Potentiation of gamma-aminobutyric acid-induced chloride currents by various benzodiazepine site agonists with the alpha 1 gamma 2, beta 2 gamma 2 and alpha 1 beta 2 gamma 2 subtypes of cloned gamma-aminobutyric acid type A receptors.
@article{Im1993PotentiationOG, title={Potentiation of gamma-aminobutyric acid-induced chloride currents by various benzodiazepine site agonists with the alpha 1 gamma 2, beta 2 gamma 2 and alpha 1 beta 2 gamma 2 subtypes of cloned gamma-aminobutyric acid type A receptors.}, author={Haesook K. Im and Wha Bin Im and Beverly J. Hamilton and Donald B. Carter and Philip F. Vonvoigtlander}, journal={Molecular pharmacology}, year={1993}, volume={44 4}, pages={ 866-70 } }
Previous studies with cloned gamma-aminobutyric acid type A receptors expressed in human embryonic kidney cells have indicated that the alpha 1 beta 2 gamma 2 and alpha 1 gamma 2 (but not alpha 1 beta 2) subtypes have benzodiazepine sites. We found in this study that even the beta 2 gamma 2 subtype displays gamma-aminobutyric acid-induced Cl- currents that are potentiated by triazolam (a triazolobenzodiazepine). The maximal efficacy of the drug among the subtypes was highest with the alpha 1…
38 Citations
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Mutagenesis of the Rat α1 Subunit of the γ-Aminobutyric AcidA Receptor Reveals the Importance of Residue 101 in Determining the Allosteric Effects of Benzodiazepine Site Ligands
- Biology, Chemistry
- 1999
The results indicate that the characteristics of the residue at position 101 of the α1 subunit play a crucial role in determining the efficacy of benzodiazepine-site ligands.
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