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Article

Fast and slow voltage sensor movements in HERG potassium channels.

The Journal of general physiology - 1 Mar 2002

Smith Paula L, Yellen Gary

Abstract excerpt

HERG encodes an inwardly-rectifying potassium channel that plays an important role in repolarization of the cardiac action potential. Inward rectification of HERG channels results from rapid and voltage-dependent inactivation gating, combined with very slow activation gating. We asked whether the voltage sensor is implicated in the unusual properties of HERG gating: does the voltage sensor move slowly to account...

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Identifiers

PMID: 11865022
DOI: 10.1085/jgp.20028534
PMCID: PMC2217288

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

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fast and slow voltage sensor movements in HERG potassium channels.PMID 11865022Read ↗

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

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

Conformational switch between slow and fast gating modes: allosteric regulation of voltage sensor mobility in the EAG K+ channel.Semantic proximity Read ↗

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

Potassium dependent structural changes in the selectivity filter of HERG potassium channelsSemantic proximity Read ↗

Domain IV voltage-sensor movement is both sufficient and rate limiting for fast inactivation in sodium channels.Semantic proximity Read ↗

The Fast Component of hERG Gating Charge: An Interaction between D411 in the S1 and S4 Residues.Semantic proximity Read ↗

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

Cooperative interactions between R531 and acidic residues in the voltage sensing module of hERG1 channels.Semantic proximity Read ↗

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

The neutral, hydrophobic isoleucine at position I521 in the extracellular S4 domain of hERG contributes to channel gating equilibrium.Semantic proximity Read ↗

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