Rochet J C, Lansbury P T
Department of Neurology, Center for Neurologic Diseases, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.
Curr Opin Struct Biol. 2000 Feb;10(1):60-8. doi: 10.1016/s0959-440x(99)00049-4.
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.
最近的进展增进了我们对蛋白质如何形成淀粉样纤维的了解。“天然未折叠”蛋白和球状蛋白均已被证明通过采用部分结构化构象来启动纤维化过程。寡聚前纤维中间体在形态和时间演变方面已得到广泛表征。使用生物物理和计算方法获得的三维模型提供了有关纤维结构的信息。所有这些进展都表明了自组装途径的共同特征，细微的差异解释了不同淀粉样纤维之间的差异。
