Evidence map›Paper›PMID 17451912›Full record

ReviewBiochimica et biophysica acta2007

The cellular prion protein (PrP(C)): its physiological function and role in disease.

Laura Westergard, Heather M Christensen, David A Harris

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 195 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
195citing papers in PubMed, 2 pooled it
–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

195 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
  2. Pooled it
  3. Article
  4. Article
  5. Review
  6. PrPEnvironmental science & technology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Pharmaceuticals (Basel, Switzerland) · 2025
    Review
  12. Pathogens that infect mammalian cells via sulfonated glycosaminoglycans.Frontiers in cellular and infection microbiology · 2025
    Review
  13. Review
  14. Article
  15. MRI changes observed in a case of atypical scrapie in a 7-year-old Herdwick ewe.Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc · 2024
    Article
  16. Article
  17. Article
  18. Review
  19. Adaptation of the protein misfolding cyclic amplification (PMCA) technique for the screening of anti-prion compounds.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  20. Review

135 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.

Laura WestergardDepartment of Cell Biology and Physiology, Washington University School of Medicine, St Louis, MO 63110, USA.
Heather M Christensen
David A Harris

Funding

MURINE TRANSGENIC MODELS OF PRION DISEASESR01NS040975 · NINDS · WASHINGTON UNIVERSITY · PI HARRIS, DAVID A · 2001 to 2015
$7.0M
Cellular Functions of the Prion ProteinR01NS052526 · NINDS · WASHINGTON UNIVERSITY · PI HARRIS, DAVID A · 2006 to 2010
$1.7M
NINDS NIH HHS NS040975NINDS NIH HHS NS04691003NINDS NIH HHS NS052526NINDS NIH HHS R01 NS040975NINDS NIH HHS R01 NS052526
6 · The paper itself

Abstract

Prion diseases are caused by conversion of a normal cell-surface glycoprotein (PrP(C)) into a conformationally altered isoform (PrP(Sc)) that is infectious in the absence of nucleic acid. Although a great deal has been learned about PrP(Sc) and its role in prion propagation, much less is known about the physiological function of PrP(C). In this review, we will summarize some of the major proposed functions for PrP(C), including protection against apoptotic and oxidative stress, cellular uptake or binding of copper ions, transmembrane signaling, formation and maintenance of synapses, and adhesion to the extracellular matrix. We will also outline how loss or subversion of the cytoprotective or neuronal survival activities of PrP(C) might contribute to the pathogenesis of prion diseases, and how similar mechanisms are probably operative in other neurodegenerative disorders.

Indexed as

AnimalsApoptosisHumansModels, BiologicalPrion DiseasesPrPC ProteinsSignal TransductionPrPC Proteins

Identifiers

PMID17451912
PMCPMC1986710

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.