Evidence map›Paper›PMID 11553771›Full record

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

Comprehensive survey of proteins targeted by chloroplast thioredoxin.

K Motohashi, A Kondoh, M T Stumpp, T Hisabori

Open access · greenAbstract 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 135 papers.

0numbers the graph read from it
0cells of the map it votes in
135citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

135 citing papers in PubMed, 381 citations in OpenAlex.

  1. Article
  2. Emerging roles of glutaredoxins in plant metabolism.Journal of experimental botany · 2026
    Review
  3. The Wheat NucleoredoxinPlants (Basel, Switzerland) · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. NewAntioxidants (Basel, Switzerland) · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. 12-Frontiers in plant science · 2021
    Review
  17. Article
  18. Article
  19. Article
  20. Article

75 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

4 authors at 1 institution in 1 country.

K MotohashiChemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Midori-ku, Yokohama 226-8503, Japan.
A Kondoh
M T Stumpp
T Hisabori
Tokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Possible target proteins of chloroplast thioredoxin (Trx) have been investigated in the stroma lysate of spinach chloroplasts. For that purpose, we immobilized a mutant of m-type Trx in which an internal cysteine at the active site was substituted with serine, on cyanogen bromide-activated resin. By using this resin, the target proteins in chloroplast were efficiently acquired when they formed the mixed-disulfide intermediates with the immobilized Trxs. We could acquire Rubisco activase (45 kDa) and 2-Cys-type peroxiredoxin (Prx), which were recently identified as targets of chloroplast Trxs. Glyceraldehyde-3-phosphate dehydrogenase and sedoheputulose 1,7-bisphosphatase, well-known thiol enzymes in the Calvin cycle, also were recognized among the collected proteins, suggesting the method is applicable for our purpose. Furthermore, four proteins were identified from a homology search of the NH(2)-terminal sequence of the acquired proteins: glutamine synthetase, a protein homologous to chloroplast cyclophilin, a homolog of Prx-Q, and the Rubisco small subunit. The Trx susceptibilities of the recombinant cyclophilin and Prx-Q of Arabidopsis thaliana were then examined. The method developed in the present study is thus applicable to investigate the various redox networks via Trxs and the related enzymes in the cell.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionArabidopsisBinding SitesChloroplastsCloning, MolecularCyclophilinsCysteineDisulfidesGlutamate-Ammonia LigaseGlyceraldehyde-3-Phosphate DehydrogenasesKineticsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPeroxidasesCyclophilinsCysteineDisulfidesGlutamate-Ammonia LigaseGlyceraldehyde-3-Phosphate DehydrogenasesPeroxidasesPeroxiredoxinsPhosphoric Monoester HydrolasesPlant ProteinsProtein Subunitsrca protein, plantRecombinant ProteinsResins, PlantRibulose-Bisphosphate Carboxylasesedoheptulose-bisphosphataseSerineThioredoxins

Identifiers

PMID11553771
PMCPMC58711
OpenAlexW2142709713

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.