Protein misfolding and disease: the case of prion disorders

被引：43

作者：

Hetz, C

Soto, C

机构：

[1] Univ Chile, Inst Ciencias Biomed, Santiago, Chile

[2] Serono Pharmaceut Res Inst, CH-1228 Plan les Ouates, Switzerland

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2003年 / 60卷 / 01期

关键词：

protein conformational disorders; prion protein misfolding; transmissible spongiform encephalopathies; neuronal apoptosis; brain inflammation; prion protein function;

D O I：

10.1007/s000180300009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent findings strongly support the hypothesis that diverse human disorders, including the most common neurodegenerative diseases, arise from misfolding and aggregation of an underlying protein. Despite the good evidence for the involvement of protein misfolding in disease pathogenesis, the mechanism by which protein conformational changes participate in the disease is still unclear. Among the best-studied diseases of this group are the transmissible spongiform encephalopathies or prion-related disorders, in which misfolding of the normal prion protein plays a key role in the disease. In this article we review recent data on the link between prion protein misfolding and the pathogensis of spongiform encephalopathies.

引用

页码：133 / 143

页数：11

共 123 条

[81] A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform [J].