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Article

Mechanism of charybdotoxin block of a voltage-gated K+ channel.

Biophysical journal - 1 Oct 1993

Goldstein S A, Miller C

Abstract excerpt

Charybdotoxin block of a Shaker K+ channel was studied in Xenopus oocyte macropatches. Toxin on rate increases linearly with toxin concentration in an ionic strength-dependent fashion and is competitively diminished by tetraethylammonium. On rate is insensitive to transmembrane voltage and to K+ on the opposite side of the membrane. Conversely, toxin off rate is insensitive to toxin concentration, ionic strength,...

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Identifiers

PMID: 7506068
DOI: 10.1016/S0006-3495(93)81200-1
PMCID: PMC1225887

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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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Mechanism of charybdotoxin block of a voltage-gated K+ channel.PMID 7506068Read ↗

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The influence of surface charges on quaternary ammonium block of shaker K+ channels.Semantic proximity Read ↗

Discovery and characterisation of a novel toxin from Dendroaspis angusticeps, named Tx7335, that activates the potassium channel KcsA.Semantic proximity Read ↗

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