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

Structural basis for the interference between nicorandil and sulfonylurea action.

Diabetes - 1 Oct 2001

Reimann F, Ashcroft F M, Gribble F M

Abstract excerpt

Nicorandil is a new antianginal agent that potentially may be used to treat the cardiovascular side effects of diabetes. It is both a nitric oxide donor and an opener of ATP-sensitive K(+) (K(ATP)) channels in muscle and thereby causes vasodilation of the coronary vasculature. The aim of this study was to investigate the domains of the K(ATP) channel involved in nicorandil activity and to determine whether...

Read the complete abstract on PubMed

Topics

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

Share to Drug Interactions
Share to Electrophysiology
Share to Mixed Function Oxygenases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Oocytes

Share to Potassium Channels

Share to Potassium Channels, Inwardly Rectifying

Share to Sulfonylurea Compounds

Share to Xenopus laevis

Source

Identifiers

PMID: 11574406
DOI: 10.2337/diabetes.50.10.2253

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for the interference between nicorandil and sulfonylurea action.PMID 11574406Read ↗

A functional role of the C-terminal 42 amino acids of SUR2A and SUR2B in the physiology and pharmacology of cardiovascular ATP-sensitive K(+) channels.Semantic proximity Read ↗

Molecular determinants of KATP channel inhibition by ATP.Semantic proximity Read ↗

Functional analysis of six Kir6.2 (KCNJ11) mutations causing neonatal diabetes.Semantic proximity Read ↗

Nucleotide modulation of pinacidil stimulation of the cloned K(ATP) channel Kir6.2/SUR2A.Semantic proximity Read ↗

Differential response of K(ATP) channels containing SUR2A or SUR2B subunits to nucleotides and pinacidil.Semantic proximity Read ↗

The G53D mutation in Kir6.2 (KCNJ11) is associated with neonatal diabetes and motor dysfunction in adulthood that is improved with sulfonylurea therapy.Semantic proximity Read ↗

Substitution of the Walker A lysine by arginine in the nucleotide-binding domains of sulphonylurea receptor SUR2B: effects on ligand binding and channel activity.Semantic proximity Read ↗

Three C-terminal residues from the sulphonylurea receptor contribute to the functional coupling between the K(ATP) channel subunits SUR2A and Kir6.2.Semantic proximity Read ↗

Mutation in nucleotide-binding domains of sulfonylurea receptor 2 evokes Na-ATP-dependent activation of ATP-sensitive K+ channels: implication for dimerization of nucleotide-binding domains to induce channel opening.Semantic proximity Read ↗

Functional effects of mutations at F35 in the NH2-terminus of Kir6.2 (KCNJ11), causing neonatal diabetes, and response to sulfonylurea therapy.Semantic proximity Read ↗

The Pharmacology of ATP-Sensitive K+ Channels (KATP).Semantic proximity Read ↗

Potassium channel regulation.Semantic proximity Read ↗

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