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

Susceptibility of glucokinase-MODY mutants to inactivation by oxidative stress in pancreatic β-cells.

Diabetes - 1 Dec 2011

Cullen Kirsty S, Matschinsky Franz M, Agius Loranne, Arden Catherine

Abstract excerpt

OBJECTIVE: The posttranslational regulation of glucokinase (GK) differs in hepatocytes and pancreatic β-cells. We tested the hypothesis that GK mutants that cause maturity-onset diabetes of the young (GK-MODY) show compromised activity and posttranslational regulation in β-cells. RESEARCH DESIGN AND METHODS: Activity and protein expression of GK-MODY and persistent hyperinsulinemic hypoglycemia of infancy (PHHI)...

Read the complete abstract on PubMed

Topics

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

Share to Diabetes Mellitus, Type 2
Share to Glucokinase
Share to Glutathione

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

Share to Hydrogen Peroxide

Share to Insulin-Secreting Cells

Share to Nitric Oxide

Share to Oxidative Stress

Share to Rats, Wistar

Source

Open in PubMed Open full text

Identifiers

PMID: 22028181
DOI: 10.2337/db11-0423
PMCID: PMC3219952

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Susceptibility of glucokinase-MODY mutants to inactivation by oxidative stress in pancreatic β-cells.PMID 22028181Read ↗

Characterization of glucokinase mutations associated with maturity-onset diabetes of the young type 2 (MODY-2): different glucokinase defects lead to a common phenotype.Semantic proximity Read ↗

GCK-MODY diabetes associated with protein misfolding, cellular self-association and degradation.Semantic proximity Read ↗

Effects of novel maturity-onset diabetes of the young (MODY)-associated mutations on glucokinase activity and protein stability.Semantic proximity Read ↗

Functional analysis of human glucokinase gene mutations causing MODY2: exploring the regulatory mechanisms of glucokinase activity.Semantic proximity Read ↗

Glucokinase (GCK) in diabetes: from molecular mechanisms to disease pathogenesis.Semantic proximity Read ↗

From clinicogenetic studies of maturity-onset diabetes of the young to unraveling complex mechanisms of glucokinase regulation.Semantic proximity Read ↗

Glucokinase (GCK) mutations in hyper- and hypoglycemia: maturity-onset diabetes of the young, permanent neonatal diabetes, and hyperinsulinemia of infancy.Semantic proximity Read ↗

Biochemical characterization of MODY2 glucokinase variants V62M and G72R reveals reduced enzymatic activities relative to wild type.Semantic proximity Read ↗

A clinical mutation in glucokinase causing maturity-onset diabetes in the young type 2 increases enzyme activity.Semantic proximity Read ↗

Characterization of two MODY2 mutations with different susceptibility to activation.Semantic proximity Read ↗

Phenotypic severity of homozygous GCK mutations causing neonatal or childhood-onset diabetes is primarily mediated through effects on protein stability.Semantic proximity Read ↗

GCK-MODY diabetes as a protein misfolding disease: the mutation R275C promotes protein misfolding, self-association and cellular degradation.Semantic proximity Read ↗

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