Evidence map›Paper›PMID 11717467›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Identification and characterization of a mitochondrial thioredoxin system in plants.

C Laloi, N Rayapuram, Y Chartier, J M Grienenberger, G Bonnard, Y Meyer

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

74 citing papers in PubMed, 266 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. ThioredoxinAntioxidants (Basel, Switzerland) · 2021
    Article
  12. Overexpression ofInternational journal of molecular sciences · 2020
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. MitochondrialAntioxidants (Basel, Switzerland) · 2018
    Article
  20. Article

14 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

6 authors at 3 institutions in 1 country.

C LaloiLaboratoire Génome et Développement des Plantes, Unité Mixte de Recherche Centre National de la Recherche Scientifique 5096, Université de Perpignan, 52 Avenue de Villeneuve, F-66860 Perpignan, France.
N Rayapuram
Y Chartier
J M Grienenberger
G Bonnard
Y Meyer
Université de Perpignan · FRCentre National de la Recherche Scientifique · FRLaboratoire Génome et Développement des Plantes · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants possess two well described thioredoxin systems: a cytoplasmic system including several thioredoxins and an NADPH-dependent thioredoxin reductase and a specific chloroplastic system characterized by a ferredoxin-dependent thioredoxin reductase. On the basis of biochemical activities, plants also are supposed to have a mitochondrial thioredoxin system as described in yeast and mammals, but no gene encoding plant mitochondrial thioredoxin or thioredoxin reductase has been identified yet. We report the characterization of a plant thioredoxin system located in mitochondria. Arabidopsis thaliana genome sequencing has revealed numerous thioredoxin genes among which we have identified AtTRX-o1, a gene encoding a thioredoxin with a potential mitochondrial transit peptide. AtTRX-o1 and a second gene, AtTRX-o2, define, on the basis of the sequence and intron positions, a new thioredoxin type up to now specific to plants. We also have characterized AtNTRA, a gene encoding a protein highly similar to the previously described cytosolic NADPH-dependent thioredoxin reductase AtNTRB but with a putative presequence for import into mitochondria. Western blot analysis of A. thaliana subcellular and submitochondrial fractions and in vitro import experiments show that AtTRX-o1 and AtNTRA are targeted to the mitochondrial matrix through their cleavable N-terminal signal. The two proteins truncated to the estimated mature forms were produced in Escherichia coli; AtTRX-o1 efficiently reduces insulin in the presence of DTT and is reduced efficiently by AtNTRA and NADPH. Therefore, the thioredoxin and the NADPH-dependent thioredoxin reductase described here are proposed to constitute a functional plant mitochondrial thioredoxin system.

Indexed as

Arabidopsis ProteinsAmino Acid SequenceArabidopsisBase SequenceBiological TransportDNA, PlantEnzyme ActivationEnzyme PrecursorsGenes, PlantMitochondriaMolecular Sequence DataPeptidesPlant ProteinsProtein PrecursorsSubcellular FractionsThioredoxin-Disulfide ReductaseArabidopsis ProteinsATO2 protein, ArabidopsisATTRX1 protein, ArabidopsisDNA, PlantEnzyme PrecursorsPeptidesPlant ProteinsProtein PrecursorsThioredoxin-Disulfide ReductaseThioredoxin hThioredoxins

Identifiers

PMID11717467
PMCPMC61182
OpenAlexW2037212449

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.