Evidence map›Paper›PMID 14709540›Full record

ArticleThe Journal of cell biology2004

PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins.

Jacob M Jones, James C Morrell, Stephen J Gould

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

120 citing papers in PubMed, 248 citations in OpenAlex.

  1. Article
  2. Chaperone-mediated remodelling of mutant huntingtin.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Evolutionary remodeling of a remnant GET pathway factor into PEX38, an essential peroxin.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
  8. Review
  9. Aging impairs peroxisome biogenesis in human B cells.The journals of gerontology. Series A, Biological sciences and medical sciences · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Mammalian pexophagy at a glance.Journal of cell science · 2024
    Review
  18. Article
  19. Article
  20. Article

60 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 2 institutions in 1 country.

Jacob M JonesDept. of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
James C Morrell
Stephen J Gould
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

Peroxisome Membrane BiogenesisR01DK059479 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI GOULD, STEPHEN J · 2001 to 2004
$1.4M
NIDDK NIH HHS DK 59479NIDDK NIH HHS R01 DK059479
6 · The paper itself

Abstract

Integral peroxisomal membrane proteins (PMPs) are synthesized in the cytoplasm and imported posttranslationally. Here, we demonstrate that PEX19 binds and stabilizes newly synthesized PMPs in the cytosol, binds to multiple PMP targeting signals (mPTSs), interacts with the hydrophobic domains of PMP targeting signals, and is essential for PMP targeting and import. These results show that PEX19 functions as both a chaperone and an import receptor for newly synthesized PMPs. We also demonstrate the existence of two PMP import mechanisms and two classes of mPTSs: class 1 mPTSs, which are bound by PEX19 and imported in a PEX19-dependent manner, and class 2 mPTSs, which are not bound by PEX19 and mediate protein import independently of PEX19.

Indexed as

Cell LineCytosolHumansIntracellular MembranesMembrane ProteinsMembrane Transport ProteinsMolecular ChaperonesPeroxisomesProtein BindingProtein Structure, TertiaryProtein TransportRNA InterferenceSignal TransductionMembrane ProteinsMembrane Transport ProteinsMolecular ChaperonesPEX19 protein, human

Identifiers

PMID14709540
PMCPMC2171958
OpenAlexW2063896117

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.