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4-Fluorophenibut (developmental code name CGP-11130; also known as β-(4-fluorophenyl)-γ-aminobutyric acid or β-(4-fluorophenyl)-GABA) is a GABA B receptor agonist which was never marketed. [1] It is selective for the GABA B receptor over the GABA A receptor ( IC 50 = 1.70 μM and > 100 μM, respectively). [ 1 ]
Gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the brain, mediates neuronal inhibition by binding to GABA receptors. The type A GABA receptors are pentameric chloride channels assembled from among many genetic variants of GABA(A) subunits. This gene encodes the gamma 2 subunit of GABA(A) receptor.
A subclass of ionotropic GABA receptors, insensitive to typical allosteric modulators of GABA A receptor channels such as benzodiazepines and barbiturates, [27] [28] [29] was designated GABA С receptor. [30] [31] Native responses of the GABA C receptor type occur in retinal bipolar or horizontal cells across vertebrate species. [32] [33] [34] [35]
GABA B receptors also reduces the activity of adenylyl cyclase and Ca 2+ channels by using G-proteins with G i /G 0 α subunits. [4] GABA B receptors are involved in behavioral actions of ethanol, [5] [6] gamma-hydroxybutyric acid (GHB), [7] and possibly in pain. [8] Recent research suggests that these receptors may play an important ...
Valerenic acid acts as a subtype-selective GABA A receptor positive allosteric modulator via a binding site in the transmembrane domain at the β + α − interface. [4] At receptors expressed in Xenopus oocytes (frog eggs) it was shown that only assemblies incorporating β2 or β3 subunits were stimulated by valerenic acid.
The ionotropic GABA A receptor protein complex is also the molecular target of the benzodiazepine class of tranquilizer drugs. Benzodiazepines do not bind to the same receptor site on the protein complex as does the endogenous ligand GABA (whose binding site is located between α- and β-subunits), but bind to distinct benzodiazepine binding sites situated at the interface between the α- and ...
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