Evidence map›Paper›PMID 21194355›Full record

ReviewAntioxidants & redox signaling2011

Peroxiredoxins in plants and cyanobacteria.

Karl-Josef Dietz

Open access · hybridAbstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
151citing papers in PubMed, 1 pooled it
11.0field-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

151 citing papers in PubMed, 1 synthesis or guideline pooled it, 390 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Antioxidants (Basel, Switzerland) · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Identification ofAntioxidants (Basel, Switzerland) · 2025
    Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Involvement of Abscisic Acid in Transition of Pea (Plants (Basel, Switzerland) · 2024
    Article
  16. Redox dynamics in seeds ofFrontiers in plant science · 2024
    Article
  17. Article
  18. Article
  19. Review
  20. Article

91 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 DietzDepartment of Biochemistry and Physiology of Plants, Bielefeld University, Bielefeld, Germany. karl-josef.dietz@uni-bielefeld.de
Bielefeld University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxiredoxins (Prx) are central elements of the antioxidant defense system and the dithiol-disulfide redox regulatory network of the plant and cyanobacterial cell. They employ a thiol-based catalytic mechanism to reduce H2O2, alkylhydroperoxide, and peroxinitrite. In plants and cyanobacteria, there exist 2-CysPrx, 1-CysPrx, PrxQ, and type II Prx. Higher plants typically contain at least one plastid 2-CysPrx, one nucleo-cytoplasmic 1-CysPrx, one chloroplast PrxQ, and one each of cytosolic, mitochondrial, and plastidic type II Prx. Cyanobacteria express variable sets of three or more Prxs. The catalytic cycle consists of three steps: (i) peroxidative reduction, (ii) resolving step, and (iii) regeneration using diverse electron donors such as thioredoxins, glutaredoxins, cyclophilins, glutathione, and ascorbic acid. Prx proteins undergo major conformational changes in dependence of their redox state. Thus, they not only modulate cellular reactive oxygen species- and reactive nitrogen species-dependent signaling, but depending on the Prx type they sense the redox state, transmit redox information to binding partners, and function as chaperone. They serve in context of photosynthesis and respiration, but also in metabolism and development of all tissues, for example, in nodules as well as during seed and fruit development. The article surveys the current literature and attempts a mostly comprehensive coverage of present day knowledge and concepts on Prx mechanism, regulation, and function and thus on the whole Prx systems in plants.

Indexed as

AntioxidantsArabidopsisChloroplastsCyanobacteriaCysteineGene Expression Regulation, PlantGlutathioneHydrogen PeroxideOxidation-ReductionPeroxiredoxinsPhotosynthesisPlantsReactive Oxygen SpeciesThioredoxinsAntioxidantsCysteineGlutathioneHydrogen PeroxidePeroxiredoxinsReactive Oxygen SpeciesThioredoxins

Identifiers

PMID21194355
PMCPMC3135184
OpenAlexW2092809012

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.