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

Discrete M3-M4 intracellular loop subdomains control specific aspects of γ-aminobutyric acid type A receptor function.

The Journal of biological chemistry - 4 Nov 2011

O'Toole Kate K, Jenkins Andrew

Abstract excerpt

The GABA type A receptor (GABA(A)R) is a member of the pentameric ligand gated ion channel (pLGIC) family that mediates ionotropic neurotransmission. Residues in the intracellular loop domain (ILD) have recently been shown to define part of the ion permeation pathway in several closely related members of the pentameric ligand gated ion channel family. In this study, we investigated the role the ILD of the...

Read the complete abstract on PubMed

Topics

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

Share to Gene Deletion
Share to HEK293 Cells
Share to Ligands

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

Share to Patch-Clamp Techniques

Share to Point Mutation

Share to Receptors, GABA-A

Share to Sequence Homology, Amino Acid

Share to Torpedo

Source

Open in PubMed Open full text

Identifiers

PMID: 21903587
DOI: 10.1074/jbc.M111.258012
PMCID: PMC3207432

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

Discrete M3-M4 intracellular loop subdomains control specific aspects of γ-aminobutyric acid type A receptor function.PMID 21903587Read ↗

Mutations at the M2 and M3 Transmembrane Helices of the GABAARs α1 and β2 Subunits Affect Primarily Late Gating Transitions Including Opening/Closing and Desensitization.Semantic proximity Read ↗

A mutation in the GABAA receptor alpha 1 subunit linked to human epilepsy affects channel gating properties.Semantic proximity Read ↗

Mutations of α1F45 residue of GABAA receptor loop G reveal its involvement in agonist binding and channel opening/closing transitions.Semantic proximity Read ↗

The human GABA <sub>A</sub> receptor α4 subunit variant Ile114Asn linked to epilepsy impairs membrane expression with β3 and δ subunitsSemantic proximity Read ↗

A conserved Cys-loop receptor aspartate residue in the M3-M4 cytoplasmic loop is required for GABAA receptor assembly.Semantic proximity Read ↗

A conserved salt bridge critical for GABA(A) receptor function and loop C dynamics.Semantic proximity Read ↗

Glycine substitution of α1F64 residue at the loop D of GABAA receptor impairs gating - Implications for importance of binding site-channel gate linker rigidity.Semantic proximity Read ↗

Understanding paralogous epilepsy–associated GABA A receptor variants: Clinical implications, mechanisms, and potential pitfallsSemantic proximity Read ↗

A cationic lipid site at the outward transmembrane face of a pentameric ligand-gated ion channelSemantic proximity Read ↗

Characterization of the effects of charged residues in the intracellular loop on ion permeation in alpha1 glycine receptor channels.Semantic proximity Read ↗

Mutation of valine 53 at the interface between extracellular and transmembrane domains of the β2 principal subunit affects the GABAA receptor gating.Semantic proximity Read ↗

Role of the ρ1 GABA(C) receptor N-terminus in assembly, trafficking and function.Semantic proximity Read ↗

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