Evidence map›Paper›PMID 38473975›Full record

ReviewInternational journal of molecular sciences2024

The Single Toxin Origin of Alzheimer's Disease and Other Neurodegenerative Disorders Enables Targeted Approach to Treatment and Prevention.

Martin Tolar, John A Hey, Aidan Power, Susan Abushakra

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

15 citing papers in PubMed, 14 citations in OpenAlex.

  1. Trial
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  11. 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
  12. Review
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  15. APOLLOE4 Phase 3 study of oral ALZ-801/valiltramiprosate inAlzheimer's & dementia (New York, N. Y.)
    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

4 authors at 1 institution in 1 country.

Martin TolarAlzheon, Inc., Framingham, MA 01701, USA.ORCID 0000-0002-3910-091X
John A HeyAlzheon, Inc., Framingham, MA 01701, USA.
Aidan PowerAlzheon, Inc., Framingham, MA 01701, USA.
Susan AbushakraAlzheon, Inc., Framingham, MA 01701, USA.
Framingham State University · US

Funding

Randomized, Double-Blind, Placebo-Controlled, Phase 3 Study - COVID supplementR01AG065253 · NIA · ALZHEON, INC. · PI ABUSHAKRA, SUSAN · 2020 to 2024
$51.2M
NIA NIH HHS 1R01AG065253-01A1NIA NIH HHS R01 AG065253
6 · The paper itself

Abstract

New data suggest that the aggregation of misfolded native proteins initiates and drives the pathogenic cascade that leads to Alzheimer's disease (AD) and other age-related neurodegenerative disorders. We propose a unifying single toxin theory of brain neurodegeneration that identifies new targets and approaches to the development of disease-modifying treatments. An extensive body of genetic evidence suggests soluble aggregates of beta-amyloid (Aβ) as the primary neurotoxin in the pathogenesis of AD. New insights from fluid biomarkers, imaging, and clinical studies provide further evidence for the decisive impact of toxic Aβ species in the initiation and progression of AD. Understanding the distinct roles of soluble and insoluble amyloid aggregates on AD pathogenesis has been the key missing piece of the Alzheimer's puzzle. Data from clinical trials with anti-amyloid agents and recent advances in the diagnosis of AD demonstrate that the driving insult in biologically defined AD is the neurotoxicity of soluble Aβ aggregates, called oligomers and protofibrils, rather than the relatively inert insoluble mature fibrils and amyloid plaques. Amyloid oligomers appear to be the primary factor causing the synaptic impairment, neuronal stress, spreading of tau pathology, and eventual cell death that lead to the clinical syndrome of AD dementia. All other biochemical effects and neurodegenerative changes in the brain that are observed in AD are a response to or a downstream effect of this initial toxic insult by oligomers. Other neurodegenerative disorders follow a similar pattern of pathogenesis, in which normal brain proteins with important biological functions become trapped in the aging brain due to impaired clearance and then misfold and aggregate into neurotoxic species that exhibit prion-like behavior. These aggregates then spread through the brain and cause disease-specific neurodegeneration. Targeting the inhibition of this initial step in neurodegeneration by blocking the misfolding and aggregation of healthy proteins has the potential to slow or arrest disease progression, and if treatment is administered early in the course of AD and other neurodegenerative disorders, it may delay or prevent the onset of clinical symptoms.

Indexed as

Alzheimer DiseaseToxins, BiologicalAgingAmyloidAmyloid beta-PeptidesBrainHumansAmyloidAmyloid beta-PeptidesToxins, BiologicaladucanumabALZ-801Alzheimer’s diseaseAPOE4beta-amyloid oligomersdisease modificationdonanemablecanemabneurodegenerationprotofibrilsvaliltramiprosate

Identifiers

PMID38473975
PMCPMC10932387
OpenAlexW4392197777

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.