Dominant negative mutant of ionotropic glutamate receptor subunit GluR3: implications for the role of a cysteine residue for its channel activity and pharmacological properties.

doi:10.1042/bj3220385

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Article

Dominant negative mutant of ionotropic glutamate receptor subunit GluR3: implications for the role of a cysteine residue for its channel activity and pharmacological properties.

The Biochemical journal - 1 Mar 1997

Watase K, Sekiguchi M, Matsui T A, Tagawa Y, Wada K

Abstract excerpt

We reported that a 33-amino-acid deletion (from tyrosine-715 to glycine-747) in a putative extracellular loop of GluR3 produced a mutant that exhibited dominant negative effects upon the functional expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors [Sekiguchi...

Topics

Amino Acid Sequence
Animals
Cell Compartmentation
Cell Membrane
Cysteine
Dose-Response Relationship, Drug
Electrophysiology
Glutamic Acid
Ion Channels
Kainic Acid
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oocytes

Phenotype

Point Mutation

Protein Conformation

Receptors, AMPA

Recombinant Proteins

Structure-Activity Relationship

Source

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Identifiers

PMID: 9065754
DOI: 10.1042/bj3220385
PMCID: PMC1218203

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9065754-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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