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Article

Gamma-amino butyric acid type A receptor mutations at beta2N265 alter etomidate efficacy while preserving basal and agonist-dependent activity.

Anesthesiology - 1 Oct 2009

Desai Rooma, Ruesch Dirk, Forman Stuart A

Abstract excerpt

BACKGROUND: Etomidate acts at gamma-Aminobutyric acid type A (GABAA) receptors containing beta2 or beta3, but not beta1 subunits. Mutations at beta residue 265 (Ser in beta1; Asn in beta2 or beta3) profoundly affect etomidate sensitivity. Whether these mutations alter etomidate binding remains uncertain. METHODS: Heterologously expressed alpha1beta2gamma2L GABAA receptors and receptors with beta2(N265S) or...

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Identifiers

PMID: 19741491
DOI: 10.1097/ALN.0b013e3181b55fae
PMCID: PMC2798018

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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