Evidence map›Paper›PMID 31154163›Full record

ArticleRedox biology2019

Quantification of cellular protein and redox imbalance using SILAC-iodoTMT methodology.

Marie Vajrychova, Barbora Salovska, Kristyna Pimkova, Ivo Fabrik, Vojtech Tambor, Alexandra Kondelova, Jiri Bartek, Zdenek Hodny

Abstract read
In one paragraph

Article in Redox biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Review
  2. Article
  3. IL-6 Mutation Attenuates Liver Injury Caused byInternational journal of molecular sciences · 2023
    Article
  4. Article
  5. SILAC-IodoTMT for Assessment of the Cellular Proteome and Its Redox Status.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  6. Article
  7. Article
  8. Sod1 integrates oxygen availability to redox regulate NADPH production and the thiol redoxome.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Review
  10. Article
  11. Article
  12. 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

8 authors.

Marie VajrychovaBiomedical Research Center, University Hospital Hradec Kralove, Sokolska 581, 500 05, Hradec Kralove, Czech Republic.
Barbora SalovskaDepartment of Genome Integrity, Institute of Molecular Genetics of the ASCR, v. v. i., Videnska 1083, 142 20, Prague, Czech Republic.
Kristyna PimkovaBiomedical Research Center, University Hospital Hradec Kralove, Sokolska 581, 500 05, Hradec Kralove, Czech Republic.
Ivo FabrikBiomedical Research Center, University Hospital Hradec Kralove, Sokolska 581, 500 05, Hradec Kralove, Czech Republic.
Vojtech TamborBiomedical Research Center, University Hospital Hradec Kralove, Sokolska 581, 500 05, Hradec Kralove, Czech Republic.
Alexandra KondelovaDepartment of Genome Integrity, Institute of Molecular Genetics of the ASCR, v. v. i., Videnska 1083, 142 20, Prague, Czech Republic.
Jiri BartekDepartment of Genome Integrity, Institute of Molecular Genetics of the ASCR, v. v. i., Videnska 1083, 142 20, Prague, Czech Republic; Danish Cancer Society Research Center, Strandboulevarden 49, DK-2100 Copenhagen, Denmark; Department of Medical Biochemistry and Biophysics, Division of Genome Biology, Science for Life Laboratory, Karolinska Institute, Tomtebodavägen 23A, 171 65, Stockholm, Sweden. Electronic address: jb@cancer.dk.
Zdenek HodnyDepartment of Genome Integrity, Institute of Molecular Genetics of the ASCR, v. v. i., Videnska 1083, 142 20, Prague, Czech Republic. Electronic address: hodny@img.cas.cz.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Under normal conditions, the cellular redox status is maintained in a steady state by reduction and oxidation processes. These redox alterations in the cell are mainly sensed by protein thiol residues of cysteines thus regulating protein function. The imbalance in redox homeostasis may therefore regulate protein turnover either directly by redox modulating of transcription factors or indirectly by the degradation of damaged proteins due to oxidation. A new analytical method capable of simultaneously assessing cellular protein expression and cysteine oxidation would provide a valuable tool for the field of cysteine-targeted biology. Here, we show a workflow based on protein quantification using metabolic labeling and determination of cysteine oxidation using reporter ion quantification. We applied this approach to determine protein and redox changes in cells after 5-min, 60-min and 32-h exposure to H

Indexed as

Oxidation-ReductionProteomeProteomicsChromatography, LiquidCysteineHydrogen PeroxideOxidative StressPeroxiredoxinsTandem Mass SpectrometryCysteineHydrogen PeroxidePeroxiredoxinsProteomeCysteineLiquid chromatography/mass spectrometryPeroxiredoxinProteomeRedoxomeSILAC-iodoTMT labeling

Identifiers

PMID31154163
PMCPMC6545335

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.