Evidence map›Paper›PMID 32023927›Full record

ReviewInternational journal of molecular sciences2020

Protofibrils of Amyloid-β are Important Targets of a Disease-Modifying Approach for Alzheimer's Disease.

Kenjiro Ono, Mayumi Tsuji

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
4.9field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Article
  5. Article
  6. Article
  7. Observational
  8. Lecanemab appropriate use recommendations for clinical practice in the UK.Journal of neurology, neurosurgery, and psychiatry · 2026
    Review
  9. Review
  10. Decoding the mechanisms of amyloid-β in synaptic toxicity.Journal of Alzheimer's disease : JAD · 2026
    Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. ALZ-801 prevents amyloid β-protein assembly and reduces cytotoxicity: A preclinical experimental study.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  17. Review
  18. Review
  19. Article
  20. Article
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 1 institution in 1 country.

Kenjiro OnoDepartment of Internal Medicine, Division of Neurology, School of Medicine, Showa University, Tokyo 142-8666, Japan.ORCID 0000-0001-8454-6155
Mayumi TsujiDepartment of Pharmacology, School of Medicine, Showa University, Tokyo 142-8666, Japan.
Showa University · JP

Funding

Grant for Research and Development Grants for Dementia from the Japan Agency for Medical Research and Development 16dk0207021h0001Grant-in-Aid for Scientific Research (C) from the Ministry of Education, Culture, Sports, Science and Technology, Japan 26461266
6 · The paper itself

Abstract

Worldwide, Alzheimer's disease (AD) is the most common age-related neurodegenerative disease and is characterized by unique pathological hallmarks in the brain, including plaques composed of amyloid β-protein (Aβ) and neurofibrillary tangles of tau protein. Genetic studies, biochemical data, and animal models have suggested that Aβ is responsible for the pathogenesis of AD (i.e., the amyloid hypothesis). Indeed, Aβ molecules tend to aggregate, forming oligomers, protofibrils, and mature fibrils. However, while these Aβ species form amyloid plaques of the type implicated in AD neurodegeneration, recent clinical trials designed to reduce the production of Aβ and/or the plaque burden have not demonstrated clinical efficacy. In addition, recent studies using synthetic Aβ peptides, cell culture models, Arctic transgenic mice, and human samples of AD brain tissues have suggested that the pre-fibrillar forms of Aβ, particularly Aβ protofibrils, may be the most critical species, compared with extracellular fibrillar forms. We recently reported that protofibrils of Aβ

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesAnimalsHumansLipid PeroxidationMolecular Targeted TherapyReactive Oxygen SpeciesAmyloidAmyloid beta-PeptidesReactive Oxygen SpeciesAlzheimer’s diseaseamyloid β-protein (Aβ)mAb158oligomersprotofibrils

Identifiers

PMID32023927
PMCPMC7037706
OpenAlexW3004262704

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.