Dobson Christopher M
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Semin Cell Dev Biol. 2004 Feb;15(1):3-16. doi: 10.1016/j.semcdb.2003.12.008.
This review summarises our current understanding of the underlying and universal mechanism by which newly synthesised proteins achieve their biologically functional states. Protein molecules, however, all have a finite tendency either to misfold, or to fail to maintain their correctly folded states, under some circumstances. This article describes some of the consequences of such behaviour, particularly in the context of the aggregation events that are frequently associated with aberrant folding. It focuses in particular on the emerging links between protein aggregation and the increasingly prevalent forms of debilitating disease with which it is now known to be associated.
本综述总结了我们目前对新合成蛋白质达到其生物功能状态的潜在通用机制的理解。然而，在某些情况下，蛋白质分子都有有限的倾向，要么错误折叠，要么无法维持其正确折叠状态。本文描述了这种行为的一些后果，特别是在与异常折叠频繁相关的聚集事件的背景下。它特别关注蛋白质聚集与现在已知与之相关的日益普遍的使人衰弱的疾病形式之间新出现的联系。
