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

Modulation of HERG gating by a charge cluster in the N-terminal proximal domain.

Biophysical journal - 15 Dec 2006

Saenen J B, Labro A J, Raes A, Snyders D J

Abstract excerpt

Human ether-a-go-go-related gene (HERG) potassium channels contribute to the repolarization of the cardiac action potential and display unique gating properties with slow activation and fast inactivation kinetics. Deletions in the N-terminal 'proximal' domain (residues 135-366) have been shown to induce hyperpolarizing shifts in the voltage dependence of activation, suggesting that it modulates activation....

Read the complete abstract on PubMed

Topics

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

Share to Cell Line
Share to ERG1 Potassium Channel
Share to Ether-A-Go-Go Potassium Channels

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ion Channel Gating

Share to Mutation

Share to Patch-Clamp Techniques

Share to Protein Structure, Tertiary

Share to Static Electricity

Source

Open in PubMed Open full text

Identifiers

PMID: 16997865
DOI: 10.1529/biophysj.106.087247
PMCID: PMC1779935

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Modulation of HERG gating by a charge cluster in the N-terminal proximal domain.PMID 16997865Read ↗

Sequence of gating charge movement and pore gating in HERG activation and deactivation pathways.Semantic proximity Read ↗

Molecular basis of slow activation of the human ether-a-go-go related gene potassium channel.Semantic proximity Read ↗

Functional interactions of voltage sensor charges with an S2 hydrophobic plug in hERG channels.Semantic proximity Read ↗

Functional characterization of the C-terminus of the human ether-à-go-go-related gene K(+) channel (HERG).Semantic proximity Read ↗

Voltage sensor movement in the hERG K+ channel.Semantic proximity Read ↗

An intracellular hydrophobic nexus is critical for slow deactivation in hERG channelsSemantic proximity Read ↗

Role of intracellular domains in the function of the herg potassium channel.Semantic proximity Read ↗

The evolutionarily conserved residue A653 plays a key role in HERG channel closing.Semantic proximity Read ↗

Molecular determinants for activation and inactivation of HERG, a human inward rectifier potassium channel.Semantic proximity Read ↗

HERG, a human inward rectifier in the voltage-gated potassium channel family.Semantic proximity Read ↗

The pore domain outer helix contributes to both activation and inactivation of the HERG K+ channel.Semantic proximity Read ↗

Molecular analysis of PIP2 regulation of HERG and IKr.Semantic proximity Read ↗

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