Evidence map›Paper›PMID 33467703›Full record

ReviewMolecules (Basel, Switzerland)2021

Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation.

Elena Kalinina, Maria Novichkova

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

54 citing papers in PubMed, 111 citations in OpenAlex.

  1. Epigenetic regulation and ROS signaling in plant stress adaptation: an integrated framework.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026
    Review
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  13. The Molecular Pathology of Pre-Eclamptic Hypertension.Current issues in molecular biology · 2025
    Article
  14. Effects of short term dietary zinc deficiency and zinc supplementation on nitro-oxidative stress in testes of Wistar rats.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025
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  19. International journal of molecular sciences · 2024
    Article
  20. Shade-induced ROS/NO reinforce COP1-mediated diffuse cell growth.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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 at 1 institution in 1 country.

Elena KalininaT.T. Berezov Department of Biochemistry, Peoples' Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya Street, 117198 Moscow, Russia.
Maria NovichkovaT.T. Berezov Department of Biochemistry, Peoples' Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya Street, 117198 Moscow, Russia.ORCID 0000-0001-9697-5053
Peoples' Friendship University of Russia · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S-glutathionylation and S-nitrosylation are reversible post-translational modifications on the cysteine thiol groups of proteins, which occur in cells under physiological conditions and oxidative/nitrosative stress both spontaneously and enzymatically. They are important for the regulation of the functional activity of proteins and intracellular processes. Connecting link and "switch" functions between S-glutathionylation and S-nitrosylation may be performed by GSNO, the generation of which depends on the GSH content, the GSH/GSSG ratio, and the cellular redox state. An important role in the regulation of these processes is played by Trx family enzymes (Trx, Grx, PDI), the activity of which is determined by the cellular redox status and depends on the GSH/GSSG ratio. In this review, we analyze data concerning the role of GSH/GSSG in the modulation of S-glutathionylation and S-nitrosylation and their relationship for the maintenance of cell viability.

Indexed as

Protein Processing, Post-TranslationalAnimalsGlutathioneHumansNitric OxideOxidation-ReductionProteinsGlutathioneNitric OxideProteinsGSHnitrosoglutathioneredox-regulationS-glutathionylationS-nitrosylation

Identifiers

PMID33467703
PMCPMC7838997
OpenAlexW3119017924

What Socratic 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 Socratic graph.