Evidence map›Paper›PMID 24893130›Full record

ArticleAntioxidants & redox signaling2015

S-glutathionylation enhances human cystathionine β-synthase activity under oxidative stress conditions.

Wei-Ning Niu, Pramod Kumar Yadav, Jiri Adamec, Ruma Banerjee

Open access · hybridAbstract read
In one paragraph

Article in Antioxidants & redox signaling, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–field-weighted citation impact, top 83% 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

65 citing papers in PubMed, 0 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Sulfide regulation and catabolism in health and disease.Signal transduction and targeted therapy · 2025
    Review
  6. Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism.International journal of molecular sciences · 2025
    Review
  7. Article
  8. Persulfidation of Human CystathionineAntioxidants (Basel, Switzerland) · 2024
    Article
  9. Review
  10. Review
  11. Hydrogen Sulfide (HBiomolecules · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. A Metabolic Paradigm for Hydrogen Sulfide SignalingAntioxidants & redox signaling · 2023
    Review
  16. SELENBP1 overexpression in the prefrontal cortex underlies negative symptoms of schizophrenia.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Biological Functions of Hydrogen Sulfide in Plants.International journal of molecular sciences · 2022
    Review
  18. Review
  19. Article
  20. Review

5 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 2 countries.

Wei-Ning Niu1 The Key Laboratory for Space Bioscience and Biotechnology, School of Life Sciences, Northwestern Polytechnical University , Xi'an, China .
Pramod Kumar Yadav
Jiri Adamec
Ruma Banerjee
University of Nebraska–Lincoln · USNorthwestern Polytechnical University · CNUniversity of Michigan · US

Funding

Transsulfuration and HyperhomocysteinemiaR01HL058984 · NHLBI · UNIVERSITY OF NEBRASKA LINCOLN · PI BANERJEE, RUMA V · 1997 to 2020
$6.0M
Redox Biology CenterP30GM103335 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI BECKER, DONALD F · 2012 to 2016
$4.3M
NHLBI NIH HHS HL58984NIGMS NIH HHS P30 GM103335
6 · The paper itself

Abstract

aimsCystathionine β-synthase (CBS) catalyzes the first and rate-limiting step in the two-step trans-sulfuration pathway that converts homocysteine to cysteine. It is also one of three major enzymes responsible for the biogenesis of H2S, a signaling molecule. We have previously demonstrated that CBS is activated in cells challenged by oxidative stress, but the underlying molecular mechanism of this regulation has remained unclear.

resultsHere, we demonstrate that S-glutathionylation of CBS enhances its activity ∼2-fold in vitro. Loss of this post-translational modification in the presence of dithiothreitol results in reversal to basal activity. Cys346 was identified as the site for S-glutathionylation by a combination of mass spectrometric, mutagenesis, and activity analyses. To test the physiological relevance of S-glutathionylation-dependent regulation of CBS, HEK293 cells were oxidatively challenged with peroxide, which is known to enhance the trans-sulfuration flux. Under these conditions, CBS glutathionylation levels increased and were correlated with a ∼3-fold increase in CBS activity. INNOVATION: Collectively, our results reveal a novel post-translational modification of CBS, that is, glutathionylation, which functions as an allosteric activator under oxidative stress conditions permitting enhanced synthesis of both cysteine and H2S.

conclusionsOur study elucidates a molecular mechanism for increased cysteine and therefore glutathione, synthesis via glutathionylation of CBS. They also demonstrate the potential for increased H2S production under oxidative stress conditions, particularly in tissues where CBS is a major source of H2S.

Indexed as

Oxidative StressProtein Processing, Post-TranslationalCystathionine beta-SynthaseCysteineEnzyme ActivationGlutathioneHEK293 CellsHumansHydrogen PeroxideHydrogen SulfideMutationOxidantsCystathionine beta-SynthaseCysteineGlutathioneHydrogen PeroxideHydrogen SulfideOxidants

Identifiers

PMID24893130
PMCPMC4307034
OpenAlexW2294990821

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.