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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 4 Aug 2009

Gustina Ahleah S, Trudeau Matthew C

Abstract excerpt

Human ether á go-go related gene (hERG) potassium channels play a central role in cardiac repolarization where channel closing (deactivation) regulates current density during action potentials. Consequently, mutations in hERG that perturb deactivation are linked to long QT syndrome (LQTS), a cata...

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Identifiers

PMID: 19651618
DOI: 10.1073/pnas.0900180106
PMCID: PMC2722319

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19651618-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

A recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channels.PMID 19651618Read ↗

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 ↗

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 ↗

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

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

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

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 ↗

C-terminal HERG (LQT2) mutations disrupt IKr channel regulation through 14-3-3epsilon.Semantic proximity Read ↗

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

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

Photo-crosslinking hERG channels causes a U.V.-driven, state-dependent disruption of kinetics and voltage dependence of activationSemantic proximity Read ↗

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