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

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

Toxicology letters - 23 Nov 1998

Moody E J, Knauer C S, Granja R, Strakhovaua M, Skolnick P

Abstract excerpt

1. The intravenous anaesthetic etomidate augments GABA-gated chloride currents (indirect action) and, at higher concentrations, evokes chloride currents in the absence of GABA (direct action). 2. In order to identify amino acid residues essential for these actions, site directed mutagenesis was performed on the beta3 subunit. 3. Mutation of an asparagine to a serine residue at position 290 dramatically reduced...

Read the complete abstract on PubMed

Topics

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

Share to Asparagine
Share to Binding, Competitive
Share to Chloride Channels

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electrophysiology

Share to Ion Channel Gating

Share to Radioligand Assay

Share to Receptors, GABA-A

Share to Tumor Cells, Cultured

Source

Identifiers

PMID: 10049144
DOI: 10.1016/s0378-4274(98)00187-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Distinct structural requirements for the direct and indirect actions of the anaesthetic etomidate at GABA(A) receptors.PMID 10049144Read ↗

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

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

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

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

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

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

Recent Progress in the Development of Etomidate AnaloguesSemantic proximity Read ↗

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

Clinical and molecular pharmacology of etomidate.Semantic proximity Read ↗

Distinct molecular targets for the central respiratory and cardiac actions of the general anesthetics etomidate and propofol.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 ↗

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