Evidence map›Paper›PMID 25416785›Full record

ArticleThe Journal of biological chemistry2015

Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues.

Gilbert Richarme, Mouadh Mihoub, Julien Dairou, Linh Chi Bui, Thibaut Leger, Aazdine Lamouri

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed, 1 pooled it
10.6field-weighted citation impact, top 1% 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

140 citing papers in PubMed, 1 synthesis or guideline pooled it, 261 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Reversible formation ofRSC chemical biology · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. 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
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. The chemical language of protein glycation.Nature chemical biology · 2025
    Review
  16. Article
  17. Article
  18. Peptide Activator Stabilizes DJ-1 Structure and Enhances Its Activity.International journal of molecular sciences · 2024
    Article
  19. Proteomic Profiling ofInternational journal of molecular sciences · 2024
    Article
  20. Article

80 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

6 authors at 3 institutions in 1 country.

Gilbert RicharmeFrom the Stress Molecules, Institut Jacques Monod, Université Paris 7, CNRS UMR 7592, 75013 Paris, France, richarme@paris7.jussieu.fr.
Mouadh MihoubFrom the Stress Molecules, Institut Jacques Monod, Université Paris 7, CNRS UMR 7592, 75013 Paris, France.
Julien Dairouthe Université Paris Diderot, Sorbonne Paris Cité, Unité de Biologie Fonctionnelle et Adaptative UMR 8251 CNRS, Bioprofiler Facility, F-75205, Paris, France.
Linh Chi Buithe Université Paris Diderot, Sorbonne Paris Cité, Unité de Biologie Fonctionnelle et Adaptative UMR 8251 CNRS, Bioprofiler Facility, F-75205, Paris, France.
Thibaut Legerthe Proteomics Facility, Institut Jacques Monod, Université Paris 7, CNRS, UMR 7592, 75013 Paris, France, and.
Aazdine Lamourithe Université Paris Diderot, Sorbonne Paris Cite, ITODYS, UMR 7086 CNRS, 75013 Paris, France.
Centre National de la Recherche Scientifique · FRDélégation Paris 7 · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycation is an inevitable nonenzymatic covalent reaction between proteins and endogenous reducing sugars or dicarbonyls (methylglyoxal, glyoxal) that results in protein inactivation. DJ-1 was reported to be a multifunctional oxidative stress response protein with poorly defined function. Here, we show that human DJ-1 is a protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins by acting on early glycation intermediates and releases repaired proteins and lactate or glycolate, respectively. DJ-1 deglycates cysteines, arginines, and lysines (the three major glycated amino acids) of serum albumin, glyceraldehyde-3-phosphate dehydrogenase, aldolase, and aspartate aminotransferase and thus reactivates these proteins. DJ-1 prevented protein glycation in an Escherichia coli mutant deficient in the DJ-1 homolog YajL and restored cell viability in glucose-containing media. These results suggest that DJ-1-associated Parkinsonism results from excessive protein glycation and establishes DJ-1 as a major anti-glycation and anti-aging protein.

Indexed as

AcetylcysteineAlbuminsApoptosisArginineAspartate AminotransferasesCatalysisCell SurvivalCysteineEscherichia coliFructose-Bisphosphate AldolaseGlucoseGlycolatesGlyoxalHumansIntracellular Signaling Peptides and ProteinsLactatesAcetylcysteineAlbuminsArginineAspartate AminotransferasesCysteineFructose-Bisphosphate AldolaseGlucoseGlycolatesglycolic acidGlyoxalIntracellular Signaling Peptides and ProteinsLactatesLysineOncogene ProteinsPARK7 protein, humanProtein Deglycase DJ-1PyruvaldehydeCarbonyl StressDicarbonyl CompoundsElectrophile StressGlycationProtein AggregationProtein Chemical ModificationProtein ConformationProtein Denaturation

Identifiers

PMID25416785
PMCPMC4340429
OpenAlexW2079182319

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.