Abstract |
Many types of amyloidoses are pathologically characterized by the deposition of amyloid, which is comprised of fibrils formed by abnormally aggregated proteins, in various peripheral tissues and the central nervous system (CNS). Neurodegenerative disorders, such as Alzheimer disease (AD), Parkinson disease (PD), frontotemporal dementia (FTD), and amyotrophic lateral sclerosis (ALS), are well-known CNS amyloidoses that are characterized by amyloid deposition both inside and outside of cells. The amyloidogenic proteins of each disease have distinct primary sequences, and they normally function as soluble proteins. However, these proteins all aggregate and form amyloid with a common intermolecular tertiary structure, namely, a cross-β-sheet structure, finally leading to the onset of each disease. Therefore, inhibition of the aggregation of amyloid proteins or efficient clearance of the already formed amyloids are thought to be promising therapeutic strategies against amyloidoses.
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Authors | Tetsuo Ikeda, Yukiko Hori, Youhei Sohma, Motomu Kanai, Taisuke Tomita |
Journal | Advances in experimental medicine and biology
(Adv Exp Med Biol)
Vol. 1339
Pg. 415-422
( 2021)
ISSN: 0065-2598 [Print] United States |
PMID | 35023134
(Publication Type: Journal Article)
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Copyright | © 2021. The Author(s), under exclusive license to Springer Nature Switzerland AG. |
Chemical References |
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Topics |
- Alzheimer Disease
- Amyloid
- Amyloidosis
(therapy)
- Frontotemporal Dementia
- Humans
- Parkinson Disease
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