ArticleACS omega2026
Quantitative Analysis of Amyloid Fibril Nucleation by Linking Folding and Nucleation Pathways Using a Robust Ultrasonic Assay.
Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding the mechanism of amyloid fibril formation, a nucleation-dependent process influenced by physicochemical conditions, is crucial for eradicating amyloidosis, as it represents the initial step in the pathological cascade of the disease. In this study, we develop a miniaturized ultrasonic platform for the amyloid fibril study, μHANABI, which enables reproducible and rapid analysis of amyloid formation kinetics. Leveraging the robustness of the developed system, we investigate the nucleation rate of α-synuclein, an intrinsically disordered protein, and β
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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 Socratic graph.