Evidence map›Paper›PMID 28106725›Full record

ReviewInternational journal of molecular sciences2017

Bacterial Responses to Glyoxal and Methylglyoxal: Reactive Electrophilic Species.

Changhan Lee, Chankyu Park

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Identification of glyoxalase A in group BInfection and immunity · 2025
    Article
  16. Article
  17. Article
  18. Methylglyoxal Formation-Metabolic Routes and Consequences.Antioxidants (Basel, Switzerland) · 2025
    Review
  19. Review
  20. Identification of Glyoxalase A in Group BbioRxiv : the preprint server for biology · 2024
    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 1 institution in 1 country.

Changhan LeeDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Yuseong-gu, Daejeon 305-701, Korea. nasa@kaist.ac.kr.
Chankyu ParkDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Yuseong-gu, Daejeon 305-701, Korea. ckpark@kaist.ac.kr.
Korea Advanced Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glyoxal (GO) and methylglyoxal (MG), belonging to α-oxoaldehydes, are produced by organisms from bacteria to humans by glucose oxidation, lipid peroxidation, and DNA oxidation. Since glyoxals contain two adjacent reactive carbonyl groups, they are referred to as reactive electrophilic species (RES), and are damaging to proteins and nucleotides. Therefore, glyoxals cause various diseases in humans, such as diabetes and neurodegenerative diseases, from which all living organisms need to be protected. Although the glyoxalase system has been known for some time, details on how glyoxals are sensed and detoxified in the cell have not been fully elucidated, and are only beginning to be uncovered. In this review, we will summarize the current knowledge on bacterial responses to glyoxal, and specifically focus on the glyoxal-associated regulators YqhC and NemR, as well as their detoxification mediated by glutathione (GSH)-dependent/independent glyoxalases and NAD(P)H-dependent reductases. Furthermore, we will address questions and future directions.

Indexed as

Aldehyde OxidoreductasesBacteriaBacterial ProteinsGlutathioneGlyoxalHydroxyacylglutathione HydrolaseInactivation, MetabolicLactoylglutathione LyaseOxidative StressPyruvaldehydeThiolester HydrolasesAldehyde OxidoreductasesBacterial ProteinsGlutathioneGlyoxalglyoxalase IIIHydroxyacylglutathione HydrolaseLactoylglutathione LyasePyruvaldehydeThiolester Hydrolasesglyoxalglyoxalasereactive electrophilic species (RES)

Identifiers

PMID28106725
PMCPMC5297802
OpenAlexW2571964874

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.