Evidence map›Paper›PMID 20190788›Full record

ReviewNature reviews. Drug discovery2010

Protein aggregation diseases: pathogenicity and therapeutic perspectives.

Adriano Aguzzi, Tracy O'Connor

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Drug discovery, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 301 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
301citing papers in PubMed, 1 pooled it
24.6field-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

301 citing papers in PubMed, 1 synthesis or guideline pooled it, 748 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Depleting prion protein using splice-switching small molecules.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026
    Review
  12. Article
  13. Review
  14. Regulation of autophagy-mediated pathways by diet, physical activity, and sleep in Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Review
  15. Article
  16. Gapmers: Invention and Early History.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  17. Article
  18. Review
  19. Article
  20. Article

241 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 at 2 institutions in 1 country.

Adriano AguzziInstitute of Neuropathology, University Hospital of Zürich, Schmelzbergstrasse 12, CH8091 Zürich, Switzerland. adriano.aguzzi@usz.ch
Tracy O'Connor
University Hospital of Zurich · CHUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A growing number of diseases seem to be associated with inappropriate deposition of protein aggregates. Some of these diseases--such as Alzheimer's disease and systemic amyloidoses--have been recognized for a long time. However, it is now clear that ordered aggregation of pathogenic proteins does not only occur in the extracellular space, but in the cytoplasm and nucleus as well, indicating that many other diseases may also qualify as amyloidoses. The common structural and pathogenic features of these diverse protein aggregation diseases is only now being fully understood, and may provide novel opportunities for overarching therapeutic approaches such as depleting the monomeric precursor protein, inhibiting aggregation, enhancing aggregate clearance or blocking common aggregation-induced cellular toxicity pathways.

Indexed as

Alzheimer DiseaseAmyloidAmyloidosisAmyloid Precursor Protein SecretasesAnimalsAnti-Inflammatory Agents, Non-SteroidalBrainCentral Nervous System DiseasesDrug Evaluation, PreclinicalHumansImmunotherapyPeptidesPrion DiseasesAmyloidAmyloid Precursor Protein SecretasesAnti-Inflammatory Agents, Non-SteroidalPeptides

Identifiers

PMID20190788
OpenAlexW2076713412

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.