Evidence map›Paper›PMID 25810097›Full record

ArticlePlant physiology2015

S-sulfhydration: a cysteine posttranslational modification in plant systems.

Ángeles Aroca, Antonio Serna, Cecilia Gotor, Luis C Romero

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
9.4field-weighted citation impact, top 2% 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

123 citing papers in PubMed, 315 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Aboveground whole-plant live HRedox biology · 2026
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  8. Review
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  10. Integration of NO and HPlant communications · 2026
    Review
  11. Article
  12. HMolecular plant pathology · 2025
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. Article

63 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

4 authors at 1 institution in 1 country.

Ángeles ArocaInstituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas y Universidad de Sevilla, 41092 Seville, Spain (A.A., C.G., L.C.R.); andAB Sciex, 28108 Alcobendas, Madrid, Spain (A.S.).ORCID http://orcid.org/0000-0003-4915-170X
Antonio SernaInstituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas y Universidad de Sevilla, 41092 Seville, Spain (A.A., C.G., L.C.R.); andAB Sciex, 28108 Alcobendas, Madrid, Spain (A.S.).
Cecilia GotorInstituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas y Universidad de Sevilla, 41092 Seville, Spain (A.A., C.G., L.C.R.); andAB Sciex, 28108 Alcobendas, Madrid, Spain (A.S.).ORCID http://orcid.org/0000-0003-4272-7446
Luis C RomeroInstituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas y Universidad de Sevilla, 41092 Seville, Spain (A.A., C.G., L.C.R.); andAB Sciex, 28108 Alcobendas, Madrid, Spain (A.S.) lromero@ibvf.csic.es.ORCID http://orcid.org/0000-0002-2414-4813
Consejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydrogen sulfide is a highly reactive molecule that is currently accepted as a signaling compound. This molecule is as important as carbon monoxide in mammals and hydrogen peroxide in plants, as well as nitric oxide in both eukaryotic systems. Although many studies have been conducted on the physiological effects of hydrogen sulfide, the underlying mechanisms are poorly understood. One of the proposed mechanisms involves the posttranslational modification of protein cysteine residues, a process called S-sulfhydration. In this work, a modified biotin switch method was used for the detection of Arabidopsis (Arabidopsis thaliana) proteins modified by S-sulfhydration under physiological conditions. The presence of an S-sulfhydration-modified cysteine residue on cytosolic ascorbate peroxidase was demonstrated using liquid chromatography-tandem mass spectrometry analysis, and a total of 106 S-sulfhydrated proteins were identified. Immunoblot and enzyme activity analyses of some of these proteins showed that the sulfide added through S-sulfhydration reversibly regulates the functions of plant proteins in a manner similar to that described in mammalian systems.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceArabidopsisArabidopsis ProteinsAscorbate PeroxidasesBiotinCysteineCytosolImmunoblottingMass SpectrometryMolecular Sequence DataRecombinant ProteinsSulfidesAPX1 protein, ArabidopsisArabidopsis ProteinsAscorbate PeroxidasesBiotinCysteineRecombinant ProteinsSulfides

Identifiers

PMID25810097
PMCPMC4424021
OpenAlexW2107898534

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.