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

Occupancy of a single anesthetic binding pocket is sufficient to enhance glycine receptor function.

The Journal of biological chemistry - 10 Feb 2006

Roberts Michael T, Phelan Rachel, Erlichman Beth S, Pillai Rathi N, Ma Lan, Lopreato Gregory F, Mihic S John

Abstract excerpt

Alcohols and volatile anesthetics enhance the function of inhibitory glycine receptors (GlyRs). This is hypothesized to occur by their binding to a pocket formed between the transmembrane domains of individual alpha1 GlyR subunits. Because GlyRs are pentameric, it follows that each GlyR contains up to five alcohol/anesthetic binding sites, with one in each subunit. We asked how many subunits per pentamer need be...

Read the complete abstract on PubMed

Topics

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

Share to Alcohols
Share to Anesthetics

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Electrophysiology

Share to Ethanol

Share to Glycine

Share to Mesylates

Share to Receptors, Glycine

Share to Xenopus laevis

Source

Identifiers

PMID: 16361257
DOI: 10.1074/jbc.M502000200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Occupancy of a single anesthetic binding pocket is sufficient to enhance glycine receptor function.PMID 16361257Read ↗

Propofol modulation of α1 glycine receptors does not require a structural transition at adjacent subunits that is crucial to agonist-induced activation.Semantic proximity Read ↗

Characterization of two mutations, M287L and Q266I, in the α1 glycine receptor subunit that modify sensitivity to alcohols.Semantic proximity Read ↗

An isoflurane- and alcohol-insensitive mutant GABA(A) receptor alpha(1) subunit with near-normal apparent affinity for GABA: characterization in heterologous systems and production of knockin mice.Semantic proximity Read ↗

Ethanol enhances taurine-activated glycine receptor function.Semantic proximity Read ↗

Acetylcholine and alcohol sensitivity of neuronal nicotinic acetylcholine receptors: mutations in transmembrane domains.Semantic proximity Read ↗

Effects of isoflurane on gamma-aminobutyric acid type A receptors activated by full and partial agonists.Semantic proximity Read ↗

Evidence that ethanol acts on a target in Loop 2 of the extracellular domain of alpha1 glycine receptors.Semantic proximity Read ↗

Accessibility to residues in transmembrane segment four of the glycine receptor.Semantic proximity Read ↗

Sites in TM2 and 3 are critical for alcohol-induced conformational changes in GABA receptors.Semantic proximity Read ↗

Functional and structural analysis of the GABAA receptor alpha 1 subunit during channel gating and alcohol modulation.Semantic proximity Read ↗

Enhancement of α5-containing γ-aminobutyric acid type A receptors by the nonimmobilizer 1,2-dichlorohexafluorocyclobutane (F6) is abolished by the β3(N265M) mutation.Semantic proximity Read ↗

Probing the pharmacological properties of distinct subunit interfaces within heteromeric glycine receptors reveals a functional ββ agonist-binding site.Semantic proximity Read ↗

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