Evidence map›Paper›PMID 11230119›Full record

ArticleThe EMBO journal2001

The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria.

N Wiedemann, N Pfanner, M T Ryan

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

86 citing papers in PubMed, 251 citations in OpenAlex.

  1. Article
  2. Article
  3. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
    Review
  4. From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026
    Review
  5. Functions of J-domain proteins in mitochondrial protein biogenesis.Protein science : a publication of the Protein Society · 2026
    Review
  6. Article
  7. A dynamic displacement mechanism drives protein import into mitochondria.bioRxiv : the preprint server for biology · 2026
    Article
  8. Review
  9. Mitochondrial protein import stress.Nature cell biology · 2025
    Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Sensing, signaling and surviving mitochondrial stress.Cellular and molecular life sciences : CMLS · 2021
    Review
  17. Article
  18. Review
  19. Review
  20. Article

26 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

3 authors at 1 institution in 1 country.

N WiedemannInstitut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Strasse 7, D-79104 Freiburg, Germany.
N Pfanner
M T Ryan
University of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ADP/ATP carrier (AAC) is a major representative of mitochondrial preproteins lacking an N-terminal presequence. AAC contains targeting information in each of its three modules, which has led to a search for the dominant targeting region. An alternative, not yet tested model would be that several distinct targeting signals function simultaneously in import of the preprotein. We report that the three AAC modules cooperate in binding to the receptor Tom70 such that three Tom70 dimers are recruited to one preprotein. The modules are transferred to the import pore in a stepwise manner and cooperate again in the accumulation of AAC in the general import pore complex. AAC can cross the outer membrane with an internal segment first, i.e. in a loop formation. Each module of AAC is required for dimerization in the inner membrane. We propose a new concept for import of the hydrophobic carrier proteins into mitochondria where multiple signals cooperate in receptor recruitment, outer membrane translocation via loop formation and assembly in the inner membrane.

Indexed as

Saccharomyces cerevisiae ProteinsAdenosine TriphosphateCross-Linking ReagentsDimerizationFungal ProteinsIntracellular MembranesMembrane ProteinsMethotrexateMitochondriaMitochondrial ADP, ATP TranslocasesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsProtein BindingProtein PrecursorsProtein Structure, TertiaryProtein TransportAdenosine TriphosphateCross-Linking ReagentsFungal ProteinsMembrane ProteinsMethotrexateMitochondrial ADP, ATP TranslocasesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex Proteinsm-maleimidobenzoyl-N-hydroxysulfosuccinimide esterProtein PrecursorsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSuccinimidesTetrahydrofolate DehydrogenaseTOM70 protein, S cerevisiae

Identifiers

PMID11230119
PMCPMC145466
OpenAlexW2171380662

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.