Evidence map›Paper›PMID 23749990›Full record

ArticleThe Journal of biological chemistry2013

Mechanisms of nitrosylation and denitrosylation of cytoplasmic glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana.

Mirko Zaffagnini, Samuel Morisse, Mariette Bedhomme, Christophe H Marchand, Margherita Festa, Nicolas Rouhier, Stéphane D Lemaire, Paolo Trost

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

37 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
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  5. De-nitrosylation Coordinates Appressorium Function for Infection of the Rice Blast Fungus.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  6. Redox dynamics in seeds ofFrontiers in plant science · 2024
    Article
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  15. Quantitative Proteome Profiling of aFrontiers in plant science · 2021
    Article
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  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

8 authors at 3 institutions in 3 countries.

Mirko ZaffagniniLaboratory of Plant Redox Biology, Department of Pharmacy and Biotechnology, University of Bologna, Via Irnerio 42, 40126 Bologna, Italy.
Samuel Morisse
Mariette Bedhomme
Christophe H Marchand
Margherita Festa
Nicolas Rouhier
Stéphane D Lemaire
Paolo Trost
Centre National de la Recherche Scientifique · FRUniversity of Bologna · ITInstitut National de la Recherche Agronomique · MA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitrosylation is a reversible post-translational modification of protein cysteines playing a major role in cellular regulation and signaling in many organisms, including plants where it has been implicated in the regulation of immunity and cell death. The extent of nitrosylation of a given cysteine residue is governed by the equilibrium between nitrosylation and denitrosylation reactions. The mechanisms of these reactions remain poorly studied in plants. In this study, we have employed glycolytic GAPDH from Arabidopsis thaliana as a tool to investigate the molecular mechanisms of nitrosylation and denitrosylation using a combination of approaches, including activity assays, the biotin switch technique, site-directed mutagenesis, and mass spectrometry. Arabidopsis GAPDH activity was reversibly inhibited by nitrosylation of catalytic Cys-149 mediated either chemically with a strong NO donor or by trans-nitrosylation with GSNO. GSNO was found to trigger both GAPDH nitrosylation and glutathionylation, although nitrosylation was widely prominent. Arabidopsis GAPDH was found to be denitrosylated by GSH but not by plant cytoplasmic thioredoxins. GSH fully converted nitrosylated GAPDH to the reduced, active enzyme, without forming any glutathionylated GAPDH. Thus, we found that nitrosylation of GAPDH is not a step toward formation of the more stable glutathionylated enzyme. GSH-dependent denitrosylation of GAPC1 was found to be linked to the [GSH]/[GSNO] ratio and to be independent of the [GSH]/[GSSG] ratio. The possible importance of these biochemical properties for the regulation of Arabidopsis GAPDH functions in vivo is discussed.

Indexed as

ArabidopsisCytoplasmGlutathioneGlyceraldehyde-3-Phosphate DehydrogenasesNitric OxideOxidation-ReductionSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationGlutathioneGlyceraldehyde-3-Phosphate DehydrogenasesNitric OxideArabidopsisDenitrosylationGlutathioneGlutathionylationGlyceraldehyde-3-phosphate DehydrogenaseNitrosylationRedox SignalingThioredoxin

Identifiers

PMID23749990
PMCPMC3829362
OpenAlexW2107453482

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.