Evidence map›Paper›PMID 19197237›Full record

ArticleThe EMBO journal2009

Structural basis for competitive interactions of Pex14 with the import receptors Pex5 and Pex19.

Christian Neufeld, Fabian V Filipp, Bernd Simon, Alexander Neuhaus, Nicole Schüller, Christine David, Hamed Kooshapur, Tobias Madl, Ralf Erdmann, Wolfgang Schliebs and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

35 citing papers in PubMed, 88 citations in OpenAlex.

  1. Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026
    Review
  2. Dibenzo[International journal of molecular sciences · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Membrane Interactions of the Peroxisomal Proteins PEX5 and PEX14.Frontiers in cell and developmental biology · 2021
    Article
  12. Article
  13. Anaerobic peroxisomes inProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Peroxisome protein import recapitulated inThe Journal of cell biology · 2019
    Article
  15. Review
  16. Article
  17. Article
  18. 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

12 authors at 4 institutions in 1 country.

Christian NeufeldEMBL Heidelberg, Heidelberg, Germany.
Fabian V Filipp
Bernd Simon
Alexander Neuhaus
Nicole Schüller
Christine David
Hamed Kooshapur
Tobias Madl
Ralf Erdmann
Wolfgang Schliebs
Matthias Wilmanns
Michael Sattler
Ruhr University Bochum · DEEuropean Molecular Biology Laboratory · DETechnical University of Munich · DEHelmholtz Zentrum München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein import into peroxisomes depends on a complex and dynamic network of protein-protein interactions. Pex14 is a central component of the peroxisomal import machinery and binds the soluble receptors Pex5 and Pex19, which have important function in the assembly of peroxisome matrix and membrane, respectively. We show that the N-terminal domain of Pex14, Pex14(N), adopts a three-helical fold. Pex5 and Pex19 ligand helices bind competitively to the same surface in Pex14(N) albeit with opposite directionality. The molecular recognition involves conserved aromatic side chains in the Pex5 WxxxF/Y motif and a newly identified F/YFxxxF sequence in Pex19. The Pex14-Pex5 complex structure reveals molecular details for a critical interaction in docking Pex5 to the peroxisomal membrane. We show that mutations of Pex14 residues located in the Pex5/Pex19 binding region disrupt Pex5 and/or Pex19 binding in vitro. The corresponding full-length Pex14 variants are impaired in peroxisomal membrane localisation in vivo, showing that the molecular interactions mediated by the N-terminal domain modulate peroxisomal targeting of Pex14.

Indexed as

Binding, CompetitiveAmino Acid SequenceBinding SitesCell LineDNA Mutational AnalysisHumansMagnetic Resonance SpectroscopyMembrane ProteinsModels, MolecularMolecular Sequence DataMutationPeptidesPeroxisome-Targeting Signal 1 ReceptorProtein BindingProtein Structure, SecondaryProtein TransportMembrane ProteinsPeptidesPeroxisome-Targeting Signal 1 ReceptorPEX14 protein, humanPEX19 protein, humanPEX5 protein, humanReceptors, Cytoplasmic and NuclearRepressor ProteinsSolutions

Identifiers

PMID19197237
PMCPMC2666029
OpenAlexW1968846419

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.