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

A cytosolic factor that inhibits KATP channels expressed in Xenopus oocytes by impairing Mg-nucleotide activation by SUR1.

The Journal of physiology - 15 Apr 2009

Tammaro Paolo, Ashcroft Frances M

Abstract excerpt

ATP-sensitive K(+) (K(ATP)) channels couple cell metabolism to cell electrical activity. Wild-type (Kir6.2/SUR1) K(ATP) channels heterologously expressed in Xenopus oocytes give rise to very small inward currents in cell-attached patches. A large increase in the current is observed on patch excision into zero ATP solution. This is presumably due to loss of intracellular ATP leading to unblock of K(ATP) channels....

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Diphosphate
Share to Electrophysiology
Share to KATP Channels

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Potassium Channel Blockers

Share to Potassium Channels, Inwardly Rectifying

Share to Receptors, Drug

Share to Sulfonylurea Receptors

Share to Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 19237428
DOI: 10.1113/jphysiol.2008.165126
PMCID: PMC2683953

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

A cytosolic factor that inhibits KATP channels expressed in Xenopus oocytes by impairing Mg-nucleotide activation by SUR1.PMID 19237428Read ↗

A gating mutation at the internal mouth of the Kir6.2 pore is associated with DEND syndrome.Semantic proximity Read ↗

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

Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions.Semantic proximity Read ↗

A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit.Semantic proximity Read ↗

MgATP activates the beta cell KATP channel by interaction with its SUR1 subunit.Semantic proximity Read ↗

Functional effects of naturally occurring KCNJ11 mutations causing neonatal diabetes on cloned cardiac KATP channels.Semantic proximity Read ↗

Functional effects of KCNJ11 mutations causing neonatal diabetes: enhanced activation by MgATP.Semantic proximity Read ↗

The Kir6.2-F333I mutation differentially modulates KATP channels composed of SUR1 or SUR2 subunits.Semantic proximity Read ↗

A universally conserved residue in the SUR1 subunit of the KATP channel is essential for translating nucleotide binding at SUR1 into channel opening.Semantic proximity Read ↗

A novel method for measurement of submembrane ATP concentration.Semantic proximity Read ↗

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

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