Evidence map›Paper›PMID 27913623›Full record

ArticleThe Journal of biological chemistry2017

ChaC2, an Enzyme for Slow Turnover of Cytosolic Glutathione.

Amandeep Kaur, Ruchi Gautam, Ritika Srivastava, Avinash Chandel, Akhilesh Kumar, Subramanian Karthikeyan, Anand Kumar Bachhawat

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.5field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Lysosomal reduced thiols are essential for mouse embryonic development.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  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

7 authors at 2 institutions in 1 country.

Amandeep KaurFrom the Department of Biological Sciences, Indian Institute of Science Education and Research, Mohali, S.A.S. Nagar, Punjab 140306, India and.
Ruchi Gautamthe CSIR-Institute of Microbial Technology, Council of Scientific and Industrial Research (CSIR), Sector 39A, Chandigarh 160036, India.
Ritika Srivastavathe CSIR-Institute of Microbial Technology, Council of Scientific and Industrial Research (CSIR), Sector 39A, Chandigarh 160036, India.
Avinash ChandelFrom the Department of Biological Sciences, Indian Institute of Science Education and Research, Mohali, S.A.S. Nagar, Punjab 140306, India and.
Akhilesh KumarFrom the Department of Biological Sciences, Indian Institute of Science Education and Research, Mohali, S.A.S. Nagar, Punjab 140306, India and.
Subramanian Karthikeyanthe CSIR-Institute of Microbial Technology, Council of Scientific and Industrial Research (CSIR), Sector 39A, Chandigarh 160036, India skarthik@imtech.res.in.
Anand Kumar BachhawatFrom the Department of Biological Sciences, Indian Institute of Science Education and Research, Mohali, S.A.S. Nagar, Punjab 140306, India and anand@iisermohali.ac.in.
Indian Institute of Science Education and Research Mohali · INInstitute of Microbial Technology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutathione degradation plays an important role in glutathione and redox homeostasis, and thus it is imperative to understand the enzymes and the mechanisms involved in glutathione degradation in detail. We describe here ChaC2, a member of the ChaC family of γ-glutamylcyclotransferases, as an enzyme that degrades glutathione in the cytosol of mammalian cells. ChaC2 is distinct from the previously described ChaC1, to which ChaC2 shows ∼50% sequence identity. Human and mouse ChaC2 proteins purified in vitro show 10-20-fold lower catalytic efficiency than ChaC1, although they showed comparable K

Indexed as

AnimalsCatalysisCatalytic DomainCell LineCrystallography, X-Raygamma-GlutamylcyclotransferaseGene Expression Regulation, EnzymologicGlutathioneHumansMiceSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsgamma-GlutamylcyclotransferaseGGCT protein, humanGlutathioneSaccharomyces cerevisiae ProteinsChaC2ChaC proteinscrystal structureGCG1glutathione degradationMichaelis-Mentenprotein expressionprotein structureX-ray crystallographyγ-glutamylcyclotransferase fold

Identifiers

PMID27913623
PMCPMC5241738
OpenAlexW2557738316

What OpenQuestion holds

Textmetadata
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.