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• W2560598375 endingPage "95" @default.
• W2560598375 startingPage "69" @default.
• W2560598375 abstract "Dozens of proteins are known to convert to the aggregated amyloid state. These include fibrils associated with systemic and neurodegenerative diseases and cancer, functional amyloid fibrils in microorganisms and animals, and many denatured proteins. Amyloid fibrils can be much more stable than other protein assemblies. In contrast to globular proteins, a single protein sequence can aggregate into several distinctly different amyloid structures, termed polymorphs, and a given polymorph can reproduce itself by seeding. Amyloid polymorphs may be the molecular basis of prion strains. Whereas the Protein Data Bank contains some 100,000 globular protein and 3,000 membrane protein structures, only a few dozen amyloid protein structures have been determined, and most of these are short segments of full amyloid-forming proteins. Regardless, these amyloid structures illuminate the architecture of the amyloid state, including its stability and its capacity for formation of polymorphs." @default.
• W2560598375 created "2016-12-16" @default.
• W2560598375 creator A5053075000 @default.
• W2560598375 creator A5080439570 @default.
• W2560598375 date "2017-06-20" @default.
• W2560598375 modified "2023-10-10" @default.
• W2560598375 title "Structural Studies of Amyloid Proteins at the Molecular Level" @default.
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