Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Characterization of KCNQ1 atrial fibrillation mutations reveals distinct dependence on KCNE1.

The Journal of general physiology - 1 Feb 2012

Chan Priscilla J, Osteen Jeremiah D, Xiong Dazhi, Bohnen Michael S, Doshi Darshan, Sampson Kevin J, Marx Steven O, Karlin Arthur, Kass Robert S

Abstract excerpt

The I(Ks) potassium channel, critical to control of heart electrical activity, requires assembly of α (KCNQ1) and β (KCNE1) subunits. Inherited mutations in either I(Ks) channel subunit are associated with cardiac arrhythmia syndromes. Two mutations (S140G and V141M) that cause familial atrial fibrillation (AF) are located on adjacent residues in the first membrane-spanning domain of KCNQ1, S1. These mutations...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Action Potentials
Share to Atrial Fibrillation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to CHO Cells

Share to Cricetinae

Share to Cysteine

Share to KCNQ1 Potassium Channel

Share to Potassium Channels, Voltage-Gated

Share to Protein Interaction Domains and Motifs

Source

Open in PubMed Open full text

Identifiers

PMID: 22250012
DOI: 10.1085/jgp.201110672
PMCID: PMC3269792

Genes

KCNQ1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of KCNQ1 atrial fibrillation mutations reveals distinct dependence on KCNE1.PMID 22250012Read ↗

Mechanisms by which atrial fibrillation-associated mutations in the S1 domain of KCNQ1 slow deactivation of IKs channels.Semantic proximity Read ↗

KCNQ1 gain-of-function mutation in familial atrial fibrillation.Semantic proximity Read ↗

Structural basis of slow activation gating in the cardiac I Ks channel complex.Semantic proximity Read ↗

Gating mechanisms underlying deactivation slowing by two KCNQ1 atrial fibrillation mutations.Semantic proximity Read ↗

KCNQ1 K+ channel-mediated cardiac channelopathies.Semantic proximity Read ↗

Selective targeting of gain-of-function KCNQ1 mutations predisposing to atrial fibrillation.Semantic proximity Read ↗

Functional Interactions between KCNE1 C-Terminus and the KCNQ1 ChannelSemantic proximity Read ↗

KCNE1 alters the voltage sensor movements necessary to open the KCNQ1 channel gate.Semantic proximity Read ↗

Insights into Cardiac IKs (KCNQ1/KCNE1) Channels RegulationSemantic proximity Read ↗

Dysfunctional potassium channel subunit interaction as a novel mechanism of long QT syndrome.Semantic proximity Read ↗

Overlapping cardiac phenotype associated with a familial mutation in the voltage sensor of the KCNQ1 channel.Semantic proximity Read ↗

In silico investigation of a KCNQ1 mutation associated with familial atrial fibrillation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.