Evidence map›Paper›PMID 10704444›Full record

ArticleThe Journal of cell biology2000

PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis.

K A Sacksteder, J M Jones, S T South, X Li, Y Liu, S J Gould

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. 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
7.8field-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

120 citing papers in PubMed, 315 citations in OpenAlex.

  1. Article
  2. Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. 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
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Allelopathy and underlying mechanism of mango (Frontiers in plant science · 2024
    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

6 authors at 2 institutions in 1 country.

K A SackstederDepartment of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
J M Jones
S T South
X Li
Y Liu
S J Gould
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

VERY LONG CHAIN FATTY ACYL-COA SYNTHETASE IN ADRENOLEUKODYSTROPHYP01HD010981 · NICHD · KENNEDY KRIEGER CHILDRENS HOSPITAL · PI SMITH, KIRBY D · 1985 to 2006
$11.5M
MOLECULAR ANALYSIS OF PEROXISOME ASSEMBLYR01DK045787 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI GOULD, STEPHEN J · 1993 to 2011
$4.7M
NICHD NIH HHS HD10981NICHD NIH HHS P01 HD010981NIDDK NIH HHS DK45787NIDDK NIH HHS R01 DK045787
6 · The paper itself

Abstract

Peroxisomes are components of virtually all eukaryotic cells. While much is known about peroxisomal matrix protein import, our understanding of how peroxisomal membrane proteins (PMPs) are targeted and inserted into the peroxisome membrane is extremely limited. Here, we show that PEX19 binds a broad spectrum of PMPs, displays saturable PMP binding, and interacts with regions of PMPs required for their targeting to peroxisomes. Furthermore, mislocalization of PEX19 to the nucleus leads to nuclear accumulation of newly synthesized PMPs. At steady state, PEX19 is bimodally distributed between the cytoplasm and peroxisome, with most of the protein in the cytoplasm. We propose that PEX19 may bind newly synthesized PMPs and facilitate their insertion into the peroxisome membrane. This hypothesis is supported by the observation that the loss of PEX19 results in degradation of PMPs and/or mislocalization of PMPs to the mitochondrion.

Indexed as

Molecular ChaperonesRepressor ProteinsAnimalsBiological TransportCell NucleusCytoplasmFibroblastsFluorescent Antibody TechniqueFungal ProteinsGenetic VectorsHumansIntracellular MembranesMembrane ProteinsMitochondriaNuclear Localization SignalsPeptide FragmentsFungal ProteinsMembrane ProteinsMolecular ChaperonesNuclear Localization SignalsPeptide FragmentsPEX14 protein, humanPex14 protein, ratPEX19 protein, ratRecombinant ProteinsRepressor Proteins

Identifiers

PMID10704444
PMCPMC2174547
OpenAlexW2069547574

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.