Evidence map›Paper›PMID 28358304›Full record

ReviewInternational journal of molecular sciences2017

Characteristic Variations and Similarities in Biochemical, Molecular, and Functional Properties of Glyoxalases across Prokaryotes and Eukaryotes.

Charanpreet Kaur, Shweta Sharma, Mohammad Rokebul Hasan, Ashwani Pareek, Sneh L Singla-Pareek, Sudhir K Sopory

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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Applied and environmental microbiology · 2024
    Article
  7. Review
  8. Article
  9. The Human Glyoxalase Gene Family in Health and Disease.Chemical research in toxicology · 2022
    Review
  10. Genetic Conservation of CBS Domain Containing Protein Family inInternational journal of molecular sciences · 2022
    Article
  11. Article
  12. Methylglyoxal-glyoxalase system as a possible selection module for raising marker-safe plants in rice.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Article
  13. Article
  14. Functional characterization of the Glyoxalase-I (Plant signaling & behavior · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  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

6 authors at 3 institutions in 1 country.

Charanpreet KaurStress Physiology and Molecular Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India. charanpreet06@gmail.com.
Shweta SharmaPlant Stress Biology Group, International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India. shweta2u@gmail.com.
Mohammad Rokebul HasanPlant Stress Biology Group, International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India. rokebbrri@gmail.com.
Ashwani PareekStress Physiology and Molecular Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India. ashwanip@mail.jnu.ac.in.
Sneh L Singla-PareekPlant Stress Biology Group, International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India. sneh@icgeb.res.in.
Sudhir K SoporyPlant Stress Biology Group, International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India. sopory@icgeb.res.in.
International Centre for Genetic Engineering and Biotechnology · INJawaharlal Nehru University · INUniversity of Delhi · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glyoxalase system is the ubiquitous pathway for the detoxification of methylglyoxal (MG) in the biological systems. It comprises two enzymes, glyoxalase I (GLYI) and glyoxalase II (GLYII), which act sequentially to convert MG into d-lactate, thereby helping living systems get rid of this otherwise cytotoxic byproduct of metabolism. In addition, a glutathione-independent GLYIII enzyme activity also exists in the biological systems that can directly convert MG to d-lactate. Humans and

Indexed as

Aldehyde OxidoreductasesAnimalsBacterial ProteinsEvolution, MolecularHydroxyacylglutathione HydrolaseLactoylglutathione LyasePlant ProteinsPlantsThiolester HydrolasesAldehyde OxidoreductasesBacterial Proteinsglyoxalase IIIHydroxyacylglutathione HydrolaseLactoylglutathione LyasePlant ProteinsThiolester Hydrolasesabiotic stress toleranceglyoxalase IIIglyoxalase pathwaymethylglyoxalmultigene familyplantsprokaryotes

Identifiers

PMID28358304
PMCPMC5412262
OpenAlexW2601829925

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.