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Article

Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation.

The Journal of general physiology - 1 Mar 1999

Ledwell J L, Aldrich R W

Abstract excerpt

Charged residues in the S4 transmembrane segment play a key role in determining the sensitivity of voltage-gated ion channels to changes in voltage across the cell membrane. However, cooperative interactions between subunits also affect the voltage dependence of channel opening, and these interac...

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Identifiers

PMID: 10051516
DOI: 10.1085/jgp.113.3.389
PMCID: PMC2222902

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-10051516-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

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Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation.PMID 10051516Read ↗

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Resolving the gating charge movement associated with late transitions in K channel activation.Semantic proximity Read ↗

Electrostatic interactions between transmembrane segments mediate folding of Shaker K+ channel subunits.Semantic proximity Read ↗

Functional interactions at the interface between voltage-sensing and pore domains in the Shaker K(v) channel.Semantic proximity Read ↗

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Hydrophobic substitution mutations in the S4 sequence alter voltage-dependent gating in Shaker K+ channels.Semantic proximity Read ↗

The conserved phenylalanine in the K+ channel voltage-sensor domain creates a barrier with unidirectional effects.Semantic proximity Read ↗

Atomic proximity between S4 segment and pore domain in Shaker potassium channels.Semantic proximity Read ↗

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