Evidence map›Paper›PMID 16481623›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

A complete ferredoxin/thioredoxin system regulates fundamental processes in amyloplasts.

Yves Balmer, William H Vensel, Nick Cai, Wanda Manieri, Peter Schürmann, William J Hurkman, Bob B Buchanan

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
8.0field-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

71 citing papers in PubMed, 176 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. NewAntioxidants (Basel, Switzerland) · 2022
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Proteomic Analyses of ThioredoxinsAntioxidants (Basel, Switzerland) · 2019
    Article
  15. Plant Immune Responses to Parasitic Nematodes.Frontiers in plant science · 2019
    Review
  16. Article
  17. Article
  18. Starch Trek: The Search for Yield.Frontiers in plant science · 2018
    Review
  19. Article
  20. Article

11 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

7 authors at 3 institutions in 2 countries.

Yves BalmerDepartment of Plant and Biology, University of California, 111 Koshland Hall, Berkeley, CA 94720, USA.
William H Vensel
Nick Cai
Wanda Manieri
Peter Schürmann
William J Hurkman
Bob B Buchanan
University of California, Berkeley · USUniversity of Neuchâtel · CHWestern Regional Research Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A growing number of processes throughout biology are regulated by redox via thiol-disulfide exchange. This mechanism is particularly widespread in plants, where almost 200 proteins have been linked to thioredoxin (Trx), a widely distributed small regulatory disulfide protein. The current study extends regulation by Trx to amyloplasts, organelles prevalent in heterotrophic plant tissues that, among other biosynthetic activities, catalyze the synthesis and storage of copious amounts of starch. Using proteomics and immunological methods, we identified the components of the ferredoxin/Trx system (ferredoxin, ferredoxin-Trx reductase, and Trx), originally described for chloroplasts, in amyloplasts isolated from wheat starchy endosperm. Ferredoxin is reduced not by light, as in chloroplasts, but by metabolically generated NADPH via ferredoxin-NADP reductase. However, once reduced, ferredoxin appears to act as established for chloroplasts, i.e., via ferredoxin-Trx reductase and a Trx (m-type). A proteomics approach in combination with affinity chromatography and a fluorescent thiol probe led to the identification of 42 potential Trx target proteins, 13 not previously recognized, including a major membrane transporter (Brittle-1 or ADP-glucose transporter). The proteins function in a range of processes in addition to starch metabolism: biosynthesis of lipids, amino acids, and nucleotides; protein folding; and several miscellaneous reactions. The results suggest a mechanism whereby light is initially recognized as a thiol signal in chloroplasts, then as a sugar during transit to the sink, where it is converted again to a thiol signal. In this way, amyloplast reactions in the grain can be coordinated with photosynthesis taking place in leaves.

Indexed as

Amino AcidsFerredoxinsIron-Sulfur ProteinsLipidsNucleotidesOxidoreductasesPhotosynthesisPlant ProteinsPlastidsProtein FoldingProteomicsSeedsStarchThioredoxinsTriticumAmino AcidsFerredoxinsferredoxin-thioredoxin reductaseIron-Sulfur ProteinsLipidsNucleotidesOxidoreductasesPlant ProteinsStarchThioredoxins

Identifiers

PMID16481623
PMCPMC1413819
OpenAlexW2109046892

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.