Prion protein interconversions

被引：16

作者：

Caughey, B ^{[1
]}

机构：

[1] NIAID, Rocky Mt Labs, Persistent Viral Dis Lab, Hamilton, MT 59840 USA

来源：

PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES | 2001年 / 356卷 / 1406期

关键词：

prion; transmissible spongiform encephalopathies; structure; conversion; Creutzfeldt-Jakob disease; bovine spongiform encephalopathy;

D O I：

10.1098/rstb.2000.0765

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The transmissible spongiform encephalopathies (TSEs), or prion diseases, remain mysterious neuro-degenerative diseases that involve perturbations in prion protein (PrP) structure. This article summarizes our use of in vitro models to describe how PrP is converted to the disease-associated, protease-resistant form. These models reflect many important biological parameters of TSE diseases and have been used to identify inhibitors of the PrP conversion as lead compounds in the development of anti-TSE drugs.

引用

页码：197 / 200

页数：4

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