Evidence map›Paper›PMID 23479001›Full record

ReviewCellular & molecular biology letters2013

Prion protein and its role in signal transduction.

Alessandro Didonna

Abstract readReview
In one paragraph

Review in Cellular & molecular biology letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Upregulated PrPNPJ precision oncology · 2024
    Article
  4. Review
  5. Review
  6. Article
  7. Prion Protein at the Leading Edge: Its Role in Cell Motility.International journal of molecular sciences · 2020
    Review
  8. Review
  9. Prion disease.Handbook of clinical neurology · 2018
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
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

1 author.

Alessandro DidonnaDavee Department of Neurology, Feinberg School of Medicine Northwestern University, Chicago, IL 60611, USA. a-didonna@northwestern.edu

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prion diseases are a class of fatal neurodegenerative disorders that can be sporadic, genetic or iatrogenic. They are characterized by the unique nature of their etiologic agent: prions (PrP(Sc)). A prion is an infectious protein with the ability to convert the host-encoded cellular prion protein (PrP(C)) into new prion molecules by acting as a template. Since Stanley B. Prusiner proposed the "protein-only" hypothesis for the first time, considerable effort has been put into defining the role played by PrP(C) in neurons. However, its physiological function remains unclear. This review summarizes the major findings that support the involvement of PrP(C) in signal transduction.

Indexed as

Signal TransductionAnimalsGene Knockout TechniquesHumansLigandsModels, BiologicalPrionsProtein KinasesLigandsPrionsProtein Kinases

Identifiers

PMID23479001
PMCPMC6275729

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.