Evidence map›Paper›PMID 22122882›Full record

ArticleMolecular & cellular proteomics : MCP2012

Glutathionylation in the photosynthetic model organism Chlamydomonas reinhardtii: a proteomic survey.

Mirko Zaffagnini, Mariette Bedhomme, Hayam Groni, Christophe H Marchand, Carine Puppo, Brigitte Gontero, Corinne Cassier-Chauvat, Paulette Decottignies, Stéphane D Lemaire

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

62 citing papers in PubMed, 158 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. The activation ofPlant direct · 2024
    Article
  6. Plant Life with and without Oxygen: A Metabolomics Approach.International journal of molecular sciences · 2023
    Review
  7. Review
  8. Review
  9. Article
  10. Adapting from Low to High: An Update to COPlants (Basel, Switzerland) · 2023
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Review
  20. Review

2 more citing papers are in PubMed but not listed here.

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

9 authors at 5 institutions in 1 country.

Mirko ZaffagniniLaboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, FRE3354 Centre National de la Recherche Scientifique, Université Pierre et Marie Curie, Institut de Biologie Physico-Chimique, 75005 Paris, France.
Mariette Bedhomme
Hayam Groni
Christophe H Marchand
Carine Puppo
Brigitte Gontero
Corinne Cassier-Chauvat
Paulette Decottignies
Stéphane D Lemaire
Centre National de la Recherche Scientifique · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRUniversité Paris-Sud · FRAix-Marseille Université · FRInstitut de Microbiologie de la Méditerranée · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein glutathionylation is a redox post-translational modification occurring under oxidative stress conditions and playing a major role in cell regulation and signaling. This modification has been mainly studied in nonphotosynthetic organisms, whereas much less is known in photosynthetic organisms despite their important exposure to oxidative stress caused by changes in environmental conditions. We report a large scale proteomic analysis using biotinylated glutathione and streptavidin affinity chromatography that allowed identification of 225 glutathionylated proteins in the eukaryotic unicellular green alga Chlamydomonas reinhardtii. Moreover, 56 sites of glutathionylation were also identified after peptide affinity purification and tandem mass spectrometry. The targets identified belong to a wide range of biological processes and pathways, among which the Calvin-Benson cycle appears to be a major target. The glutathionylation of four enzymes of this cycle, phosphoribulokinase, glyceraldehyde-3-phosphate dehydrogenase, ribose-5-phosphate isomerase, and phosphoglycerate kinase was confirmed by Western blot and activity measurements. The results suggest that glutathionylation could constitute a major mechanism of regulation of the Calvin-Benson cycle under oxidative stress conditions.

Indexed as

Oxidative StressPhotosynthesisProteomicsAldose-Ketose IsomerasesBlotting, WesternCells, CulturedChlamydomonas reinhardtiiChromatography, AffinityChromatography, LiquidGlutathioneGlyceraldehyde-3-Phosphate DehydrogenasesOxidation-ReductionPhosphoglycerate KinasePhosphotransferases (Alcohol Group Acceptor)Plant ProteinsPlasmidsAldose-Ketose IsomerasesGlutathioneGlyceraldehyde-3-Phosphate DehydrogenasesPhosphoglycerate KinasephosphoribulokinasePhosphotransferases (Alcohol Group Acceptor)Plant Proteinsribosephosphate isomerase

Identifiers

PMID22122882
PMCPMC3277769
OpenAlexW1992104581

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.