Evidence map›Paper›PMID 32783963›Full record

ReviewCell chemical biology2020

Small Substrate or Large? Debate Over the Mechanism of Glycation Adduct Repair by DJ-1.

Yong Woong Jun, Eric T Kool

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Kinetic evidence in favor of glyoxalase III and against deglycase activity of DJ-1.Protein science : a publication of the Protein Society · 2023
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. The Human Glyoxalase Gene Family in Health and Disease.Chemical research in toxicology · 2022
    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

2 authors at 2 institutions in 1 country.

Yong Woong JunDepartment of Chemistry, ChEM-H Institute, and Stanford Cancer Institute, Stanford University, Stanford, CA 94305, USA.
Eric T KoolDepartment of Chemistry, ChEM-H Institute, and Stanford Cancer Institute, Stanford University, Stanford, CA 94305, USA. Electronic address: kool@stanford.edu.
Cardiovascular Institute of the South · USStanford University · US

Funding

Measuring and Modulating Oxidative DNA Damage Surveillance PathwaysR01CA217809 · NCI · STANFORD UNIVERSITY · PI KOOL, ERIC T. · 2017 to 2024
$3.7M
NCI NIH HHS R01 CA217809
6 · The paper itself

Abstract

Glycation, the term for non-enzymatic covalent reactions between aldehyde metabolites and nucleophiles on biopolymers, results in deleterious cellular damage and diseases. Since Parkinsonism-associated protein DJ-1 was proposed as a novel deglycase that directly repairs glycated adducts, it has been considered a major contributor to glycation damage repair. Recently, an interesting debate over the mechanism of glycation repair by DJ-1 has emerged, focusing on whether the substrate of DJ-1 is glycated adducts or the free small aldehydes. The physiological significance of DJ-1 on glycation defense also remains in question. This debate is complicated by the fact that glycated biomolecular adducts are in rapid equilibrium with free aldehydes. Here, we summarize experimental evidence for the two possibilities, highlighting both consistencies and conflicts. We discuss the experimental complexities from a mechanistic perspective, and suggest classes of experiments that should help clarify this debate.

Indexed as

CysteineGlycation End Products, AdvancedHumansKineticsNucleic AcidsProtein Deglycase DJ-1ProteinsPyruvaldehydeSubstrate SpecificityCysteineGlycation End Products, AdvancedNucleic AcidsPARK7 protein, humanProtein Deglycase DJ-1ProteinsPyruvaldehydecarbonyl stressdeglycaseDJ-1DNA damageDNA repairenzyme mechanismglycationmethyl glyoxal

Identifiers

PMID32783963
PMCPMC8442549
OpenAlexW3048520848

What OpenQuestion holds

Textmetadata
LicenceTDM
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.