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- W1983111544 abstract "Amyloid oligomers are believed to play important causal roles in many types of amyloid-related degenerative diseases. Many different laboratories have reported amyloid oligomers that differ in size, morphology, toxicity, and method of preparation or purification, raising the question of the structural relationships among these oligomer preparations. The structural plasticity that has been reported to occur in amyloid formed from the same protein sequence indicates that it is quite possible that different oligomer preparations may represent distinct structural variants. In view of the difficulty in determining the precise structure of amyloids, conformation- and epitope-specific antibodies may provide a facile means of classifying amyloid oligomer structures. Conformation-dependent antibodies that recognize generic epitopes that are specifically associated with distinct aggregation states of many different amyloid-forming sequences indicate that there are at least two fundamentally distinct types of amyloid oligomers: fibrillar and prefibrillar oligomers. Classification of amyloid oligomers according to their underlying structures may be a more useful and rational approach than relying on differences in size and morphology." @default.
- W1983111544 created "2016-06-24" @default.
- W1983111544 creator A5016400438 @default.
- W1983111544 date "2014-06-30" @default.
- W1983111544 modified "2023-09-25" @default.
- W1983111544 title "A Mini Review on Aβ Oligomers and its Pathogencity" @default.
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- W1983111544 doi "https://doi.org/10.13160/ricns.2014.7.2.79" @default.
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