ArticleJournal of the American Chemical Society2025
Design of Tau Aggregation Inhibitors Using Iterative Machine Learning and a Polymorph-Specific Brain-Seeded Fibril Amplification Assay.
Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.
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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.
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Who cites it
6 citing papers in PubMed.
- Life at the interface: Byron Caughey's search for prion disease inhibitors through chemistry, structure, and cell physiology.Acta neuropathologica · 2026Review
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
- α,β-Dehydroamino-Acid-Containing Peptides Resist Proteolysis and Inhibit Aggregation of a Tau-Derived Model Peptide.The Journal of organic chemistry · 2026Article
- Peptide-Based Therapeutics for Alzheimer's Disease: Medicinal Chemistry, AI-Guided Computational Design, and Blood-Brain Barrier Delivery.Drug design, development and therapy · 2026Review
- Serial amplification of tau filaments using Alzheimer's brain homogenates and C322A or C322S recombinant tau.FEBS letters · 2025Article
- Cambridge neuroscience symposium: Interventions and recovery.Brain and neuroscience advancesArticle
Corrections and comments
- Erratum issued
Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aggregation of tau into amyloid fibrils is associated with Alzheimer's disease (AD) and related tauopathies. Since different tauopathies are characterized by the formation of distinct tau fibril morphologies, it is important to combine the search of tau aggregation inhibitors with the development of in vitro tau aggregation assays that recapitulate aggregation as it may occur in the brain. Here we address this problem by reporting an in vitro tau aggregation assay in which AD brain homogenates are used to seed the generation of first-generation tau fibrils in a polymorph-specific manner under quiescent conditions. These fibrils are then used to create amyloid seed libraries from which second-generation kinetic assays can be readily performed. Using this strategy, we illustrate an iterative machine learning method for the identification of small molecules for the polymorph-specific inhibition of the in vitro formation of tau fibrils. We further show that the small molecules selected by this procedure are potent inhibitors in a
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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.