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Article

Differential effects of homologous S4 mutations in human skeletal muscle sodium channels on deactivation gating from open and inactivated states.

The Journal of physiology - 1 May 1999

Groome J R, Fujimoto E, George A L, Ruben P C

Abstract excerpt

1. The outermost charged amino acid of S4 segments in the alpha subunit of human skeletal muscle sodium channels was mutated to cysteine in domains I (R219C), II (R669C), III (K1126C), and IV (R1448C). Double mutations in DIS4 and DIVS4 (R219C/R1448C), DIIS4 and DIVS4 (R669C/R1448C), and DIIIS4 a...

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Identifiers

PMID: 10200418
DOI: 10.1111/j.1469-7793.1999.0687u.x
PMCID: PMC2269298

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-10200418-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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