Misfolding and aggregation of proteins play a central role in the pathogenesis of several neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's and Lewy Body diseases, Frontotemporal Lobar Degeneration and prion diseases. Increasing evidence supports the view that Aβ and tau, which are the two main molecular players in AD, share with the prion protein several “prion-like” features that can be relevant for disease pathogenesis. These features essentially include structural/conformational/biochemical variations, resistance to degradation by endogenous proteases, seeding ability, attitude to form neurotoxic assemblies, spreading and propagation of toxic aggregates, transmissibility of tau- and Aβ-related pathology to animal models. Following this view, part of the recent scientific literature has generated a new reading frame for AD pathophysiology, based on the application of the prion paradigm to the amyloid cascade hypothesis in an attempt to definitely explain the key events causing the disease and inducing its occurrence under different clinical phenotypes.

蛋白质的错误折叠和聚集在几种神经退行性疾病的发病机理中起着核心作用，包括阿尔茨海默氏病（AD），帕金森氏病和路易体病，额颞叶变性和病毒病。越来越多的证据支持以下观点：Aβ和tau是AD中的两个主要分子，它们与the病毒蛋白共享一些与疾病发病机理相关的“ pr病毒样”特征。这些特征基本上包括结构/构象/生化变化，对内源蛋白酶降解的抵抗力，播种能力，形成神经毒性组装体的态度，毒性聚集体的扩散和传播，tau和Aβ相关病理学向动物模型的传播性。按照这种观点，