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2011_956104.pdf | 2.29 MB | Adobe PDF | 見る/開く |
タイトル: | Formation of Toxic Amyloid Fibrils by Amyloid β-Protein on Ganglioside Clusters. |
著者: | Matsuzaki, Katsumi https://orcid.org/0000-0002-0182-1690 (unconfirmed) |
著者名の別形: | 松崎, 勝巳 |
発行日: | 2011 |
出版者: | Hindawi Publishing Corporation |
誌名: | International journal of Alzheimer's disease |
巻: | 2011 |
論文番号: | 956104 |
抄録: | It is widely accepted that the conversion of the soluble, nontoxic amyloid β-protein (Aβ) monomer to aggregated toxic Aβ rich in β-sheet structures is central to the development of Alzheimer's disease. However, the mechanism of the abnormal aggregation of Aβ in vivo is not well understood. Accumulating evidence suggests that lipid rafts (microdomains) in membranes mainly composed of sphingolipids (gangliosides and sphingomyelin) and cholesterol play a pivotal role in this process. This paper summarizes the molecular mechanisms by which Aβ aggregates on membranes containing ganglioside clusters, forming amyloid fibrils. Notably, the toxicity and physicochemical properties of the fibrils are different from those of Aβ amyloids formed in solution. Furthermore, differences between Aβ-(1-40) and Aβ-(1-42) in membrane interaction and amyloidogenesis are also emphasized. |
著作権等: | © 2011 Katsumi Matsuzaki. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
URI: | http://hdl.handle.net/2433/197145 |
DOI(出版社版): | 10.4061/2011/956104 |
PubMed ID: | 21318142 |
出現コレクション: | 学術雑誌掲載論文等 |
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