Evidence map›Paper›PMID 11706208›Full record

ArticlePlant physiology2001

Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor.

N Rouhier, E Gelhaye, P E Sautiere, A Brun, P Laurent, D Tagu, J Gerard, E de Faÿ, Y Meyer, J P Jacquot

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

63 citing papers in PubMed, 220 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Function and Regulation of Chloroplast Peroxiredoxin IIE.Antioxidants (Basel, Switzerland) · 2021
    Article
  6. Frontiers in plant science · 2021
    Article
  7. Article
  8. Overexpression of a CPYC-Type Glutaredoxin,Frontiers in plant science · 2019
    Article
  9. Peroxiredoxins and Redox Signaling in Plants.Antioxidants & redox signaling · 2018
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

3 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

10 authors at 3 institutions in 1 country.

N RouhierUnité Mixte de Recherche Interaction Arbres Microorganisms, Institut National de la Recherche Agronomique-Université Henri Poincaré Nancy I. Biochimie et Biologie Moléculaire Végétales, Université Henri Poincaré, 54506 Vandoeuvre cedex, France.
E Gelhaye
P E Sautiere
A Brun
P Laurent
D Tagu
J Gerard
E de Faÿ
Y Meyer
J P Jacquot
Université de Lorraine · FRUniversité de Lille · FRUniversité de Perpignan · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A sequence coding for a peroxiredoxin (Prx) was isolated from a xylem/phloem cDNA library from Populus trichocarpa and subsequently inserted into an expression plasmid yielding the construction pET-Prx. The recombinant protein was produced in Escherichia coli cells and purified to homogeneity with a high yield. The poplar Prx is composed of 162 residues, a property that makes it the shortest plant Prx sequence isolated so far. It was shown that the protein is monomeric and possesses two conserved cysteines (Cys). The Prx degrades hydrogen peroxide and alkyl hydroperoxides in the presence of an exogenous proton donor that can be either thioredoxin or glutaredoxin (Grx). Based on this finding, we propose that the poplar protein represents a new type of Prx that differs from the so-called 2-Cys and 1-Cys Prx, a suggestion supported by the existence of natural fusion sequences constituted of a Prx motif coupled to a Grx motif. The protein was shown to be highly expressed in sieve tubes where thioredoxin h and Grx are also major proteins.

Indexed as

OxidoreductasesAmino Acid SequenceBiological Transport, ActiveCloning, MolecularEscherichia coliGene Expression Regulation, PlantGlutaredoxinsMolecular Sequence DataOxidation-ReductionPeroxidasePeroxidasesPeroxiredoxinsPlant StemsProteinsProtonsSalicaceaeGlutaredoxinsOxidoreductasesPeroxidasePeroxidasesPeroxiredoxinsProteinsProtonsSulfhydryl CompoundsThioredoxins

Identifiers

PMID11706208
PMCPMC129297
OpenAlexW2118940991

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.