Evidence map›Paper›PMID 31434242›Full record

ReviewNutrients2019

Role of Glutathionylation in Infection and Inflammation.

Paola Checconi, Dolores Limongi, Sara Baldelli, Maria Rosa Ciriolo, Lucia Nencioni, Anna Teresa Palamara

Open access · goldAbstract readReview
In one paragraph

Review in Nutrients, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.7field-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

34 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Robust AMBER Force Field Parameters for Glutathionylated Cysteines.International journal of molecular sciences · 2023
    Article
  14. Review
  15. Chemistry and biology of enzymes in protein glutathionylation.Current opinion in chemical biology · 2023
    Review
  16. Article
  17. Coenzyme QJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2023
    Article
  18. Emerging chemistry and biology in protein glutathionylation.Current opinion in chemical biology · 2022
    Review
  19. Review
  20. Review
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

6 authors at 3 institutions in 1 country.

Paola ChecconiIRCCS San Raffaele Pisana, Department of Human Sciences and Promotion of the Quality of Life, San Raffaele Roma Open University, 00166 Rome, Italy. paola.checconi@unisanraffaele.gov.it.ORCID 0000-0001-7518-5730
Dolores LimongiIRCCS San Raffaele Pisana, Department of Human Sciences and Promotion of the Quality of Life, San Raffaele Roma Open University, 00166 Rome, Italy.ORCID 0000-0003-2095-8112
Sara BaldelliIRCCS San Raffaele Pisana, Department of Human Sciences and Promotion of the Quality of Life, San Raffaele Roma Open University, 00166 Rome, Italy.
Maria Rosa CirioloIRCCS San Raffaele Pisana, Department of Human Sciences and Promotion of the Quality of Life, San Raffaele Roma Open University, 00166 Rome, Italy.
Lucia NencioniDepartment of Public Health and Infectious Diseases, laboratory affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, Sapienza University of Rome, 00185 Rome, Italy.ORCID 0000-0003-4427-4823
Anna Teresa PalamaraIRCCS San Raffaele Pisana, Department of Human Sciences and Promotion of the Quality of Life, San Raffaele Roma Open University, 00166 Rome, Italy.
Istituti di Ricovero e Cura a Carattere Scientifico · ITIstituto Pasteur · ITUniversity of Rome Tor Vergata · IT

Funding

Ateneo Sapienza 2016Ministero dell'Istruzione, dell'Università e della Ricerca MIUR PRIN 2017KM79NNMinistero dell'Istruzione, dell'Università e della Ricerca PRIN 2017
6 · The paper itself

Abstract

Glutathionylation, that is, the formation of mixed disulfides between protein cysteines and glutathione (GSH) cysteines, is a reversible post-translational modification catalyzed by different cellular oxidoreductases, by which the redox state of the cell modulates protein function. So far, most studies on the identification of glutathionylated proteins have focused on cellular proteins, including proteins involved in host response to infection, but there is a growing number of reports showing that microbial proteins also undergo glutathionylation, with modification of their characteristics and functions. In the present review, we highlight the signaling role of GSH through glutathionylation, particularly focusing on microbial (viral and bacterial) glutathionylated proteins (GSSPs) and host GSSPs involved in the immune/inflammatory response to infection; moreover, we discuss the biological role of the process in microbial infections and related host responses.

Indexed as

Bacterial InfectionsCysteineDisulfidesGlutathioneHumansInfectionsInflammationOxidation-ReductionOxidoreductasesProtein Processing, Post-TranslationalProteinsSignal TransductionVirus DiseasesCysteineDisulfidesGlutathioneOxidoreductasesProteinsglutathioneglutathionylationinfectioninflammationredox signaling

Identifiers

PMID31434242
PMCPMC6723385
OpenAlexW2969782800

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.