Article

Inhibition mechanism of pancreatic KATP channels by centipede toxins

2025-10-27

Abstract excerpt

The pancreatic ATP-sensitive potassium (KATP) channel acts as a crucial metabolic sensor by regulating insulin secretion to maintain whole-body energy homeostasis. Gain-of-functional mutations in this channel lead to neonatal diabetes mellitus, a rare disorder in which certain mutants demonstrate resistance to standard sulfonylurea therapy. Recent studies have identified a centipede toxin, SpTx1, as a potent inhib...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 98c55d4e-6dd1-56af-a34c-9b2944e71235
DOI: 10.1101/2025.10.27.684718

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Inhibition mechanism of pancreatic KATP channels by centipede toxinsDOI 10.1101/2025.10.27.684718Read

New insights into KATP channel gene mutations and neonatal diabetes mellitus.Semantic proximity Read

Mutations in the Kir6.2 subunit of the KATP channel and permanent neonatal diabetes: new insights and new treatment.Semantic proximity Read

Molecular structure of an open human KATP channel.Semantic proximity Read

Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization.Semantic proximity Read

Conformational decoupling in acid-sensing ion channels uncovers mechanism and stoichiometry of PcTx1-mediated inhibition.Semantic proximity Read

Structure of the receptor-activated human TRPC6 ion channelSemantic proximity Read

Discovery and characterisation of a novel toxin from Dendroaspis angusticeps, named Tx7335, that activates the potassium channel KcsA.Semantic proximity Read

PIP2 inhibits pore opening of the cyclic nucleotide-gated channel SthK.Semantic proximity Read

A novel KCNJ11 mutation associated with congenital hyperinsulinism reduces the intrinsic open probability of beta-cell ATP-sensitive potassium channels.Semantic proximity Read

Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterizationSemantic proximity Read

The Shifting Landscape of K<sub>Atp</sub>Channelopathies and the Need for ‘Sharper’ TherapeuticsSemantic proximity Read

ATP-sensitive potassium channels: a model of heteromultimeric potassium channel/receptor assemblies.Semantic proximity Read