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

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

The Journal of physiology - 1 Oct 2018

Kume Shinichiro, Shimomura Takushi, Tateyama Michihiro, Kubo Yoshihiro

Abstract excerpt

KEY POINTS: In the human ether-a-go-go related gene (hERG) channel, both the ether-a-go-go (EAG) domain in the N-terminal and the cyclic nucleotide (CN) binding homology (CNBH) domain in the C-terminal cytoplasmic region are known to contribute to the characteristic slow deactivation. Mutations of Phe860 in the CNBH domain, reported to fill the CN binding pocket, accelerate the deactivation and decrease the...

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 Fluorescence Resonance Energy Transfer

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ion Channel Gating

Share to Oocytes

Share to Protein Domains

Share to Sequence Homology

Share to Static Electricity

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 30086184
DOI: 10.1113/JP276208
PMCID: PMC6166088

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

Two mutations at different positions in the CNBH domain of the hERG channel accelerate deactivation and impair the interaction with the EAG domain.PMID 30086184Read ↗

Direct interaction of eag domains and cyclic nucleotide-binding homology domains regulate deactivation gating in hERG channels.Semantic proximity Read ↗

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

A recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channels.Semantic proximity Read ↗

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

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

Concerted all-or-none subunit interactions mediate slow deactivation of human ether-à-go-go-related gene K+ 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 ↗

Structure of the C-terminal region of an ERG channel and functional implications.Semantic proximity Read ↗

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

Multiple interactions between cytoplasmic domains regulate slow deactivation of Kv11.1 channels.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 ↗

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