Evidence map›Paper›PMID 20698011›Full record

ArticleEMBO molecular medicine2010

Prion protein in Alzheimer's pathogenesis: a hot and controversial issue.

Iryna Benilova, Bart De Strooper

Open access · goldAbstract readComment
In one paragraph

Article in EMBO molecular medicine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 34 citations in OpenAlex.

  1. Creutzfeldt-Jakob disease and other prion diseases.Nature reviews. Disease primers · 2024
    Review
  2. Frontiers in neuroscience · 2022
    Review
  3. Article
  4. Review
  5. The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.Journal of Alzheimer's disease : JAD · 2018
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. The prion protein ligand, stress-inducible phosphoprotein 1, regulates amyloid-β oligomer toxicity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. The complex PrP(c)-Fyn couples human oligomeric Aβ with pathological tau changes in Alzheimer's disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  18. Article
  19. Allosteric function and dysfunction of the prion protein.Cellular and molecular life sciences : CMLS · 2012
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Iryna BenilovaDepartment for Molecular and Developmental Genetics, Flanders Institute for Biotechnology (VIB), Leuven, Belgium.
Bart De Strooper
KU Leuven · BEVlaams Instituut voor Biotechnologie · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role for cellular prion protein PrP(c) in beta-amyloid (Abeta) oligomer-induced synaptic impairment is a topic of great interest and some controversy. In this issue of EMBO Molecular Medicine Aguzzi and co-workers explore the contribution of PrP(c) to deficient long term potentiation (LTP) and soluble Abeta levels in an Alzheimer's disease mouse model and show that the role of prions in Abeta related toxicity is far from 'black and white' suggesting complex interpretations of the data available thus far.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsDisease Models, AnimalHumansMicePrionsAmyloid beta-PeptidesPrions

Identifiers

PMID20698011
PMCPMC3377329
OpenAlexW2105358774

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.