Evidence map›Paper›PMID 8790288›Full record

ArticlePlant molecular biology1996

Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases.

M Baier, K J Dietz

Abstract read
PubMed Publisher
In one paragraph

Article in Plant molecular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Peroxiredoxins and Redox Signaling in Plants.Antioxidants & redox signaling · 2018
    Review
  6. Article
  7. The Plant Immunity Regulating F-Box ProteinFrontiers in plant science · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Peroxiredoxins in plants and cyanobacteria.Antioxidants & redox signaling · 2011
    Review
  15. Article
  16. Review
  17. Article
  18. Thioredoxins in chloroplasts.Current genetics · 2007
    Review
  19. Article
  20. 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

2 authors at 2 institutions in 1 country.

M BaierJulius-von-Sachs-Institut für Biowissenschaften, Lehrstuhl für Botanik I, Würzburg, Germany.
K J Dietz
Leibniz Association · DEUniversity of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Higher plants express genes encoding peroxiredoxins of the two-cysteine type. This is concluded from the isolation of cDNAs from spinach (Spinacia oleracea) and barley (Hordeum vulgare cv. Gerbel) which are homologous to animal, fungal, and bacterial two-cysteine peroxiredoxins. Northern blot analysis indicated the presence of at least one corresponding gene in all angiosperms analyzed suggesting that bas1 is a member of an ubiquitous gene family encoding a protein of fundamental importance in oxidative stress defense also in plants. In barley, expression increased upon application of methyl viologen but was not affected by ozone. mRNA levels increased during deetiolation in the light. Maximal abundance of bas1 transcripts was observed in young developing shoot segments where cell division and elongation take place. Expression was insignificant in roots. The amount of bas1 protein was high in the leaf blade, particularly in etiolated plants, and did not respond to oxidative stress. bas1 protein was not detected in roots. From our data, we suggest that bas1 is an antioxidant enzyme particularly important in the developing shoot and photosynthesizing leaf.

Indexed as

Gene Expression Regulation, DevelopmentalGene Expression Regulation, PlantMultigene FamilyPeroxidasesTranscription, GeneticAmino Acid SequenceAnimalsAntibodiesBase SequenceCloning, MolecularFungiGene Expression Regulation, EnzymologicHordeumMolecular Sequence DataOxidative StressOxidoreductasesAntibodiesOxidoreductasesOzoneParaquatPeptide FragmentsPeroxidasesPeroxiredoxinsThioredoxins

Identifiers

PMID8790288
OpenAlexW2087895332

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.