Evidence map›Paper›PMID 22424229›Full record

ReviewCell2012

The amyloid state of proteins in human diseases.

David Eisenberg, Mathias Jucker

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 771 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
771citing papers in PubMed, 3 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

771 citing papers in PubMed, 3 syntheses or guidelines pooled it.

  1. Pooled it
  2. Targeting p53 pathways: mechanisms, structures, and advances in therapy.Signal transduction and targeted therapy · 2023
    Pooled it
  3. Pooled it
  4. Review
  5. Article
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  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. TDP-43 Aggregation: The Healthy-Toxic Balance of the Prion-Like Domain.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

711 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

2 authors.

David EisenbergHoward Hughes Medical Institute, Department of Biological Chemistry, University of California, Los Angeles, Los Angeles CA 90095-1570, USA. david@mbi.ucla.edu
Mathias Jucker

Funding

Structural Biology of Amyloid DiseaseR01AG029430 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EISENBERG, DAVID · 2007 to 2016
$3.9M
Howard Hughes Medical InstituteNIA NIH HHS R01 AG029430
6 · The paper itself

Abstract

Amyloid fibers and oligomers are associated with a great variety of human diseases including Alzheimer's disease and the prion conditions. Here we attempt to connect recent discoveries on the molecular properties of proteins in the amyloid state with observations about pathological tissues and disease states. We summarize studies of structure and nucleation of amyloid and relate these to observations on amyloid polymorphism, prion strains, coaggregation of pathogenic proteins in tissues, and mechanisms of toxicity and transmissibility. Molecular studies have also led to numerous strategies for biological and chemical interventions against amyloid diseases.

Indexed as

Amyloid beta-Protein PrecursorAnimalsDisease Models, AnimalHumansModels, MolecularNeurodegenerative DiseasesPlaque, AmyloidProtein Structure, SecondaryAmyloid beta-Protein PrecursorAPP protein, human

Identifiers

PMID22424229
PMCPMC3353745

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.