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- W3158996866 endingPage "394" @default.
- W3158996866 startingPage "394" @default.
- W3158996866 abstract "Proteins can perform their specific function due to their molecular structure. Partial or complete unfolding of the polypeptide chain may lead to the misfolding and aggregation of proteins in turn, resulting in the formation of different structures such as amyloid aggregates. Amyloids are rigid protein aggregates with the cross-β structure, resistant to most solvents and proteases. Because of their resistance to proteolysis, amyloid aggregates formed in the organism accumulate in tissues, promoting the development of various diseases called amyloidosis, for instance Alzheimer’s diseases (AD). According to the main hypothesis, it is considered that the cause of AD is the formation and accumulation of amyloid plaques of Aβ. That is why Aβ-amyloid is the most studied representative of amyloids. Therefore, in this review, special attention is paid to the history of Aβ-amyloid toxicity. We note the main problems with anti-amyloid therapy and write about new views on amyloids that can play positive roles in the different organisms including humans." @default.
- W3158996866 created "2021-05-10" @default.
- W3158996866 creator A5033853302 @default.
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- W3158996866 creator A5049512331 @default.
- W3158996866 creator A5058007718 @default.
- W3158996866 creator A5088914817 @default.
- W3158996866 date "2021-05-01" @default.
- W3158996866 modified "2023-10-17" @default.
- W3158996866 title "Amyloids: The History of Toxicity and Functionality" @default.
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