Evidence map›Paper›PMID 28993701›Full record

ArticleScientific reports2017

Parkinson's disease-related DJ-1 functions in thiol quality control against aldehyde attack in vitro.

Noriyuki Matsuda, Mayumi Kimura, Bruno Barros Queliconi, Waka Kojima, Masaki Mishima, Kenji Takagi, Fumika Koyano, Koji Yamano, Tsunehiro Mizushima, Yutaka Ito and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
1.8field-weighted citation impact, top 15% 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, 53 citations in OpenAlex.

  1. 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
  2. Article
  3. Article
  4. Hypoxia-inducible factor-1 as targets for neuroprotection : from ferroptosis to Parkinson's disease.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2025
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Epigenetic meets metabolism: novel vulnerabilities to fight cancer.Cell communication and signaling : CCS · 2023
    Review
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  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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  19. Article
  20. PARK7/DJ-1 as a Therapeutic Target in Gut-Brain Axis Diseases.International journal of molecular sciences · 2022
    Review
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

11 authors at 4 institutions in 1 country.

Noriyuki MatsudaUbiquitin Project, Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya, Tokyo, 156-8506, Japan. matsuda-nr@igakuken.or.jp.
Mayumi KimuraUbiquitin Project, Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya, Tokyo, 156-8506, Japan.
Bruno Barros QueliconiUbiquitin Project, Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya, Tokyo, 156-8506, Japan.
Waka KojimaUbiquitin Project, Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya, Tokyo, 156-8506, Japan.
Masaki MishimaGraduate School of Science and Engineering, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, 192-0397, Japan.
Kenji TakagiPicobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamighori, Ako, Hyogo, 678-1297, Japan.
Fumika KoyanoUbiquitin Project, Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya, Tokyo, 156-8506, Japan.
Koji YamanoUbiquitin Project, Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya, Tokyo, 156-8506, Japan.
Tsunehiro MizushimaPicobiology Institute, Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamighori, Ako, Hyogo, 678-1297, Japan.
Yutaka ItoGraduate School of Science and Engineering, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, 192-0397, Japan.ORCID 0000-0002-1030-4660
Keiji TanakaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya, Tokyo, 156-8506, Japan. tanaka-kj@igakuken.or.jp.
Tokyo Metropolitan Institute of Medical Science · JPTokyo Metropolitan University · JPUniversity of Hyogo · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DJ-1 (also known as PARK7) has been identified as a causal gene for hereditary recessive Parkinson's disease (PD). Consequently, the full elucidation of DJ-1 function will help decipher the molecular mechanisms underlying PD pathogenesis. However, because various, and sometimes inconsistent, roles for DJ-1 have been reported, the molecular function of DJ-1 remains controversial. Recently, a number of papers have suggested that DJ-1 family proteins are involved in aldehyde detoxification. We found that DJ-1 indeed converts methylglyoxal (pyruvaldehyde)-adducted glutathione (GSH) to intact GSH and lactate. Based on evidence that DJ-1 functions in mitochondrial homeostasis, we focused on the possibility that DJ-1 protects co-enzyme A (CoA) and its precursor in the CoA synthetic pathway from aldehyde attack. Here, we show that intact CoA and β-alanine, an intermediate in CoA synthesis, are recovered from methylglyoxal-adducts by recombinant DJ-1 purified from E. coli. In this process, methylglyoxal is converted to L-lactate rather than the D-lactate produced by a conventional glyoxalase. PD-related pathogenic mutations of DJ-1 (L10P, M26I, A104T, D149A, and L166P) impair or abolish detoxification activity, suggesting a pathological significance. We infer that a key to understanding the biological function of DJ-1 resides in its methylglyoxal-adduct hydrolase activity, which protects low-molecular thiols, including CoA, from aldehydes.

Indexed as

AcetylcysteineAldehydesAmino Acid Sequencebeta-AlanineCoenzyme AGlutathioneHeLa CellsHumansInactivation, MetabolicLactic AcidMutant ProteinsMutationParkinson DiseaseProtein Deglycase DJ-1PyruvaldehydeRecombinant ProteinsAcetylcysteineAldehydesbeta-AlanineCoenzyme AGlutathioneLactic AcidMutant ProteinsProtein Deglycase DJ-1PyruvaldehydeRecombinant ProteinsSulfhydryl Compounds

Identifiers

PMID28993701
PMCPMC5634459
OpenAlexW2761114128

What OpenQuestion holds

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Registered trials

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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.