Evidence map›Paper›PMID 22137337›Full record

ReviewTrends in neurosciences2012

Prion protein at the crossroads of physiology and disease.

Emiliano Biasini, Jessie A Turnbaugh, Ursula Unterberger, David A Harris

Open access · greenAbstract readReview
In one paragraph

Review in Trends in neurosciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
8.1field-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

90 citing papers in PubMed, 164 citations in OpenAlex.

  1. Review
  2. Physics of Protein Aggregation in Normal and Accelerated Brain Aging.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  3. Article
  4. Article
  5. Therapeutic Trajectories in Human Prion Diseases.Sub-cellular biochemistry · 2025
    Review
  6. Article
  7. New Light on Prions: Putative Role of PrPInternational journal of molecular sciences · 2024
    Review
  8. Review
  9. Review
  10. Structural biology of ex vivo mammalian prions.The Journal of biological chemistry · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. PrPFrontiers in molecular neuroscience · 2021
    Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

30 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

4 authors at 1 institution in 1 country.

Emiliano BiasiniDepartment of Biochemistry, Boston University School of Medicine, Boston, MA 02118, USA.
Jessie A Turnbaugh
Ursula Unterberger
David A Harris
Boston University · US

Funding

Mechanisms of Prion Protein ToxicityR01NS065244 · NINDS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI HARRIS, DAVID A · 2010 to 2025
$8.9M
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
UPTAKE, TRANSPORT, AND SPREAD OF PRIONSR01NS056376 · NINDS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI HARRIS, DAVID A · 2009 to 2010
$786k
NINDS NIH HHS NS040975NINDS NIH HHS NS052526NINDS NIH HHS NS056376NINDS NIH HHS NS065244NINDS NIH HHS R01 NS040975NINDS NIH HHS R01 NS052526NINDS NIH HHS R01 NS056376NINDS NIH HHS R01 NS065244
6 · The paper itself

Abstract

The presence of the cellular prion protein (PrP(C)) on the cell surface is critical for the neurotoxicity of prions. Although several biological activities have been attributed to PrP(C), a definitive demonstration of its physiological function remains elusive. In this review, we discuss some of the proposed functions of PrP(C), focusing on recently suggested roles in cell adhesion, regulation of ionic currents at the cell membrane and neuroprotection. We also discuss recent evidence supporting the idea that PrP(C) may function as a receptor for soluble oligomers of the amyloid β peptide and possibly other toxic protein aggregates. These data suggest surprising new connections between the physiological function of PrP(C) and its role in neurodegenerative diseases beyond those caused by prions.

Indexed as

HumansPeptide FragmentsPrion DiseasesPrionsPeptide FragmentsPrions

Identifiers

PMID22137337
PMCPMC3273588
OpenAlexW1982119464

What OpenQuestion holds

Textmetadata
LicenceTDM
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.