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

Effect of substituting amino acids in extracellular disulfide loop on GABA rho1 subunit function.

Brain research - 9 May 1997

Lu L

Abstract excerpt

Common features of GABA receptor/channels include a large extracellular NH2-terminal region that is the receptor domain, and four putative transmembrane segments that contribute to form the channel. A conserved Cys-Cys loop of the NH2-terminal domain in GABA receptor/channels is essential for maintaining the receptor and channel function. It has been suggested by other investigators that alteration of amino acids...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Isomerism
Share to Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Oocytes

Share to Structure-Activity Relationship

Share to Xenopus laevis

Source

Identifiers

PMID: 9187308
DOI: 10.1016/s0006-8993(96)01417-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effect of substituting amino acids in extracellular disulfide loop on GABA rho1 subunit function.PMID 9187308Read ↗

A single amino acid change within the ion-channel domain of the gamma-aminobutyric acid rho1 receptor accelerates desensitization and increases taurine agonism.Semantic proximity Read ↗

Mapping the rho1 GABA(C) receptor agonist binding pocket. Constructing a complete model.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 ↗

A single amino acid in the second transmembrane domain of GABA rho receptors regulates channel conductance.Semantic proximity Read ↗

Structural determinants for antagonist pharmacology that distinguish the rho1 GABAC receptor from GABAA receptors.Semantic proximity Read ↗

[GABAC receptors: structure and functions].Semantic proximity Read ↗

Three arginines in the GABAA receptor binding pocket have distinct roles in the formation and stability of agonist- versus antagonist-bound complexes.Semantic proximity Read ↗

A Single phenylalanine residue in the main intracellular loop of α1 γ-aminobutyric acid type A and glycine receptors influences their sensitivity to propofol.Semantic proximity Read ↗

A highly conserved aspartic acid residue in the signature disulfide loop of the alpha 1 subunit is a determinant of gating in the glycine receptor.Semantic proximity Read ↗

Spontaneous activity, singly bound states and the impact of alpha1Phe64 mutation on GABAAR gating in the novel kinetic model based on the single-channel recordings.Semantic proximity Read ↗

Relative impact of residues at the intracellular and extracellular ends of the human GABAC rho1 receptor M2 domain on picrotoxinin activity.Semantic proximity Read ↗

Mutations at the GABA receptor selectivity filter: a possible role for effective charges.Semantic proximity Read ↗

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