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

The first clinical case of a mutation at residue K185 of Kir6.2 (KCNJ11): a major ATP-binding residue.

Diabetic medicine : a journal of the British Diabetic Association - 1 Feb 2010

Shimomura K, de Nanclares G P, Foutinou C, Caimari M, Castaño L, Ashcroft F M

Abstract excerpt

BACKGROUND: Closure of the adenosine triphosphate (ATP)-sensitive potassium (K(ATP)) channel plays a key role in insulin secretion from the pancreatic beta-cells. Many mutations in KCNJ11 and ABCC8, which respectively encode the pore-forming (Kir6.2) and regulatory (SUR1) subunits of the K(ATP) channel, cause neonatal diabetes. All such mutations impair the ability of metabolically generated ATP to close the...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to ATP-Binding Cassette Transporters

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Child, Preschool

Share to Diabetes Complications

Share to Diabetes Mellitus

Share to Hyperglycemia

Share to Infant, Newborn

Share to Potassium Channels, Inwardly Rectifying

Source

Identifiers

PMID: 20546268
DOI: 10.1111/j.1464-5491.2009.02901.x

Genes

KCNJ11
ABCC8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The first clinical case of a mutation at residue K185 of Kir6.2 (KCNJ11): a major ATP-binding residue.PMID 20546268Read ↗

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 ↗

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

The role of lysine 185 in the kir6.2 subunit of the ATP-sensitive channel in channel inhibition by ATP.Semantic proximity Read ↗

Mutations at the same residue (R50) of Kir6.2 (KCNJ11) that cause neonatal diabetes produce different functional effects.Semantic proximity Read ↗

Focus on Kir6.2: a key component of the ATP-sensitive potassium channel.Semantic proximity Read ↗

Functional analysis of two Kir6.2 (KCNJ11) mutations, K170T and E322K, causing neonatal diabetes.Semantic proximity Read ↗

A Kir6.2 mutation causing severe functional effects in vitro produces neonatal diabetes without the expected neurological complications.Semantic proximity Read ↗

Mutation of the pancreatic islet inward rectifier Kir6.2 also leads to familial persistent hyperinsulinemic hypoglycemia of infancy.Semantic proximity Read ↗

Neonatal diabetes caused by a homozygous KCNJ11 mutation demonstrates that tiny changes in ATP sensitivity markedly affect diabetes risk.Semantic proximity Read ↗

Diabetes and hypoglycaemia in young children and mutations in the Kir6.2 subunit of the potassium channel: therapeutic consequences.Semantic proximity Read ↗

Update of mutations in the genes encoding the pancreatic beta-cell K(ATP) channel subunits Kir6.2 (KCNJ11) and sulfonylurea receptor 1 (ABCC8) in diabetes mellitus and hyperinsulinism.Semantic proximity Read ↗

A conserved tryptophan at the membrane-water interface acts as a gatekeeper for Kir6.2/SUR1 channels and causes neonatal diabetes when mutated.Semantic proximity Read ↗

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