期刊
JAMA NEUROLOGY
卷 70, 期 3, 页码 304-310出版社
AMER MEDICAL ASSOC
DOI: 10.1001/jamaneurol.2013.1453
关键词
-
资金
- National Institutes of Health [R21AG040589, P51RR165, P51OD11132, P01AG005119, R01NS071835, 1F31NS079039, R01NS074874, R21AG038835-01A1, R21NS067127]
- CART Foundation
- Muscular Dystrophy Association
- Tau Consortium
- American Health Assistance Foundation
Most age-associated neurodegenerative diseases involve the aggregation of specific proteins within the nervous system. In Alzheimer disease, the insidious pathogenic process begins many years before the symptoms emerge, and the lesions that characterize the disease-senile plaques and neurofibrillary tangles-ramify systematically through the brain. We review evidence that the beta-amyloid and tau proteins, which aggregate to form senile plaques and neurofibrillary tangles, respectively, are induced to misfold and self-assemble by a process of templated conformational change that amplifies a toxic species. Recent data also indicate that the spread of these lesions from one site to another is mediated by the cellular uptake, transport, and release of endogenous seeds formed by the cognate proteins. This simple pathogenic principle suggests that the formation, trafficking, and metabolism of pathogenic protein seeds are promising therapeutic targets for Alzheimer disease and other neurodegenerative disorders. JAMA Neurol. 2013; 70(3):304-310. Published online December 10, 2012. doi:10.1001/jamaneurol.2013.1453
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据