Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of gamma-aminobutyric acid (GABA, 4-aminobutyrate) into a neuron or glial cell.

Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of L-glutamate into a neuron or glial cell.

Any process that stops, prevents or reduces the frequency, rate or extent of L-glutamate import into a cell.

Binding to the catalytic subunit of a phosphatidylinositol 3-kinase. The catalytic subunit catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring.

Binding to a phosphatidylinositol 3-kinase, any enzyme that catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring.

Binding to a regulatory subunit of phosphatidylinositol 3-kinase. The regulatory subunit associates with the catalytic subunit to regulate both its activity and subcellular location.

Catalysis of the reaction: 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O = 2-(acetylamino)-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-beta-D-glucopyranose + acetate.

An ATP-dependent activity that facilitates the formation of a complementary double-stranded DNA molecule.

Catalysis of the hydrolysis of a 5' tyrosyl-RNA phosphodiester bond between a protein and RNA. In picornaviruses, this covalent bond connects VPg, a viral-encoded protein essential for RNA replication, to the 5' end of all nascent picornavirus genomes; it is cleaved from viral RNA prior to its engaging in protein synthesis.

Any process in which the SREBP-SCAP complex is maintained in the endoplasmic reticulum and prevented from moving elsewhere. The SREBP-SCAP complex is formed by the association of sterol regulatory element binding protein (SREBP) and SREBP-cleavage-activating protein (SCAP). In the absence of sterols, the SREBP-SCAP complex is packaged into COPII vesicles and travels to the Golgi apparatus to be processed. In the presence of sterols, the complex binds ER-resident proteins such as INSIG, which retain the complex in the ER.

Catalysis of the reaction: coenzyme B + coenzyme M + methanophenazine = N-{7-[(2-sulfoethyl)dithio]heptanoyl}-3-O-phospho-L-threonine + dihydromethanophenazine.

Catalysis of the reaction: H2 + 2-(2,3-dihydropentaprenyloxy)phenazine = 2-dihydropentaprenyloxyphenazine.

Any process that stops, prevents, or reduces the frequency, rate or extent of fibrinolysis, an ongoing process that solubilizes fibrin, resulting in the removal of small blood clots.

Any process that modulates the frequency, rate or extent of fibrinolysis, an ongoing process that solubilizes fibrin, resulting in the removal of small blood clots.

Combining with the mating-type peptide pheromone M-factor and transmitting the signal across the membrane to initiate a change in cell activity. M-factor is a nine-membered oligopeptide that consists of tyrosyl, threonyl, prolyl, lysyl, valyl, prolyl, tyrosyl, methionyl and methyl S-farnesylcysteinate residues joined in sequence, and is a peptide pheromone released by Schizosaccharomyces pombe cells of the cellular mating type Minus.

Any process that activates, maintains or increases the frequency, rate or extent of fibrinolysis, an ongoing process that solubilizes fibrin, resulting in the removal of small blood clots.

The process in which a chemical substance increases synaptic plasticity, the ability of synapses to change as circumstances require.

A process that increases synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.

The process in which a chemical substance modulates synaptic plasticity, the ability of synapses to change as circumstances require.