Evidence map›Paper›PMID 26644511›Full record

ArticleThe Journal of cell biology2015

Yeast pex1 cells contain peroxisomal ghosts that import matrix proteins upon reintroduction of Pex1.

Kèvin Knoops, Rinse de Boer, Anita Kram, Ida J van der Klei

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. PEX1The Journal of biological chemistry · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Structural Mapping of Missense Mutations in the Pex1/Pex6 Complex.International journal of molecular sciences · 2019
    Review
  8. Lipid Droplet and Peroxisome Biogenesis: Do They Go Hand-in-Hand?Frontiers in cell and developmental biology · 2019
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
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

4 authors at 1 institution in 1 country.

Kèvin KnoopsMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, Netherlands.
Rinse de BoerMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, Netherlands.
Anita KramMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, Netherlands.
Ida J van der KleiMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, Netherlands i.j.van.der.klei@rug.nl.
University of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pex1 and Pex6 are two AAA-ATPases that play a crucial role in peroxisome biogenesis. We have characterized the ultrastructure of the Saccharomyces cerevisiae peroxisome-deficient mutants pex1 and pex6 by various high-resolution electron microscopy techniques. We observed that the cells contained peroxisomal membrane remnants, which in ultrathin cross sections generally appeared as double membrane rings. Electron tomography revealed that these structures consisted of one continuous membrane, representing an empty, flattened vesicle, which folds into a cup shape. Immunocytochemistry revealed that these structures lack peroxisomal matrix proteins but are the sole sites of the major peroxisomal membrane proteins Pex2, Pex10, Pex11, Pex13, and Pex14. Upon reintroduction of Pex1 in Pex1-deficient cells, these peroxisomal membrane remnants (ghosts) rapidly incorporated peroxisomal matrix proteins and developed into peroxisomes. Our data support earlier views that Pex1 and Pex6 play a role in peroxisomal matrix protein import.

Indexed as

Adenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesDNA, FungalElectron Microscope TomographyImmunohistochemistryLightMembrane ProteinsMembrane Transport ProteinsMicroscopy, ElectronMutationPeroxinsPeroxisomesProtein TransportRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesDNA, FungalMembrane ProteinsMembrane Transport ProteinsPeroxinsPEX11 protein, S cerevisiaePEX14 protein, S cerevisiaePEX1 protein, S cerevisiaePEX6 protein, S cerevisiaeRepressor ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID26644511
PMCPMC4674281
OpenAlexW2194898862

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.