Evidence map›Paper›PMID 24665391›Full record

ReviewTissue barriers2013

Roles of the cellular prion protein in the regulation of cell-cell junctions and barrier function.

Constance S V Petit, Laura Besnier, Etienne Morel, Monique Rousset, Sophie Thenet

Abstract readReview
In one paragraph

Review in Tissue barriers, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. PrPFrontiers in molecular neuroscience · 2021
    Review
  6. Inflammatory mediators reduce surface PrPLaboratory investigation; a journal of technical methods and pathology · 2018
    Article
  7. Article
  8. Prions: Beyond a Single Protein.Clinical microbiology reviews · 2016
    Review
  9. Article
  10. Article
  11. Genetics of Prion Disease in Cattle.Bioinformatics and biology insights · 2015
    Review
  12. To develop with or without the prion protein.Frontiers in cell and developmental biology · 2014
    Review
  13. 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

5 authors.

Constance S V PetitCentre de Recherche des Cordeliers; Université Pierre et Marie Curie; Paris, France ; INSERM; Paris, France ; Université Paris Descartes; Paris, France.
Laura BesnierCentre de Recherche des Cordeliers; Université Pierre et Marie Curie; Paris, France ; INSERM; Paris, France ; Université Paris Descartes; Paris, France.
Etienne MorelCentre de Recherche des Cordeliers; Université Pierre et Marie Curie; Paris, France ; INSERM; Paris, France ; Université Paris Descartes; Paris, France.
Monique RoussetCentre de Recherche des Cordeliers; Université Pierre et Marie Curie; Paris, France ; INSERM; Paris, France ; Université Paris Descartes; Paris, France.
Sophie ThenetCentre de Recherche des Cordeliers; Université Pierre et Marie Curie; Paris, France ; INSERM; Paris, France ; Université Paris Descartes; Paris, France ; Ecole Pratique des Hautes Etudes; Laboratoire de Pharmacologie Cellulaire et Moléculaire ; Paris, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cellular prion protein was historically characterized owing to its misfolding in prion disease. Although its physiological role remains incompletely understood, PrP(C) has emerged as an evolutionary conserved, multifaceted protein involved in a wide-range of biological processes. PrP(C) is a GPI-anchored protein targeted to the plasma membrane, in raft microdomains, where its interaction with a repertoire of binding partners, which differ depending on cell models, mediates its functions. Among identified PrP(C) partners are cell adhesion molecules. This review will focus on the multiple implications of PrP(C) in cell adhesion processes, mainly the regulation of cell-cell junctions in epithelial and endothelial cells and the consequences on barrier properties. We will show how recent findings argue for a role of PrP(C) in the recruitment of signaling molecules, which in turn control the targeting or the stability of adhesion complexes at the plasma membrane.

Indexed as

adherens junctionscell adhesioncell signalingcellular prion protein PrPCdesmosomesintestinal barrierraftSrc family kinasestight junctions

Identifiers

PMID24665391
PMCPMC3887058

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.