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Article

State-dependent changes in the electrostatic potential in the pore of a GluR channel.

Biophysical journal - 1 Jan 2005

Sobolevsky Alexander I, Yelshansky Maria V, Wollmuth Lonnie P

Abstract excerpt

The M2 loop and the M3 segment are the major pore-lining domains in the GluR channel. These domains determine ion permeation and channel block processes and are extensively involved in gating. To study the distribution of the membrane electric potential across the GluR channel pore, we recorded from alpha-amino-3-hydroxy-5-methylisoxazole-4-proprionic acid receptors containing M2 and M3 cysteine substitutions in...

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Identifiers

PMID: 15516523
DOI: 10.1529/biophysj.104.049411
PMCID: PMC1305001

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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