Evidence map›Paper›PMID 29054072›Full record

ArticleRedox biology2018

Cysteine perthiosulfenic acid (Cys-SSOH): A novel intermediate in thiol-based redox signaling?

David E Heppner, Milena Hristova, Tomoaki Ida, Ana Mijuskovic, Christopher M Dustin, Virág Bogdándi, Jon M Fukuto, Tobias P Dick, Péter Nagy, Jianing Li and 2 more

Abstract read
In one paragraph

Article in Redox biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Review
  2. Raman signatures ofFrontiers in microbiology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Emerging Chemical Biology of Protein Persulfidation.Antioxidants & redox signaling · 2023
    Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Regulation of the redox metabolome and thiol proteome by hydrogen sulfide.Critical reviews in biochemistry and molecular biology · 2021
    Article
  18. Article
  19. Review
  20. Sulfur Metabolism Under Stress.Antioxidants & redox signaling · 2020
    Article
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

12 authors.

David E HeppnerDepartment of Pathology and Laboratory Medicine, Robert Larner M.D., College of Medicine, University of Vermont, Burlington, VT, USA.
Milena HristovaDepartment of Pathology and Laboratory Medicine, Robert Larner M.D., College of Medicine, University of Vermont, Burlington, VT, USA.
Tomoaki IdaDepartment of Environmental Health Sciences and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai, Japan.
Ana MijuskovicDivision of Redox Regulation, DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ), Heidelberg, Germany.
Christopher M DustinDepartment of Pathology and Laboratory Medicine, Robert Larner M.D., College of Medicine, University of Vermont, Burlington, VT, USA.
Virág BogdándiDepartment of Molecular Immunology and Toxicology, National Institute of Oncology, Budapest, Hungary.
Jon M FukutoDepartment of Chemistry, Sonoma State University, Rohnert Park, CA, USA.
Tobias P DickDivision of Redox Regulation, DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ), Heidelberg, Germany.
Péter NagyDepartment of Molecular Immunology and Toxicology, National Institute of Oncology, Budapest, Hungary.
Jianing LiDepartment of Chemistry, University of Vermont, Burlington, VT, USA.
Takaaki AkaikeDepartment of Environmental Health Sciences and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai, Japan. Electronic address: takaike@med.tohoku.ac.jp.
Albert van der VlietDepartment of Pathology and Laboratory Medicine, Robert Larner M.D., College of Medicine, University of Vermont, Burlington, VT, USA. Electronic address: albert.van-der-vliet@med.uvm.edu.

Funding

Multidisciplinary Training in Lung BiologyT32HL076122 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI IRVIN, CHARLES G, POYNTER, MATTHEW E · 2004 to 2023
$6.1M
Dual Oxidase in Airway Epithelial Repair and RemodelingR01HL085646 · NHLBI · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI VAN DER VLIET, ALBERT · 2008 to 2020
$4.7M
DUOX1 and Mitochondria in Obese AsthmaR01HL138708 · NHLBI · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI VAN DER VLIET, ALBERT · 2017 to 2020
$2.1M
Cigarette Smoke-derived Electrophilic Aldehydes and Airway InflammationR01ES021476 · NIEHS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI VAN DER VLIET, ALBERT · 2012 to 2016
$1.9M
DUOX1 Silencing in Age-Related COPDR21AG055325 · NIA · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI VAN DER VLIET, ALBERT · 2017 to 2018
$429k
Investigations of Redox-dependent Processes of the Airway EpitheliumF32HL129706 · NHLBI · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI HEPPNER, DAVID E. · 2016 to 2016
$50k
NHLBI NIH HHS F32 HL129706NHLBI NIH HHS R01 HL085646NHLBI NIH HHS R01 HL138708NHLBI NIH HHS T32 HL076122NIA NIH HHS R21 AG055325NIEHS NIH HHS R01 ES021476
6 · The paper itself

Abstract

The reversible oxidation of protein cysteine residues (Cys-SH) is a key reaction in cellular redox signaling involving initial formation of sulfenic acids (Cys-SOH), which are commonly detected using selective dimedone-based probes. Here, we report that significant portions of dimedone-tagged proteins are susceptible to cleavage by DTT reflecting the presence of perthiosulfenic acid species (Cys-SSOH) due to similar oxidation of hydropersulfides (Cys-SSH), since Cys-S-dimedone adducts are stable toward DTT. Combined studies using molecular modeling, mass spectrometry, and cell-based experiments indicate that Cys-SSH are readily oxidized to Cys-SSOH, which forms stable adducts with dimedone-based probes. We additionally confirm the presence of Cys-SSH within protein tyrosine kinases such as EGFR, and their apparent oxidation to Cys-SSOH in response NADPH oxidase activation, suggesting that such Cys-SSH oxidation may represent a novel, as yet uncharacterized, event in redox-based signaling.

Indexed as

CyclohexanonesCysteineDithiothreitolHEK293 CellsHumansHydrogen PeroxideModels, MolecularNADPH OxidasesOxidation-ReductionProteinsProtein-Tyrosine KinasesSignal TransductionSulfenic AcidsSulfhydryl CompoundsCyclohexanonesCysteinecysteinesulfenic aciddimedoneDithiothreitolHydrogen PeroxideNADPH OxidasesProteinsProtein-Tyrosine KinasesSulfenic AcidsSulfhydryl CompoundsDimedoneHydrogen peroxideNADPH oxidaseRedox signalingSulfenic acidThiol oxidation

Identifiers

PMID29054072
PMCPMC5647513

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.