Evidence map›Paper›PMID 36358501›Full record

ReviewAntioxidants (Basel, Switzerland)2022

Glyoxalase 2: Towards a Broader View of the Second Player of the Glyoxalase System.

Andrea Scirè, Laura Cianfruglia, Cristina Minnelli, Brenda Romaldi, Emiliano Laudadio, Roberta Galeazzi, Cinzia Antognelli, Tatiana Armeni

Open access · goldAbstract readReview
In one paragraph

Review in Antioxidants (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Identification ofEndocrine, metabolic & immune disorders drug targets · 2026
    Article
  6. Review
  7. Exploring the causal impact of mitochondrial dysfunction on epilepsy: a mendelian randomization study.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas · 2026
    Article
  8. Article
  9. Review
  10. Can the Quality of Semen Affect the Fertilisation Indices of Turkey Eggs?International journal of molecular sciences · 2025
    Article
  11. Article
  12. Development andRSC advances · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Methylglyoxal Formation-Metabolic Routes and Consequences.Antioxidants (Basel, Switzerland) · 2025
    Review
  17. Article
  18. Review
  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 2 institutions in 1 country.

Andrea ScirèDepartment of Life and Environmental Sciences, Polytechnic University of Marche, 60131 Ancona, Italy.ORCID 0000-0002-8288-6989
Laura CianfrugliaDepartment of Clinical Sciences, Polytechnic University of Marche, 60126 Ancona, Italy.ORCID 0000-0002-0322-0282
Cristina MinnelliDepartment of Life and Environmental Sciences, Polytechnic University of Marche, 60131 Ancona, Italy.ORCID 0000-0001-8034-8557
Brenda RomaldiDepartment of Clinical Sciences, Polytechnic University of Marche, 60126 Ancona, Italy.
Emiliano LaudadioDepartment of Science and Engineering of Materials, Environment and Urban Planning, Polytechnic University of Marche, 60131 Ancona, Italy.ORCID 0000-0002-8053-6539
Roberta GaleazziDepartment of Life and Environmental Sciences, Polytechnic University of Marche, 60131 Ancona, Italy.ORCID 0000-0003-1792-654X
Cinzia AntognelliDepartment of Medicine and Surgery, University of Perugia, 06132 Perugia, Italy.ORCID 0000-0002-8259-680X
Tatiana ArmeniDepartment of Clinical Sciences, Polytechnic University of Marche, 60126 Ancona, Italy.ORCID 0000-0003-0931-1342
Marche Polytechnic University · ITUniversity of Perugia · IT

Funding

Marche Polytechnic University 040017_R.SCIENT.A_2019
6 · The paper itself

Abstract

Glyoxalase 2 is a mitochondrial and cytoplasmic protein belonging to the metallo-β-lactamase family encoded by the hydroxyacylglutathione hydrolase (HAGH) gene. This enzyme is the second enzyme of the glyoxalase system that is responsible for detoxification of the α-ketothaldehyde methylglyoxal in cells. The two enzymes glyoxalase 1 (Glo1) and glyoxalase 2 (Glo2) form the complete glyoxalase pathway, which utilizes glutathione as cofactor in eukaryotic cells. The importance of Glo2 is highlighted by its ubiquitous distribution in prokaryotic and eukaryotic organisms. Its function in the system has been well defined, but in recent years, additional roles are emerging, especially those related to oxidative stress. This review focuses on Glo2 by considering its genetics, molecular and structural properties, its involvement in post-translational modifications and its interaction with specific metabolic pathways. The purpose of this review is to focus attention on an enzyme that, from the most recent studies, appears to play a role in multiple regulatory pathways that may be important in certain diseases such as cancer or oxidative stress-related diseases.

Indexed as

glutathioneglyoxalase systemmetallo beta-lactamasemethylglyoxalpost-translational modification (PTM)

Identifiers

PMID36358501
PMCPMC9686547
OpenAlexW4307945174

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.