Protein aggregation and its consequences for human disease
Protein aggregation and its consequences for human disease
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DOI：
10.2174/092986606775338362
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发表时间：
2006-01-01
影响因子：
1.6
通讯作者：
Dobson, CM
中科院分区：
文献类型：
--
作者：
Dobson, CM
蛋白质分子通过进化而出现，因此它们能够在正常生理条件下保持其功能和可溶性状态，尽管在其他情况下它们通常具有高度的聚集倾向。体内聚集与广泛的人类疾病有关，包括阿尔茨海默病和II型糖尿病，这些疾病在现代世界变得越来越普遍。在这类疾病中，通常可以观察到聚集的蛋白质是高度难缠的丝状物质，即淀粉样原纤维。本文概述了我们目前对这些纤维聚集体的性质和它们形成的方式的了解，并讨论了它们及其前体相关的致病特性的起源和潜在的抑制方法。
Protein molecules have emerged through evolution so that they are able to remain in their functional and soluble states under normal physiological conditions, although in other situations they often have a high propensity to aggregate. Aggregation in vivo is associated with a wide range of human disorders, including Alzheimer's disease and type II diabetes, medical conditions that are becoming increasingly common in the modern world. In such diseases, aggregated proteins can often be observed as highly intractable thread-like species known as amyloid fibrils. This article provides an overview of our present knowledge of the nature of these fibrillar aggregates and the manner in which they form, and discusses the origins and potential means of suppression of the pathogenic properties with which they and their precursors are associated.