Evidence map›Paper›PMID 18349143›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Three thioredoxin targets in the inner envelope membrane of chloroplasts function in protein import and chlorophyll metabolism.

Sandra Bartsch, Julie Monnet, Kristina Selbach, Françoise Quigley, John Gray, Diter von Wettstein, Steffen Reinbothe, Christiane Reinbothe

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

23 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
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  8. Article
  9. A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019
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  11. Review
  12. Article
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  15. Thioredoxin-dependent regulatory networks in chloroplasts under fluctuating light conditions.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    Review
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  18. Article
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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

8 authors at 5 institutions in 3 countries.

Sandra BartschLehrstuhl für Pflanzenphysiologie, Universität Bayreuth, Universitätsstrasse 30, D-95447 Bayreuth, Germany.
Julie Monnet
Kristina Selbach
Françoise Quigley
John Gray
Diter von Wettstein
Steffen Reinbothe
Christiane Reinbothe
Centre de Recherches sur les Macromolécules Végétales · FRUniversity of Bayreuth · DECentre National de la Recherche Scientifique · FRUniversity of Toledo · USWashington State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thioredoxins (Trxs) are ubiquitous small proteins with a redox-active disulfide bridge. In their reduced form, they constitute very efficient protein disulfide oxidoreductases. In chloroplasts, two types of Trxs (f and m) coexist and play central roles in the regulation of the Calvin cycle and other processes. Here, we identified a class of Trx targets in the inner plastid envelope membrane of chloroplasts that share a CxxC motif approximately 73 aa from their carboxyl-terminal end. Members of this group belong to a superfamily of Rieske iron-sulfur proteins involved in protein translocation and chlorophyll metabolism. These proteins include the protein translocon protein TIC55, the precursor NADPH:protochlorophyllide oxidoreductase translocon protein PTC52, which operates as protochlorophyllide a-oxygenase, and the lethal leaf spot protein LLS1, which is identical with pheophorbide a oxygenase. The role of these proteins in dark/light regulation and oxidative control by the Trx system is discussed.

Indexed as

Amino Acid SequenceChlorophyllChloroplastsChromatography, AffinityDarknessHordeumIntracellular MembranesMolecular Sequence DataOxidation-ReductionPlant ProteinsProtein BindingProtein TransportThioredoxinsChlorophyllPlant ProteinsThioredoxins

Identifiers

PMID18349143
PMCPMC2290756
OpenAlexW2021470528

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.