ArticleInternational journal of molecular sciences2020
Real-Time 3D Imaging and Inhibition Analysis of Various Amyloid Aggregations Using Quantum Dots.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- A high-throughput conditioned-media-based screening system identifies inhibitors of aggregation induced by iPSC-secreted amyloid β.Nature communications · 2026Article
- Aggregation Characteristics of Tau Phosphorylated by Various Kinases as Observed by Quantum Dot Fluorescence Imaging.International journal of molecular sciences · 2025Article
- Microtubule-associated protein 4 forms aggregates consisting of helical filaments.Biochemistry and biophysics reports · 2025Article
- Screening of a Fraction with Higher Amyloid β Aggregation Inhibitory Activity from a Library Containing 210 Mushroom Extracts Using a Microliter-Scale High-Throughput Screening System with Quantum Dot Imaging.Foods (Basel, Switzerland) · 2024Article
- Analyzing Amylin Aggregation Inhibition Through Quantum Dot Fluorescence Imaging.International journal of molecular sciences · 2024Article
- Real-Time 3D Imaging and Inhibition Analysis of Human Serum Amyloid A Aggregations Using Quantum Dots.International journal of molecular sciences · 2024Article
- Review
- Metal-Organic Frameworks as Sensors for Human Amyloid Diseases.ACS sensors · 2023Review
- Amyloid β aggregation induces human brain microvascular endothelial cell death with abnormal actin organization.Biochemistry and biophysics reports · 2022Article
- Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A.International journal of molecular sciences · 2021Article
- Dietary Intake of Rosmarinic Acid Increases Serum Inhibitory Activity in Amyloid A Aggregation and Suppresses Deposition in the Organs of Mice.International journal of molecular sciences · 2020Article
- Evaluation of Amyloid βFoods (Basel, Switzerland) · 2020Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Amyloidosis refers to aggregates of protein that accumulate and are deposited as amyloid fibrils into plaques. When these are detected in organs, they are the main hallmark of Alzheimer's disease, Parkinson's disease, and other related diseases. Recent medical advances have shown that many precursors and proteins can induce amyloidosis even though the mechanism of amyloid aggregation and the relationship of these proteins to amyloidosis remains mostly unclear. In this study, we report the real-time 3D-imaging and inhibition analysis of amyloid β (Aβ), tau, and α-synuclein aggregation utilizing the affinity between quantum dots (QD) and amyloid aggregates. We successfully visualized these amyloid aggregations in real-time using fluorescence microscopy and confocal microscopy simply by adding commercially available QD. The observation by transmission electron microscopy (TEM) showed that QD particles bound to all amyloid fibrils. The 3D-imaging with QD revealed differences between amyloid aggregates composed of different amyloid peptides that could not be detected by TEM. We were also able to quantify the inhibition activities of these proteins by rosmarinic acid, which has high activity for Aβ aggregation, from fluorescence micrographs as half-maximal effective concentrations. These imaging techniques with QD serve as quick, easy, and powerful tools to understand amyloidosis and to discover drugs for therapies.
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Registered trials
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