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

Erythromycin block of the HERG K+ channel: accessibility to F656 and Y652.

Biochemical and biophysical research communications - 10 Mar 2006

Duncan Rona S, Ridley John M, Dempsey Christopher E, Leishman Derek J, Leaney Joanne L, Hancox Jules C, Witchel Harry J

Abstract excerpt

The HERG potassium channel might have a non-canonical drug binding site, distinct from the channel's inner cavity, that could be responsible for elements of closed-state pharmacological inhibition of the channel. The macrolide antibiotic erythromycin is a drug that may block unconventionally because of its size. Here we used whole-cell patch-clamp recording at 37 degrees C from heterologously expressed HERG...

Read the complete abstract on PubMed

Topics

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

Share to Electrophysiology
Share to Erythromycin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ether-A-Go-Go Potassium Channels

Share to Inhibitory Concentration 50

Share to Models, Chemical

Share to Patch-Clamp Techniques

Share to Potassium Channels, Voltage-Gated

Share to Protein Synthesis Inhibitors

Source

Identifiers

PMID: 16446155
DOI: 10.1016/j.bbrc.2006.01.008

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

Erythromycin block of the HERG K+ channel: accessibility to F656 and Y652.PMID 16446155Read ↗

Inhibition of the HERG K+ channel by the antifungal drug ketoconazole depends on channel gating and involves the S6 residue F656.Semantic proximity Read ↗

The strength of hERG inhibition by Erythromycin at different temperature might be due to its different critical binding sites on the channelsSemantic proximity Read ↗

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

A novel mutation in hERG gene associated with azithromycin-induced acquired long QT syndrome.Semantic proximity Read ↗

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

Structural implications of hERG K+ channel block by a high-affinity minimally structured blocker.Semantic proximity Read ↗

Probing the molecular basis of hERG drug block with unnatural amino acids.Semantic proximity Read ↗

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

Blockage of hERG current and the disruption of trafficking as induced by roxithromycin.Semantic proximity Read ↗

Pharmacological corrections of the mutant hERG channels by posaconazole.Semantic proximity Read ↗

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

Blockade of the human ether-a-go-go-related gene potassium channel by ketanserin.Semantic proximity Read ↗

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