Evidence map›Paper›PMID 27830781›Full record

ReviewNature2016

Mammalian prions and their wider relevance in neurodegenerative diseases.

John Collinge

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed
15.0field-weighted citation impact, top 1% 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

140 citing papers in PubMed, 245 citations in OpenAlex.

  1. Article
  2. From aggregate structure to disease trajectory: the role of the proteostasis network.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  3. Article
  4. Article
  5. A scalable, dividing cell model for the robust propagation and quantification of human sporadic Creutzfeldt-Jakob disease prions.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Roles of C/EBPβ/AEP in Neurodegenerative Diseases.Current topics in medicinal chemistry · 2025
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024
    Article

80 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

1 author at 1 institution in 1 country.

John CollingeMedical Research Council Prion Unit, University College London Institute of Neurology, London WC1N 3BG, UK.
Medical Research Council · GB

Funding

Medical Research Council MC_U123192748
6 · The paper itself

Abstract

Prions are notorious protein-only infectious agents that cause invariably fatal brain diseases following silent incubation periods that can span a lifetime. These diseases can arise spontaneously, through infection or be inherited. Remarkably, prions are composed of self-propagating assemblies of a misfolded cellular protein that encode information, generate neurotoxicity and evolve and adapt in vivo. Although parallels have been drawn with Alzheimer's disease and other neurodegenerative conditions involving the deposition of assemblies of misfolded proteins in the brain, insights are now being provided into the usefulness and limitations of prion analogies and their aetiological and therapeutic relevance.

Indexed as

Neurodegenerative DiseasesAmyloid beta-PeptidesAnimalsHumansKineticsMammalsPrionsProtein FoldingAmyloid beta-PeptidesPrions

Identifiers

PMID27830781
OpenAlexW2549098625

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.