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Article

Hyperekplexia mutations of the glycine receptor unmask the inhibitory subsite for beta-amino-acids.

Neuroreport - 19 Apr 1995

Laube B, Langosch D, Betz H, Schmieden V

Abstract excerpt

beta-Alanine and taurine are agonists of the glycine receptor (GlyR) which, at low concentrations, antagonize the action of the principal agonist glycine. We analysed the potency of these ligands on alpha 1 subunits mutated at residue R271. GlyRs formed from alpha 1R271K subunits showed a reducti...

Topics

Animals
Glycine
Humans
Ligands
Membranes
Mutation
Nervous System Diseases
Oocytes
RNA
Receptors, Amino Acid
Receptors, Glycine
Taurine
Xenopus laevis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

beta-Alanine

Source

Identifiers

PMID: 7542038
DOI: 10.1097/00001756-199504190-00018

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7542038-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Hyperekplexia mutations of the glycine receptor unmask the inhibitory subsite for beta-amino-acids.PMID 7542038Read ↗

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Properties of human glycine receptors containing the hyperekplexia mutation alpha1(K276E), expressed in Xenopus oocytes.Semantic proximity Read ↗

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