期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 10, 期 1, 页码 60-68出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/S0959-440X(99)00049-4
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资金
- NIA NIH HHS [AG08470] Funding Source: Medline
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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