Review
doi: 10.1016/s0959-440x(99)00049-4.
Amyloid fibrillogenesis: themes and variations
Affiliations
- PMID: 10679462
- DOI: 10.1016/s0959-440x(99)00049-4
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Review
Amyloid fibrillogenesis: themes and variations
Curr Opin Struct Biol.
2000 Feb.
Abstract
Recent progress has improved our knowledge of how proteins form amyloid fibrils. Both 'natively unfolded' and globular proteins have been shown to initiate fibrillization by adopting a partially structured conformation. Oligomeric prefibrillar intermediates have been extensively characterized with respect to their morphology and temporal evolution. Three-dimensional models obtained using biophysical and computational methods have provided information about fibril structure. All of these advances suggest common features of self-assembly pathways, with subtle variations accounting for differences among distinct amyloid fibrils.
Comment in
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Folding and binding: problems with proteins.Curr Opin Struct Biol. 2000 Feb;10(1):13-5. doi: 10.1016/s0959-440x(99)90003-9. Curr Opin Struct Biol. 2000. PMID: 10766516 No abstract available.
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