Evidence map›Paper›PMID 31772010›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Glutathionylation primes soluble glyceraldehyde-3-phosphate dehydrogenase for late collapse into insoluble aggregates.

Mirko Zaffagnini, Christophe H Marchand, Marco Malferrari, Samuel Murail, Sara Bonacchi, Damiano Genovese, Marco Montalti, Giovanni Venturoli, Giuseppe Falini, Marc Baaden and 3 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

23 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Implication ofInternational journal of molecular sciences · 2025
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  8. Article
  9. Robust AMBER Force Field Parameters for Glutathionylated Cysteines.International journal of molecular sciences · 2023
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Mechanism of GAPDH Redox Signaling by HInternational journal of molecular sciences · 2022
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  16. Review
  17. Review
  18. Article
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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

13 authors at 3 institutions in 2 countries.

Mirko ZaffagniniDepartment of Pharmacy and Biotechnology, University of Bologna, 40126 Bologna, Italy; mirko.zaffagnini3@unibo.it paolo.trost@unibo.it.ORCID 0000-0001-5115-0859
Christophe H MarchandLaboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, UMR8226 Centre National de la Recherche Scientifique, Institut de Biologie Physico-Chimique, Sorbonne Université, 75005 Paris, France.ORCID 0000-0002-0729-3841
Marco MalferrariDepartment of Pharmacy and Biotechnology, University of Bologna, 40126 Bologna, Italy.
Samuel MurailLaboratoire de Biochimie Théorique, Unités Propre de Recherche Centre National de la Recherche Scientifique, Université Paris Diderot, Sorbonne Paris Cité, 75005 Paris, France.ORCID 0000-0002-3842-5333
Sara BonacchiDepartment of Chemistry G. Ciamician, University of Bologna, 40126 Bologna, Italy.
Damiano GenoveseDepartment of Chemistry G. Ciamician, University of Bologna, 40126 Bologna, Italy.ORCID 0000-0002-4389-7247
Marco MontaltiDepartment of Chemistry G. Ciamician, University of Bologna, 40126 Bologna, Italy.
Giovanni VenturoliDepartment of Pharmacy and Biotechnology, University of Bologna, 40126 Bologna, Italy.
Giuseppe FaliniDepartment of Chemistry G. Ciamician, University of Bologna, 40126 Bologna, Italy.
Marc BaadenLaboratoire de Biochimie Théorique, Unités Propre de Recherche Centre National de la Recherche Scientifique, Université Paris Diderot, Sorbonne Paris Cité, 75005 Paris, France.ORCID 0000-0001-6472-0486
Stéphane D LemaireLaboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, UMR8226 Centre National de la Recherche Scientifique, Institut de Biologie Physico-Chimique, Sorbonne Université, 75005 Paris, France.
Simona FermaniDepartment of Chemistry G. Ciamician, University of Bologna, 40126 Bologna, Italy.ORCID 0000-0002-3056-3432
Paolo TrostDepartment of Pharmacy and Biotechnology, University of Bologna, 40126 Bologna, Italy; mirko.zaffagnini3@unibo.it paolo.trost@unibo.it.ORCID 0000-0002-6347-8701
University of Bologna · ITDélégation Paris 7 · FRSorbonne Université · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein aggregation is a complex physiological process, primarily determined by stress-related factors revealing the hidden aggregation propensity of proteins that otherwise are fully soluble. Here we report a mechanism by which glycolytic glyceraldehyde-3-phosphate dehydrogenase of

Indexed as

Molecular Sequence AnnotationArabidopsisArabidopsis ProteinsCatalytic DomainGlutaredoxinsGlutathioneGlutathione DisulfideGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)Glyceraldehyde-3-Phosphate DehydrogenasesKineticsMolecular Dynamics SimulationOxidation-ReductionProtein FoldingSolubilityThioredoxinsArabidopsis ProteinsGAPC1 protein, ArabidopsisGlutaredoxinsGlutathioneGlutathione DisulfideGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)Glyceraldehyde-3-Phosphate DehydrogenasesThioredoxinscysteinedisulfide bondglyceraldehyde-3-phosphate dehydrogenaseprotein aggregationS-glutathionylation

Identifiers

PMID31772010
PMCPMC6926014
OpenAlexW2990770240

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.