Evidence map›Paper›PMID 22527720›Full record

ReviewCellular and molecular life sciences : CMLS2012

γ-Glutamyltranspeptidases: sequence, structure, biochemical properties, and biotechnological applications.

Immacolata Castellano, Antonello Merlino

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
–field-weighted citation impact
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

55 citing papers in PubMed.

  1. Article
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  3. Review
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  7. Observational
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  13. Article
  14. A Prognostic Activity of Glutaredoxin 1 Protein (Grx1) in Colon Cancer.International journal of molecular sciences · 2024
    Article
  15. Diverse roles of low-molecular weight thiol GSH inCurrent research in microbial sciences · 2024
    Article
  16. Self-DNA Inhibition inBiology · 2023
    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

2 authors.

Immacolata CastellanoInstitute of Protein Biochemistry, CNR, via Pietro Castellino, Naples, Italy. i.castellano@ibp.cnr.it
Antonello Merlino

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

γ-Glutamyltranspeptidases (γ-GTs) are ubiquitous enzymes that catalyze the hydrolysis of γ-glutamyl bonds in glutathione and glutamine and the transfer of the released γ-glutamyl group to amino acids or short peptides. These enzymes are involved in glutathione metabolism and play critical roles in antioxidant defense, detoxification, and inflammation processes. Moreover, γ-GTs have been recently found to be involved in many physiological disorders, such as Parkinson's disease and diabetes. In this review, the main biochemical and structural properties of γ-GTs isolated from different sources, as well as their conformational stability and mechanism of catalysis, are described and examined with the aim of contributing to the discussion on their structure-function relationships. Possible applications of γ-glutamyltranspeptidases in different fields of biotechnology and medicine are also discussed.

Indexed as

BiotechnologyAmino Acid SequenceAnimalsgamma-GlutamyltransferaseGlutamineHumansMolecular ConformationMolecular Sequence DataSequence Homology, Amino Acidgamma-GlutamyltransferaseGlutamine

Identifiers

PMID22527720
PMCPMC11115026

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.