Evidence map›Paper›PMID 41758970›Full record

ReviewChembiochem : a European journal of chemical biology2026

Amyloid Alpha: The Neglected Cousin of Amyloid Beta.

Jevgenij A Raskatov

Abstract readReview
In one paragraph

Review in Chembiochem : a European journal of chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Jevgenij A RaskatovDept. of Chemistry and Biochemistry, UCSC, Santa Cruz, California, USA.ORCID https://orcid.org/0000-0002-0082-9113

Funding

Using Chirality to Understand and Control Amyloid Beta Neuronal Uptake and ToxicityR01AG074954 · NIA · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI Jevgenij Raskatov · 2022 to 2026
$1.9M
NIA NIH HHS R01 AG074954NIA NIH HHS R01AG074954
6 · The paper itself

Abstract

For decades, amyloid β (Aβ) has been the principal therapeutic target for therapies of Alzheimer's disease (AD). An alternative processing product, known as P3, may form if the amyloid precursor protein is cleaved by α-secretase instead of β-secretase. This shorter peptide has received little attention and is often dismissed as nonamyloidogenic and nontoxic. Our research, and that of others, has shown that the shorter peptide is anything but innocuous. We demonstrated that P3-or Amyloid α (Aα) as we termed it-readily forms oligomers and fibrils and is itself potentially neurotoxic and may interact with Aβ to modulate the aggregation behavior and toxicity of Aβ. This perspective article provides a succinct overview of current uncertainties around P3/Aα. A revision of the amyloid cascade hypothesis to include P3/Aα is urgently needed. This peptide is, most likely, not an innocent bystander, but a distinct aggregating peptide that is itself potentially neurotoxic and may be contributing to AD.

Indexed as

AmyloidAmyloid beta-PeptidesAlzheimer DiseaseAmyloid Precursor Protein SecretasesAnimalsHumansAmyloidAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAlzheimer's diseaseamyloid alphaamyloid betaamyloid cascade hypothesisprotein aggregation

Identifiers

PMID41758970
PMCPMC12980454

What OpenQuestion holds

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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.