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1 yl)-3-amino-6-(4-methoxyphenyl)pyridazinium (SR-95531)].
2 ssed using the GABAA receptor antagonist [3H]SR 95531.
3 modification were decreased both by GABA and SR-95531.
4 K(I) values for the competitive antagonist, SR-95531.
5 s uncoupling by pregnanolone is resistant to SR-95531.
7 ockade (p = 0.008, using bath-applied 200 nm SR 95531 [6-Imino-3-(4-methoxyphenyl)-1(6H)-p yridazineb
8 a(1)H101C located at the BZD-site, gabazine (SR-95531, a GABA binding site antagonist) decreased the
9 gamma-subunits have little effect on GABA or SR-95531 actions, suggesting that asymmetric motions in
13 l)pyridazin-1-yl]butanoic acid hydrobromide (SR-95531; antagonist), pentobarbital (allosteric modulat
15 r GABA or pentobarbital but was unaltered by SR-95531 binding, whereas alpha1L127C reactivity was dec
17 by the GABA(A)-R antagonists bicuculline and SR-95531 (gabazine) and increased in frequency and durat
20 ino-6-(4 methoxyphenyl)pyridazinium bromide (SR-95531), indicating that this arginine poses a barrier
21 tion and converts the competitive antagonist SR-95531 into a partial agonist, demonstrating that this
26 eceptor-mediated transmission application of SR-95531 or bicuculline, while abolishing GABAA receptor
27 also found that equilibrium applications of SR-95531 reduced the response to brief glycine applicati
28 idine-4-sulfonic acid (partial agonist), and SR-95531 sensitivities, indicating that the mutation per
29 of either GABA or the competitive antagonist SR-95531 significantly slows MTSEA-biotin modification o
31 64C, alpha(1)R66C, and alpha(1)S68C, whereas SR-95531 slowed modification of alpha(1)D62C, alpha(1)F6
33 one is inhibited by the GABA site antagonist SR-95531, whereas homologous uncoupling by pregnanolone
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