Evidence map›Paper›PMID 35323963›Full record

ReviewPlant & cell physiology2022

Thiol-based Oxidative Posttranslational Modifications (OxiPTMs) of Plant Proteins.

Francisco J Corpas, Salvador González-Gordo, Marta Rodríguez-Ruiz, María A Muñoz-Vargas, José M Palma

Open access · bronzeAbstract readReview
In one paragraph

Review in Plant & cell physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
9.7field-weighted citation impact, top 1% 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

30 citing papers in PubMed, 73 citations in OpenAlex.

  1. HHorticulture research · 2026
    Article
  2. Integration of NO and HPlant communications · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Redox regulation of meristem quiescence: outside/in.Journal of experimental botany · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. NO and HInternational journal of molecular sciences · 2024
    Review
  15. Article
  16. Review
  17. Roles of Reactive Carbonyl Species (RCS) in Plant Response to Abiotic Stress.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  18. Review
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Francisco J CorpasDepartment of Biochemistry, Cell and Molecular Biology of Plants, Group of Antioxidants, Free Radicals and Nitric Oxide in Biotechnology, Food and Agriculture, Estación Experimental del Zaidín (Spanish National Research Council, CSIC), C/ Professor Albareda, 1, Granada 18008, Spain.ORCID 0000-0002-1814-9212
Salvador González-GordoDepartment of Biochemistry, Cell and Molecular Biology of Plants, Group of Antioxidants, Free Radicals and Nitric Oxide in Biotechnology, Food and Agriculture, Estación Experimental del Zaidín (Spanish National Research Council, CSIC), C/ Professor Albareda, 1, Granada 18008, Spain.ORCID 0000-0002-3678-5503
Marta Rodríguez-RuizDepartment of Biochemistry, Cell and Molecular Biology of Plants, Group of Antioxidants, Free Radicals and Nitric Oxide in Biotechnology, Food and Agriculture, Estación Experimental del Zaidín (Spanish National Research Council, CSIC), C/ Professor Albareda, 1, Granada 18008, Spain.ORCID 0000-0002-7034-6117
María A Muñoz-VargasDepartment of Biochemistry, Cell and Molecular Biology of Plants, Group of Antioxidants, Free Radicals and Nitric Oxide in Biotechnology, Food and Agriculture, Estación Experimental del Zaidín (Spanish National Research Council, CSIC), C/ Professor Albareda, 1, Granada 18008, Spain.ORCID 0000-0002-1599-6803
José M PalmaDepartment of Biochemistry, Cell and Molecular Biology of Plants, Group of Antioxidants, Free Radicals and Nitric Oxide in Biotechnology, Food and Agriculture, Estación Experimental del Zaidín (Spanish National Research Council, CSIC), C/ Professor Albareda, 1, Granada 18008, Spain.ORCID 0000-0001-6673-3571
Consejo Superior de Investigaciones Científicas · ES

Funding

Spanish Ministry of Science and Innovation PID2019-103924GB-I00
6 · The paper itself

Abstract

The thiol group of cysteine (Cys) residues, often present in the active center of the protein, is of particular importance to protein function, which is significantly determined by the redox state of a protein's environment. Our knowledge of different thiol-based oxidative posttranslational modifications (oxiPTMs), which compete for specific protein thiol groups, has increased over the last 10 years. The principal oxiPTMs include S-sulfenylation, S-glutathionylation, S-nitrosation, persulfidation, S-cyanylation and S-acylation. The role of each oxiPTM depends on the redox cellular state, which in turn depends on cellular homeostasis under either optimal or stressful conditions. Under such conditions, the metabolism of molecules such as glutathione, NADPH (reduced nicotinamide adenine dinucleotide phosphate), nitric oxide, hydrogen sulfide and hydrogen peroxide can be altered, exacerbated and, consequently, outside the cell's control. This review provides a broad overview of these oxiPTMs under physiological and unfavorable conditions, which can regulate the function of target proteins.

Indexed as

Plant ProteinsSulfhydryl CompoundsGlutathioneOxidation-ReductionOxidative StressProtein Processing, Post-TranslationalGlutathionePlant ProteinsSulfhydryl CompoundsPersulfidationS-cyanylation and S-acylationS-glutathionylationS-nitrosationS-sulfenylation

Identifiers

PMID35323963
PMCPMC9282725
OpenAlexW4220983209

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.