Evidence map›Paper›PMID 22847419›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) induces cancer cell senescence by interacting with telomerase RNA component.

Craig Nicholls, Alexander Ruvantha Pinto, He Li, Ling Li, Lihui Wang, Richard Simpson, Jun-Ping Liu

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
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

44 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Article
  3. The moonlighting functions of glycolytic enzymes in tumorigenesis.Cellular oncology (Dordrecht, Netherlands) · 2026
    Review
  4. Article
  5. Evaluation of Salivary GAPDH as a Predictor Biomarker for Periodontitis.International journal of molecular sciences · 2025
    Article
  6. Stress-induced nuclear GAPDH: Scientific update and clinical application.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Enzymes in a human cytoplasm model organize into submetabolon complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Multiparametric identification of putative senescent cells in skeletal muscle via mass cytometry.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2024
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
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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

7 authors at 4 institutions in 2 countries.

Craig NichollsInstitute of Aging Research, School of Medicine, Hangzhou Normal University, Hangzhou, Zhejiang Province 310036, China.
Alexander Ruvantha Pinto
He Li
Ling Li
Lihui Wang
Richard Simpson
Jun-Ping Liu
Monash University · AUHangzhou Normal University · CNLa Trobe University · AUMurdoch Children's Research Institute · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxidative stress regulates telomere homeostasis and cellular aging by unclear mechanisms. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a key mediator of many oxidative stress responses, involving GAPDH nuclear translocation and induction of cell death. We report here that GAPDH interacts with the telomerase RNA component (TERC), inhibits telomerase activity, and induces telomere shortening and breast cancer cell senescence. The Rossmann fold containing NAD(+) binding region on GAPDH is responsible for the interaction with TERC, whereas a lysine residue in the GAPDH catalytic domain is required for inhibiting telomerase activity and disrupting telomere maintenance. Furthermore, the GAPDH substrate glyceraldehyde-3-phosphate (G3P) and the nitric oxide donor S-nitrosoglutathione (GSNO) both negatively regulate GAPDH inhibition of telomerase activity. Thus, we demonstrate that GAPDH is regulated to target the telomerase complex, resulting in an arrest of telomere maintenance and cancer cell proliferation.

Indexed as

Cellular SenescenceBreast NeoplasmsCell Line, TumorFemaleGene Expression Regulation, NeoplasticGlyceraldehyde 3-PhosphateGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)Green Fluorescent ProteinsHumansNADProtein BindingProtein Structure, TertiaryRNAS-NitrosoglutathioneStructure-Activity RelationshipTelomeraseGlyceraldehyde 3-PhosphateGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)Green Fluorescent ProteinsNADRNAS-NitrosoglutathioneTelomerasetelomerase RNA

Identifiers

PMID22847419
PMCPMC3421169
OpenAlexW2042890329

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.