Evidence map›Paper›PMID 35793584›Full record

ArticleRedox biology2022

Structural snapshots of nitrosoglutathione binding and reactivity underlying S-nitrosylation of photosynthetic GAPDH.

Edoardo Jun Mattioli, Jacopo Rossi, Maria Meloni, Marcello De Mia, Christophe H Marchand, Andrea Tagliani, Silvia Fanti, Giuseppe Falini, Paolo Trost, Stéphane D Lemaire and 3 more

Abstract read
In one paragraph

Article in Redox biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
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  5. 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

13 authors.

Edoardo Jun MattioliDepartment of Chemistry "G. Ciamician", University of Bologna, I-40126, Bologna, Italy.
Jacopo RossiDepartment of Pharmacy and Biotechnologies, University of Bologna, I-40126, Bologna, Italy.
Maria MeloniDepartment of Pharmacy and Biotechnologies, University of Bologna, I-40126, Bologna, Italy.
Marcello De MiaCNRS, Sorbonne Université, Institut de Biologie Physico-Chimique, UMR8226, F-75005, Paris, France.
Christophe H MarchandCNRS, Sorbonne Université, Institut de Biologie Physico-Chimique, UMR8226, F-75005, Paris, France; CNRS, Institut de Biologie Physico-Chimique, Plateforme de Protéomique, FR550, F-75005, Paris, France.
Andrea TaglianiDepartment of Pharmacy and Biotechnologies, University of Bologna, I-40126, Bologna, Italy; CNRS, Sorbonne Université, Institut de Biologie Physico-Chimique, UMR8226, F-75005, Paris, France.
Silvia FantiDepartment of Chemistry "G. Ciamician", University of Bologna, I-40126, Bologna, Italy.
Giuseppe FaliniDepartment of Chemistry "G. Ciamician", University of Bologna, I-40126, Bologna, Italy.
Paolo TrostDepartment of Pharmacy and Biotechnologies, University of Bologna, I-40126, Bologna, Italy.
Stéphane D LemaireCNRS, Sorbonne Université, Institut de Biologie Physico-Chimique, UMR8226, F-75005, Paris, France; Sorbonne Université, CNRS, Institut de Biologie Paris-Seine, Laboratory of Computational and Quantitative Biology, UMR7238, F-75005, Paris, France.
Simona FermaniDepartment of Chemistry "G. Ciamician", University of Bologna, I-40126, Bologna, Italy; CIRI Health Sciences & Technologies (HST), University of Bologna, I-40064, Bologna, Italy. Electronic address: simona.fermani@unibo.it.
Matteo CalvaresiDepartment of Chemistry "G. Ciamician", University of Bologna, I-40126, Bologna, Italy; CIRI Health Sciences & Technologies (HST), University of Bologna, I-40064, Bologna, Italy. Electronic address: matteo.calvaresi3@unibo.it.
Mirko ZaffagniniDepartment of Pharmacy and Biotechnologies, University of Bologna, I-40126, Bologna, Italy. Electronic address: mirko.zaffagnini3@unibo.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S-nitrosylation is a redox post-translational modification widely recognized to play an important role in cellular signaling as it can modulate protein function and conformation. At the physiological level, nitrosoglutathione (GSNO) is considered the major physiological NO-releasing compound due to its ability to transfer the NO moiety to protein thiols but the structural determinants regulating its redox specificity are not fully elucidated. In this study, we employed photosynthetic glyceraldehyde-3-phosphate dehydrogenase from Chlamydomonas reinhardtii (CrGAPA) to investigate the molecular mechanisms underlying GSNO-dependent thiol oxidation. We first observed that GSNO causes reversible enzyme inhibition by inducing S-nitrosylation. While the cofactor NADP

Indexed as

Glyceraldehyde-3-Phosphate DehydrogenasesS-NitrosoglutathioneNADPNitric OxideOxidation-ReductionPhotosynthesisSulfhydryl CompoundsGlyceraldehyde-3-Phosphate DehydrogenasesNADPNitric OxideS-NitrosoglutathioneSulfhydryl CompoundsAnd S-NitrosylationChlamydomonasCysteineNitrosoglutathionePhotosynthetic GAPDH

Identifiers

PMID35793584
PMCPMC9287727

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Registered trials

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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.