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- W2397339748 abstract "The potency of 30 benzodiazepine binding site ligands from 14 different structural classes for inhibition of [3H]Ro 15-4513 (ethyl-8-azido-5,6-dihydro-5-methyl-6-oxo-4H-imidazo[1,5-a][1,4]benzodiazepine-3-carboxylate) binding to human embryonic kidney (HEK) 293 cells transiently transfected with α4β3γ2S or α1β3γ2S subunits of GABAA receptors was investigated. Most of these compounds were unable to significantly inhibit [3H]Ro 15-4513 binding to α4β3γ2S receptors under conditions where they potently inhibited binding to α1β3γ2S receptors. Nevertheless, compounds from four different structural classes were identified which exhibited a high affinity for α4β3γ2S receptors. Variation of the structure of these compounds could lead to new ligands selectively interacting with α4β3γ2S receptors. Compounds interacting with α4β3γ2S receptors were also able to inhibit [3H]Ro 15-4513 binding to receptors consisting of α4γ2S subunits with comparable potency. These results support the conclusion that the α subunit is a major determinant of the benzodiazepine binding site properties of GABAA receptors containing α and γ subunits." @default.
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- W2397339748 date "1996-05-01" @default.
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- W2397339748 title "Affinity of various ligands for GABAA receptors containing α4β3γ2, α4γ2, or α1β3γ2 subunits" @default.
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- W2397339748 doi "https://doi.org/10.1016/0014-2999(96)00088-x" @default.
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