Evidence map›Paper›PMID 26282677›Full record

SynthesisRedox biology2015

Differential alkylation-based redox proteomics--Lessons learnt.

Katarzyna Wojdyla, Adelina Rogowska-Wrzesinska

Abstract readMeta-AnalysisReview
In one paragraph

Synthesis in Redox biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Cysteine Proteome Reveals Response to Endogenous Oxidative Stress inInternational journal of molecular sciences · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Dynamic redox balance directs the oocyte-to-embryo transition via developmentally controlled reactive cysteine changes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Comprehensive Redox Profiling of the Thiol Proteome ofMolecular & cellular proteomics : MCP · 2018
    Article
  20. 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

2 authors.

Katarzyna WojdylaProtein Research Group, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, 5230 Odense M, Denmark.
Adelina Rogowska-WrzesinskaProtein Research Group, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, 5230 Odense M, Denmark. Electronic address: adelinar@bmb.sdu.dk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cysteine is one of the most reactive amino acids. This is due to the electronegativity of sulphur atom in the side chain of thiolate group. It results in cysteine being present in several distinct redox forms inside the cell. Amongst these, reversible oxidations, S-nitrosylation and S-sulfenylation are crucial mediators of intracellular redox signalling, with known associations to health and disease. Study of their functionalities has intensified thanks to the development of various analytical strategies, with particular contribution from differential alkylation-based proteomics methods. Presented here is a critical evaluation of differential alkylation-based strategies for the analysis of S-nitrosylation and S-sulfenylation. The aim is to assess the current status and to provide insights for future directions in the dynamically evolving field of redox proteomics. To achieve that we collected 35 original research articles published since 2010 and analysed them considering the following parameters, (i) resolution of modification site, (ii) quantitative information, including correction of modification levels by protein abundance changes and determination of modification site occupancy, (iii) throughput, including the amount of starting material required for analysis. The results of this meta-analysis are the core of this review, complemented by issues related to biological models and sample preparation in redox proteomics, including conditions for free thiol blocking and labelling of target cysteine oxoforms.

Indexed as

AlkylationAnimalsArsenitesAscorbic AcidCysteineDithiothreitolEthylmaleimideEukaryotic CellsHumansIodoacetamideModels, BiologicalOxidation-ReductionPhosphinesProteomicsStaining and LabelingSulfhydryl CompoundsarseniteArsenitesAscorbic AcidCysteineDithiothreitolEthylmaleimideIodoacetamidePhosphinesSulfhydryl Compoundstris(2-carboxyethyl)phosphineCysteine oxidationDifferential alkylationModification site occupancyQuantitative redox proteomics

Identifiers

PMID26282677
PMCPMC4543216

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Registered trials

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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.