Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor-Reference-Cited by-同舟云学术

Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor

Published:2021-08-05 Issue:32 Volume:93 Page:11176-11183
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Noi Kentaro¹,Ikenaka Kensuke²,Mochizuki Hideki²,Goto Yuji³^ORCID,Ogi Hirotsugu¹^ORCID

Affiliation:

1. Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan

2. Department of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan

3. Global Center for Medical Engineering and Informatics, Osaka University, Suita, Osaka 565-0871, Japan

Funder

Japan Agency for Medical Research and Development

Publisher

American Chemical Society (ACS)

Subject

Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.1c01720

Reference58 articles.

1. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

2. The Amyloid State of Proteins in Human Diseases

3. Alzheimer's Disease: The Amyloid Cascade Hypothesis

4. What does make an amyloid toxic: Morphology, structure or interaction with membrane?

5. Spherical aggregates of -amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3

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