Evidence map›Paper›PMID 24328795›Full record

ArticleAntioxidants & redox signaling2014

Insight into protein S-nitrosylation in Chlamydomonas reinhardtii.

Samuel Morisse, Mirko Zaffagnini, Xing-Huang Gao, Stéphane D Lemaire, Christophe H Marchand

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Article in Antioxidants & redox signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

39 citing papers in PubMed.

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  3. The activation ofPlant direct · 2024
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  17. Plant Proteomics and Systems Biology.Advances in experimental medicine and biology · 2021
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  18. Quantitative Proteome Profiling of aFrontiers in plant science · 2021
    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

5 authors.

Samuel Morisse1 Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, FRE3354 Centre National de la Recherche Scientifique, Institut de Biologie Physico-Chimique, Université Pierre et Marie Curie , Paris, France .
Mirko Zaffagnini
Xing-Huang Gao
Stéphane D Lemaire
Christophe H Marchand

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

aimsProtein S-nitrosylation, a post-translational modification (PTM) consisting of the covalent binding of nitric oxide (NO) to a cysteine thiol moiety, plays a major role in cell signaling and is recognized to be involved in numerous physiological processes and diseases in mammals. The importance of nitrosylation in photosynthetic eukaryotes has been less studied. The aim of this study was to expand our knowledge on protein nitrosylation by performing a large-scale proteomic analysis of proteins undergoing nitrosylation in vivo in Chlamydomonas reinhardtii cells under nitrosative stress.

resultsUsing two complementary proteomic approaches, 492 nitrosylated proteins were identified. They participate in a wide range of biological processes and pathways, including photosynthesis, carbohydrate metabolism, amino acid metabolism, translation, protein folding or degradation, cell motility, and stress. Several proteins were confirmed in vitro by western blot, site-directed mutagenesis and activity measurements. Moreover, 392 sites of nitrosylation were also identified. These results strongly suggest that S-nitrosylation could constitute a major mechanism of regulation in C. reinhardtii under nitrosative stress conditions. INNOVATION: This study constitutes the largest proteomic analysis of protein nitrosylation reported to date.

conclusionThe identification of 381 previously unrecognized targets of nitrosylation further extends our knowledge on the importance of this PTM in photosynthetic eukaryotes. The data have been deposited to the ProteomeXchange repository with identifier PXD000569.

Indexed as

Chlamydomonas reinhardtiiPlant ProteinsProtein Processing, Post-TranslationalPlant Proteins

Identifiers

PMID24328795
PMCPMC4158989

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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.