Pharmacology of recombinant γ-aminobutyric acidAreceptors rendered diazepam-insensitive by point-mutated α-subunits (original) (raw)

Cloning and characterization of the human GABAA receptor α4 subunit: identification of a unique diazepam-insensitive binding site

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European Journal of Pharmacology: Molecular Pharmacology, 1995

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Selective labelling of diazepam-insensitive GABA A receptors in vivo using [ 3 H]Ro 15-4513

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Structural Elements of the γ-Aminobutyric Acid Type A Receptor Conferring Subtype Selectivity for Benzodiazepine Site Ligands

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Structural Elements of the gamma -Aminobutyric Acid Type A Receptor Conferring Subtype Selectivity for Benzodiazepine Site Ligands

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Inhibition of γ-aminobutyric acid stimulated [3H]diazepam binding by benzodiazepine receptor ligands

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Biochemical Pharmacology, 1981

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GABAA Receptor α Subunits Differentially Contribute to Diazepam Tolerance after Chronic Treatment

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Structural Determinants of Benzodiazepine Allosteric Regulation of GABAAReceptor Currents

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Triazolam is more efficacious than diazepam in a broad spectrum of recombinant GABAA receptors

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Actions of two GABAA receptor benzodiazepine-site ligands that are mediated via non-γ2-dependent modulation

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GABA antagonists differentiate between recombinant GABAA/benzodiazepine receptor subtypes

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The Journal of Neuroscience, 1995

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Enhancement of γ-Aminobutyric Acid Binding by Quazepam, a Benzodiazepine Derivative with Preferential Affinity for Type I Benzodiazepine Receptors

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Biological function of GABAA/benzodiazepine receptor heterogeneity

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Journal of Psychiatric Research, 1995

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Kucken AM, Wagner DA, Ward PR, Teissere JA, Boileau AJ, Czajkowski C (2000) "Identification of benzodiazepine binding site residues in the gamma2 subunit of the GABA(A) receptor" Molecular Pharmacology 57:932-9.

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erratum: Benzodiazepine actions mediated by specific γ-aminobutyric acidA receptor subtypes

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Nature, 2000

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Estimating the efficiency of benzodiazepines on GABA A receptors comprising γ1 or γ2 subunits

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Sh-I-048A, an in vitro non-selective super-agonist at the benzodiazepine site of GABAA receptors: The approximated activation of receptor subtypes may explain behavioral effects

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An Updated Unified Pharmacophore Model of the Benzodiazepine Binding Site on γ-Aminobutyric Acida Receptors: Correlation with Comparative Models

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The novel anxiolytic ELB139 displays selectivity to recombinant GABAA receptors different from diazepam

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Structural Mechanisms Underlying Benzodiazepine Modulation of the GABAA Receptor

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Allosteric uncoupling and up-regulation of benzodiazepine and GABA recognition sites following chronic diazepam treatment of HEK 293 cells stably transfected with α 1 β 2 γ 2S subunits of GABA A receptors

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Benzodiazepine-insensitive mice generated by targeted disruption of the gamma 2 subunit gene of gamma-aminobutyric acid type A receptors

Jack Benson

Proceedings of the National Academy of Sciences, 1995

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