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 tale of two subunits: how the neomorphic R132H IDH1 mutation enhances production of αHG.

Biochemistry - 31 May 2011

Pietrak Beth, Zhao Huizhen, Qi Hongwei, Quinn Chad, Gao Enoch, Boyer Joseph G, Concha Nestor, Brown Kristin, Duraiswami Chaya, Wooster Richard, Sweitzer Sharon, Schwartz Benjamin

Abstract excerpt

Heterozygously expressed single-point mutations in isocitrate dehydrogenase 1 and 2 (IDH1 and IDH2, respectively) render these dimeric enzymes capable of producing the novel metabolite α-hydroxyglutarate (αHG). Accumulation of αHG is used as a biomarker for a number of cancer types, helping to identify tumors with similar IDH mutations. With IDH1, it has been shown that one role of the mutation is to increase the...

Read the complete abstract on PubMed

Topics

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

Share to Chromatography, High Pressure Liquid
Share to IDH2 gene

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glutarates

Share to Isocitrate Dehydrogenase

Share to Models, Molecular

Share to Mutagenesis

Share to Mutation

Share to Tandem Mass Spectrometry

Source

Identifiers

PMID: 21524095
DOI: 10.1021/bi200499m

Genes

IDH1
IDH2

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

A tale of two subunits: how the neomorphic R132H IDH1 mutation enhances production of αHG.PMID 21524095Read ↗

Mutant IDH1 enhances the production of 2-hydroxyglutarate due to its kinetic mechanism.Semantic proximity Read ↗

Molecular mechanisms of isocitrate dehydrogenase 1 (IDH1) mutations identified in tumors: The role of size and hydrophobicity at residue 132 on catalytic efficiency.Semantic proximity Read ↗

Evaluating Mechanisms of IDH1 Regulation through Site-Specific Acetylation Mimics.Semantic proximity Read ↗

Active site remodeling in tumor-relevant IDH1 mutants drives distinct kinetic features and potential resistance mechanismsSemantic proximity Read ↗

Active site remodeling in tumor-relevant IDH1 mutants drives distinct kinetic features and potential resistance mechanisms.Semantic proximity Read ↗

Single arginine mutation in two yeast isocitrate dehydrogenases: biochemical characterization and functional implication.Semantic proximity Read ↗

Active site remodeling in tumor-relevant IDH1 mutants drives distinct kinetic features and potential resistance mechanismsSemantic proximity Read ↗

Low pH Facilitates Heterodimerization of Mutant Isocitrate Dehydrogenase IDH1-R132H and Promotes Production of 2-Hydroxyglutarate.Semantic proximity Read ↗

Gaining Insight into the Catalytic Mechanism of the R132H IDH1 Mutant: A Synergistic DFT Cluster and Experimental Investigation.Semantic proximity Read ↗

Novel Insights for Inhibiting Mutant Heterodimer IDH1wt-R132H in Cancer: An In-Silico Approach.Semantic proximity Read ↗

IDH1 and IDH2 mutants identified in cancer lose inhibition by isocitrate because of a change in their binding sitesSemantic proximity Read ↗

Discovery of a new binding site and a possible gain in neomorphic activity in R132H_IDH1.Semantic proximity Read ↗

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