Evidence map›Paper›PMID 20513808›Full record

ReviewJournal of the National Cancer Institute2010

Isocitrate dehydrogenase 1 and 2 mutations in cancer: alterations at a crossroads of cellular metabolism.

Zachary J Reitman, Hai Yan

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Journal of the National Cancer Institute, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 300 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
300citing papers in PubMed, 2 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

300 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
  2. Pooled it
  3. Review
  4. Article
  5. Circulating tumor DNA-based detection of molecular residual disease in isocitrate dehydrogenase-mutant cholangiocarcinoma for biomarker-guided therapy.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
    Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Isocitrate dehydrogenase mutations as potential tumour agnostic targets.EJC supplements : EJC : official journal of EORTC, European Organization for Research and Treatment of Cancer ... [et al.] · 2026
    Article
  13. Review
  14. Review
  15. State of the Art of IDH Inhibitors: Emerging Questions and Perspectives.Anti-cancer agents in medicinal chemistry · 2026
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

240 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Zachary J ReitmanDepartment of Pathology, The Pediatric Brain Tumor Foundation Institute, Duke University Medical Center, Durham, NC 27710, USA. zjr@duke.edu
Hai Yan

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007171 · NIGMS · DUKE UNIVERSITY · PI KONTOS, CHRISTOPHER D · 1985 to 2021
$31.2M
The Role of IDH1 Mutations in Gliomagenesis and MetabolismR01CA140316 · NCI · DUKE UNIVERSITY · PI YAN, HAI · 2010 to 2019
$3.2M
The Role of OTX2 in Molecular Pathogenesis of MedulloblastomaR01CA118822 · NCI · DUKE UNIVERSITY · PI YAN, HAI · 2006 to 2010
$1.2M
NCI NIH HHS R01 CA118822NCI NIH HHS R01CA118822NCI NIH HHS R01 CA140316NIGMS NIH HHS 2T32GM007171NIGMS NIH HHS T32 GM007171
6 · The paper itself

Abstract

Dysregulation of metabolism is a common phenomenon in cancer cells. The NADP(+)-dependent isocitrate dehydrogenases 1 and 2 (IDH1 and IDH2) function at a crossroads of cellular metabolism in lipid synthesis, cellular defense against oxidative stress, oxidative respiration, and oxygen-sensing signal transduction. We review the normal functions of the encoded enzymes, frequent mutations of IDH1 and IDH2 recently found in human cancers, and possible roles for the mutated enzymes in human disease. IDH1 and IDH2 mutations occur frequently in some types of World Health Organization grades 2-4 gliomas and in acute myeloid leukemias with normal karyotype. IDH1 and IDH2 mutations are remarkably specific to codons that encode conserved functionally important arginines in the active site of each enzyme. To date, all IDH1 mutations have been identified at the Arg132 codon. Mutations in IDH2 have been identified at the Arg140 codon, as well as at Arg172, which is aligned with IDH1 Arg132. IDH1 and IDH2 mutations are usually heterozygous in cancer, and they appear to confer a neomorphic enzyme activity for the enzymes to catalyze the production of D-2-hydroxyglutarate. Study of alterations in these metabolic enzymes may provide insights into the metabolism of cancer cells and uncover novel avenues for development of anticancer therapeutics.

Indexed as

Genes, Tumor SuppressorMutationOncogenesAnimalsArginineBrain NeoplasmsCodonGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticGlioblastomaGlucoseGlutaratesHumansHypoxiaIsocitrate DehydrogenaseNADPalpha-hydroxyglutarateArginineCodonGlucoseGlutaratesIDH1 protein, humanIDH2 protein, humanIsocitrate DehydrogenaseNADP

Identifiers

PMID20513808
PMCPMC2897878

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.