Evidence map›Paper›PMID 39370248›Full record

ReviewInternal medicine (Tokyo, Japan)2026

The Basis of Anti-Aβ Antibody Therapy: The Toxicity of Aβ Aggregates and the Mechanism of Action of Anti-Aβ Antibodies.

Kenjiro Ono, Moeko Noguchi-Shinohara, Takahiro Watanabe-Nakayama

Abstract readReview
In one paragraph

Review in Internal medicine (Tokyo, Japan), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–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

2 citing papers in PubMed.

  1. Article
  2. 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
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

3 authors.

Kenjiro OnoDepartment of Neurology, Kanazawa University Graduate School of Medical Sciences, Kanazawa University, Japan.
Moeko Noguchi-ShinoharaDepartment of Neurology, Kanazawa University Graduate School of Medical Sciences, Kanazawa University, Japan.
Takahiro Watanabe-NakayamaWPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the pathophysiology of Alzheimer's disease (AD), the amyloid hypothesis, which posits that amyloid β-protein (Aβ) abnormally aggregates and damages neurons with tau, has been proposed. It was originally thought that the accumulation of insoluble amyloid fibrils in the brain leads to AD-inducing neurotoxicity; however, in recent years, the positioning of early and intermediate aggregates has also been emphasized. In particular, following the positive results of phase 3 clinical trials of lecanemab and its approval in Japan and the United States, the pathology of protofibrils, which are the target molecules of lecanemab, has attracted attention. Using high-speed atomic force microscopy, we have previously reported that lecanemab, which has a high affinity for protofibrils, binds to and surrounds them. Donanemab, a recombinant monoclonal antibody that primarily targets fibrils composed of N3pG Aβ, has also attracted attention because of its efficacy in phase 3 clinical trials in patients with early stage AD.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAntibodies, MonoclonalAnimalsHumansProtein AggregatesProtein Aggregation, PathologicalAmyloid beta-PeptidesAntibodies, MonoclonalProtein AggregatesAlzheimer's diseaseamyloid β-protein (Aβ)lecanemabprotofibrils

Identifiers

PMID39370248
PMCPMC12854941

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.