Evidence map›Paper›PMID 40464736›Full record

ArticleThe Journal of cell biology2025

The reaction mechanism for glycolysis side product degradation by Parkinson's disease-linked DJ-1.

Aiko Watanabe, Shizuka Ogiwara, Mirei Saito, Masaki Mishima, Masahiro Yamashina, Ryuichiro Ishitani, Yutaka Ito, Keiji Tanaka, Fumika Koyano, Koji Yamano and 3 more

Abstract read
In one paragraph

Article in The Journal of cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Reversible formation ofRSC chemical biology · 2026
    Article
  2. Review
  3. Article
  4. 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
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

13 authors.

Aiko WatanabeDepartment of Biomolecular Pathogenesis, Division of Advanced Pathophysiological Science, Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Tokyo, Japan.ORCID 0009-0009-1821-430X
Shizuka OgiwaraDepartment of Biomolecular Pathogenesis, Division of Advanced Pathophysiological Science, Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Tokyo, Japan.ORCID 0009-0004-5135-5888
Mirei SaitoDepartment of Biomolecular Pathogenesis, Division of Advanced Pathophysiological Science, Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Tokyo, Japan.ORCID 0009-0008-8275-5402
Masaki MishimaDepartment of Molecular Biophysics, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan.ORCID 0000-0001-7626-7287
Masahiro YamashinaDepartment of Chemistry, School of Science, Institute of Science Tokyo, Tokyo, Japan.ORCID 0000-0002-0887-2458
Ryuichiro IshitaniDepartment of Computational Drug Discovery and Design, Division of Biological Data Science, Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Tokyo, Japan.ORCID 0000-0002-4136-5685
Yutaka ItoDepartment of Chemistry, Tokyo Metropolitan University, Tokyo, Japan.ORCID 0000-0002-1030-4660
Keiji TanakaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.ORCID 0000-0003-3098-4760
Fumika KoyanoDepartment of Biomolecular Pathogenesis, Division of Advanced Pathophysiological Science, Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Tokyo, Japan.ORCID 0000-0003-4298-0492
Koji YamanoDepartment of Biomolecular Pathogenesis, Division of Advanced Pathophysiological Science, Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Tokyo, Japan.ORCID 0000-0002-4692-161X
Hidetaka KosakoDivision of Cell Signaling, Fujii Memorial Institute of Medical Sciences, Institute of Advanced Medical Sciences, Tokushima University, Tokushima, Japan.ORCID 0000-0003-3228-6368
Yoshitaka MoriwakiDepartment of Computational Drug Discovery and Design, Division of Biological Data Science, Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Tokyo, Japan.ORCID 0000-0003-0448-9790
Noriyuki MatsudaDepartment of Biomolecular Pathogenesis, Division of Advanced Pathophysiological Science, Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Tokyo, Japan.ORCID 0000-0001-8199-952X

Funding

Basis for Supporting Innovative Drug Discovery and Life Science ResearchInstitute of Science TokyoJapan Society for the Promotion of Science JP18K14708Japan Society for the Promotion of Science JP19H05712Japan Society for the Promotion of Science JP21K06161Japan Society for the Promotion of Science JP22gm1410004Japan Society for the Promotion of Science JP22H02562Japan Society for the Promotion of Science JP22H02577Japan Society for the Promotion of Science JP23H04923Japan Society for the Promotion of Science JP24ama121012Japan Society for the Promotion of Science JP24ama121027Japan Society for the Promotion of Science JP24H01290Japan Society for the Promotion of Science JP24H02094Japan Society for the Promotion of Science P18H02443Ministry of Education, Culture, Sports, Science and Technology JPMXP1323015483Takeda Science FoundationTMDU Nanken-Kyoten FoundationTokushima University
6 · The paper itself

Abstract

DJ-1/PARK7 is the causative gene for hereditary recessive Parkinson's disease. Recent studies have reported that DJ-1 hydrolyzes cyclic 3-phosphoglyceric anhydride (cPGA), a highly reactive metabolite. However, the molecular mechanisms underlying cPGA hydrolase activity have yet to be fully elucidated. To gain a more comprehensive understanding of this activity in DJ-1, we performed molecular simulations that predicted how DJ-1 recognizes and hydrolyzes cPGA. The accuracy of these structural predictions was validated through systematic mutational analyses exemplified by loss of activity with the A107P mutation. Although DJ-1 possesses both cPGA hydrolase and α-oxoaldehyde hydratase activities in vitro, we confirmed that DJ-1 dysfunction caused an increase in cPGA-derived modifications but had no effect on α-oxoaldehyde-derived modifications in cells. Importantly, A107 and P158, pathogenic missense mutation sites found in Parkinson's disease patients, are critical for cPGA hydrolysis both in vitro and in cells. The evidence-based catalytic mechanism for DJ-1 hydrolysis of cPGA that we propose here explains their pathophysiological significance.

Indexed as

GlycolysisParkinson DiseaseProtein Deglycase DJ-1HEK293 CellsHumansHydrolysisMutation, MissensePARK7 protein, humanProtein Deglycase DJ-1

Identifiers

PMID40464736
PMCPMC12135873

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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.