Evidence map›Paper›PMID 9356496›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and alpha-ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length.

A J Cooper, K R Sheu, J R Burke, O Onodera, W J Strittmatter, A D Roses, J P Blass

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 92 citations in OpenAlex.

  1. Review
  2. Article
  3. The vicious cycle between transglutaminase 2 and reactive oxygen species in hyperglycemic memory-induced endothelial dysfunction.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Transglutaminases and neurodegeneration.Journal of neurochemistry · 2009
    Review
  15. Article
  16. Mutant huntingtin: nuclear translocation and cytotoxicity mediated by GAPDH.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  17. Article
  18. Review
  19. The energetics of Huntington's disease.Neurochemical research · 2004
    Review
  20. Article
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 5 institutions in 1 country.

A J CooperDepartment of Biochemistry, Cornell University Medical College, New York, NY 10021, USA. ajlc@mail.med.cornell.edu
K R Sheu
J R Burke
O Onodera
W J Strittmatter
A D Roses
J P Blass
Burke Medical Research Institute · USDuke University · USDuke University Hospital · USNational Institutes of Health · USSociety for Neuroscience · US

Funding

IMMUN.QUANT. OF PAIRED HEL.FIL. AND RELATED PROT. IN ALZ.BRAIN AND FIB.R35AG009014 · NIA · WINIFRED MASTERSON BURKE MED RES INST · PI BLACK, RONALD · 1991 to 1998
–
NIA NIH HHS AG 09014
6 · The paper itself

Abstract

Several adult-onset neurodegenerative diseases are caused by genes with expanded CAG triplet repeats within their coding regions and extended polyglutamine (Qn) domains within the expressed proteins. Generally, in clinically affected individuals n >/= 40. Glyceraldehyde 3-phosphate dehydrogenase binds tightly to four Qn disease proteins, but the significance of this interaction is unknown. We now report that purified glyceraldehyde 3-phosphate dehydrogenase is inactivated by tissue transglutaminase in the presence of glutathione S-transferase constructs containing a Qn domain of pathological length (n = 62 or 81). The dehydrogenase is less strongly inhibited by tissue transglutaminase in the presence of constructs containing shorter Qn domains (n = 0 or 10). Purified alpha-ketoglutarate dehydrogenase complex also is inactivated by tissue transglutaminase plus glutathione S-transferase constructs containing pathological-length Qn domains (n = 62 or 81). The results suggest that tissue transglutaminase-catalyzed covalent linkages involving the larger poly-Q domains may disrupt cerebral energy metabolism in CAG/Qn expansion diseases.

Indexed as

AnimalsBinding SitesGlyceraldehyde-3-Phosphate DehydrogenasesGuinea PigsKetoglutarate Dehydrogenase ComplexNeurodegenerative DiseasesPeptide FragmentsRabbitsSubstrate SpecificityTransglutaminasesglyceraldehyde 3-phosphate dehydrogenase (304-313)Glyceraldehyde-3-Phosphate DehydrogenasesKetoglutarate Dehydrogenase ComplexPeptide FragmentsTransglutaminases

Identifiers

PMID9356496
PMCPMC25053
OpenAlexW2050310623

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.