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- W2952651278 abstract "Amyloid fibrils are found in association with at least two dozen fatal diseases. The tendency of numerous proteins to convert into amyloid-like fibrils poses fundamental questions for structural biology and for protein science in general. Among these are the following: What is the structure of the cross-beta spine, common to amyloid-like fibrils? Is there a sequence signature for proteins that form amyloid-like fibrils? What is the nature of the structural conversion from native to amyloid states, and do fibril-forming proteins have two distinct stable states, the native state and the amyloid state? What is the basis of protein complementarity, in which a protein chain can bind to itself? We offer tentative answers here, based on our own recent structural studies." @default.
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- W2952651278 date "2006-12-29" @default.
- W2952651278 modified "2023-10-01" @default.
- W2952651278 title "The Structural Biology of Protein Aggregation Diseases: Fundamental Questions and Some Answers" @default.
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- W2952651278 doi "https://doi.org/10.1002/chin.200651267" @default.
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