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Article

N-Glycosylation-dependent block is a novel mechanism for drug-induced cardiac arrhythmia.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Dec 2003

Park Ki-Ho, Kwok Suk-Mei, Sharon Chetna, Baerga Rebecca, Berga Rebecca, Sesti Federico

Abstract excerpt

Voltage-gated potassium channels formed with the cardiac subunit HERG and a polymorphic variant of MinK-related peptide 1 (MiRP1) exhibit increased susceptibility to the antibiotic sulfamethoxazole (SMX) compared with channels formed with wild-type (WT) subunits. Here the molecular bases for SMX high-affinity block are investigated. The polymorphism causes a benign T to A amino acid mutation at position 8 (T8A)...

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Share to Arrhythmias, Cardiac
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 14563681
DOI: 10.1096/fj.03-0577fje

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.

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N-Glycosylation-dependent block is a novel mechanism for drug-induced cardiac arrhythmia.PMID 14563681Read ↗

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Structural determinants for high-affinity block of hERG potassium channels.Semantic proximity Read ↗

Does hERG coassemble with a beta subunit? Evidence for roles of MinK and MiRP1.Semantic proximity Read ↗

Molecular determinants of inactivation and dofetilide block in ether a-go-go (EAG) channels and EAG-related K(+) channels.Semantic proximity Read ↗

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The low-potency, voltage-dependent HERG blocker propafenone--molecular determinants and drug trapping.Semantic proximity Read ↗

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Physicochemical features of the HERG channel drug binding site.Semantic proximity Read ↗

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