Subtle Changes in Residue 77 of the γ Subunit of α1β2γ2 GABAA Receptors Drastically Alter the Affinity for Ligands of the Benzodiazepine Binding Site
Open Access
- 1 May 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (18) , 11799-11804
- https://doi.org/10.1074/jbc.272.18.11799
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- The Major Site of Photoaffinity Labeling of the γ-Aminobutyric Acid Type A Receptor by [3H]Flunitrazepam Is Histidine 102 of the α SubunitJournal of Biological Chemistry, 1996
- Four amino acid exchanges convert a diazepam-insensitive, inverse agonist-preferring GABAA receptor into a diazepam-preferring GABAA receptorJournal of Medicinal Chemistry, 1994
- GABAA Receptor ChannelsAnnual Review of Neuroscience, 1994
- Expression and properties of recombinant α1β2γ2 and α5β2γ2 forms of the rat GABAA receptorEuropean Journal of Pharmacology: Molecular Pharmacology, 1993
- Benzodiazepine-induced motor impairment linked to point mutation in cerebeilar GABAA receptorNature, 1993
- Importance of a novel GABAA receptor subunit for benzodiazepine pharmacologyNature, 1989
- Cloning and expression of a novel rat GABAA receptorFEBS Letters, 1989
- Sequence and functional expression of the GABAA receptor shows a ligand-gated receptor super-familyNature, 1987
- Irreversible Binding of [3H]Flunitrazepam to Different Proteins in Various Brain RegionsJournal of Neurochemistry, 1983
- Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reactionBiochemical Pharmacology, 1973