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Article

Mutations in the M4 domain of the Torpedo californica nicotinic acetylcholine receptor alter channel opening and closing.

The Journal of membrane biology - 1 Jul 1997

Ortiz-Miranda S I, Lasalde J A, Pappone P A, McNamee M G

Abstract excerpt

We studied the functional effects of single amino acid substitutions in the postulated M4 transmembrane domains of Torpedo californica nicotinic acetylcholine receptors (nAChRs) expressed in Xenopus oocytes at the single-channel level. At low ACh concentrations and cold temperatures, the replacement of wild-type alpha418Cys residues with the large, hydrophobic amino acids tryptophan or phenylalanine increased...

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Source

Identifiers

PMID: 9211718
DOI: 10.1007/s002329900240

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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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