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

Cysteine 723 in the C-linker segment confers oxidative inhibition of hERG1 potassium channels.

The Journal of physiology - 15 Aug 2010

Kolbe Katrin, Schönherr Roland, Gessner Guido, Sahoo Nirakar, Hoshi Toshinori, Heinemann Stefan H

Abstract excerpt

Excess reactive oxygen species (ROS) play a crucial role under pathophysiological conditions, such as ischaemia/reperfusion and diabetes, potentially contributing to cardiac arrhythmia. hERG1 (KCNH2) potassium channels terminate the cardiac action potential and malfunction can lead to long-QT syndrome and fatal arrhythmia. To investigate the molecular mechanisms of hERG1 channel alteration by ROS, hERG1 and...

Read the complete abstract on PubMed

Topics

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

Share to Cysteine
Share to Ether-A-Go-Go Potassium Channels

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Ion Channel Gating

Share to Membrane Potentials

Share to Oxidants

Share to Patch-Clamp Techniques

Share to Potassium Channel Blockers

Share to Sulfhydryl Reagents

Source

Open in PubMed Open full text

Identifiers

PMID: 20547678
DOI: 10.1113/jphysiol.2010.192468
PMCID: PMC2956941

Genes

KCNH2

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cysteine 723 in the C-linker segment confers oxidative inhibition of hERG1 potassium channels.PMID 20547678Read ↗

A highly conserved alanine in the S6 domain of the hERG1 K+ channel is required for normal gating.Semantic proximity Read ↗

State-dependent and site-directed photodynamic transformation of HCN2 channel by singlet oxygen.Semantic proximity Read ↗

Interactions between the N-terminal tail and the gating machinery of hERG K⁺ channels both in closed and open/inactive states.Semantic proximity Read ↗

Three methionine residues located within the regulator of conductance for K+ (RCK) domains confer oxidative sensitivity to large-conductance Ca2+-activated K+ channels.Semantic proximity Read ↗

Constitutive Inhibition of Transient Receptor Potential Canonical Type 6 (TRPC6) by O-GlcNAcylation at Threonine-221Semantic proximity Read ↗

Evidence for redox sensing by a human cardiac calcium channel.Semantic proximity Read ↗

Impairment of human ether-à-go-go-related gene (HERG) K+ channel function by hypoglycemia and hyperglycemia. Similar phenotypes but different mechanisms.Semantic proximity Read ↗

Clinical and electrophysiological characterization of a novel mutation R863X in HERG C-terminus associated with long QT syndrome.Semantic proximity Read ↗

Thiol dependent intramolecular locking of Orai1 channels.Semantic proximity Read ↗

Structural Basis for Rapid Voltage Dependent Inactivation of HERG Potassium ChannelsSemantic proximity Read ↗

Regulation of Glutathione S-Transferase Omega 1 Mediated by Cysteine Residues Sensing the Redox Environment.Semantic proximity Read ↗

Eag1 K+ Channel: Endogenous Regulation and Functions in Nervous System.Semantic proximity Read ↗

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