Evidence map›Paper›PMID 23403928›Full record

ArticleThe EMBO journal2013

Signal recognition initiates reorganization of the presequence translocase during protein import.

Oleksandr Lytovchenko, Jonathan Melin, Christian Schulz, Markus Kilisch, Dana P Hutu, Peter Rehling

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.3field-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

27 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Crosstalk between Mitochondrial Protein Import and Lipids.International journal of molecular sciences · 2022
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Transport of Proteins into Mitochondria.The protein journal · 2019
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  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

6 authors at 3 institutions in 1 country.

Oleksandr LytovchenkoDepartment of Biochemistry II, University of Göttingen, Göttingen, Germany.
Jonathan Melin
Christian Schulz
Markus Kilisch
Dana P Hutu
Peter Rehling
University of Göttingen · DEMax Planck Institute for Biophysical Chemistry · DEUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial presequence translocase interacts with presequence-containing precursors at the intermembrane space (IMS) side of the inner membrane to mediate their translocation into the matrix. Little is known as too how these matrix-targeting signals activate the translocase in order to initiate precursor transport. Therefore, we analysed how signal recognition by the presequence translocase initiates reorganization among Tim-proteins during import. Our analyses revealed that the presequence receptor Tim50 interacts with Tim21 in a signal-sensitive manner in a process that involves the IMS-domain of the Tim23 channel. The signal-driven release of Tim21 from Tim50 promotes recruitment of Pam17 and thus triggers formation of the motor-associated form of the TIM23 complex required for matrix transport.

Indexed as

Protein TransportBinding SitesCarrier ProteinsMembrane ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsModels, MolecularProtein BindingProtein Interaction Domains and MotifsProtein Sorting SignalsProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityCarrier ProteinsMembrane ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsPam17 protein, S cerevisiaeProtein Sorting SignalsSaccharomyces cerevisiae ProteinsTim21 protein, S cerevisiaeTIM23 protein, S cerevisiaeTIM50 protein, S cerevisiae

Identifiers

PMID23403928
PMCPMC3604718
OpenAlexW2117380620

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.