose <=> H+ + kaempferol-3-rhamnoside + UDP(3-)
Catalysis of the reaction: kaempferol-3-rhamnoside + UDP-L-rhamnose <=> kaempferol-3-rhamnoside-7-rhamnoside + UDP.
Catalysis of the reaction: ATP(4-) + H2O + a trans-methoxy-C60-meroacyl-[acp] <=> diphosphoric acid + a trans-methoxy-meroacyl-adenylate + a holo-[acyl-carrier protein]
Catalysis of the reaction: ATP(4-) + H2O + a cis-keto-C60-meroacyl-[acp] <=> diphosphoric acid + a cis-keto-meroacyl-adenylate + a holo-[acyl-carrier protein]
Catalysis of the reaction: ATP(4-) + H2O + a trans-keto-C61-meroacyl-[acp] <=> diphosphoric acid + a trans-keto-meroacyl-adenylate + a holo-[acyl-carrier protein]
Catalysis of the reaction: GDP-alpha-D-mannose + an inositol-phospho-alpha hydroxyphytoceramide = H+ + GDP + a mannosyl-inositol-phospho-alpha hydroxyphytoceramide
Catalysis of the reaction: 4alpha-carboxy-4beta-methyl-5alpha-cholesta-8-en-3beta-ol + NAD(P) = 4alpha-methyl-5alpha-cholesta-8-en-3-one + carbon dioxide + NAD(P)H
Catalysis of the reaction: 4alpha-carboxy-5alpha-cholesta-8-en-3beta-ol + NAD(P) = 5alpha-cholesta-8-en-3-one + carbon dioxide + NAD(P)H
Catalysis of the reaction: leukotriene C4 + a standard alpha amino acid = leukotriene D4 + an (gamma-L-glutamyl)-L-amino acid
Catalysis of the reaction: 17alpha-hydroxyprogesterone + NADPH + H+ + O2 <=> NADP + H2O + 11-deoxycortisol
Catalysis of the reaction: a 2-hydroxy-3-methyl-branched 2,3,4-saturated fatty acyl-CoA <=> formyl-CoA + a 2-methyl branched 2,3,4-saturated fatty aldehyde
Catalysis of the reaction: a (R)-2-hydroxy even numbered straight chain 2,3,4-saturated fatty acyl CoA = formyl-CoA + an odd numbered straight chain 2,3,4-saturated fatty aldehyde
Catalysis of the reaction: anandamide + H2O <=> arachidonate + ethanolaminium(1+)
Catalysis of the reaction: NAD + D-glucopyranose 6-phosphate = NADH + H+ + 3-dehydro-D-glucose 6-phosphate
Catalysis of the reaction: 3-(indol-3-yl)pyruvate + NADPH + O2 + H+ <=> indole-3-acetate + carbon dioxide + NADP + H2O
Catalysis of the reaction: quercetin-3-glucoside + UDP-L-rhamnose <=> quercetin-3-O-glucoside-7-O-rhamnoside + UDP
Catalysis of the reaction: H+ + quercetin 3-O-rhamnoside + UDP-L-rhamnose <=> quercetin-3-rhamnoside-7-rhamnoside + UDP
Catalysis of the reaction: 5-methylthio-2-oxopentanoate + acetyl-CoA + H2O <=> H+ + 2-(3-methylthiopropyl)malate + coenzyme A
Catalysis of the reaction: 2-(3-methylthiopropyl)malate(2-) <=> 3-(3'-methylthio)propylmalate
Catalysis of the reaction: 3-(3'-methylthio)propylmalate <=> H+ + 2-oxo-6-methylthiohexanoate + carbon dioxide
Catalysis of the reaction: 2-oxo-6-methylthiohexanoate + acetyl-CoA + H2O <=> H+ + 2-(4'-methylthio)butylmalate + coenzyme A
Catalysis of the reaction: 2-(4'-methylthio)butylmalate <=> 3-(4'-methylthio)butylmalate
Catalysis of the reaction: 3-(4'-methylthio)butylmalate <=> H+ + 2-oxo-7-methylthioheptanoate + carbon dioxide
Catalysis of the reaction: 2-oxo-7-methylthioheptanoate + acetyl-CoA + H2O <=> H+ + 2-(5'-methylthio)pentylmalate + coenzyme A
Catalysis of the reaction: 2-(5'-methylthio)pentylmalate <=> 3-(5'-methylthio)pentylmalate
Catalysis of the reaction: 3-(5'-methylthio)pentylmalate <=> H+ + 2-oxo-8-methylthiooctanoate + carbon dioxide
Catalysis of the reaction: 2-oxo-8-methylthiooctanoate + acetyl-CoA + H2O <=> H+ + 2-(6'-methylthio)hexylmalate + coenzyme A
Catalysis of the reaction: 2-(6'-methylthio)hexylmalate <=> 3-(6'-methylthio)hexylmalate
Catalysis of the reaction: 3-(6'-methylthio)hexylmalate <=> H+ + 2-oxo-9-methylthiononanoate + carbon dioxide
Catalysis of the reaction: 2-oxo-9-methylthiononanoate + acetyl-CoA + H2O <=> H+ + 2-(7'-methylthio)heptylmalate + coenzyme A
Catalysis of the reaction: 2-(7'-methylthio)heptylmalate <=> 3-(7'-methylthio)heptylmalate
Catalysis of the reaction: 3-(7'-methylthio)heptylmalate <=> H+ + 2-oxo-10-methylthiodecanoate + carbon dioxide
Catalysis of the reaction: a very long chain alcohol + a long-chain acyl-CoA <=> coenzyme A(4-) + a wax ester
Catalysis of the reaction: dihomomethionine + 2 O2 + 2 NADPH + 2 H+ <=> 5-methylthiopentanaldoxime + 3 H2O + carbon dioxide + 2 NADP
Catalysis of the reaction: trihomomethionine + 2 O2 + 2 NADPH + 2 H+ <=> 3 H2O + carbon dioxide + 2 NADP + 6-methylthiohexanaldoxime
Catalysis of the reaction: 2 H+ + tetrahomomethionine + 2 O2 + 2 NADPH <=> 3 H2O + carbon dioxide + 2 NADP + 7-methylthioheptanaldoxime
Catalysis of the reaction: UDP-alpha-D-glucose + 5-methylthiopentylhydroximate <=> H+ + 4-methylthiobutyldesulfoglucosinolate + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + 6-methylthiohexylhydroximate <=> H+ + 5-methylthiopentyldesulfoglucosinolate + UDP(3-)
Catalysis of the reaction: UDP-alpha-D-glucose + 7-methylthioheptylhydroximate <=> H+ + 6-methylthiohexyldesulfoglucosinolate + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + 8-methylthiooctylhydroximate <=> H+ + 7-methylthioheptyldesulfoglucosinolate + UDP
Catalysis of the reaction: UDP-alpha-D-glucose + 9-methylthiononylhydroximate <=> 8-methylthiooctyldesulfoglucosinolate + UDP + H+
Catalysis of the reaction: 6-methylthiohexyldesulfoglucosinolate + 3'-phosphonato-5'-adenylyl sulfate <=> adenosine 3',5'-bismonophosphate + H+ + 6-methylthiohexylglucosinolate
Catalysis of the reaction: 2-oxo-6-methylthiohexanoate + a standard alpha amino acid <=> dihomomethionine + a 2-oxo carboxylate
Catalysis of the reaction: brassinolide + UDP-alpha-D-glucose <=> brassinolide-23-O-glucoside + UDP + H+
Catalysis of the reaction: castasterone + UDP-alpha-D-glucose <=> castasterone-23-O-glucoside + UDP + H+
Catalysis of the reaction: a [PTS enzyme I]-Npi-phospho-L-histidine + D-glucosamine <=> D-glucosamine 6-phosphate + a [PTS enzyme I]-L-histidine
Catalysis of the reaction: glucosyl-oleandomycin + ATP + H2O <=> glucosyl-oleandomycin + ADP + hydrogenphosphate + H+
Catalysis of the reaction: ATP + H2O + heme b <=> hydrogenphosphate + ADP + H+ + heme b
Catalysis of the reaction: alpha-D-galactofuranose + ATP + H2O <=> alpha-D-galactofuranose + hydrogenphosphate + ADP + H+
Catalysis of the reaction: UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetylglucosamine(2-) + H2O <=> UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine(1-) + acetate
Catalysis of the reaction: UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine(1-) + an (3R)-3-hydroxymyristoyl-[acp] <=> UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + H+ + a holo-[acyl-carrier protein]
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 environmental stimulus.
A function that was not selected for in the evolution of an organism, but arises from co-option by another organism, e.g. a human protein used as a virus receptor.
Uptake of hexoses, notably D-glucose, fructose, and galactose, into the blood by absorption from the small intestine.
A protein complex that binds to, and promotes stabilization of, mRNA molecules containing the major coding region instability determinant (mCRD) by bridging the mCRD domain and the poly(A) tail of the mRNA. In human, it consists of CSDE1, HNRPD, PABPC1, PAIP1 and SYNCRIP.
A protein complex that binds to, and promotes stabilization of, mRNA molecules containing the major coding region instability determinant (mCRD) by bridging the mCRD domain and the poly(A) tail of the mRNA. In human, it consists of CSDE1, HNRPD, PABPC1, PAIP1 and SYNCRIP.
A protein complex that binds to, and promotes stabilization of, mRNA molecules containing the major coding region instability determinant (mCRD) by bridging the mCRD domain and the poly(A) tail of the mRNA. In human, it consists of CSDE1, HNRPD, PABPC1, PAIP1 and SYNCRIP.
A protein complex that binds to, and promotes stabilization of, mRNA molecules containing the major coding region instability determinant (mCRD) by bridging the mCRD domain and the poly(A) tail of the mRNA. In human, it consists of CSDE1, HNRPD, PABPC1, PAIP1 and SYNCRIP.
A protein complex that binds to, and promotes stabilization of, mRNA molecules containing the major coding region instability determinant (mCRD) by bridging the mCRD domain and the poly(A) tail of the mRNA. In human, it consists of CSDE1, HNRPD, PABPC1, PAIP1 and SYNCRIP.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. Forms dimers and multimers of amyloid beta peptide 40 and peptide 42 (proteolytic cleavage products of amyloid beta A4 protein, also known as amyloid beta precursor protein). Mostly found in the extracellular space with a proportion occurring as membrane-bound species. Influences synaptic plasticity through various receptors, mediates dendritic spine loss leading to decreased synapse density, inhibits long-term potentiation (LTP) and enhances long-term depression (LTD). Soluble multimeric form is the main pathogenic species linked to Alzheimer's disease.
The process whereby a guanine in a tRNA is methylated at the N7 position of guanine.
The process whereby a guanine in 5-cap is methylated at the N7 position of guanine.
The binding activity that attaches a microtubule to the cell cortex.
Any process in which a microtubule is maintained in a specific location at the cell tip by attachment to the cell cortex.
Catalysis of the reaction: 2-oxoglutaramate + H(2)O = 2-oxoglutarate + NH(3).
Catalysis of the reaction:(4S)-4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate.
Any process that regulates the localization of a protein to the medial cortex.
Any process that activates or increases the frequency, rate or extent of protein localization to the medial cortex.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to the cell cortex of the cell tip.
Any process that modulates the frequency, rate or extent of the inflammatory response to wounding.
Any process that stops, prevents, or reduces the frequency, rate or extent of the inflammatory response to wounding.
Any process that activates or increases the frequency, rate or extent of the inflammatory response to wounding.
Catalysis of the reaction: 1-phosphatidyl-myo-inositol 3,4-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol phosphate + phosphate.
Catalysis of the reaction: 1-phosphatidyl-myo-inositol 3,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol phosphate + phosphate.
Catalysis of the reaction: 1-phosphatidyl-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol phosphate + phosphate.
Any process that modulates the frequency, rate or extent of vesicle docking.
Any process that stops, prevents, or reduces the frequency, rate or extent of vesicle docking.
Any process that activates or increases the frequency, rate or extent of vesicle docking.
Any process that modulates the onset of pupariation.
Any process that stops, prevents or reduces the rate of onset of pupariation.
Any process that activates or increases the frequency, rate or extent of onset of pupariation.
Catalysis of the hydrolysis of misacylated Gly-tRNA(Ala).
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 neuron, e.g. an axon, or a dendrite.
The organization process which results in the disassembly (either partial or complete) of constituent parts of a neuron projection. A neuron projection is a prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
Catalysis of the reaction: tRNA uridine = tRNA pseudouridine. Conversion of uridine in a tRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
The collection of neuronal projections into a bundle of rods, known as a fascicle.
Catalysis of the reaction: an snRNA uridine = an snRNA pseudouridine. Conversion of uridine in an snRNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5.
A type of synapse occurring between an axon and a dendritic spine.
The transfer of an assembled [2Fe-2S] cluster from a scaffold protein to an acceptor protein that contributes to the attainment of the full functional capacity of a protein.
The transfer of an assembled 4Fe-4S] cluster from a scaffold protein to an acceptor protein that contributes to the attainment of the full functional capacity of a protein.
A process which results in the assembly or arrangement of constituent parts apicomedial cortex actomyosin.
The region that lies just beneath the plasma membrane in the middle of the apical edge of a cell.
Any process that modulates the frequency, rate or extent of GABA-A receptor activity.
Any process that activates or increases the frequency, rate or extent of GABA-A receptor activity.
Any process that stops, prevents or reduces the frequency, rate or extent of GABA-A receptor activity.
The removal of a sugar or dicarbonyl from a glycated guanine.
The removal of methylglyoxal from a glycated guanine, to form lactate and a deglycated guanine.
The removal of glyoxal from a glycated guanine, to form glycolate and a deglycated guanine.
The modification of acetylpolyamine by the removal of acetyl groups.
The modification of acetylspermadine by the removal of acetyl groups.
Any process that modulates the frequency, rate or extent of the cellular response to osmotic stress.
Catalysis of the reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing a 2'-O-nucleotide.
Catalysis of the reaction: uridine34 in tRNA + a [TusE sulfur carrier protein]-S-sulfanylcysteine + ATP + a reduced electron acceptor = a 2-thiouridine34 in tRNA + a [TusE sulfur carrier protein]-L-cysteine + AMP + an oxidized electron acceptor + diphosphate + H+.
Catalysis of the reaction: uridine34 in tRNA + a [TusE sulfur carrier protein]-S-sulfanylcysteine + ATP + a reduced electron acceptor = a 2-thiouridine34 in tRNA + a [TusE sulfur carrier protein]-L-cysteine + AMP + an oxidized electron acceptor + diphosphate + H+.
A protein complex capable of catalysing the hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in an oligo-mannose oligosaccharide.
Any process that modulates the frequency, rate or extent of calcineurin-mediated signaling.
Any process that stops, prevents or reduces the frequency, rate or extent of calcineurin-mediated signalling.
Any process that activates or increases the frequency, rate or extent of calcineurin-mediated signaling.
Catalysis of the reaction: S-adenosyl-L-methionine + cytidine56 in tRNA= S-adenosyl-L-homocysteine + 2'-O-methylcytidine56 in tRNA
Any process that modulates the frequency, rate or extent of exit from mitosis.
Any process that stops, prevents or reduces the frequency, rate or extent of exit from meiosis.
Any process that activates or increases the frequency, rate or extent of exit from meiosis.
Combining with folate and transmitting the signal from one side of the membrane to the other by activating an associated G-protein, initiating a change in cell activity.
Combining with folate and transmitting the signal from one side of the membrane to the other by activating an associated G-protein, initiating a change in cell activity.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
A protein ligase complex that enables protein sumoylation. Consists of a SUMO-protein transferase and other proteins that may confer substrate specificity of the complex.
A protein ligase complex that enables protein sumoylation. Consists of a SUMO-protein transferase and other proteins that may confer substrate specificity of the complex.
A protein ligase complex that enables protein sumoylation. Consists of a SUMO-protein transferase and other proteins that may confer substrate specificity of the complex.
A SUMO-E3 ligase complex capable of promoting synapsis, the meiotic cell cycle process where side by side pairing and physical juxtaposition of homologous chromosomes is created during meiotic prophase.
Any process that modulates the frequency, rate or extent of an adenylate cyclase-activating G protein-coupled receptor signaling pathway
Any process that activates or increases the frequency, rate or extent of an adenylate cyclase-activating G protein-coupled receptor signaling pathway.
Any process that stops, prevents or reduces the frequency, rate or extent of an adenylate cyclase-activating G protein-coupled receptor signaling pathway.
Catalysis of the addition of the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation; the transfer of glucose from dolichyl phosphate glucose (Dol-P-Glc) on to the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Any process which detects an amino-acid acetylated tRNA is charged with the correct amino acid, or removes incorrect amino acids from a charged tRNA. This process can be performed by tRNA synthases, or by subsequent reactions after tRNA aminoacylation.
Any process which detects an amino-acid acetylated tRNA is charged with the correct amino acid, or removes incorrect amino acids from a charged tRNA. This process can be performed by tRNA synthases, or by subsequent reactions after tRNA aminoacylation.
Any process which detects an amino-acid acetylated tRNA is charged with the correct amino acid, or removes incorrect amino acids from a charged tRNA. This process can be performed by tRNA synthases, or by subsequent reactions after tRNA aminoacylation.
Catalysis of the acetylation of an amino acid residue of a peptide or protein, according to the reaction: succinyl-CoA + peptide = CoA + N-succinylpeptide.
Catalysis of the reaction: succinyl-CoA + lysine in peptide = CoA + N-succinyl-lysine-peptide.
The modification of a histone by the addition of an succinyl group.
Catalysis of the reaction: succinyl-CoA + histone = CoA + succinyl-histone.
Interacting selectively and non-covalently with the GATOR1 complex.
The directed movement of maltose from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of sucrose from outside of a cell, across the plasma membrane and into the cytosol.
Any protein complex that is part of the nuclear membrane.
A protein complex capable of interacting with the spindle pole body and the nuclear envelope, in order to embed the spindle pole body in the nuclear envelope at fusion sites of the inner and outer nuclear membrane.
Any process that modulates the frequency, rate or extent of cell adhesion involved in sprouting angiogenesis.
Any process that stops, prevents or reduces the frequency, rate or extent of cell adhesion involved in sprouting angiogenesis.
Any process that activates or increases the frequency, rate or extent of cell adhesion involved in sprouting angiogenesis.
The process of creating an elongation or projection from a glial cell.
The extension of a glial cell process or projection to wrap around an axon.
A plant complex involved in basal disease resistance and resistance (R) gene-mediated effector triggered immunity (ETI). Regulates accumulation of the hormone salicylic acid (SA) which is a necessary component of systemic immunity. Involved in responds to bacteria, viruses and oomycetes.
A plant complex involved in basal disease resistance and resistance (R) gene-mediated effector triggered immunity (ETI). Regulates accumulation of the hormone salicylic acid (SA) which is a necessary component of systemic immunity. Involved in responds to bacteria, viruses and oomycetes.
A plant complex involved in basal disease resistance and resistance (R) gene-mediated effector triggered immunity (ETI). Regulates accumulation of the hormone salicylic acid (SA) which is a necessary component of systemic immunity. Involved in responds to bacteria, viruses and oomycetes.
A nuclear membrane protein complex which connects the nuclear outer and inner membranes together, and links thereby links the nuclear lumen to cytoplasmic microtubules.
A homodimeric protein complex that catalyzes the reaction: 7-methylguanosine-5'-triphospho-5'-pholynucleotide + H20 = 7-methylguanosine-5'-phosphate + polynucleotide.
A homodimeric protein complex that catalyzes the reaction: 7-methylguanosine-5'-triphospho-5'-pholynucleotide + H20 = 7-methylguanosine-5'-phosphate + polynucleotide.
A homodimeric protein complex that catalyzes the reaction: 7-methylguanosine-5'-triphospho-5'-pholynucleotide + H20 = 7-methylguanosine-5'-phosphate + polynucleotide.
A homodimeric protein complex that catalyzes the reaction: 7-methylguanosine-5'-triphospho-5'-pholynucleotide + H20 = 7-methylguanosine-5'-phosphate + polynucleotide.
A homodimeric protein complex that catalyzes the reaction: 7-methylguanosine-5'-triphospho-5'-pholynucleotide + H20 = 7-methylguanosine-5'-phosphate + polynucleotide.
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 ceramide 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 ceramide stimulus.
A protein complex that acts both as N-acetylglutamate synthase (NAGS) catalysing the production of N-Acetylglutamate from glutamate and acetyl-CoA, and as N-acetylglutamate kinase (NAGK) catalysing the reaction ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate.
Catalysis of the reaction 2-dehydro-3-deoxy-L-rhamnonate = pyruvate + (S)-lactaldehyde.
Catalysis of the cyclization of geranylgeranyl pyrophosphate (GGPP) to yield the monocyclic diterpene beta-pinacene.
A process in which a protein is transported to, or maintained at, a location in a peroxisome via the endoplasmic reticulum.
A protein complex that resides in the cis-golgi membrane and plays a role in the tethering of COPII vesicles, through an interaction with vesicle tethering proteins (p115 in H. Sapiens and Uso1 S. cerevisiae), granting the cis-Golgi and endoplasmic reticulum to Golgi vesicle-mediated transport. It is composed by GRASP65 and GM130 protein in H. sapiens and by Bug1 and Grh1 proteins in S. cerevisiae.
A protein complex that resides in the cis-golgi membrane and plays a role in the tethering of COPII vesicles, through an interaction with vesicle tethering proteins (p115 in H. Sapiens and Uso1 S. cerevisiae), granting the cis-Golgi and endoplasmic reticulum to Golgi vesicle-mediated transport. It is composed by GRASP65 and GM130 protein in H. sapiens and by Bug1 and Grh1 proteins in S. cerevisiae.
Any process that modulates the frequency, rate or extent of glutamate receptor clustering.
Catalysis of the hydrolysis of misacylated ala-tRNA(thr).
The process by which heat is generated by increasing metabolism in response to cold ambient temperatures in order to maintain a stable core body temperature.
Any process that modulates the frequency, rate or extent of (R)-mevalonic acid biosynthetic process
Any process that stops, prevents or reduces the frequency, rate or extent of (R)-mevalonic acid biosynthetic process
Any process that activates or increases the frequency, rate or extent of (R)-mevalonic acid biosynthetic process
The chemical reactions and pathways resulting in the formation of type B trichothecene vomitoxin, a poisonous substance produced by some species of fungi and predominantly occurs in grains such as wheat, barley and oats.
The chemical reactions and pathways resulting in the formation of type B trichothecene vomitoxin, a poisonous substance produced by some species of fungi and predominantly occurs in grains such as wheat, barley and oats.
The chemical reactions and pathways resulting in the formation of type B trichothecene vomitoxin, a poisonous substance produced by some species of fungi and predominantly occurs in grains such as wheat, barley and oats.
The chemical reactions and pathways resulting in the formation of type B trichothecene vomitoxin, a poisonous substance produced by some species of fungi and predominantly occurs in grains such as wheat, barley and oats.
The chemical reactions and pathways resulting in the formation of type B trichothecene vomitoxin, a poisonous substance produced by some species of fungi and predominantly occurs in grains such as wheat, barley and oats.
The chemical reactions and pathways resulting in the formation of type B trichothecene vomitoxin, a poisonous substance produced by some species of fungi and predominantly occurs in grains such as wheat, barley and oats.
Any process that modulates the frequency, rate or extent of mitotic cohesin ssDNA (lagging strand) loading.
Any process that stops, prevents or reduces the frequency, rate or extent of mitotic cohesin ssDNA (lagging strand) loading.
Any process that activates or increases the frequency, rate or extent of mitotic cohesin ssDNA (lagging strand) loading.
Any process that modulates the frequency, rate or extent of mitotic cohesin dsDNA (leading strand) loading.
Any process that stops, prevents or reduces the frequency, rate or extent of mitotic cohesin dsDNA (leading strand) loading.
Any process that activates or increases the frequency, rate or extent of mitotic cohesin dsDNA (leading strand) loading.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an acidocalcisome. An acidocalcisome is an electron-dense acidic membrane-bounded organelle which contains a matrix of pyrophosphate and polyphosphates with bound calcium and other cations.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an acidocalcisome. An acidocalcisome is an electron-dense acidic membrane-bounded organelle which contains a matrix of pyrophosphate and polyphosphates with bound calcium and other cations.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an acidocalcisome. An acidocalcisome is an electron-dense acidic membrane-bounded organelle which contains a matrix of pyrophosphate and polyphosphates with bound calcium and other cations.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an acidocalcisome. An acidocalcisome is an electron-dense acidic membrane-bounded organelle which contains a matrix of pyrophosphate and polyphosphates with bound calcium and other cations.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an acidocalcisome. An acidocalcisome is an electron-dense acidic membrane-bounded organelle which contains a matrix of pyrophosphate and polyphosphates with bound calcium and other cations.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an acidocalcisome. An acidocalcisome is an electron-dense acidic membrane-bounded organelle which contains a matrix of pyrophosphate and polyphosphates with bound calcium and other cations.
Any process that modulates the frequency, rate or extent of a sterol biosynthetic process.
Any process that stops, prevents or reduces the frequency, rate or extent of a sterol biosynthetic process.
Any process that activates or increases the frequency, rate or extent of a sterol biosynthetic process.
Any process that activates or increases the frequency, rate or extent of a cobalamin metabolic process.
Any process that stops, prevents or reduces the frequency, rate or extent of a cobalamin metabolic process.
A large membrane-bound endocytic organelle present only in members of the Schizotrypanum subgenus of the Trypanosoma genus and is defined as the site of storage of endocytosed macromolecules and lysosomal enzymes. It is found at the posterior end of epimastigote forms of Trypanosoma cruzi, but absent in amastigotes and trypomastigotes.
The volume enclosed by the membranes of a reservosome.
A matrix composed of planar membranes, vesicles and lipid inclusions within the reservosome.
The lipid bilayer surrounding a reservosome.
Any process that stops, prevents or reduces the frequency, rate or extent of store-operated calcium entry.
Any process that activates or increases the frequency, rate or extent of store-operated calcium entry.
Catalysis of the reaction: RMP + diphosphate = R + 5-phospho-alpha-D-ribose 1-diphosphate.
Any process that activates or increases the frequency, rate or extent of cardiac muscle cell contraction.
Any process that stops, prevents, or reduces the frequency, rate or extent of cardiac muscle cell contraction.
The process in which an organism effects a change in the structure or function of a symbiont organism, mediated by secretion of lectins which bind to the bacterial surface. The symbiont is defined as the smaller of the organisms involved in a symbiotic interaction.
Interacting selectively and non-covalently with the IkappaB kinase complex.
Interacting selectively and non-covalently with a Sec61 translocon complex.
The cell surface of a secondary, endosymbiont organism with which the first organism is interacting. The symbiont is defined as the smaller of the organisms involved in a symbiotic interaction.
Interacting selectively and non-covalently with the P-TEFb complex.
Catalysis of the reaction: dimethylallylphosphate + FMNH2 = prenylated FMNH2 + phosphate.
Catalysis of the reaction:  S-adenosyl-L-methionine + adenine(645) in 25S rRNA = S-adenosyl-L-homocysteine + N(1)-methyladenine(645) in 25S rRNA.
Catalysis of the reaction:  S-adenosyl-L-methionine + adenine(645) in 25S rRNA = S-adenosyl-L-homocysteine + N(1)-methyladenine(645) in 25S rRNA.
A protein complex involved in the catalysis of the formation of the modified nucleotide 7-methylguanine (at position 46 in certain tRNAs, such as tRNA(phe) and tRNA(met). In yeast, it is a heterotetramer of two subunits, Trm8 (catalytic) and Trm82 (WD repeat).
A protein complex involved in the catalysis of the formation of the modified nucleotide 7-methylguanine (at position 46 in certain tRNAs, such as tRNA(phe) and tRNA(met). In yeast, it is a heterotetramer of two subunits, Trm8 (catalytic) and Trm82 (WD repeat).
A protein complex involved in the catalysis of the formation of the modified nucleotide 7-methylguanine (at position 46 in certain tRNAs, such as tRNA(phe) and tRNA(met). In yeast, it is a heterotetramer of two subunits, Trm8 (catalytic) and Trm82 (WD repeat).
Catalyzes the reaction fraxetin+ NAD(P)H + 02= sideretin + NAD(P)(+) + H20.
Catalyzes of the reaction: scopoletin + 2-oxoglutarate+O2=fraxetin +succinate+ CO2).
The chemical reactions and pathways resulting in the formation of sideretin.
The chemical reactions and pathways resulting in the formation of fraxetin.
The chemical reactions and pathways resulting in the formation of 4-hydroxyindole-3- carbonyl nitrile (4-OH-ICN), a cyanogenic glucoside.
Catalysis of the reaction: indole-3-carbonyl nitrile + NADPH +O2=4-hydroxyindole-3- carbonyl nitrile + NADP(+) + H20.
The chemical reactions and pathways resulting in the formation of zearalenone, a mycotoxin produced by several Fusarium species, is most commonly found as a contaminant in stored grain and has chronic estrogenic effects on mammals.
nteracting selectivity and noncovalently with a cyclic nucleotide mimicking protein motif that is part of the same protein. The CNBHD is a domain on KCNH channels that creates a binding pocket on the KCNH channel that resembles the cyclic nucleotide- binding domain on other ion channels. It binds to a peptide motif that is part of the same protein rather than a cyclic nucleotide.
Interacting selectively and non-covalently with a histone in which a residue has been modified by phosphorylation. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes.
The process of producing flask-shaped fruiting bodies, called perithecia. In the ascomycetous fungi such as Neurospora crassa and Sordaria macrospora, these perithecia are formed in the sexual phase and they discharge ascospores through the ostiolum at the tip of the perithecial neck.
A bacterial protein complex that neutralises its own toxin by complexing the toxin with the antitoxin. The antitoxin can be either a protein or an RNA. The neutralising toxin-antitoxin complex also acts as a transcriptional repressor of the toxin-antitoxin operon.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving tRNA methylation.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving tRNA C5-cytosine methylation.
Any process that activates or increases the frequency, rate or extent of tRNA methylation.
Any process that activates or increases the frequency, rate or extent of tRNA C5-cytosine methylation.
Shortening of the poly(A) tail of a nuclear-transcribed ncRNA.
A process that results in the assembly, arrangement of constituent parts, or disassembly of a formin-nucleated actin cable.
The controlled release of proteins from a cell at the sides which interface adjacent cells and near the base.
Any process that modulates the frequency, rate or extent of the assembly, disassembly or arrangement of constituent parts of the basement membrane.
Any process in which a protein is transported to, or maintained at, a P-body.
Any process in which a protein is transported to, or maintained at, a P-body.
Any process in which a protein is transported to, or maintained at, a P-body.
Any process that increases the frequency, rate or extent of aggregation involved in sorocarp development. Aggregation involved in sorocarp development is 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.
Any process that decreases the frequency, rate or extent of aggregation involved in sorocarp development. Aggregation involved in sorocarp development is 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.
Any process that activates or increases the frequency, rate or extent of elastin catabolism, the chemical reactions and pathways resulting in the breakdown of elastin.
A chromatin remodeling complex that positively regulates histone H3 acetylation, in particular H3K9, by recruiting histone acetyltransferases to rDNA gene regions. Located in the nucleolus where it assembles on RNA Polymerase I (Pol I) and possibly on RNA Polymerase III (Pol III) promoter and coding regions during early G1 phase and activates the post-initiation phases of Pol I transcription. May also activate RNA Polymerase II (Pol II) gene transcription. In mammals, B-WICH contains the WICH complex core of BAZ1B and SMARCA5, additional protein subunits and possibly rRNAs. Although it contains several catalytic subunits it is not clear which functions are carried out by the complex itself.
The process where translation initiation recruits the 40S ribosomal subunits in a cap and 5' end independent fashion before an AUG codon is encountered in an appropriate sequence context to initiate linear mRNA translation.
The process where translation initiation recruits the 40S ribosomal subunits in a cap and 5' end independent fashion before an AUG codon is encountered in an appropriate sequence context to initiate circRNA translation.
The process where translation initiation recruits the 40S ribosomal subunits via an internal ribosome entry segment (IRES) before an AUG codon is encountered in an appropriate sequence context to initiate circular mRNA translation.
Any process that modulates the frequency, rate or extent of the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures containing both actin and myosin or paramyosin.
The multiplication or reproduction of cardiac muscle myoblasts, resulting in the expansion of a cardiac muscle myoblast cell population.  A cardiac myoblast is a precursor cell that has been committed to a cardiac muscle cell fate but retains the ability to divide and proliferate throughout life.
Any process that modulates the frequency, rate or extent of cardiac muscle myoblast proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of cardiac muscle myoblast proliferation.
Any process that activates or increases the frequency, rate or extent of cardiac muscle myoblast proliferation.
The 5' to 3' exonucleolytic resection of DNA at the site of a stalled replication fork that contributes to replication fork processing.
Any process that modulates the frequency, rate or extent of DNA strand resection involved in replication fork processing.
Any process that stops, prevents, or reduces the frequency, rate or extent of DNA strand resection involved in replication fork processing.
Any process that activates or increases the frequency, rate or extent of mitotic spindle organization.
Any process that stops, prevents, or reduces the frequency, rate or extent of meiosis I, a cell cycle process comprising the steps by which a cell progresses through the first phase of meiosis, in which cells divide and homologous chromosomes are paired and segregated from each other, producing two daughter cells.
Any process that modulates the frequency, rate or extent of the G2/MI transition of the meiotic cell cycle, the cell cycle process in which a cell progresses from meiotic G2 phase to M phase of meiosis I.
Any process that stops, prevents, or reduces the frequency, rate or extent of the G2/MI transition of the meiotic cell cycle, the cell cycle process in which a cell progresses from meiotic G2 phase to M phase of meiosis I.
Any process that activates or increases the frequency, rate or extent of the G2/MI transition of the meiotic cell cycle, the cell cycle process in which a cell progresses from meiotic G2 phase to M phase of meiosis I.
Any process that modulates the frequency, rate or extent of the adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway, the series of molecular signals generated as a consequence of glucose binding to a G protein-coupled receptor, where the pathway proceeds with activation of adenylyl cyclase and a subsequent increase in the concentration of cyclic AMP (cAMP).
Any process that stops, prevents, or reduces the frequency, rate or extent of the adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway.
The activity of binding selectively, and in a sequence-specific manner, a replication fork barrier found in rDNA spacers, and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence.
Interacting selectively and non-covalently with the C2 domain of a protein, a protein structural domain involved in targeting proteins to cell membranes.
Any process that modulates the frequency, rate or extent of nematode male tail tip morphogenesis, the process in which the anatomical structure of the adult male tail tip is generated and organized.
Any process that stops, prevents, or reduces the frequency, rate or extent of nematode male tail tip morphogenesis.
Any process that activates or increases the frequency, rate or extent of nematode male tail tip morphogenesis.
The process in which the anatomical structures of the pharynx are generated and organized.
Any process that modulates the frequency, rate or extent of pharynx morphogenesis, the process in which the anatomical structure of the pharynx is generated and organized.
Any process that stops, prevents, or reduces the frequency, rate or extent of pharynx morphogenesis.
Any process that activates or increases the frequency, rate or extent of pharynx morphogenesis.
Any process that modulates the frequency, rate, or extent of mitotic to meiotic cell cycle switching, the process in which a cell switches cell cycle mode from mitotic to meiotic division.
Any process that stops, prevents, or reduces the frequency, rate, or extent of mitotic to meiotic cell cycle switching, the process in which a cell switches cell cycle mode from mitotic to meiotic division.
A signal transduction process that contributes to cell cycle switching, mitotic to meiotic cell cycle.
Catalysis of the reaction: N-(4-oxoglutarate)-L-cysteinylglycine + H(2)O = 2-oxoglutarate + L-cysteinylglycine
A cellular process that, through single- or multi-step enzymatic reactions, repairs useless or toxic endogenous compounds, formed as by-products of primary metabolism, by converting them into useful metabolites.
A cellular process that, through single- or multi-step enzymatic reactions, repairs toxic endogenous compounds, formed as by-products of primary metabolism, by converting them into useful metabolites.
Any process that modulates the frequency, rate or extent of actin filament organization.
Any process that modulates the frequency, rate or extent of actin filament annealing, i.e. the end-to-end joining of existing actin filaments.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament annealing, i.e. the end-to-end joining of existing actin filaments.
Any process that activates or increases the frequency, rate or extent of actin filament annealing, i.e. the end-to-end joining of existing actin filaments.
Any process that modulates the frequency, rate or extent of blood vessel endothelial cell differentiation.
Any process that activates or increases the frequency, rate or extent of blood vessel endothelial cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of blood vessel endothelial cell differentiation.
Any process that modulates the frequency, rate or extent of the angiotensin-activated signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of the angiotensin-activated signaling pathway.
Any process that activates or increases the frequency, rate or extent of the angiotensin-activated signaling pathway.
The chemical reactions and pathways resulting in the breakdown of lncRNAs, non-coding RNAs over 200 nucleotides in length.
The chemical reactions and pathways resulting in the breakdown of lncRNAs, non-coding RNAs over 200 nucleotides in length.
The chemical reactions and pathways resulting in the breakdown of lncRNAs, non-coding RNAs over 200 nucleotides in length.
Any process that modulates the frequency, rate or extent of mitotic telomere clustering during interphase.
Any process that stops, prevents, or reduces the frequency, rate or extent of mitotic telomere clustering during interphase.
Any process that stops, prevents, or reduces the frequency, rate or extent of mitotic telomere clustering during interphase.
High affinity ammonium transporter complex that enables the transfer of ammonium from one side of a membrane to the other.
Catalysis of the reaction: glucosylglycerate + phosphate = glucose-1-phosphate + D-glycerate
The separation of a syncytial embryo into individual cells.
A plasma membrane invagination at the site of separation of a multi-nucleate cell or syncytium into individual cells.
The base of the cellularization invagination or cleavage furrow most distal to the original multi-nucleate cell or syncytium plasma membrane.
The actin-mediated process that results in contraction of the apical end of a polarized columnar epithelial cell, contributing to formation of a ventral indentation (furrow) from the blastoderm epithelium, which is internalized to form a tube in the interior of the embryo, marking the start of gastrulation.
Any process that modulates the frequency, rate or extent of apical constriction involved in ventral furrow formation.
Any process that activates or increases the frequency, rate or extent of apical constriction involved in ventral furrow formation.
Any process that modulates the frequency, rate or extent of ferroptosis.
Any process that stops, prevents, or reduces the frequency, rate or extent of ferroptosis.
A cellular transport process in which transported substances are moved in extracellular vesicles between cells; transported substances are enclosed in the vesicle lumen or located in the extracellular vesicle membrane.
A protein complex responsible for the stabilisation of protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex can also be found as part of the ASTRA complex (GO:0070209).
A protein complex responsible for the stabilisation of protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex can also be found as part of the ASTRA complex (GO:0070209).
A protein complex responsible for the stabilisation of protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex can also be found as part of the ASTRA complex (GO:0070209).
Any process that modulates the frequency, rate or extent of placenta blood vessel development.
Any process that activates or increases the frequency, rate or extent of placenta blood vessel development.
Any process that stops, prevents or reduces the frequency, rate or extent of placenta blood vessel development.
Any process that modulates the frequency, rate or extent of protein localization to cell division site involved in mitotic actomyosin contractile ring assembly.
Any process that activates or increases the frequency, rate or extent of protein localization to cell division site involved in mitotic actomyosin contractile ring assembly.
Any process that stops, prevents, or reduces the frequency, rate or extent of protein localization to cell division site involved in mitotic actomyosin contractile ring assembly.
A cytoskeletal structure composed of actin filaments, myosin, and myosin-associated proteins that forms beneath the plasma membrane of many cells, including animal cells and yeast cells, in a plane perpendicular to the axis of the mitotic spindle, i.e. the cell division plane. Ring contraction is associated with centripetal growth of the membrane that divides the cytoplasm of the two future daughter cells. In animal cells, the mitotic contractile ring is located inside the plasma membrane at the location of the cleavage furrow. In budding fungal cells, e.g. mitotic S. cerevisiae cells, the mitotic contractile ring forms beneath the plasma membrane at the mother-bud neck before mitosis.
A cytoskeletal structure composed of actin filaments, myosin, and myosin-associated proteins that forms beneath the plasma membrane of many cells, including animal cells and yeast cells, in a plane perpendicular to the axis of the meiotic spindle, i.e. the cell division plane. Ring contraction is associated with centripetal growth of the membrane that divides the cytoplasm of the two future daughter cells. In animal cells, the meiotic contractile ring is located inside the plasma membrane at the location of the cleavage furrow. In fungal cells, the meiotic contractile ring forms beneath the plasma membrane of the prospore envelope in preparation for completing cytokinesis.
Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host protease activator activity.
Any apoptotic process that occurs in a hippocampal neuron.
Any process that modulates the occurrence or rate of cell death by apoptotic process in hippocampal neurons.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process in hippocampal neurons.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process in hippocampal neurons.
The area of a motile nucleus closest to the direction of movement.
The area of a motile nucleus furthest from the direction of movement.
Any process that mediates the transfer of information from one cell to another using polyphosphate as the signal.
Any process carried out at the cellular level that reduces or removes the toxicity of an aldehyde. These may include transport of aldehydes away from sensitive areas and to compartments or complexes whose purpose is sequestration of the toxic substance.
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 aldehyde stimulus.
Any process that modulates the frequency, rate or extent of calcium import into the mitochondrion.
Any process that activates or increases the frequency, rate or extent of calcium import into the mitochondrion.
Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion import into the mitochondrion.
The release of duplicated spindle pole bodies (SPBs) and their migration away from each other within the nuclear membrane. Duplicated SPBs are connected by a bridge structure that is severed in order to release the SPBs from one another. Following liberation, SPBs diffuse through the nuclear membrane until they are across from each other. SPB separation must take place in order for a bipolar spindle to assemble.
The directed movement of L-valine into the vacuole across the vacuolar membrane.
The aggregation, arrangement and bonding together of a set of components to form a chloroplast ribulose bisphosphate carboxylase complex.
A conserved protein complex capable of 5'-3' exoribonuclease activity. It is able to promote RNA polymerase II (RNAPII) transcription termination by degrading pre-mRNA from the newly formed 5' phosphorylated end.
The process of generating multiple mRNA molecules with variable 3'-end length formation from a given pre-mRNA by differential use of cleavage and polyadenylation signals (pA signals).
The aggregation, arrangement and bonding together of a set of components to form the mRNA cleavage and polyadenylation specificity factor complex.
Any process that modulates the frequency, rate or extent of imaginal disc-derived wing vein specification.
Any process that activates or increases the frequency, rate or extent of imaginal disc-derived wing vein specification.
Any process that stops, prevents, or reduces the frequency, rate or extent of imaginal disc-derived wing vein specification.
Any process that activates or increases the frequency, rate or extent of animal organ morphogenesis.
Any process that stops, prevents, or reduces the frequency, rate or extent of animal organ morphogenesis.
Any process that modulates the frequency, rate, or extent of lipid transporter activity.
Any process that increases the frequency, rate, or extent of lipid transporter activity.
Any process that decreases the frequency, rate, or extent of lipid transporter activity.
A megadalton-sized complex organized as an oligomeric core of SAD family protein kinases involved in cell size-dependent regulation of Wee1 localization and required for phosphorylation of Wee1 in vivo.
Any process that modulates the frequency, rate or extent of compound eye photoreceptor cell differentiation.
Any process that activates or increases the frequency, rate or extent of compound eye photoreceptor cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of compound eye photoreceptor cell differentiation.
Any process that increases the frequency, rate or extent of very-low-density lipoprotein particle clearance.
Any process in which a gamma-tubulin complex is transported to, or maintained in, a specific location at the nuclear side of the mitotic spindle pole body.
Any process in which a gamma-tubulin complex is transported to, or maintained in, a specific location at the cytoplasmic side of the mitotic spindle pole body.
The orderly movement of a myotube cell from one site to another, often during the development of a multicellular organism. Myotubes are multinucleated cells that are formed when proliferating myoblasts exit the cell cycle, differentiate, and fuse.
Any process that modulates the frequency, rate or extent of myotube cell migration.
Any process that activates, maintains or increases the frequency, rate or extent of myotube cell migration.
Any process that stops, prevents, or reduces the frequency, rate or extent of myotube cell migration.
The process of loading solutes into the sieve tube or companion cell of the phloem for long distance transport from source to sink.
The process of unloading solutes that are produced in the source tissues, from the sieve tube or companion cell of the phloem into the sink tissues.
The process of unloading sucrose that is produced in the source tissues, from the sieve tube or companion cell of the phloem into the sink tissues.
A scallop-shaped plaque, also referred to as an asymmetric unit membrane (AUM), found in the apical plasma membrane of urothelial superficial (umbrella) cells which form a a barrier to the passage of water and soluble toxic compounds found in urine. The plaques are thickened regions of membrane composed of uroplakin transmembrane proteins which form a crystalline array.
A scallop-shaped plaque, also referred to as an asymmetric unit membrane (AUM), found in the apical plasma membrane of urothelial superficial (umbrella) cells which form a a barrier to the passage of water and soluble toxic compounds found in urine. The plaques are thickened regions of membrane composed of uroplakin transmembrane proteins which form a crystalline array.
A cytoplasmic vesicle which contains two urothelial plaques and can deliver these plaques to the apical plasma membrane of urothelial superficial (umbrella) cells. It can also be formed by endocytosis of apical plasma membrane during contractions of the urinary bladder.
A narrow rim of non-thickened membrane in between urothelial plaques in apical plasma membrane.
Any process that modulates the frequency, rate or extent of glutamatergic neuron differentiation.
Any process that stops, prevents or reduces the frequency, rate or extent of glutamatergic neuron differentiation.
Any process that activates or increases the frequency, rate or extent of glutamatergic neuron differentiation.
The transport of phospholipids between membranes in which a phospholipid molecule is transported through an aqueous phase from the outer leaflet of a donor membrane to the outer leaflet of an acceptor membrane.
The transport of sterols between membranes in which a sterol molecule is transported through an aqueous phase from the outer leaflet of a donor membrane to the outer leaflet of an acceptor membrane. This process does not require metabolic energy and can be either spontaneous or mediated by lipid transfer proteins (LTPs).
The transport of sphingolipids between membranes in which a sphingolipid molecule is transported through an aqueous phase from the outer leaflet of a donor membrane to the outer leaflet of an acceptor membrane. This process does not require metabolic energy and can be either spontaneous or mediated by lipid transfer proteins (LTPs).
Enables the removal of a lipid from the outer leaflet of a donor membrane, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to the outer leaflet of an acceptor membrane.
Enables the removal of a phospholipid from the outer leaflet of a donor membrane, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to the outer leaflet of an acceptor membrane.
Enables the removal of a sterol from the outer leaflet of a donor membrane, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to the outer leaflet of an acceptor membrane.
Enables the removal of a sphingolipid from the outer leaflet of a donor membrane, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to the outer leaflet of an acceptor membrane.
Enables the removal of a ceramide from the outer leaflet of a donor membrane, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to the outer leaflet of an acceptor membrane.
Enables the removal of a phosphotidylinositol from the outer leaflet of a donor membrane, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to the outer leaflet of an acceptor membrane.
Enables the removal of a phosphotidylcholine from the outer leaflet of a donor membrane, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to the outer leaflet of an acceptor membrane.
Enables the removal of a cholesterol from the outer leaflet of a donor membrane, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to the outer leaflet of an acceptor membrane.
Enables the removal of a oxysterol from the outer leaflet of a donor membrane, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to the outer leaflet of an acceptor membrane.
Interacting selectively and non-covalently with glucagon, a polypeptide hormone involved in glucose response. It is produced by pancreatic alpha cells and raises the concentration of glucose in the blood.
Interacting selectively and non-covalently with somatostatin, a polypeptide hormone involved in regulating pancreatic alpha and pancreatic beta cells and controlling growth hormone secretion as well as many other functions. Somatostatin is produced by several cell types including pancreatic delta cells. There are several different mature forms of somatostatin.
Interacting selectively and non-covalently with glucagon-like peptide, a antihyperglycemic hormone. Glucagon-like peptide is derived from the glucagon gene produced by pancreatic alpha cells.
A prolongation or process extending from a cell and that is bounded by plasma membrane, e.g. a cilium, lamellipodium, or axon.
A host cell membrane projection with related cytoskeletal components at the trailing edge of a cell in the process of migrating or being activated, found on the opposite side of the cell from the leading edge or immunological synapse, respectively.
Any process that modulates the frequency, rate or extent of osmosensory signaling pathway.
Any process that stops, prevents or reduces the frequency, rate or extent of osmosensory signaling pathway.
The directed movement of hydrogen ions (protons) from inside a cell, across the plasma membrane and into the extracellular region.
The directed movement of hydrogen ions (protons) from inside a cell, across the plasma membrane and into the extracellular region.
The directed movement of hydrogen ions (protons) from inside a cell, across the plasma membrane and into the extracellular region.
The directed movement of hydrogen ions (protons) from inside a cell, across the plasma membrane and into the extracellular region.
Any process that activates or increases the frequency of cilium beating involved in ciliary motility.
Formation of a prolongation or process extending and that is bounded by plasma membrane, e.g. a cilium, lamellipodium, or axon.
Any process that modulates the rate, frequency, or extent of plasma membrane bounded cell projection assembly.
Any process that stops, prevents or reduces the frequency, rate or extent of plasma membrane bounded cell projection assembly.
Any process that activates or increases the frequency, rate or extent of plasma membrane bounded cell projection assembly.
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of plasma membrane bounded cell projections.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a plasma membrane bounded prolongation or process extending from a cell, e.g. a cilium or axon.
Any constituent part of a plasma membrane bounded cell projection, a prolongation or process extending from a cell, e.g. a cilium or axon.
The process in which the anatomical structures of a plasma membrane bounded cell projection are generated and organized.
Any process that modulates the frequency, rate or extent of macrophage proliferation.
Any process that activates or increases the frequency, rate or extent of macrophage proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of macrophage proliferation.
The shaft comprises the majority of the length of the stereocilium. This region is notable for the extreme stability of actin filaments, which are highly crosslinked into a parallel bundle.
The tapered base of the stereocilium adjacent to where it joins the hair cell body. This region contains a rootlet comprised of bundled actin filaments which spans the joint and stabilizes the stereocilium.
The organization process that preserves a stereocilium in a stable functional or structural state.
Any process that modulates the frequency, rate or extent of protein localization to a medial cortical node.
Any process that activates or increases the frequency, rate or extent of protein localization to a medial cortical node.
Catalysis of the reaction: S-adenosyl-L-methionine + adenine(43) in U6 snRNA = S-adenosyl-L-homocysteine + N(6)-methyladenine(43) in U6 snRNA
The posttranscriptional N6-methylation of an adenine residue in an snRNA molecule.
Catalysis of the reaction: UDP-D-xylose + D-ribitol 5-phosphate-R = UDP + beta1,4-xylosyl-D-ribitol 5-phosphate-R.
Contractions of the intestinal tract that include peristalsis (moving contents onward) and non-peristaltic movement (moving contents back and forth).
Migration of ingested material along the length of the small intestine.
Migration of ingested material along the length of the small intestine.
Migration of ingested material along the length of the large intestine.
Migration of ingested material along the length of the large intestine.
Migration of ingested material along the length of the large intestine.
Migration of ingested material along the length of the large intestine.
Any process that modulates the frequency, rate or extent of any small intestinal transit process, the migration of ingested material along the length of the small intestine.
Any process that modulates the frequency, rate or extent of any small intestinal transit process, the migration of ingested material along the length of the small intestine.
Any process that increases the frequency, rate or extent of any small intestinal transit process, the migration of ingested material along the length of the small intestine.
Any process that increases the frequency, rate or extent of any small intestinal transit process, the migration of ingested material along the length of the small intestine.
Any process that decreases the frequency, rate or extent of any small intestinal transit process, the migration of ingested material along the length of the small intestine.
Any process that decreases the frequency, rate or extent of any small intestinal transit process, the migration of ingested material along the length of the small intestine.
Any process that modulates the frequency, rate or extent of any gastric emptying process, the process in which the liquid and liquid-suspended solid contents of the stomach exit through the pylorus into the duodenum.
Any process that modulates the frequency, rate or extent of any gastric emptying process, the process in which the liquid and liquid-suspended solid contents of the stomach exit through the pylorus into the duodenum.
Any process that decreases the frequency, rate or extent of any gastric emptying process, the process in which the liquid and liquid-suspended solid contents of the stomach exit through the pylorus into the duodenum.
Any process that increases the frequency, rate or extent of any gastric emptying process, the process in which the liquid and liquid-suspended solid contents of the stomach exit through the pylorus into the duodenum.
A process in which force is generated within gastric smooth muscle tissue, resulting in a change in muscle geometry. This process occurs throughout the length of the stomach.
A process in which force is generated within gastric smooth muscle tissue, resulting in a change in muscle geometry. This process occurs in the most distal part of the stomach.
A process in which force is generated within gastric smooth muscle tissue, resulting in a change in muscle geometry. This process occurs in the widest part of the pylorus that is continuous with the body of the stomach.
A process in which force is generated within gastric smooth muscle tissue, resulting in a change in muscle geometry. This process occurs in the distal part of the pylorus between the pyloric antrum and the pyloric sphincter.
A process in which force is generated within gastric smooth muscle tissue, resulting in a change in muscle geometry. This process occurs in the narrowest part of the pylorus that separates the stomach from the duodenum.
Any process that modulates the frequency, rate or extent of any stomach fundus smooth muscle contraction.
Any process that increases the frequency, rate or extent of any stomach fundus smooth muscle contraction.
Any process that decreases the frequency, rate or extent of any stomach fundus smooth muscle contraction.
Any process that modulates the frequency, rate or extent of any pyloric antrum smooth muscle contraction.
Any process that increases the frequency, rate or extent of any pyloric antrum smooth muscle contraction.
Any process that decreases the frequency, rate or extent of any pyloric antrum smooth muscle contraction.
Any process that modulates the frequency, rate or extent of cell differentiation, the process in which a relatively unspecialized cell acquires the specialized structural and/or functional features of an endocardial cushion cell.
Any process that activates or increases the frequency, rate or extent of endocardial cushion cell differentiation.
Any process that stops, prevents, or reduces the frequency, rate or extent of endocardial cushion cell differentiation.
Def: The connection of an angiogenic sprout to another vessel or sprout during the formation of vascular networks by sprouting angiogenesis.
Def: The connection of an angiogenic sprout to another vessel or sprout during the formation of vascular networks by sprouting angiogenesis.
The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules that contributes to the formation of a vascular network.nnnDef: The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules that contributes to the formation of a blood vessel network.
The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules that contributes to the formation of a vascular network.nnnDef: The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules that contributes to the formation of a blood vessel network.
Any process that modulates the frequency, rate or extent of microfilament motor activity.
Any process that modulates the frequency, rate or extent of microfilament motor activity.
Any process that modulates the frequency, rate or extent of microfilament motor activity.
Any process that modulates the frequency, rate or extent of microfilament motor activity.
Any process that stops, prevents or reduces the frequency, rate or extent of microfilament motor activity.
Any process that stops, prevents or reduces the frequency, rate or extent of microfilament motor activity.
Any process that stops, prevents or reduces the frequency, rate or extent of microfilament motor activity.
Any process that stops, prevents or reduces the frequency, rate or extent of microfilament motor activity.
Any process that activates or increases the frequency, rate or extent of microfilament motor activity.
Any process that activates or increases the frequency, rate or extent of microfilament motor activity.
Any process that activates or increases the frequency, rate or extent of microfilament motor activity.
Any process that activates or increases the frequency, rate or extent of microfilament motor activity.
A subcompartment of the smooth endoplasmic reticulum consisting of lumenal expansion into a flattened, disc-shaped cavity.
A subcompartment of the rough endoplasmic reticulum consisting of lumenal expansion into a flattened, disc-shaped cavity.
The assembly of a filopodium, a thin, stiff protrusion extended by the endothelial tip cell of a vascular sprout.
Any transposon integration that contributes to a process of RNA-mediated transposition.
Catalysis of the reaction: 2-trans,6-trans-farnesyl diphosphate = diphosphate + (3S)-(+)-asterisca-2(9),6-diene
Catalyzes the hydroxylation of jasmonic acid to 12OH-jasmonic acid.
Catalysis of the reaction: Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine.
Any process that modulates the frequency, rate or extent of crotonylation of a lysine residue in a protein.
Any process that stops or reduces the rate of crotonylation of a lysine residue in a protein.
An organelle membrane contact site formed at the junction of the vacuolar membrane and the isolation membrane or phagophore in response to starvation or other stresses, leading to the formation of the autophagosome.
An organelle membrane contact site formed at the junction of the vacuolar membrane and the isolation membrane or phagophore in response to starvation or other stresses, leading to the formation of the autophagosome.
An organelle membrane contact site formed at the junction of the vacuolar membrane and the isolation membrane or phagophore in response to starvation or other stresses, leading to the formation of the autophagosome.
A protein complex that is involved in the transfer of the second mannose to the glycosylphosphatidylinositol (GPI) during GPI precursor assembly. In yeast S. cerevisiae this complex consists of GPI18p and PGA1p.
A cellular structure that is the site of a developing centriole, which will become a microtubule organizing center. During the canonical pathway of centriole duplication that occurs during the cell division cycle, procentrioles grow at the proximal ends of both mother and daughter centrioles. In the newly divided cells, the original mother and daughter centrioles become mother centrioles while the procentrioles become the new daughter centrioles. Procentrioles can also arise from de novo pathways that occur in multiciliated cells. In ciliated epithelial cells, numerous procentrioles arise form electron dense material referred to as fibrous granules and deuterosomes. The pathway of procentriole formation in multiciliated protists appears to be similar to that in mammalian multiciliated epithelium. In sperm of primative land plants, multiple procentrioles are formed from a blepharoplast giving rise to multicilated sperm cells.
A protein complex that acts as a chaperone or scaffold for centriolar proteins during the maturation of the procentriole. Some of its members may become integrated into the growing centriole. Examples are the CPAP(CENPJ)-STIL complex, CEP192-PLK4 complex or CEP152-PLK4 complex in vertebrates.
A transmembrane complex embedded in the cytoplasmic membrane which is the motor force, or torque, generator of the bacterial-type flagellum. The motor consists of a membrane-anchored rotor complex surrounded by one or more stator complexes in the cytoplasmic membrane. The stator consists of a hetero-hexameric complex of 2 membrane proteins, A and B, with stoichiometry A4B2. Examples are the H+ driven MotA-MotB stator complex of Escherichia coli and Salmonella enterica, and the Na+ driven PomA-PomB stator complex of Vibrio and Shewanella species. The rotor complex consists of a membrane-anchored ring and the motor switch complex, which controls the direction of flagellar rotation.
A hetero-hexameric complex of 2 membrane proteins, A and B, with stoichiometry A4B2. The A and B proteins form a channel through which flow the ions that power the bacterial-type flagellum. They form the stator, or nonrotating portion, of the flagellum motor with the B protein apparently attached to the peptidoglycan cell wall. Examples include the H+ driven MotA-MotB stator complex of Escherichia coli and Salmonella enterica, and the Na+ driven PomA-PomB stator complex of Vibrio and Shewanella species.
A hetero-hexameric complex of 2 membrane proteins, A and B, with stoichiometry A4B2. The A and B proteins form a channel through which flow the ions that power the bacterial-type flagellum. They form the stator, or nonrotating portion, of the flagellum motor with the B protein apparently attached to the peptidoglycan cell wall. Examples include the H+ driven MotA-MotB stator complex of Escherichia coli and Salmonella enterica, and the Na+ driven PomA-PomB stator complex of Vibrio and Shewanella species.
A part of the bacterial-type flagellum that is located at the cytoplasmic side of the MS ring and composed of six membrane proteins (FlhA, FlhB, FliP, FliQ, FliR, and FliO, or orthologs thereof) and three soluble proteins (FliI, FliH, and FliJ, or orthologs thereof) in the cytoplasm. It is responsible for secretion of flagellar type III protein substrates, including the proteins of the flagellar rod, hook, and filament.
A protein complex which assembles on the mother centriole during cilium formation, adjacent and proximal to a centriolar distal appendage. In human, it contains ODF2, CNTRL, NIN, CCDC120c and CCDC68.
A protein complex which assembles on the mother centriole during cilium formation, adjacent and proximal to a centriolar distal appendage. In human, it contains ODF2, CNTRL, NIN, CCDC120c and CCDC68.
A protein complex which assembles on the mother centriole during cilium formation, adjacent and proximal to a centriolar distal appendage. In human, it contains ODF2, CNTRL, NIN, CCDC120c and CCDC68.
The region of the actomyosin ring adjacent to the plasma membrane where membrane bound scaffolds are located.
The region of the actomyosin ring in between the proximal layer and the actin filament layer. This region contains the accessory protein network, some actin filaments and connections between the proximal layer and the actin filament layer.
The region of the actomyosin ring containing actin filaments and cross linkers, myosin motors, and connections to the plasma membrane through the intermediate layer. It is further from the plasma membrane than the intermediate layer which it is adjacent to.
The rotor complex of the bacterial-type flagellum consists of a membrane-anchored ring and the motor switch complex, which participates in the conversion of proton/Na+ energy into the mechanical work of rotation and controls the direction of flagellar rotation.
Catalysis of the reaction: (DNA)-3'-diphospho-5'-guanosine + H(2)O <=> (DNA)-3'-phosphate + GMP.
The process in which the telomeres are gathered together to a small number of foci per chromosome (usually one per chromosome or fewer), and moved to and tethered at the nuclear periphery, as part of a mitotic cell cycle.
The process whereby the mitotic telomeres are gathered together during, or prior to, attachment to the nuclear envelope.
All of the contents of a plasma membrane bounded neuron projection, excluding the plasma membrane surrounding the projection.
The directed movement of UDP-glucose from cytosol to endoplasmic reticulum.
A pathway targeting soluble cytosolic proteins to the vacuole lumen. It uses a selective autophagy receptor protein Nbr1, which is an ortholog of mammalian NBR1, and is remotely related to S. cerevisiae Cvt pathway receptor protein Atg19. Similar to the Cvt pathway, the cargos transported by this pathway are hydrolases, which presumably contribute to the hydrolytic activities in the vacuole lumen. Different from the Cvt pathway, this pathway does not require the macroautophagy machinery, but instead relies on the ESCRT machinery for cargo sequestration. This pathway is observed in the fission yeast S. pombe.
A pathway targeting soluble cytosolic proteins to the vacuole lumen. It uses a selective autophagy receptor protein Nbr1, which is an ortholog of mammalian NBR1, and is remotely related to S. cerevisiae Cvt pathway receptor protein Atg19. Similar to the Cvt pathway, the cargos transported by this pathway are hydrolases, which presumably contribute to the hydrolytic activities in the vacuole lumen. Different from the Cvt pathway, this pathway does not require the macroautophagy machinery, but instead relies on the ESCRT machinery for cargo sequestration. This pathway is observed in the fission yeast S. pombe.
A pathway targeting soluble cytosolic proteins to the vacuole lumen. It uses a selective autophagy receptor protein Nbr1, which is an ortholog of mammalian NBR1, and is remotely related to S. cerevisiae Cvt pathway receptor protein Atg19. Similar to the Cvt pathway, the cargos transported by this pathway are hydrolases, which presumably contribute to the hydrolytic activities in the vacuole lumen. Different from the Cvt pathway, this pathway does not require the macroautophagy machinery, but instead relies on the ESCRT machinery for cargo sequestration. This pathway is observed in the fission yeast S. pombe.
A protein complex containing members of the Like-Sm family of proteins, which includes both the Sm proteins and the Lsm proteins, and which generally form hexameric or heptameric ring structures which bind to RNA. While some of these ring complexes may form independently of RNA, many only form in association with their target RNA. In addition to Lsm-family proteins, many of these complexes contain additional protein members. Members of this family of complexes include the snRNPs which comprise the majority of the spliceosome. Others are involved in the 5' to 3' degradation pathways of mRNAs in the cytoplasm and of unspliced transcripts in the nucleus, as well as other diverse roles.
A heteroheptameric, nuclear protein complex composed of Lsm2, Lsm3, Lsm4, Lsm5, Lsm6, Lsm7, and Lsm8, or orthologs thereof, that selectively binds to snRNAs, in particular the U6 snRNA, and also to unspliced transcripts localized within the nucleus.
The formation of mature glucagon by proteolysis of the precursor proglucagon.
The random-like motility observed for T cells in lymph nodes which enhances surveillance of antigens presented by major histocompatibility complex (MHC) molecules on antigen presenting cells (APCs).
The random-like motility observed for T cells in lymph nodes which enhances surveillance of antigens presented by major histocompatibility complex (MHC) molecules on antigen presenting cells (APCs).
A mobile transmembrane junction at the tip of the flagellum of some kinetoplastid species linking the tip of a new growing flagellum to an older flagellum
A network of cytoskeletal and membranous connections responsible for the lateral attachment of the cilium to the cell body in some trypanosomatid species.
A cytoskeletal structure in some kinetoplastid species linking the structures of the ciliary pocket collar and the flagellum attachment zone (aka cilium attachment zone).
A three-part cytoskeletal structure in kinetoplastid species linking mitochondrial DNA organised in a kinetoplast through the mitochondrial membranes to the basal body.
The chemical reactions and pathways involving prolactin, a protein hormone of the anterior pituitary gland that promotes lactation in response to the suckling stimulus of hungry young mammals.
A protein complex responsible for the catalysis of the reaction: E1 + ubiquitin + ATP--> E1-ubiquitin + AMP + PPi, where the E1-ubiquitin linkage is a thioester bond between the C-terminal glycine of Ub and a sulfhydryl side group of an E1 cysteine residue. This is the first step in a cascade of reactions in which ubiquitin is ultimately added to a protein substrate.
A protein complex responsible for the catalysis of the reaction: E1 + ubiquitin + ATP--> E1-ubiquitin + AMP + PPi, where the E1-ubiquitin linkage is a thioester bond between the C-terminal glycine of Ub and a sulfhydryl side group of an E1 cysteine residue. This is the first step in a cascade of reactions in which ubiquitin is ultimately added to a protein substrate.
A protein complex that primes vacuolar or vesicular membranes for fusion with other intracellular membranes, by promoting the dissociation of cis-SNARE complexes.
A protein complex that primes vacuolar or vesicular membranes for fusion with other intracellular membranes, by promoting the dissociation of cis-SNARE complexes.
A protein complex responsible for the catalysis of the reaction: 4-N-(N-acetyl-D-glucosaminyl)-protein + H2O = N-acetyl-beta-D-glucosaminylamine + peptide L-aspartate. This reaction is the hydrolysis of an N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the N-acetyl-D-glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and the peptide containing an aspartic residue.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of copper ion.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of zinc ion.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process in the bone marrow.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process in the bone marrow.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process in the bone marrow.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process in the bone marrow.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process in the bone marrow.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process in the bone marrow.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process in the bone marrow.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process in the bone marrow.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process in the bone marrow.
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process in the bone marrow.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of actin cortical patches.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of actin cortical patches.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of actin cortical patches.
Any process that stops, prevents, or reduces the frequency, rate or extent of the assembly of actin cortical patches.
The portion of the axoneme that is close to the base of the cilium.
The portion of the axoneme that is close to the tip of the cilium.
Catalysis of the reaction: ATP + dUMP = ADP + dUDP.
Catalysis of the reaction: ATP + dUMP = ADP + dUDP.
Catalysis of the reaction: ATP + dUMP = ADP + dUDP.
Any process that activates or increases the frequency or rate of all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity.
Any process that modulates the frequency, rate or extent of phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity.
Any process that activates or increases the frequency, rate or extent of phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity.
Any process that modulates the frequency, rate or extent of the activity of any ecdysone receptor-mediated signaling pathway.
Any process that activates or increases the frequency, rate or extent of any ecdysone receptor-mediated signaling pathway.
Any process that stops, prevents, or reduces the frequency, rate or extent of any ecdysone receptor-mediated signaling pathway.
A process in which a protein is transported to, or maintained in, a location within a basal ectoplasmic specialization.
A process in which a protein is transported to, or maintained in, a location within a basal ectoplasmic specialization.
A process in which a protein is transported to, or maintained in, a location within a basal ectoplasmic specialization.
Interacting selectively and non-covalently with sulfatide, also known as 3-O-sulfogalactosylceramide, SM4, or sulfated galactocerebroside. Sulfatide is a class of sulfoglycolipid, which are glycolipids that contain a sulfate group.
Interacting selectively and non-covalently with sulfatide, also known as 3-O-sulfogalactosylceramide, SM4, or sulfated galactocerebroside. Sulfatide is a class of sulfoglycolipid, which are glycolipids that contain a sulfate group.
Interacting selectively and non-covalently with sulfatide, also known as 3-O-sulfogalactosylceramide, SM4, or sulfated galactocerebroside. Sulfatide is a class of sulfoglycolipid, which are glycolipids that contain a sulfate group.
Catalysis of the reaction: A [sulfatase]-L-cysteine + O(2) + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H(2)O.
A structure in a host cell comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
A small host cell organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.
Any process that modulates the frequency, rate or extent of mitotic actomyosin contractile ring disassembly.
Any process that modulates the frequency, rate or extent of mitotic actomyosin contractile ring disassembly.
Any process that modulates the frequency, rate or extent of mitotic actomyosin contractile ring disassembly.
Any process that modulates the frequency, rate or extent of mitotic actomyosin contractile ring disassembly.
Any process that modulates the frequency, rate or extent of mitotic actomyosin contractile ring disassembly.
Any process that activates or increases the frequency, rate or extent of mitotic actomyosin contractile ring disassembly.
Any process that activates or increases the frequency, rate or extent of mitotic actomyosin contractile ring disassembly.
Any process that activates or increases the frequency, rate or extent of mitotic actomyosin contractile ring disassembly.
Any process that activates or increases the frequency, rate or extent of mitotic actomyosin contractile ring disassembly.
Any process that activates or increases the frequency, rate or extent of mitotic actomyosin contractile ring disassembly.
Interacting selectively and non-covalently with an outer dynein arm in the presence of calcium.
Interacting selectively and non-covalently with any carbohydrate in the presence of calcium.
Any process that stops, prevents or reduces the frequency, rate or extent of ERBB4 signaling pathway.
A trimeric complex involved in cytokinesis. Proposed to bridge actomyosin ring contraction and septum synthesis in yeast, resulting in the coordination of these processes, and leading to plasma membrane ingression and fusion. In the yeast Saccharomyces cerevisiae this complex consists of Mlc1p, Iqg1p and Hof1p proteins.
A protein kinase complex that is required for the establishment of a cell polarity axis during the cell division cycle. Binds directly to activated CDC42 GTPase and is required for orchestrating a cellular gradient of CDC42. In S. cerevisiae components are: BEM1, CDC24 and CLA4; from worms to vertebrates it contains a PAR6 protein, PAR3 protein and an atypical PKC.
A protein kinase complex that is required for the establishment of a cell polarity axis during the cell division cycle. Binds directly to activated CDC42 GTPase and is required for orchestrating a cellular gradient of CDC42. In S. cerevisiae components are: BEM1, CDC24 and CLA4; from worms to vertebrates it contains a PAR6 protein, PAR3 protein and an atypical PKC.
A protein kinase complex that is required for the establishment of a cell polarity axis during the cell division cycle. Binds directly to activated CDC42 GTPase and is required for orchestrating a cellular gradient of CDC42. In S. cerevisiae components are: BEM1, CDC24 and CLA4; from worms to vertebrates it contains a PAR6 protein, PAR3 protein and an atypical PKC.
A protein kinase complex that is required for the establishment of a cell polarity axis during the cell division cycle. Binds directly to activated CDC42 GTPase and is required for orchestrating a cellular gradient of CDC42. In S. cerevisiae components are: BEM1, CDC24 and CLA4; from worms to vertebrates it contains a PAR6 protein, PAR3 protein and an atypical PKC.
A protein kinase complex that is required for the establishment of a cell polarity axis during the cell division cycle. Binds directly to activated CDC42 GTPase and is required for orchestrating a cellular gradient of CDC42. In S. cerevisiae components are: BEM1, CDC24 and CLA4; from worms to vertebrates it contains a PAR6 protein, PAR3 protein and an atypical PKC.
A protein kinase complex that is required for the establishment of a cell polarity axis during the cell division cycle. Binds directly to activated CDC42 GTPase and is required for orchestrating a cellular gradient of CDC42. In S. cerevisiae components are: BEM1, CDC24 and CLA4; from worms to vertebrates it contains a PAR6 protein, PAR3 protein and an atypical PKC.
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 L-phenylalanine derivative 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 L-phenylalanine derivative stimulus.
Any process that stops, prevents or reduces the frequency, rate or extent of ncRNA transcription associated with protein coding gene TSS/TES.
Any process that stops, prevents or reduces the frequency, rate or extent of ncRNA transcription associated with protein coding gene TSS/TES.
Any process that stops, prevents or reduces the frequency, rate or extent of ncRNA transcription associated with protein coding gene TSS/TES.
Any process that stops, prevents or reduces the frequency, rate or extent of ncRNA transcription associated with protein coding gene TSS/TES.
Any process that stops, prevents or reduces the frequency, rate or extent of ncRNA transcription associated with protein coding gene TSS/TES.
Any process that stops, prevents or reduces the frequency, rate or extent of ncRNA transcription associated with protein coding gene TSS/TES.
Any process that stops, prevents or reduces the frequency, rate or extent of ncRNA transcription associated with protein coding gene TSS/TES.
Any process that stops, prevents or reduces the frequency, rate or extent of ncRNA transcription associated with protein coding gene TSS/TES.
Any process that stops, prevents or reduces the frequency, rate or extent of ncRNA transcription associated with protein coding gene TSS/TES.
The process in which a relatively unspecialized cell acquires the specialized features of a rod bipolar cell.
The process in which a relatively unspecialized cell acquires the specialized features of a cone retinal bipolar cell.
The process in which a relatively unspecialized cell acquires the specialized features of a cone retinal bipolar cell.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a ciliary neurotrophic factor stimulus.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a ciliary neurotrophic factor stimulus.
Any process that modulates the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that modulates the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that activates or increases the frequency, rate or extent of skeletal muscle acetylcholine-gated channel clustering.
Any process that modulates the frequency, rate or extent of neuromuscular junction development.
Any process that modulates the frequency, rate or extent of neuromuscular junction development.
Any process that modulates the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that stops, prevents or reduces the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Any process that activates or increases the frequency, rate or extent of neuromuscular junction development.
Interacting selectively and non-covalently with heparan sulfate.
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 Thyroid stimulating hormone 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 Thyroid stimulating hormone stimulus.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nocodazole 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 nocodazole 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 formaldehyde 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 formaldehyde stimulus.
Any process that stops, prevents or reduces the frequency, rate or extent of nitric oxide metabolic process.
Any process that stops, prevents or reduces the frequency, rate or extent of nitric oxide metabolic process.
Any process that stops, prevents or reduces the frequency, rate or extent of nitric oxide metabolic process.
Any process that stops, prevents or reduces the frequency, rate or extent of nitric oxide metabolic process.
Any process that stops, prevents or reduces the frequency, rate or extent of nitric oxide metabolic process.
Any process that stops, prevents or reduces the frequency, rate or extent of nitric oxide metabolic process.
Any process that stops, prevents or reduces the frequency, rate or extent of nitric oxide metabolic process.
Any process that stops, prevents or reduces the frequency, rate or extent of nitric oxide metabolic process.
Any process that stops, prevents or reduces the frequency, rate or extent of nitric oxide metabolic process.
Any process that activates or increases the frequency, rate or extent of nitric oxide metabolic process.
Any process that activates or increases the frequency, rate or extent of nitric oxide metabolic process.
Any process that activates or increases the frequency, rate or extent of nitric oxide metabolic process.
Any process that activates or increases the frequency, rate or extent of nitric oxide metabolic process.
Any process that activates or increases the frequency, rate or extent of nitric oxide metabolic process.
Any process that activates or increases the frequency, rate or extent of nitric oxide metabolic process.
Any process that activates or increases the frequency, rate or extent of nitric oxide metabolic process.
Any process that activates or increases the frequency, rate or extent of nitric oxide metabolic process.
Any process that activates or increases the frequency, rate or extent of nitric oxide metabolic process.
Interacting selectively and non-covalently with melatonin.
Any process that modulates the frequency, rate or extent of secretory granule organization.
Any process that modulates the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that stops, prevents or reduces the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that activates or increases the frequency, rate or extent of secretory granule organization.
Any process that modulates the frequency, rate or extent of cardiac ventricle development.
Any process that stops, prevents or reduces the frequency, rate or extent of cardiac ventricle development.
Any process that stops, prevents or reduces the frequency, rate or extent of cardiac ventricle development.
Any process that stops, prevents or reduces the frequency, rate or extent of cardiac ventricle development.
Any process that stops, prevents or reduces the frequency, rate or extent of cardiac ventricle development.
Any process that activates or increases the frequency, rate or extent of cardiac ventricle development.
Any process that activates or increases the frequency, rate or extent of cardiac ventricle development.
Any process that activates or increases the frequency, rate or extent of cardiac ventricle development.
Any process that activates or increases the frequency, rate or extent of cardiac ventricle development.
Any process that modulates the frequency, rate or extent of xenophagy.
Any process that stops, prevents or reduces the frequency, rate or extent of xenophagy.
Any process that stops, prevents or reduces the frequency, rate or extent of xenophagy.
Any process that stops, prevents or reduces the frequency, rate or extent of xenophagy.
Any process that stops, prevents or reduces the frequency, rate or extent of xenophagy.
Any process that activates or increases the frequency, rate or extent of xenophagy.
Any process that activates or increases the frequency, rate or extent of xenophagy.
Any process that activates or increases the frequency, rate or extent of xenophagy.
Any process that activates or increases the frequency, rate or extent of xenophagy.
Any process that modulates the frequency, rate or extent of telomeric loop formation.
Any process that modulates the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
Any process that activates or increases the frequency, rate or extent of telomeric loop formation.
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 D-galactosamine 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 D-galactosamine stimulus.
A protein complex which is capable of dehydrodolichyl diphosphate synthase activity.
Any process that modulates the frequency, rate or extent of GTP binding.
Any process that stops, prevents or reduces the frequency, rate or extent of GTP binding.
Any process that stops, prevents or reduces the frequency, rate or extent of GTP binding.
Any process that stops, prevents or reduces the frequency, rate or extent of GTP binding.
Any process that stops, prevents or reduces the frequency, rate or extent of GTP binding.
Any process that activates or increases the frequency, rate or extent of GTP binding.
Any process that activates or increases the frequency, rate or extent of GTP binding.
Any process that activates or increases the frequency, rate or extent of GTP binding.
Any process that activates or increases the frequency, rate or extent of GTP binding.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
Any process that stops, prevents or reduces the frequency, rate or extent of tubulin deacetylation.
Any process that stops, prevents or reduces the frequency, rate or extent of tubulin deacetylation.
Any process that stops, prevents or reduces the frequency, rate or extent of tubulin deacetylation.
Any process that stops, prevents or reduces the frequency, rate or extent of tubulin deacetylation.
Any process that modulates the frequency, rate or extent of t-circle formation.
Any process that stops, prevents or reduces the frequency, rate or extent of t-circle formation.
Any process that stops, prevents or reduces the frequency, rate or extent of t-circle formation.
Any process that stops, prevents or reduces the frequency, rate or extent of t-circle formation.
Any process that stops, prevents or reduces the frequency, rate or extent of t-circle formation.
Any process that stops, prevents or reduces the frequency, rate or extent of t-circle formation.
Any process that stops, prevents or reduces the frequency, rate or extent of t-circle formation.
Any process that stops, prevents or reduces the frequency, rate or extent of t-circle formation.
Any process that stops, prevents or reduces the frequency, rate or extent of t-circle formation.
Any process that stops, prevents or reduces the frequency, rate or extent of t-circle formation.
Any process that activates or increases the frequency, rate or extent of t-circle formation.
Any process that activates or increases the frequency, rate or extent of t-circle formation.
Any process that activates or increases the frequency, rate or extent of t-circle formation.
Any process that activates or increases the frequency, rate or extent of t-circle formation.
Any process that activates or increases the frequency, rate or extent of t-circle formation.
Any process that activates or increases the frequency, rate or extent of t-circle formation.
Any process that activates or increases the frequency, rate or extent of t-circle formation.
Any process that activates or increases the frequency, rate or extent of t-circle formation.
Any process that activates or increases the frequency, rate or extent of t-circle formation.
Any process that modulates the frequency, rate or extent of ferrous iron binding.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron binding.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron binding.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron binding.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron binding.
Any process that activates or increases the frequency, rate or extent of ferrous iron binding.
Any process that activates or increases the frequency, rate or extent of ferrous iron binding.
Any process that activates or increases the frequency, rate or extent of ferrous iron binding.
Any process that activates or increases the frequency, rate or extent of ferrous iron binding.
Any process that modulates the frequency, rate or extent of transferrin receptor binding.
Any process that stops, prevents or reduces the frequency, rate or extent of transferrin receptor binding.
Any process that stops, prevents or reduces the frequency, rate or extent of transferrin receptor binding.
Any process that stops, prevents or reduces the frequency, rate or extent of transferrin receptor binding.
Any process that stops, prevents or reduces the frequency, rate or extent of transferrin receptor binding.
Any process that activates or increases the frequency, rate or extent of transferrin receptor binding.
Any process that activates or increases the frequency, rate or extent of transferrin receptor binding.
Any process that activates or increases the frequency, rate or extent of transferrin receptor binding.
Any process that activates or increases the frequency, rate or extent of transferrin receptor binding.
Any process that modulates the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that modulates the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that modulates the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that activates or increases the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that activates or increases the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that activates or increases the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that activates or increases the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that activates or increases the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that activates or increases the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that activates or increases the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that activates or increases the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that activates or increases the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that activates or increases the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that activates or increases the frequency, rate or extent of ferrous iron import across plasma membrane.
Any process that modulates the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that modulates the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that activates or increases the frequency, rate or extent of thyroid gland epithelial cell proliferation.
Any process that modulates the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that modulates the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that modulates the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
Any process that activates or increases the frequency, rate or extent of establishment of Sertoli cell barrier.
The directed movement of folic acid from outside of a cell, across the plasma membrane and into the cytosol.
The directed movement of folic acid from outside of a cell, across the plasma membrane and into the cytosol.
Any process that modulates the frequency, rate or extent of aspartate secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of aspartate secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of aspartate secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of aspartate secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of aspartate secretion.
Any process that activates or increases the frequency, rate or extent of aspartate secretion.
Any process that activates or increases the frequency, rate or extent of aspartate secretion.
Any process that activates or increases the frequency, rate or extent of aspartate secretion.
Any process that activates or increases the frequency, rate or extent of aspartate secretion.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in positive regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any ubiquitin-specific protease activity that is involved in negative regulation of ERAD pathway.
Any process that stops, prevents or reduces the frequency, rate or extent of neuronal action potential.
Any process that stops, prevents or reduces the frequency, rate or extent of neuronal action potential.
Any process that stops, prevents or reduces the frequency, rate or extent of neuronal action potential.
Any process that stops, prevents or reduces the frequency, rate or extent of neuronal action potential.
Any process that stops, prevents or reduces the frequency, rate or extent of neuronal action potential.
Any process that stops, prevents or reduces the frequency, rate or extent of neuronal action potential.
Any process that stops, prevents or reduces the frequency, rate or extent of neuronal action potential.
Any process that stops, prevents or reduces the frequency, rate or extent of neuronal action potential.
Any process that stops, prevents or reduces the frequency, rate or extent of neuronal action potential.
Any process that activates or increases the frequency, rate or extent of neuronal action potential.
Any process that activates or increases the frequency, rate or extent of neuronal action potential.
Any process that activates or increases the frequency, rate or extent of neuronal action potential.
Any process that activates or increases the frequency, rate or extent of neuronal action potential.
Any process that activates or increases the frequency, rate or extent of neuronal action potential.
Any process that activates or increases the frequency, rate or extent of neuronal action potential.
Any process that activates or increases the frequency, rate or extent of neuronal action potential.
Any process that activates or increases the frequency, rate or extent of neuronal action potential.
Any process that activates or increases the frequency, rate or extent of neuronal action potential.
Any process that modulates the frequency, rate or extent of substance P secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of substance P secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of substance P secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of substance P secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of substance P secretion.
Any process that activates or increases the frequency, rate or extent of substance P secretion.
Any process that activates or increases the frequency, rate or extent of substance P secretion.
Any process that activates or increases the frequency, rate or extent of substance P secretion.
Any process that activates or increases the frequency, rate or extent of substance P secretion.
The chemical reactions and pathways involving ergosteryl 3-beta-D-glucoside.
The chemical reactions and pathways resulting in the breakdown of ergosteryl 3-beta-D-glucoside.
The chemical reactions and pathways resulting in the breakdown of ergosteryl 3-beta-D-glucoside.
The chemical reactions and pathways resulting in the breakdown of ergosteryl 3-beta-D-glucoside.
The chemical reactions and pathways resulting in the formation of ergosteryl 3-beta-D-glucoside.
The chemical reactions and pathways resulting in the formation of ergosteryl 3-beta-D-glucoside.
The chemical reactions and pathways resulting in the formation of ergosteryl 3-beta-D-glucoside.
The chemical reactions and pathways resulting in the formation of ergosteryl 3-beta-D-glucoside.
Any process that modulates the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that modulates the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that activates or increases the frequency, rate or extent of matrix metallopeptidase secretion.
Any process that modulates the frequency, rate or extent of tumor necrosis factor secretion.
Any process that modulates the frequency, rate or extent of tumor necrosis factor secretion.
Any process that modulates the frequency, rate or extent of tumor necrosis factor secretion.
Any process that modulates the frequency, rate or extent of tumor necrosis factor secretion.
Any process that modulates the frequency, rate or extent of tumor necrosis factor secretion.
Any process that modulates the frequency, rate or extent of tumor necrosis factor secretion.
Any process that modulates the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that activates or increases the frequency, rate or extent of tumor necrosis factor secretion.
Any process that modulates the frequency, rate or extent of endothelin secretion.
Any process that modulates the frequency, rate or extent of endothelin secretion.
Any process that modulates the frequency, rate or extent of endothelin secretion.
Any process that modulates the frequency, rate or extent of endothelin secretion.
Any process that modulates the frequency, rate or extent of endothelin secretion.
Any process that modulates the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that stops, prevents or reduces the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
Any process that activates or increases the frequency, rate or extent of endothelin secretion.
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 L-dopa 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 L-dopa stimulus.
Any process that modulates the frequency, rate or extent of Ras GTPase binding.
Any process that stops, prevents or reduces the frequency, rate or extent of Ras GTPase binding.
Any process that stops, prevents or reduces the frequency, rate or extent of Ras GTPase binding.
Any process that stops, prevents or reduces the frequency, rate or extent of Ras GTPase binding.
Any process that stops, prevents or reduces the frequency, rate or extent of Ras GTPase binding.
Any process that stops, prevents or reduces the frequency, rate or extent of Ras GTPase binding.
Any process that stops, prevents or reduces the frequency, rate or extent of Ras GTPase binding.
Any process that stops, prevents or reduces the frequency, rate or extent of Ras GTPase binding.
Any process that stops, prevents or reduces the frequency, rate or extent of Ras GTPase binding.
Any process that stops, prevents or reduces the frequency, rate or extent of Ras GTPase binding.
Any process that activates or increases the frequency, rate or extent of Ras GTPase binding.
Any process that activates or increases the frequency, rate or extent of Ras GTPase binding.
Any process that activates or increases the frequency, rate or extent of Ras GTPase binding.
Any process that activates or increases the frequency, rate or extent of Ras GTPase binding.
Any process that activates or increases the frequency, rate or extent of Ras GTPase binding.
Any process that activates or increases the frequency, rate or extent of Ras GTPase binding.
Any process that activates or increases the frequency, rate or extent of Ras GTPase binding.
Any process that activates or increases the frequency, rate or extent of Ras GTPase binding.
Any process that activates or increases the frequency, rate or extent of Ras GTPase binding.
Any process that modulates the frequency, rate or extent of intestinal absorption.
Any process that stops, prevents or reduces the frequency, rate or extent of intestinal absorption.
Any process that stops, prevents or reduces the frequency, rate or extent of intestinal absorption.
Any process that stops, prevents or reduces the frequency, rate or extent of intestinal absorption.
Any process that stops, prevents or reduces the frequency, rate or extent of intestinal absorption.
Any process that activates or increases the frequency, rate or extent of intestinal absorption.
Any process that activates or increases the frequency, rate or extent of intestinal absorption.
Any process that activates or increases the frequency, rate or extent of intestinal absorption.
Any process that activates or increases the frequency, rate or extent of intestinal absorption.
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 tetrahydrofolate 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 tetrahydrofolate stimulus.
Interacting selectively and non-covalently with synthetic cannabinoid.
The process whose specific outcome is the progression of a cloacal gland over time, from its formation to the mature structure.
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 17alpha-ethynylestradiol 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 17alpha-ethynylestradiol stimulus.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A positive regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in regulation of reactive oxygen species metabolic process.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A negative regulation of transcription from RNA polymerase II promoter that results in negative regulation of mitochondrial unfolded protein response.
A process in which a protein is transported to, or maintained in, a location within a ciliary transition zone.
A process in which a protein is transported to, or maintained in, a location within a ciliary transition zone.
A process in which a protein is transported to, or maintained in, a location within a ciliary transition zone.
Interacting selectively and non-covalently with Ac-Asp-Glu.
Interacting selectively and non-covalently with tetrahydrofolyl-poly(glutamate) polymer.
Any process that modulates the frequency, rate or extent of substance P secretion, neurotransmission.
Any process that stops, prevents or reduces the frequency, rate or extent of substance P secretion, neurotransmission.
Any process that stops, prevents or reduces the frequency, rate or extent of substance P secretion, neurotransmission.
Any process that stops, prevents or reduces the frequency, rate or extent of substance P secretion, neurotransmission.
Any process that stops, prevents or reduces the frequency, rate or extent of substance P secretion, neurotransmission.
Any process that activates or increases the frequency, rate or extent of substance P secretion, neurotransmission.
Any process that activates or increases the frequency, rate or extent of substance P secretion, neurotransmission.
Any process that activates or increases the frequency, rate or extent of substance P secretion, neurotransmission.
Any process that activates or increases the frequency, rate or extent of substance P secretion, neurotransmission.
Any heterochromatin assembly that is involved in chromatin silencing at the centromere outer repeat region.
Any heterochromatin assembly that is involved in chromatin silencing at the centromere outer repeat region.
Any heterochromatin assembly that is involved in chromatin silencing at the centromere outer repeat region.
Any heterochromatin assembly that is involved in chromatin silencing at the centromere outer repeat region.
Any heterochromatin assembly that is involved in chromatin silencing at the centromere outer repeat region.
Any protein localization to actomyosin contractile ring that is involved in mitotic cytokinesis.
Any protein localization to actomyosin contractile ring that is involved in mitotic cytokinesis.
Any protein localization to actomyosin contractile ring that is involved in mitotic cytokinesis.
Any protein localization to actomyosin contractile ring that is involved in mitotic cytokinesis.
Any protein localization to actomyosin contractile ring that is involved in mitotic cytokinesis.
Any protein localization to actomyosin contractile ring that is involved in mitotic cytokinesis.
Any process that modulates the frequency, rate or extent of chromatin-mediated maintenance of transcription.
Any process that stops, prevents or reduces the frequency, rate or extent of chromatin-mediated maintenance of transcription.
Any process that stops, prevents or reduces the frequency, rate or extent of chromatin-mediated maintenance of transcription.
Any process that stops, prevents or reduces the frequency, rate or extent of chromatin-mediated maintenance of transcription.
Any process that stops, prevents or reduces the frequency, rate or extent of chromatin-mediated maintenance of transcription.
Any process that activates or increases the frequency, rate or extent of chromatin-mediated maintenance of transcription.
Any process that activates or increases the frequency, rate or extent of chromatin-mediated maintenance of transcription.
Any process that activates or increases the frequency, rate or extent of chromatin-mediated maintenance of transcription.
Any process that activates or increases the frequency, rate or extent of chromatin-mediated maintenance of transcription.
Any process that modulates the frequency, rate or extent of lipophagy.
Any process that stops, prevents or reduces the frequency, rate or extent of lipophagy.
Any process that stops, prevents or reduces the frequency, rate or extent of lipophagy.
Any process that stops, prevents or reduces the frequency, rate or extent of lipophagy.
Any process that stops, prevents or reduces the frequency, rate or extent of lipophagy.
Any process that activates or increases the frequency, rate or extent of lipophagy.
Any process that activates or increases the frequency, rate or extent of lipophagy.
Any process that activates or increases the frequency, rate or extent of lipophagy.
Any process that activates or increases the frequency, rate or extent of lipophagy.
Any process that modulates the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that activates or increases the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that activates or increases the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that activates or increases the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that activates or increases the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that activates or increases the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that activates or increases the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that activates or increases the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that activates or increases the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that activates or increases the frequency, rate or extent of telomere maintenance in response to DNA damage.
Any process that modulates the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that modulates the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that modulates the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
Any microtubule plus-end that is part of a cytoplasmic microtubule.
Any microtubule plus-end that is part of a cytoplasmic microtubule.
Any microtubule plus-end that is part of a cytoplasmic microtubule.
Any microtubule plus-end that is part of a cytoplasmic microtubule.
Any microtubule plus-end that is part of a cytoplasmic microtubule.
Any microtubule plus-end that is part of a cytoplasmic microtubule.
Any process that modulates the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that modulates the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that modulates the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that modulates the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that stops, prevents or reduces the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of initiation of premeiotic DNA replication.
Any process that activates or increases the frequency, rate or extent of TORC2 signaling.
Any process that activates or increases the frequency, rate or extent of TORC2 signaling.
Any process that activates or increases the frequency, rate or extent of TORC2 signaling.
Any process that activates or increases the frequency, rate or extent of TORC2 signaling.
Any process that activates or increases the frequency, rate or extent of TORC2 signaling.
Any process that activates or increases the frequency, rate or extent of TORC2 signaling.
Any process that activates or increases the frequency, rate or extent of TORC2 signaling.
Any process that activates or increases the frequency, rate or extent of TORC2 signaling.
Any process that activates or increases the frequency, rate or extent of TORC2 signaling.
Any apoptotic process in a myofibroblast cell.
Any apoptotic process in a myofibroblast cell.
Any apoptotic process in a myofibroblast cell.
Interacting selectively and non-covalently with MgATP(2-).
A process in which a protein is transported to, or maintained in, a location at a cytoplasmic microtubule plus-end.
A process in which a protein is transported to, or maintained in, a location at a cytoplasmic microtubule plus-end.
A process in which a protein is transported to, or maintained in, a location at a cytoplasmic microtubule plus-end.
A process in which a protein is transported to, or maintained in, a location at a microtubule minus-end.
A process in which a protein is transported to, or maintained in, a location at a microtubule minus-end.
A process in which a protein is transported to, or maintained in, a location at a microtubule minus-end.
Any process that modulates the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that modulates the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that modulates the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that stops, prevents or reduces the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that activates or increases the frequency, rate or extent of myofibroblast cell apoptotic process.
Any process that modulates the frequency, rate or extent of DNA amplification.
Any process that stops, prevents or reduces the frequency, rate or extent of DNA amplification.
Any process that stops, prevents or reduces the frequency, rate or extent of DNA amplification.
Any process that stops, prevents or reduces the frequency, rate or extent of DNA amplification.
Any process that stops, prevents or reduces the frequency, rate or extent of DNA amplification.
Any process that activates or increases the frequency, rate or extent of DNA amplification.
Any process that activates or increases the frequency, rate or extent of DNA amplification.
Any process that activates or increases the frequency, rate or extent of DNA amplification.
Any process that activates or increases the frequency, rate or extent of DNA amplification.
Any process that modulates the frequency, rate or extent of microtubule binding.
Any process that modulates the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that stops, prevents or reduces the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that activates or increases the frequency, rate or extent of microtubule binding.
Any process that modulates the frequency, rate or extent of actin filament binding.
Any process that modulates the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that stops, prevents or reduces the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that activates or increases the frequency, rate or extent of actin filament binding.
Any process that modulates the frequency, rate or extent of telomeric loop disassembly.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop disassembly.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop disassembly.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop disassembly.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop disassembly.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop disassembly.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop disassembly.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop disassembly.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop disassembly.
Any process that stops, prevents or reduces the frequency, rate or extent of telomeric loop disassembly.
Any process that activates or increases the frequency, rate or extent of telomeric loop disassembly.
Any process that activates or increases the frequency, rate or extent of telomeric loop disassembly.
Any process that activates or increases the frequency, rate or extent of telomeric loop disassembly.
Any process that activates or increases the frequency, rate or extent of telomeric loop disassembly.
Any process that activates or increases the frequency, rate or extent of telomeric loop disassembly.
Any process that activates or increases the frequency, rate or extent of telomeric loop disassembly.
Any process that activates or increases the frequency, rate or extent of telomeric loop disassembly.
Any process that activates or increases the frequency, rate or extent of telomeric loop disassembly.
Any process that activates or increases the frequency, rate or extent of telomeric loop disassembly.
Any process that modulates the frequency, rate or extent of mitotic telomere tethering at nuclear periphery.
Any process that stops, prevents or reduces the frequency, rate or extent of mitotic telomere tethering at nuclear periphery.
Any process that stops, prevents or reduces the frequency, rate or extent of mitotic telomere tethering at nuclear periphery.
Any process that stops, prevents or reduces the frequency, rate or extent of mitotic telomere tethering at nuclear periphery.
Any process that stops, prevents or reduces the frequency, rate or extent of mitotic telomere tethering at nuclear periphery.
Any process that modulates the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that stops, prevents or reduces the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that stops, prevents or reduces the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that stops, prevents or reduces the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that stops, prevents or reduces the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that stops, prevents or reduces the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that stops, prevents or reduces the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that stops, prevents or reduces the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that stops, prevents or reduces the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that stops, prevents or reduces the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that activates or increases the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that activates or increases the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that activates or increases the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that activates or increases the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that activates or increases the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that activates or increases the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that activates or increases the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that activates or increases the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any process that activates or increases the frequency, rate or extent of glycolytic process through fructose-6-phosphate.
Any fungal-type cell wall disassembly that is involved in conjugation with cellular fusion.
Any fungal-type cell wall disassembly that is involved in conjugation with cellular fusion.
Any process that modulates the frequency, rate or extent of free ubiquitin chain polymerization.
Any process that stops, prevents or reduces the frequency, rate or extent of free ubiquitin chain polymerization.
Any process that stops, prevents or reduces the frequency, rate or extent of free ubiquitin chain polymerization.
Any process that stops, prevents or reduces the frequency, rate or extent of free ubiquitin chain polymerization.
Any process that stops, prevents or reduces the frequency, rate or extent of free ubiquitin chain polymerization.
Any process that activates or increases the frequency, rate or extent of free ubiquitin chain polymerization.
Any process that activates or increases the frequency, rate or extent of free ubiquitin chain polymerization.
Any process that activates or increases the frequency, rate or extent of free ubiquitin chain polymerization.
Any process that activates or increases the frequency, rate or extent of free ubiquitin chain polymerization.
Any process that modulates the frequency, rate or extent of cellular response to glucose starvation.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an arachidonic acid stimulus.
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an arachidonic acid stimulus.
Any process that modulates the frequency, rate or extent of chemotaxis to arachidonic acid.
Any process that stops, prevents or reduces the frequency, rate or extent of chemotaxis to arachidonic acid.
Any process that stops, prevents or reduces the frequency, rate or extent of chemotaxis to arachidonic acid.
Any process that stops, prevents or reduces the frequency, rate or extent of chemotaxis to arachidonic acid.
Any process that stops, prevents or reduces the frequency, rate or extent of chemotaxis to arachidonic acid.
Any process that activates or increases the frequency, rate or extent of chemotaxis to arachidonic acid.
Any process that activates or increases the frequency, rate or extent of chemotaxis to arachidonic acid.
Any process that activates or increases the frequency, rate or extent of chemotaxis to arachidonic acid.
Any process that activates or increases the frequency, rate or extent of chemotaxis to arachidonic acid.
The directed movement of L-proline across a membrane.
The directed movement of L-tryptophan across a membrane.
The directed movement of L-alanine across a membrane.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a dextromethorphan 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 dextromethorphan 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 diphenidol 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 diphenidol stimulus.
The chemical reactions and pathways involving phosphatidylinositol 5-phosphate.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol 5-phosphate.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol 5-phosphate.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol 5-phosphate.
The chemical reactions and pathways resulting in the formation of phosphatidylinositol 5-phosphate.
An iron-sulfur cluster assembly complex that is capable of weak ATPase activity. In yeast it consists of two subunits, Nbp35 and Cfd1.
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 1-oleoyl-sn-glycerol 3-phosphate 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 1-oleoyl-sn-glycerol 3-phosphate 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 1-oleoyl-sn-glycerol 3-phosphate 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 1-oleoyl-sn-glycerol 3-phosphate 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 1-oleoyl-sn-glycerol 3-phosphate 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 1-oleoyl-sn-glycerol 3-phosphate 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 1-oleoyl-sn-glycerol 3-phosphate 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 1-oleoyl-sn-glycerol 3-phosphate 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 1-oleoyl-sn-glycerol 3-phosphate 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 1-oleoyl-sn-glycerol 3-phosphate 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 wortmannin 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 wortmannin stimulus.
Any process that modulates the frequency, rate or extent of selenocysteine incorporation.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine incorporation.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine incorporation.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine incorporation.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine incorporation.
Any process that activates or increases the frequency, rate or extent of selenocysteine incorporation.
Any process that activates or increases the frequency, rate or extent of selenocysteine incorporation.
Any process that activates or increases the frequency, rate or extent of selenocysteine incorporation.
Any process that activates or increases the frequency, rate or extent of selenocysteine incorporation.
Any process that stops, prevents or reduces the frequency, rate or extent of mRNA binding.
Any process that stops, prevents or reduces the frequency, rate or extent of mRNA binding.
Any process that stops, prevents or reduces the frequency, rate or extent of mRNA binding.
Any process that stops, prevents or reduces the frequency, rate or extent of mRNA binding.
Any process that modulates the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that stops, prevents or reduces the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that activates or increases the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that activates or increases the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that activates or increases the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that activates or increases the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that activates or increases the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that activates or increases the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that activates or increases the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that activates or increases the frequency, rate or extent of selenocysteine insertion sequence binding.
Any process that activates or increases the frequency, rate or extent of selenocysteine insertion sequence binding.
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 tunicamycin 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 tunicamycin 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 thapsigargin stimulus.