Evidence map›Paper›PMID 24268782›Full record

ArticleCell reports2013

A peroxiredoxin promotes H2O2 signaling and oxidative stress resistance by oxidizing a thioredoxin family protein.

Jonathon D Brown, Alison M Day, Sarah R Taylor, Lewis E Tomalin, Brian A Morgan, Elizabeth A Veal

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

41 citing papers in PubMed, 77 citations in OpenAlex.

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  12. Oxidative stress response pathways in fungi.Cellular and molecular life sciences : CMLS · 2022
    Review
  13. Increasing NADPH impairs fungal HBioresources and bioprocessing · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. PRDX2 plays an oncogenic role in esophageal squamous cell carcinoma via Wnt/β-catenin and AKT pathways.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2020
    Article
  19. Article
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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

6 authors at 1 institution in 1 country.

Jonathon D BrownInstitute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle NE2 4HH, Tyne and Wear, UK.
Alison M DayInstitute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle NE2 4HH, Tyne and Wear, UK.
Sarah R TaylorInstitute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle NE2 4HH, Tyne and Wear, UK.
Lewis E TomalinInstitute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle NE2 4HH, Tyne and Wear, UK.
Brian A MorganInstitute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle NE2 4HH, Tyne and Wear, UK. Electronic address: b.a.morgan@ncl.ac.uk.
Elizabeth A VealInstitute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle NE2 4HH, Tyne and Wear, UK. Electronic address: e.a.veal@ncl.ac.uk.
Newcastle University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F023065/1Medical Research Council
6 · The paper itself

Abstract

H2O2 can cause oxidative damage associated with age-related diseases such as diabetes and cancer but is also used to initiate diverse responses, including increased antioxidant gene expression. Despite significant interest, H2O2-signaling mechanisms remain poorly understood. Here, we present a mechanism for the propagation of an H2O2 signal that is vital for the adaptation of the model yeast, Schizosaccharomyces pombe, to oxidative stress. Peroxiredoxins are abundant peroxidases with conserved antiaging and anticancer activities. Remarkably, we find that the only essential function for the thioredoxin peroxidase activity of the Prx Tpx1(hPrx1/2) in resistance to H2O2 is to inhibit a conserved thioredoxin family protein Txl1(hTxnl1/TRP32). Thioredoxins regulate many enzymes and signaling proteins. Thus, our discovery that a Prx amplifies an H2O2 signal by driving the oxidation of a thioredoxin-like protein has important implications, both for Prx function in oxidative stress resistance and for responses to H2O2.

Indexed as

Oxidative StressBasic-Leucine Zipper Transcription FactorsHydrogen PeroxidePeroxiredoxinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsThioredoxinsBasic-Leucine Zipper Transcription FactorsHydrogen PeroxidePap1 protein, S pombePeroxiredoxinsSchizosaccharomyces pombe ProteinsThioredoxinsTpx1 protein, S pombeTxl1 protein, S pombe

Identifiers

PMID24268782
PMCPMC3898613
OpenAlexW2116874572

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.