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Curr Opin Struct Biol. 2000 Feb;10(1):60-8.

Amyloid fibrillogenesis: themes and variations.

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1
Department of Neurology, Center for Neurologic Diseases, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA. rochet@cnd.bwh.harvard.edu

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.

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PMID:
10679462
[Indexed for MEDLINE]

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