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• W2950106487 abstract "The assembly of normally soluble proteins into amyloid fibrils is a hallmark of neurodegenerative diseases. Because protein aggregation is very complex, involving a variety of oligomeric metastable intermediates, the detailed aggregation paths and structural characterization of the intermediates remain to be determined. Yet, there is strong evidence that these oligomers, which form early in the process of fibrillogenesis, are cytotoxic. In this paper, we review our current understanding of the underlying factors that promote the aggregation of peptides into amyloid fibrils. We focus here on the structural and dynamic aspects of the aggregation as observed in state-of-the-art computer simulations of amyloid-forming peptides with an emphasis on the activation-relaxation technique." @default.
• W2950106487 created "2019-06-27" @default.
• W2950106487 creator A5022137374 @default.
• W2950106487 creator A5090416900 @default.
• W2950106487 date "2005-09-17" @default.
• W2950106487 modified "2023-10-18" @default.
• W2950106487 title "Exploring the Early Steps of Amyloid Peptide Aggregation by Computers" @default.
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• W2950106487 doi "https://doi.org/10.1021/ar050045a" @default.
• W2950106487 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16285711" @default.
• W2950106487 hasPublicationYear "2005" @default.
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