ArticleNature chemical biology2025
A genetically encoded selection for amyloid-β oligomer binders.
Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
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.
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Who cites it
3 citing papers in PubMed.
- De Novo Discovery of Bioactive Cyclic Peptides via Cellular Selection of Genetically Encoded Libraries.Chembiochem : a European journal of chemical biology · 2026Review
- Identification of Secondary Nucleation Inhibitors of Amyloid-β Aggregation by Cellular Selection of a SICLOPPS Library.Chembiochem : a European journal of chemical biology · 2026Article
- Stem cell therapies for diabetes.Nature medicine · 2025Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Soluble amyloid-β oligomers (AβOs) are a hypothesized source of neurotoxicity in Alzheimer disease. Binding proteins that recognize these species may have high utility in diagnostic and therapeutic applications. However, identifying binders to AβOs directly generated from the aggregation cascade is challenging because of the short lifetime and low concentrations of oligomer populations. We report a strategy to detect binding to AβOs formed during Aβ42 aggregation using a genetically encoded biosensor. We show that our method enables rapid, highly reproducible measurement of the activity of existing AβO binders and can be used to select for new binders with improved potency. We uncover hits that are >20-fold more effective than reported binders at delaying secondary nucleation, the step in Aβ aggregation thought to generate the highest number of toxic oligomers. Our approach may greatly accelerate the discovery and characterization of binding proteins that target AβOs.
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Registered trials
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.