ArticleCommunications biology2026
Engineering a dimeric single-domain antibody for improved detection and neutralization of amyloid-β oligomers.
Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
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Who cites it
2 citing papers in PubMed.
- Multimerization of a rationally designed nanobody for enhanced avidity toward Aβ42 oligomers.Protein science : a publication of the Protein Society · 2026Article
- Engineering a dimeric single-domain antibody for improved detection and neutralization of amyloid-β oligomers.Communications biology · 2026Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Soluble Aβ oligomers are regarded as major neurotoxic agents in Alzheimer's disease. Several monoclonal antibodies have been developed to target Aβ oligomers, but most of them show limited specificity binding also to monomers and fibrils. To generate an antibody with high specificity for the oligomers, we aimed to increase the efficiency and sensitivity of a human VH-derived Aβ-oligomer-specific single domain antibody, called DesAb-O. We engineered a dimeric DesAb-O variant, DiDesAb-O, which showed significantly higher binding affinity for Aβ oligomers as compared to the monomeric sdAb. DiDesAb-O selectively detected Aβ
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Registered trials
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