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

Procaine, a state-dependent blocker, inhibits HERG channels by helix residue Y652 and F656 in the S6 transmembrane domain.

Journal of pharmacological sciences - 20 Sept 2013

Wang Na, Ma Ji Hua, Zhang Pei Hua

Abstract excerpt

The article evaluated the inhibitory action of procaine on wild-type and mutated HERG potassium channel current (I(HERG)) to determine whether mutations in the S6 region are important for the inhibition of I(HERG) by procaine. HERG channels (WT, Y652A, and F656A) were expressed in Xenopus laevis oocytes and studied using the standard two-microelectrode voltage-clamp technique. The results revealed that WT HERG is...

Read the complete abstract on PubMed

Topics

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

Share to Anesthetics, Local
Share to Dose-Response Relationship, Drug

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ether-A-Go-Go Potassium Channels

Share to Helix-Loop-Helix Motifs

Share to Oocytes

Share to Patch-Clamp Techniques

Share to Protein Structure, Tertiary

Share to Xenopus laevis

Source

Identifiers

PMID: 24005047
DOI: 10.1254/jphs.13007fp

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

Procaine, a state-dependent blocker, inhibits HERG channels by helix residue Y652 and F656 in the S6 transmembrane domain.PMID 24005047Read ↗

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

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

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

Papaverine, a vasodilator, blocks the pore of the HERG channel at submicromolar concentration.Semantic proximity Read ↗

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

H(1) antihistamine drug promethazine directly blocks hERG K(+) channel.Semantic proximity Read ↗

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

Block of hERG channel by ziprasidone: biophysical properties and molecular determinants.Semantic proximity Read ↗

Inhibition of cardiac HERG potassium channels by the atypical antidepressant trazodone.Semantic proximity Read ↗

Comparison of the effects of antiarrhythmic drugs flecainide and verapamil on fKv1.4ΔN channel currents in Xenopus oocytes.Semantic proximity Read ↗

Peimine inhibits hERG potassium channels through the channel inactivation states.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 ↗

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