Structure and Pharmacology of Vertebrate GABAA Receptor Subtypes
References (208)
- et al.
Differential subcellular distribution of the α6 subunit versus the α1 and β2/3 subunits of the GABAA/benzodiazepine receptor complex in granule cells of the cerebellar cortex
Neuroscience (Oxford)
(1992) - et al.
Identification of the γ2 subunit protein in native GABA receptors in brain
Eur. J. Pharmacol.
(1990) - et al.
Identification and immunohistochemical mapping of GABAA receptor subtypes containing the δ subunit in rat brain
FEBS Lett.
(1991) - et al.
GABAA receptors display association of γ2 subunit with α1 and β2/3 subunits
J. Biol. Chem.
(1991) - et al.
Chromosomal localization of GABAA receptor subunit genes: Relationship to human genetic disease
Neuron
(1989) - et al.
Neurochemical action of the general anesthetic propofol on the chloride ion channel coupled with GABAA receptors
Brain Res.
(1991) - et al.
Identification of a putative gamma-aminobutyric acid (GABA) receptor subunit ρ2 and colocalization of the genes encoding ρ2 (GABARR1) and ρl (GABARR1) to human chromosome 6q14-q2 and mouse chromosome-4
Genomics
(1992) - et al.
Function and molecular distinction between recombinant rat GABAA receptor subtypes in Zn2+
Neuron
(1990) - et al.
Biochemical evidence for the existence of γ-aminobutyrateA receptor isooligomers
J. Biol. Chem.
(1990) - et al.
Immunoaffinity purification of GABAA receptor a-subunit iso-oligomers. Demonstration of receptor populations containing α1α2, α1α3 and α2α3 subunit pairs
J. Biol. Chem.
(1991)
Neuron-specific expression of GABAA receptor subtypes: Differential association of the α1 and α3 subunits with serotonergic and GABAergic neurons
Neuroscience (Oxford)
Modulation of GABAA and glycine receptors by chlormethiozole
Eur. J. Pharmacol.
Molecular cloning reveals the existence of a fourth γ subunit of the vertebrate brain GABAA receptor
FEBS htt.
Further evidence for clustering of human GABAA receptor subunit genes: Localization of the & subunit gene (GABRAG) to distal chromosome 5q by linkage analysis
Genomics
Regulation of neurotransmitter receptor desensitization by protein phosphorylation
Neuron
Selective potentiation of GABAA mediated CI− current by lanthanum ion in subtypes of cloned GABAA receptors
Neurosci. Lett.
Novel GABAA receptor α subunit is expressed only in cerebellar granule cells
Mol. Biol.
Function of the α1β2γ2S γ-aminobutyric acid type A receptor is modulated by protein kinase C via multiple sites
J. Biol. Chem.
The cDNA sequence and chromosomal location of the murine GABAA α1 receptor gene
Genomics
A novel α subunit in rat brain GABAA receptors
Neuron
Isolation, characterization and localization of human genomic DNA encoding the β1 subunit of the GABAA receptor (GABRB1)
Genomics
A strong promoter element is located between alternative exons of a gene encoding the human GABAR β3 subunit (GABRB3)
J. Biol. Chem.
The γ3-subunit of the GABAA receptor confers sensitivity to GABAA receptor ligands
FEBS Lett.
Regulation of GABAA receptor function by protein kinase C phosphorylation
Neuron
Effect of ivermectin on γ-aminobutyric acid-induced chloride currents in mouse hippocampal embryonic neurones
Eur. J. Pharmacol.
GABA ρ2 receptor pharmacological profile: GABA recognition site similarities to ρ1
Eur. J. Pharmacol.
Pharmacological characterization and region specific expression in brain of the β2 and β3 subunits of the rat GABAA receptor
FEBS Lett.
Quinolones and fenbufen interact with GABAA receptor in dissociated hippocampal cells of rat
J. Neurophysiol.
GABAA receptor needs two homologous domains of the β-subunit for activation by GABA but not by pentobarbital
Nature (London)
Homomeric ρl GABAA channels: Activation properties and domains
Recep. Channels
“Puppet children”: A reporl on three cases
Dev. Med. Child. Neurol.
Assemhly of GABAA receptor subunits: αlβ2 and α1β2γ2S subunits produce unique ion channels with dissimilar ion channel properties
J. Neurosci
Assembly of GABAA receptor subunits: Analysis of transient single cell expression utilizing a fluorescent substrate/marker gene combination
J. Neurosci.
Enhancement of γ-aminobutyric acid type A receptor currents by chronic activation of cAMPdependent protein kinase
Mol. Pharmacol.
Avermectins potentiate GABAsensitive current in Xenopus oocytes expressing cloned GABAA receptors
Biophys. J.
Stoichiometry of a recombinant GABAA receptor deduced from mutation-induced rectification
NeuroReport
Sequence of the chicken GABAA receptor β3 subunit cDNA
Nucleic Acids Res.
The chicken GABAA receptor α1 subunit: cDNA sequence and localization of the corresponding mRNA
Mol. Brain Res.
γ-aminobutyric acid A receptor heterogeneity is increased by alternative splicing of a novel β-subunit gene transcript
J. Neurochem.
Developmental cues modulate GABAA receptor subunit mRNA expression in cultured cerebellar granule neurons
J. Neurosci.
Modulation of human (α1β1γ2I.) recombinant GABAA receptors by pregnanediols
Can. J. Physiol. Pharmacol.
Immunochemical identification of the α1 and α3 subunits of the GABAA receptor in rat brain
J. Recept. Res.
Ubiquitous presence of GABAA receptors containing the α1 subunit in rat brain demonstrated by immunoprecipitation and immunohistochemistry
Mol. Neuropharmacol.
Distribution, prevalence, and drug binding profile of γ-aminobutyric acid type A receptor subtypes differing in the β-subunit variant
J. Biol. Chem.
Expression patterns of γ-aminobutyric acid type A receptor subunit mRNAs in primary cultures of granule neurons and astrocytes from neonatal rat cerebella
Proc. Natl. Acad. Sci. U.S.A.
Protein kinase C and CAMP dependent protein kinase phosphorylate the β-subunit of the purified GABAA receptor
Proc. Natl. Acad. Sd. U.S.A.
Phenotypic consequences of deletion of the γ3. α5. or β3 subunit of the type A γ-aminobutyric acid receptor of mice
Proc. Natl. Acad. Sci. U.S.A.
Cloning of the gamma-aminobutyric acid rhol cDNA A GABA receptor subunit highly expressed in retina
Proc. Natl. Acad. Sci. U.S.A.
Mechanism of action of ethanol: Initial central nervous system actions
Pharmacol. Rev.
Quantitative immunoprecipitation studies with anti-γ-aminobutyric acidA receptor γ2 1–15 Cys antibodies
J. Neurochem.
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2018, NeuropharmacologyCitation Excerpt :But the degree of modulation also showed regional heterogeneity. This suggested presumably circuitry and behavioral distinctions consistent with pharmacological subtypes, and the potential development of new drugs with subtype selectivity and hopefully improved clinical profiles (Barnard et al., 1998; Lüddens et al., 1995; Olsen and Sieghart, 2008; Rudolph and Möhler, 2004; Whiting et al., 1995). Despite heroic achievements on understanding the actions of these drugs, the normal functions affected and diseases treated, with brilliant advances in analyzing GABAAR subtype functions and their roles in disorders and therapeutics, using modern techniques including genetic engineering (Rudolph et al., 1999; McKernan et al., 2000; Löw et al., 2000), development of suitable disease-specific BZ-site-directed clinically used drugs has been limited, but hope springs eternal (Möhler et al., 2002).
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2015, NeuropharmacologyCitation Excerpt :These values, for different combinations of receptors and drugs, were graphically plotted using Origin. Heteromeric αβγ receptors are a predominant GABAAR subtype in the neocortex, including the hippocampus (Olsen and Sieghart, 2008; Pirker et al., 2000; Whiting et al., 1995). A smaller proportion of receptors in these areas are thought to be αβ heteromers, but to date, there is little if any direct evidence to support the existence of β3 homomers in neurons (Mortensen and Smart, 2006).
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2015, Advances in PharmacologyCitation Excerpt :However, the α2 H101R knockin lost the BZ anxiolytic effect but not the sedative action (Low et al., 2000). This strategy was able to elegantly dissect the molecular targets of BZ action on various behaviors, but even more importantly, it gave strong clues to the function of the GABAR subtypes in behaviors and neuropsychiatric disorders (Rudolph & Möhler, 2004) and could be correlated to the brain regional expression and importance of the receptor subtypes (Barnard et al., 1998; Benke et al., 2004; Whiting et al., 1995). The approach was used to study other subunits of GABAAR like β, indicating molecular roles in other phenomena such as general anesthesia (Rudolph & Antkowiak, 2004).