Evidence map›Paper›PMID 26810073›Full record

ReviewMolecules and cells2016

Thiol-Based Peroxidases and Ascorbate Peroxidases: Why Plants Rely on Multiple Peroxidase Systems in the Photosynthesizing Chloroplast?

Karl-Josef Dietz

Open access · diamondAbstract readReview
In one paragraph

Review in Molecules and cells, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
10.8field-weighted citation impact, top 1% 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

64 citing papers in PubMed, 155 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Asphaltene biotransformation by a novel enzyme thiol peroxidase fromApplied and environmental microbiology · 2025
    Article
  5. Article
  6. Transcriptomic Characterization of Candidate Genes forPathogens (Basel, Switzerland) · 2025
    Article
  7. Article
  8. Peptides and Reactive Oxygen Species Regulate Root Development.International journal of molecular sciences · 2025
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. DIA-Based Quantitative Proteomics in the Flower Buds of TwoInternational journal of molecular sciences · 2024
    Article
  17. Review
  18. Review
  19. Review
  20. Review

4 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Karl-Josef DietzBiochemistry and Physiology of Plants, Faculty of Biology, W5-134, Bielefeld University, University Street 25, 33501 Bielefeld, Germany.
Bielefeld University · DE

Funding

Medical Research Council MC_UP_1201/4
6 · The paper itself

Abstract

Photosynthesis is a highly robust process allowing for rapid adjustment to changing environmental conditions. The efficient acclimation depends on balanced redox metabolism and control of reactive oxygen species release which triggers signaling cascades and potentially detrimental oxidation reactions. Thiol peroxidases of the peroxiredoxin and glutathione peroxidase type, and ascorbate peroxidases are the main peroxide detoxifying enzymes of the chloroplast. They use different electron donors and are linked to distinct redox networks. In addition, the peroxiredoxins serve functions in redox regulation and retrograde signaling. The complexity of plastid peroxidases is discussed in context of suborganellar localization, substrate preference, metabolic coupling, protein abundance, activity regulation, interactions, signaling functions, and the conditional requirement for high antioxidant capacity. Thus the review provides an opinion on the advantage of linking detoxification of peroxides to different enzymatic systems and implementing mechanisms for their inactivation to enforce signal propagation within and from the chloroplast.

Indexed as

PhotosynthesisAscorbate PeroxidasesChloroplast ProteinsChloroplastsGene Expression Regulation, PlantGlutathione PeroxidaseOxidation-ReductionPeroxidesPeroxiredoxinsSubstrate SpecificityAscorbate PeroxidasesChloroplast ProteinsGlutathione PeroxidasePeroxidesPeroxiredoxinsacorbate peroxidasechloroplastperoxiredoxinphotosynthesisredox sensing

Identifiers

PMID26810073
PMCPMC4749869
OpenAlexW2416515627

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.