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Article

Study of permeation and blocker binding in TMEM16A calcium-activated chloride channels.

Channels (Austin, Tex.) - 1 Jan 2015

Reyes J P, Huanosta-Gutiérrez A, López-Rodríguez A, Martínez-Torres A

Abstract excerpt

We studied the effects of mutations of positively charged amino acid residues in the pore of X. tropicalis TMEM16A calcium-activated chloride channels: K613E, K628E, K630E; R646E and R761E. The activation and deactivation kinetics were not affected, and only K613E showed a lower current density. K628E and R761E affect anion selectivity without affecting Na(+) permeation, whereas K613E, R646E and the double mutant...

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Identifiers

PMID: 25853341
DOI: 10.1080/19336950.2015.1027849
PMCID: PMC4594575

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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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Study of permeation and blocker binding in TMEM16A calcium-activated chloride channels.PMID 25853341Read ↗

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