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Article

Pore helix-S6 interactions are critical in governing current amplitudes of KCNQ3 K+ channels.

Biophysical journal - 6 Jun 2012

Choveau Frank S, Bierbower Sonya M, Shapiro Mark S

Abstract excerpt

Two mechanisms have been postulated to underlie KCNQ3 homomeric current amplitudes, which are small compared with those of KCNQ4 homomers and KCNQ2/Q3 heteromers. The first involves differential channel expression governed by the D-helix within the C-terminus. The second suggests similar channel...

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Source

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Identifiers

PMID: 22713565
DOI: 10.1016/j.bpj.2012.04.019
PMCID: PMC3368123

Genes

KCNQ3
KCNQ4
KCNQ2

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22713565-2026-09-04.2. 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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Pore helix-S6 interactions are critical in governing current amplitudes of KCNQ3 K+ channels.PMID 22713565Read ↗

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