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

A hydrophobicity-dependent motif responsible for surface expression of cardiac potassium channel.

Cellular signalling - 1 Feb 2009

Pan Na, Sun Jing, Lv Caixia, Li Hui, Ding Jiuping

Abstract excerpt

The long-QT syndrome (LQTS) is an inherited cardiac disorder associated with syncope and a high risk of sudden death. The molecular basis of type-1 LQTS (LQT1) is a missense or nonsense mutation in KCNQ channels that reduces slowly activating delayed rectifier potassium channel (I(Ks)) resulting in a prolonged action potential. Noticeably, the S2-S3 linker is a highly congregating region of LQT1 mutations. To...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Electrophysiology
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to KCNQ1 Potassium Channel

Share to Long QT Syndrome

Share to Luminescent Proteins

Share to Microscopy, Fluorescence

Source

Identifiers

PMID: 19041715
DOI: 10.1016/j.cellsig.2008.11.006

Genes

KCNQ1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A hydrophobicity-dependent motif responsible for surface expression of cardiac potassium channel.PMID 19041715Read ↗

Novel mechanisms of trafficking defect caused by KCNQ1 mutations found in long QT syndrome.Semantic proximity Read ↗

A590T mutation in KCNQ1 C-terminal helix D decreases IKs channel trafficking and function but not Yotiao interaction.Semantic proximity Read ↗

A residue at the cytoplasmic entrance of BK-type channels regulating single-channel opening by its hydrophobicity.Semantic proximity Read ↗

The rate-dependent biophysical properties of the LQT1 H258R mutant are counteracted by a dominant negative effect on channel trafficking.Semantic proximity Read ↗

Functional effects of a KCNQ1 mutation associated with the long QT syndrome.Semantic proximity Read ↗

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

Microscopic mechanisms for long QT syndrome type 1 revealed by single-channel analysis of I(Ks) with S3 domain mutations in KCNQ1.Semantic proximity Read ↗

The role of abnormal trafficking of KCNE1 in long QT syndrome 5.Semantic proximity Read ↗

The N-Terminal Juxtamembranous Domain of KCNQ1 Is Critical for Channel Surface ExpressionSemantic proximity Read ↗

Phenotypic characterization of a novel long-QT syndrome mutation (R1623Q) in the cardiac sodium channel.Semantic proximity Read ↗

Trafficking and functional expression of cardiac Na+ channels.Semantic proximity Read ↗

A novel mutation KCNQ1p.Thr312del is responsible for long QT syndrome type 1.Semantic proximity Read ↗

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