Evidence map›Paper›PMID 12426385›Full record

ArticleThe EMBO journal2002

Protein import into chloroplasts involves redox-regulated proteins.

Michael Küchler, Susanne Decker, Friederike Hörmann, Jürgen Soll, Lisa Heins

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.8field-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

44 citing papers in PubMed, 187 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. An evergreen mind and a heart for the colors of fall.Journal of experimental botany · 2021
    Article
  6. Coexpressed subunits of dual genetic origin define a conserved supercomplex mediating essential protein import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. 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

5 authors at 1 institution in 1 country.

Michael KüchlerBotanisches Institut, Department Biologie I, Universität München, Menziger Strasse 67, D-80638 München, Germany.
Susanne Decker
Friederike Hörmann
Jürgen Soll
Lisa Heins
Ludwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pre-protein translocation into chloroplasts is accomplished by two distinct translocation machineries in the outer and inner envelope, respectively. We have isolated the translocon at the inner envelope membrane (Tic complex) by blue-native PAGE and describe a new Tic subunit, Tic62. Tic62, together with Tic110 and Tic55, forms a core translocation unit. The N-terminus of Tic62 shows strong homologies to NAD(H) dehydrogenases in eukaryotes and to Ycf39-like proteins present in cyanobacteria and non-green algae. The stromal-facing C-terminus of Tic62 contains a novel, repetitive module that interacts with a ferredoxin-NAD(P)(+) oxidoreductase. Ferredoxin-NAD(P)(+) oxidoreductase catalyses the final electron transfer of oxygenic photosynthesis from ferredoxin to NAD(P). Substrates that interfere with either NAD binding, such as deamino-NAD, or influence the ratio of NAD(P)/NAD(P)H, such as ruthenium hexamine trichloride, modulate the import characteristics of leaf-specific ferredoxin-NAD(P)(+) oxidoreductase isologues differently. We conclude that the Tic complex can regulate protein import into chloroplasts by sensing and reacting to the redox state of the organelle.

Indexed as

Amino Acid SequenceCarrier ProteinsChloroplastsEscherichia coli ProteinsIntracellular MembranesIron-Sulfur ProteinsMacromolecular SubstancesMolecular Sequence DataNADOxidation-ReductionPisum sativumPlant ProteinsProtein TransportRuthenium CompoundsSequence AlignmentSequence Homology, Amino AcidCarrier ProteinsEscherichia coli ProteinsFNR protein, E colihexamminerutheniumIron-Sulfur ProteinsMacromolecular SubstancesNADnicotinamide-hypoxanthine dinucleotidePlant ProteinsRuthenium Compounds

Identifiers

PMID12426385
PMCPMC137210
OpenAlexW1972499484

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.