Evidence map›Paper›PMID 14668492›Full record

ArticleMolecular biology of the cell2004

Reconstituted TOM core complex and Tim9/Tim10 complex of mitochondria are sufficient for translocation of the ADP/ATP carrier across membranes.

Andreja Vasiljev, Uwe Ahting, Frank E Nargang, Nancy E Go, Shukry J Habib, Christian Kozany, Valérie Panneels, Irmgard Sinning, Holger Prokisch, Walter Neupert and 2 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 77 citations in OpenAlex.

  1. From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026
    Review
  2. Review
  3. Altered Mitochondrial Protein Homeostasis and Proteinopathies.Frontiers in molecular neuroscience · 2022
    Review
  4. Review
  5. Review
  6. Folding and biogenesis of mitochondrial small Tim proteins.International journal of molecular sciences · 2013
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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

12 authors at 2 institutions in 2 countries.

Andreja VasiljevInstitut für Physiologische Chemie der Universität München, D-81377 Munich, Germany.
Uwe Ahting
Frank E Nargang
Nancy E Go
Shukry J Habib
Christian Kozany
Valérie Panneels
Irmgard Sinning
Holger Prokisch
Walter Neupert
Stephan Nussberger
Doron Rapaport
Ludwig-Maximilians-Universität München · DEUniversity of Alberta · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Precursor proteins of the solute carrier family and of channel forming Tim components are imported into mitochondria in two main steps. First, they are translocated through the TOM complex in the outer membrane, a process assisted by the Tim9/Tim10 complex. They are passed on to the TIM22 complex, which facilitates their insertion into the inner membrane. In the present study, we have analyzed the function of the Tim9/Tim10 complex in the translocation of substrates across the outer membrane of mitochondria. The purified TOM core complex was reconstituted into lipid vesicles in which purified Tim9/Tim10 complex was entrapped. The precursor of the ADP/ATP carrier (AAC) was found to be translocated across the membrane of such lipid vesicles. Thus, these components are sufficient for translocation of AAC precursor across the outer membrane. Peptide libraries covering various substrate proteins were used to identify segments that are bound by Tim9/Tim10 complex upon translocation through the TOM complex. The patterns of binding sites on the substrate proteins suggest a mechanism by which portions of membrane-spanning segments together with flanking hydrophilic segments are recognized and bound by the Tim9/Tim10 complex as they emerge from the TOM complex into the intermembrane space.

Indexed as

Amino Acid SequenceBinding SitesCarrier ProteinsCell MembraneLiposomesMembrane ProteinsMembrane Transport ProteinsMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMolecular Sequence DataNeurospora crassaPeptidesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCarrier ProteinsLiposomesMembrane ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsPeptidesSaccharomyces cerevisiae ProteinsTIM10 protein, S cerevisiaeTIM22 protein, S cerevisiaeTim9 protein, S cerevisiae

Identifiers

PMID14668492
PMCPMC363167
OpenAlexW2143315027

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.