期刊
SCIENCE
卷 300, 期 5618, 页码 486-489出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1079469
关键词
-
资金
- NIA NIH HHS [AG00538, AG16573] Funding Source: Medline
- NINDS NIH HHS [NS31230] Funding Source: Medline
Soluble oligomers are common to most amyloids and may represent the primary toxic species of amyloids, like the Abeta peptide in Alzheimer's disease (AD). Here we show that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomers regardless of sequence. The in vitro toxicity of soluble oligomers is inhibited by oligomer-specific antibody. Soluble oligomers have a unique distribution in human AD brain that is distinct from fibrillar amyloid. These results indicate that different types of soluble amyloid oligomers have a common structure and suggest they share a common mechanism of toxicity.
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