| First Author | Liu P | Year | 2015 |
| Journal | Cell Rep | Volume | 11 |
| Issue | 11 | Pages | 1760-71 |
| PubMed ID | 26051935 | Mgi Jnum | J:228703 |
| Mgi Id | MGI:5708479 | Doi | 10.1016/j.celrep.2015.05.021 |
| Citation | Liu P, et al. (2015) Quaternary Structure Defines a Large Class of Amyloid-beta Oligomers Neutralized by Sequestration. Cell Rep 11(11):1760-71 |
| abstractText | The accumulation of amyloid-beta (Abeta) as amyloid fibrils and toxic oligomers is an important step in the development of Alzheimer's disease (AD). However, there are numerous potentially toxic oligomers and little is known about their neurological effects when generated in the living brain. Here we show that Abeta oligomers can be assigned to one of at least two classes (type 1 and type 2) based on their temporal, spatial, and structural relationships to amyloid fibrils. The type 2 oligomers are related to amyloid fibrils and represent the majority of oligomers generated in vivo, but they remain confined to the vicinity of amyloid plaques and do not impair cognition at levels relevant to AD. Type 1 oligomers are unrelated to amyloid fibrils and may have greater potential to cause global neural dysfunction in AD because they are dispersed. These results refine our understanding of the pathogenicity of Abeta oligomers in vivo. |
