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

Role of intracellular domains in the function of the herg potassium channel.

European biophysics journal : EBJ - 1 Jun 2009

Al-Owais Moza, Bracey Kate, Wray Dennis

Abstract excerpt

The functional role of the large intracellular regions (which include the cyclic nucleotide binding domain, cNBD, and the Per-Arnt-Sim domain, PAS) in the herg channel is not well understood. We have studied possible interactions of the cNBD with other parts of the channel protein using lysine mutations to disrupt such interactions. Some lysine mutations caused significant right shifts in the voltage dependence...

Read the complete abstract on PubMed

Topics

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

Share to ERG1 Potassium Channel
Share to Ether-A-Go-Go Potassium Channels
Share to Intracellular Space

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

Share to Long QT Syndrome

Share to Models, Molecular

Share to Mutation

Share to Protein Structure, Tertiary

Source

Identifiers

PMID: 19172259
DOI: 10.1007/s00249-009-0408-2

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

Role of intracellular domains in the function of the herg potassium channel.PMID 19172259Read ↗

hERG potassium channel gating is mediated by N- and C-terminal region interactions.Semantic proximity Read ↗

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

Rescue of aberrant gating by a genetically encoded PAS (Per-Arnt-Sim) domain in several long QT syndrome mutant human ether-á-go-go-related gene potassium channels.Semantic proximity Read ↗

Structural properties of PAS domains from the KCNH potassium channels.Semantic proximity Read ↗

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

A novel missense mutation causing a G487R substitution in the S2-S3 loop of human ether-à-go-go-related gene channel.Semantic proximity Read ↗

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

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

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

Allosteric effects of mutations in the extracellular S5-P loop on the gating and ion permeation properties of the hERG potassium channel.Semantic proximity Read ↗

Two mutations at different positions in the CNBH domain of the hERG channel accelerate deactivation and impair the interaction with the EAG domain.Semantic proximity Read ↗

The inward rectification mechanism of the HERG cardiac potassium channel.Semantic proximity Read ↗

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