Evidence map›Paper›PMID 12124272›Full record

ArticleBiophysical journal2002

The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides.

Silke C Hinnah, Richard Wagner, Natalia Sveshnikova, Roswitha Harrer, Jürgen Soll

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.0field-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

67 citing papers in PubMed, 202 citations in OpenAlex.

  1. The Name Is Barrel, β-Barrel.Methods in molecular biology (Clifton, N.J.) · 2024
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  10. 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
  11. Review
  12. A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Review
  20. Article

7 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

5 authors at 3 institutions in 1 country.

Silke C HinnahFachbereich Biologie/Chemie, Universität Osnabrück, D-49034 Osnabrück, Germany.
Richard Wagner
Natalia Sveshnikova
Roswitha Harrer
Jürgen Soll
Kiel University · DEOsnabrück University · DEMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The channel properties of Toc75 (the protein import pore of the outer chloroplastic membrane) were further characterized by electrophysiological measurements in planar lipid bilayers. After improvement of the Toc75 reconstitution procedure the voltage dependence of the channel open probability resembled those observed for other beta-barrel pores. Studies concerning the pore size of the reconstituted Toc75 indicate the presence of a narrow restriction zone corresponding to the selectivity filter and a wider pore vestibule with diameters of approximately 14 A and 26 A, respectively. Interactions between Toc75 and different peptides (a genuine chloroplastic transit peptide, a synthetic peptide resembling a transit peptide, and a mitochondrial presequence) show that Toc75 itself is able to differentiate between these peptides and the recognition is based on both conformational and electrostatic interactions.

Indexed as

Plant ProteinsAmino Acid SequenceBiophysical PhenomenaBiophysicsChloroplastsElectrophysiologyHydrogen-Ion ConcentrationLipid BilayersMembrane ProteinsMolecular Sequence DataOctoxynolPeptidesPolyethylene GlycolsProtein BindingProtein ConformationProtein FoldingLipid BilayersMembrane ProteinsOctoxynolOEP75 protein precursor, plantPeptidesPlant ProteinsPolyethylene GlycolsProtein PrecursorsWater

Identifiers

PMID12124272
PMCPMC1302194
OpenAlexW2070343649

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.