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

Molecular determinant of high-affinity dofetilide binding to HERG1 expressed in Xenopus oocytes: involvement of S6 sites.

Molecular pharmacology - 1 Feb 2000

Lees-Miller J P, Duan Y, Teng G Q, Duff H J

Abstract excerpt

This study reports that the affinity of HERG1 A for dofetilide is decreased from 0.125 +/- 0.003 microM for wild-type (WT) channels to 15 +/- 3 microM for F656V, a mutation in the COOH-terminal half of the S6. Similarly, the IC(50) for quinidine was increased from 8 +/- 4 microM for WT to 219 +/- 65 microM for the F656V mutation, whereas affinity for external tetraethylammonium was similar for WT (51 +/- 10 mM)...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Anti-Arrhythmia Agents
Share to Ether-A-Go-Go Potassium Channels

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phenylalanine

Share to Potassium Channels

Share to Potassium Channels, Voltage-Gated

Share to Quinidine

Share to Sulfonamides

Share to Xenopus laevis

Source

Identifiers

PMID: 10648647

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

Molecular determinant of high-affinity dofetilide binding to HERG1 expressed in Xenopus oocytes: involvement of S6 sites.PMID 10648647Read ↗

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

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

Block effect of capsaicin on hERG potassium currents is enhanced by S6 mutation at Y652.Semantic proximity Read ↗

Molecular basis of hERG potassium channel blockade by the class Ic antiarrhythmic flecainide.Semantic proximity Read ↗

Investigating the state dependence of drug binding in hERG channels using a trapped-open channel phenotype.Semantic proximity Read ↗

Inactivation gating determines drug potency: a common mechanism for drug blockade of HERG channels.Semantic proximity Read ↗

Molecular Basis for state-dependent drug block of Kv11.1 (HERG) potassium channelsSemantic proximity Read ↗

F463L increases the potential of dofetilide on human ether-a-go-go-related gene (hERG) channels.Semantic proximity Read ↗

An inner pore residue (Asn406) in the Nav1.5 channel controls slow inactivation and enhances mibefradil block to T-type Ca2+ channel levels.Semantic proximity Read ↗

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

RNA editing in eag potassium channels: biophysical consequences of editing a conserved S6 residue.Semantic proximity Read ↗

Redox state dependency of HERGS631C channel pharmacology: relation to C-type inactivation.Semantic proximity Read ↗

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