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Article

Structural determinants of barium permeation and rectification in non-NMDA glutamate receptor channels.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 1 Oct 1992

Dingledine R, Hume R I, Heinemann S F

Abstract excerpt

A single site in recombinant glutamate receptor channels of the GluR1-GluR4 family has been previously identified as a key regulator of ion permeation. The natural amino acid at this position (arginine in GluR2 but glutamine in GluR1, GluR3, and GluR4) determines both the ability to pass outward current and the divalent cation permeability of kainate-activated receptor channels. By mutagenesis of GluR6, we...

Topics

Amino Acid Sequence
Animals
Arginine
Barium
Glutamates
Glutamic Acid
Glutamine
Molecular Sequence Data
Mutation
N-Methylaspartate
Permeability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Receptors, Glutamate

Receptors, N-Methyl-D-Aspartate

Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 1357118
PMCID: PMC6575955

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1357118-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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