Evidence map›Paper›PMID 12032074›Full record

ArticleThe EMBO journal2002

The preprotein conducting channel at the inner envelope membrane of plastids.

Lisa Heins, Alexander Mehrle, Roland Hemmler, Richard Wagner, Michael Küchler, Friederike Hörmann, Dmitry Sveshnikov, Jürgen Soll

Open access · bronzeAbstract read
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 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 156 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. 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
  8. Article
  9. New Insights Into Sunflower (Frontiers in plant science · 2018
    Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Structural characterizations of the chloroplast translocon protein Tic110.The Plant journal : for cell and molecular biology · 2013
    Article
  18. Evidence for glycoprotein transport into complex plastids.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Article
  20. Article
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 1 institution in 2 countries.

Lisa HeinsBotanisches Institut, Universität Kiel, Am Botanischen Garten 1-9, D-24118 Kiel, Germany.
Alexander Mehrle
Roland Hemmler
Richard Wagner
Michael Küchler
Friederike Hörmann
Dmitry Sveshnikov
Jürgen Soll
Institute of Botany · AZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The preprotein translocation at the inner envelope membrane of chloroplasts so far involves five proteins: Tic110, Tic55, Tic40, Tic22 and Tic20. The molecular function of these proteins has not yet been established. Here, we demonstrate that Tic110 constitutes a central part of the preprotein translocation pore. Dependent on the presence of intact Tic110, radiolabelled preprotein specifically interacts with isolated inner envelope vesicles as well as with purified, recombinant Tic110 reconstituted into liposomes. Circular dichroism analysis reveals that Tic110 consists mainly of beta-sheets, a structure typically found in pore proteins. In planar lipid bilayers, recombinant Tic110 forms a cation-selective high-conductance channel with a calculated inner pore opening of 1.7 nm. Purified transit peptide causes strong flickering and a voltage-dependent block of the channel. Moreover, at the inner envelope membrane, a peptide-sensitive channel is described that shows properties basically identical to the channel formed by recombinant Tic110. We conclude that Tic110 has a distinct preprotein binding site and functions as a preprotein translocation pore at the inner envelope membrane.

Indexed as

ChloroplastsCircular DichroismLiposomesMembrane ProteinsModels, BiologicalMutationPeptidesPisum sativumPlastidsProtein BindingProtein Structure, TertiaryRecombinant ProteinsTime FactorsLiposomesMembrane ProteinsPeptidesRecombinant Proteins

Identifiers

PMID12032074
PMCPMC126020
OpenAlexW2018329098

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.