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Article

Proton block of the pore underlies the inhibition of hERG cardiac K+ channels during acidosis.

American journal of physiology. Cell physiology - 15 Jun 2012

Van Slyke Aaron C, Cheng Yen May, Mafi Pouya, Allard Charlene R, Hull Christina M, Shi Yu Patrick, Claydon Tom W

Abstract excerpt

Human ether-a-go-go-related gene (hERG) potassium channels are critical determinants of cardiac repolarization. Loss of function of hERG channels is associated with Long QT Syndrome, arrhythmia, and sudden death. Acidosis occurring as a result of myocardial ischemia inhibits hERG channel function and may cause a predisposition to arrhythmias. Acidic pH inhibits hERG channel maximal conductance and accelerates...

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Source

Identifiers

PMID: 22517356
DOI: 10.1152/ajpcell.00324.2011

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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

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Proton block of the pore underlies the inhibition of hERG cardiac K+ channels during acidosis.PMID 22517356Read ↗

Identification of a proton sensor that regulates conductance and open time of single hERG channels.Semantic proximity Read ↗

Inhibition of G-protein-coupled inward rectifying K+ channels by intracellular acidosis.Semantic proximity Read ↗

External protons destabilize the activated voltage sensor in hERG channels.Semantic proximity Read ↗

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

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

Blockade of permeation by potassium but normal gating of the G628S nonconducting hERG channel mutant.Semantic proximity Read ↗

Extracellular K+ is a prerequisite for the function and plasma membrane stability of HERG channels.Semantic proximity Read ↗

A mutation in the pore region of HERG K+ channels expressed in Xenopus oocytes reduces rectification by shifting the voltage dependence of inactivation.Semantic proximity Read ↗

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

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

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

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