Evidence map›Paper›PMID 25316711›Full record

ArticleMolecular & cellular proteomics : MCP2015

cysTMTRAQ-An integrative method for unbiased thiol-based redox proteomics.

Jennifer Parker, Kelly Balmant, Fanchao Zhu, Ning Zhu, Sixue Chen

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. S-Nitroso-Proteome Revealed in Stomatal Guard Cell Response to Flg22.International journal of molecular sciences · 2020
    Article
  10. Review
  11. Article
  12. Comprehensive Redox Profiling of the Thiol Proteome ofMolecular & cellular proteomics : MCP · 2018
    Article
  13. Article
  14. Thiol Based Redox Signaling in Plant Nucleus.Frontiers in plant science · 2018
    Review
  15. Absence ofFrontiers in molecular neuroscience · 2018
    Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Quantifying reversible oxidation of protein thiols in photosynthetic organisms.Journal of the American Society for Mass Spectrometry · 2015
    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

5 authors at 1 institution in 1 country.

Jennifer ParkerFrom the ‡Department of Biology, Genetics Institute, University of Florida, Gainesville, Florida 32611; §Plant Molecular and Cellular Biology Program, University of Florida, Gainesville, Florida 32610;
Kelly BalmantFrom the ‡Department of Biology, Genetics Institute, University of Florida, Gainesville, Florida 32611; §Plant Molecular and Cellular Biology Program, University of Florida, Gainesville, Florida 32610;
Fanchao ZhuFrom the ‡Department of Biology, Genetics Institute, University of Florida, Gainesville, Florida 32611;
Ning ZhuFrom the ‡Department of Biology, Genetics Institute, University of Florida, Gainesville, Florida 32611;
Sixue ChenFrom the ‡Department of Biology, Genetics Institute, University of Florida, Gainesville, Florida 32611; §Plant Molecular and Cellular Biology Program, University of Florida, Gainesville, Florida 32610; ‖Interdisciplinary Center for Biotechnology Research, University of Florida, Gainesville, Florida 32610 schen@ufl.edu.
University of Florida · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Protein redox regulation plays important roles in many biological processes. Protein cysteine thiols are sensitive to redox changes and may function as redox switches, which turn signaling and metabolic pathways on or off to ensure speedy responses to environmental stimuli or stresses. Here we report a novel integrative proteomics method called cysTMTRAQ that combines two types of isobaric tags, cysteine tandem mass tags and isobaric tag for relative and absolute quantification, in one experiment. The method not only enables simultaneous analysis of cysteine redox changes and total protein level changes, but also allows the determination of bona fide redox modified cysteines in proteins through the correction of protein turnover. Overlooking the factor of protein-level changes in the course of protein posttranslational modification experiments could lead to misleading results. The capability to analyze protein posttranslational modification dynamics and protein-level changes in one experiment will advance proteomic studies in many areas of biology and medicine.

Indexed as

Protein Processing, Post-TranslationalApoproteinsbeta-GalactosidaseCysteineEscherichia coliEscherichia coli ProteinsLactalbuminLactoglobulinsMuramidaseOxidation-ReductionProteomicsSerum Albumin, BovineTransferrinApoproteinsapotransferrinbeta-GalactosidaseCysteineEscherichia coli ProteinsLactalbuminLactoglobulinsMuramidaseSerum Albumin, BovineTransferrin

Identifiers

PMID25316711
PMCPMC4288258
OpenAlexW2129307730

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.