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

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

The Journal of biological chemistry - 7 Jan 2005

Jung Sangwook, Akabas Myles H, Harris R Adron

Abstract excerpt

The substituted cysteine accessibility method has proven useful for investigating structural changes of the gamma-aminobutyric acid type A (GABA(A)) receptor during channel gating and allosteric modulation. In the present study, the surface accessibility and reaction rate of propyl- and hexyl-methanethiosulfonate to cysteine residues introduced into the third transmembrane segment of the GABA(A) receptor alpha(1)...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Ethanol
Share to Ion Channel Gating

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mesylates

Share to Protein Subunits

Share to Receptors, GABA-A

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 15522868
DOI: 10.1074/jbc.M409871200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional and structural analysis of the GABAA receptor alpha 1 subunit during channel gating and alcohol modulation.PMID 15522868Read ↗

Gamma-aminobutyric acid increases the water accessibility of M3 membrane-spanning segment residues in gamma-aminobutyric acid type A receptors.Semantic proximity Read ↗

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

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

Agonist-specific conformational changes in the α1-γ2 subunit interface of the GABA A receptor.Semantic proximity Read ↗

The substituted-cysteine accessibility method (SCAM) to elucidate membrane protein structure.Semantic proximity Read ↗

Functional consequences of sulfhydryl modification of the γ-aminobutyric acid transporter 1 at a single solvent-exposed cysteine residue.Semantic proximity Read ↗

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

Comparison of taurine- and glycine-induced conformational changes in the M2-M3 domain of the glycine receptor.Semantic proximity Read ↗

Substituted Cysteine Modification and Protection with n-Alkyl-MTS Reagents Quantifies Steric Changes Induced by a Mutation in Anesthetic Binding Sites on GABA Type A Receptors.Semantic proximity Read ↗

Methionine 286 in transmembrane domain 3 of the GABAA receptor beta subunit controls a binding cavity for propofol and other alkylphenol general anesthetics.Semantic proximity Read ↗

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

GABA(A) receptor beta 2 Tyr97 and Leu99 line the GABA-binding site. Insights into mechanisms of agonist and antagonist actions.Semantic proximity Read ↗

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