Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Two etomidate sites in α1β2γ2 γ-aminobutyric acid type A receptors contribute equally and noncooperatively to modulation of channel gating.

Anesthesiology - 1 Jun 2012

Guitchounts Grigori, Stewart Deirdre S, Forman Stuart A

Abstract excerpt

BACKGROUND: Etomidate is a potent hypnotic agent that acts via γ-aminobutyric acid receptor type A (GABA(A)) receptors. Evidence supports the presence of two etomidate sites per GABA(A) receptor, and current models assume that each site contributes equally and noncooperatively to drug effects. These assumptions remain untested. METHODS: We used concatenated dimer (β2-α1) and trimer (γ2-β2-α1) GABA(A) subunit...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to gamma-Aminobutyric Acid
Share to Ion Channel Gating

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oocytes

Share to Patch-Clamp Techniques

Share to Plasmids

Share to Receptors, GABA-A

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 22531336
DOI: 10.1097/ALN.0b013e3182567df3
PMCID: PMC3366439

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Two etomidate sites in α1β2γ2 γ-aminobutyric acid type A receptors contribute equally and noncooperatively to modulation of channel gating.PMID 22531336Read ↗

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

Tryptophan mutations at azi-etomidate photo-incorporation sites on alpha1 or beta2 subunits enhance GABAA receptor gating and reduce etomidate modulation.Semantic proximity Read ↗

State-dependent etomidate occupancy of its allosteric agonist sites measured in a cysteine-substituted GABAA receptor.Semantic proximity Read ↗

Monod-Wyman-Changeux allosteric mechanisms of action and the pharmacology of etomidate.Semantic proximity Read ↗

Mutations in the GABAA receptor that mimic the allosteric ligand etomidate.Semantic proximity Read ↗

Tryptophan and Cysteine Mutations in M1 Helices of α1β3γ2L γ-Aminobutyric Acid Type A Receptors Indicate Distinct Intersubunit Sites for Four Intravenous Anesthetics and One Orphan Site.Semantic proximity Read ↗

Distinct structural requirements for the direct and indirect actions of the anaesthetic etomidate at GABA(A) receptors.Semantic proximity Read ↗

Differentiating the role of gamma-aminobutyric acid type A (GABAA) receptor subtypes.Semantic proximity Read ↗

Structural basis for activation and potentiation in a human α5β3 GABA <sub>A</sub> receptorSemantic proximity Read ↗

Functional sites involved in modulation of the GABAA receptor channel by the intravenous anesthetics propofol, etomidate and pentobarbital.Semantic proximity Read ↗

Molecular determinants underlying DS2 activity at δ-containing GABA <sub>A</sub> receptorsSemantic proximity Read ↗

Multiple Non-Equivalent Interfaces Mediate Direct Activation of GABAA Receptors by Propofol.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.