Evidence map›Paper›PMID 33143095›Full record

ReviewInternational journal of molecular sciences2020

Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease.

Aysenur Musaogullari, Yuh-Cherng Chai

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
4.8field-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

60 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
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  4. [Exogenous nitric oxide suppresses KSheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2026
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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.

Aysenur MusaogullariDepartment of Chemistry, John Carroll University, University Heights, OH 44118, USA.
Yuh-Cherng ChaiDepartment of Chemistry, John Carroll University, University Heights, OH 44118, USA.
John Carroll University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S-glutathionylation, the post-translational modification forming mixed disulfides between protein reactive thiols and glutathione, regulates redox-based signaling events in the cell and serves as a protective mechanism against oxidative damage. S-glutathionylation alters protein function, interactions, and localization across physiological processes, and its aberrant function is implicated in various human diseases. In this review, we discuss the current understanding of the molecular mechanisms of S-glutathionylation and describe the changing levels of expression of S-glutathionylation in the context of aging, cancer, cardiovascular, and liver diseases.

Indexed as

Oxidative StressProtein Processing, Post-TranslationalAnimalsGlutathioneHumansOxidation-ReductionProteinsSignal TransductionGlutathioneProteinsGSH/GSSGoxidative stressprotein post-translational modificationredox modificationS-glutathionylation

Identifiers

PMID33143095
PMCPMC7663550
OpenAlexW3095259335

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.