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Article

Structure-function relationships of the human glycine receptor: insights from hyperekplexia mutations.

Annals of the New York Academy of Sciences - 30 Apr 1999

Lewis T M, Schofield P R

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

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PMID: 10414353
DOI: 10.1111/j.1749-6632.1999.tb11345.x

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

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Related research

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Structure-function relationships of the human glycine receptor: insights from hyperekplexia mutations.PMID 10414353Read ↗

The impact of human hyperekplexia mutations on glycine receptor structure and function.Semantic proximity Read ↗

Clinical, genetic, and functional characterization of the glycine receptor β-subunit A455P variant in a family affected by hyperekplexia syndrome.Semantic proximity Read ↗

Novel mutations in the glycine receptor alpha subunit gene in two sisters with hyperekplexia.Semantic proximity Read ↗

Pathophysiological mechanisms of dominant and recessive GLRA1 mutations in hyperekplexia.Semantic proximity Read ↗

Hyperekplexia associated with compound heterozygote mutations in the beta-subunit of the human inhibitory glycine receptor (GLRB).Semantic proximity Read ↗

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

Opposing effects of molecular volume and charge at the hyperekplexia site alpha 1(P250) govern glycine receptor activation and desensitization.Semantic proximity Read ↗

[GLYCINE RECEPTOR: MOLECULAR ORGANIZATION AND PATHOLOGY].Semantic proximity Read ↗

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

A critical role for glycine transporters in hyperexcitability disordersSemantic proximity Read ↗

A novel mutation (R218Q) at the boundary between the N-terminal and the first transmembrane domain of the glycine receptor in a case of sporadic hyperekplexia.Semantic proximity Read ↗

Statistical coassembly of glycine receptor alpha1 wildtype and the hyperekplexia mutant alpha1(P250T) in HEK 293 cells: impaired channel function is not dominant in the recombinant system.Semantic proximity Read ↗

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