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Article

Homologous mutations on different subunits cause unequal but additive effects on n-alcohol block in the nicotinic receptor pore.

Biophysical journal - 1 May 1997

Forman S A

Abstract excerpt

Hydrophobic antagonists of the nicotinic acetylcholine receptor inhibit channel activity by binding within the transmembrane pore formed by the second of four transmembrane domains (M2) on each of the receptor's subunits. Hydrophobic mutagenesis near the middle (10' locus) of the alpha-subunit M2 domain results in channels that are much more sensitive to block by long-chain alcohols and general anesthetics,...

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Identifiers

PMID: 9129819
DOI: 10.1016/S0006-3495(97)78860-X
PMCID: PMC1184411

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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