Evidence map›Paper›PMID 31653696›Full record

ArticleThe Journal of biological chemistry2019

The apparent deglycase activity of DJ-1 results from the conversion of free methylglyoxal present in fast equilibrium with hemithioacetals and hemiaminals.

Anna Andreeva, Zhanibek Bekkhozhin, Nuriza Omertassova, Timur Baizhumanov, Gaziza Yeltay, Mels Akhmetali, Daulet Toibazar, Darkhan Utepbergenov

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

36 citing papers in PubMed, 61 citations in OpenAlex.

  1. Reversible formation ofRSC chemical biology · 2026
    Article
  2. Glyoxalase activities of Parkinson's disease relevant protein DJ-1/PARK7: Past discoveries and future perspectives.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2026
    Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. The chemical language of protein glycation.Nature chemical biology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Kinetic evidence in favor of glyoxalase III and against deglycase activity of DJ-1.Protein science : a publication of the Protein Society · 2023
    Article
  17. Review
  18. Article
  19. Article
  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

8 authors at 1 institution in 1 country.

Anna AndreevaDepartment of Biology, School of Sciences and Humanities, Nazarbayev University, Nur-Sultan 010000, Kazakhstan.
Zhanibek BekkhozhinDepartment of Chemistry, School of Sciences and Humanities, Nazarbayev University, Nur-Sultan 010000, Kazakhstan.
Nuriza OmertassovaDepartment of Biology, School of Sciences and Humanities, Nazarbayev University, Nur-Sultan 010000, Kazakhstan.
Timur BaizhumanovDepartment of Chemistry, School of Sciences and Humanities, Nazarbayev University, Nur-Sultan 010000, Kazakhstan.
Gaziza YeltayDepartment of Biology, School of Sciences and Humanities, Nazarbayev University, Nur-Sultan 010000, Kazakhstan.
Mels AkhmetaliDepartment of Biology, School of Sciences and Humanities, Nazarbayev University, Nur-Sultan 010000, Kazakhstan.
Daulet ToibazarDepartment of Biology, School of Sciences and Humanities, Nazarbayev University, Nur-Sultan 010000, Kazakhstan.
Darkhan UtepbergenovDepartment of Chemistry, School of Sciences and Humanities, Nazarbayev University, Nur-Sultan 010000, Kazakhstan. Electronic address: darkhan.utepbergenov@nu.edu.kz.
Nazarbayev University · KZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Loss-of-function mutations in the gene encoding human protein DJ-1 cause early onset of Parkinson's disease, suggesting that DJ-1 protects dopaminergic neurons. The molecular mechanisms underlying this neuroprotection are unclear; however, DJ-1 has been suggested to be a GSH-independent glyoxalase that detoxifies methylglyoxal (MGO) by converting it into lactate. It has also been suggested that DJ-1 serves as a deglycase that catalyzes hydrolysis of hemithioacetals and hemiaminals formed by reactions of MGO with the thiol and amino groups of proteins. In this report, we demonstrate that the equilibrium constant of reaction of MGO with thiols is ∼500 m

Indexed as

HumansParkinson DiseaseProtein Deglycase DJ-1PyruvaldehydeSerum Albumin, BovineProtein Deglycase DJ-1PyruvaldehydeSerum Albumin, BovinedeglycaseDJ-1glycationglyoxalasehemiaminalhemithioacetalneurodegenerationParkinson diseaseParkinson disease (autosomal recessive, early onset) 7 (PARK7)thiol

Identifiers

PMID31653696
PMCPMC6901308
OpenAlexW2981928743

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.