| Autor: |
Mei GY; Pathogenic Microorganisms Department, Medical School, Anhui University of Science and Technology, Huainan, 232001, China. 06mgy@163.com, Li Y, Wang GR, Zhang BY, Tian C, Chen C, Zhou RM, Wang X, Li XL, Wang KX, Han J, Dong XP |
| Jazyk: |
čínština |
| Zdroj: |
Bing du xue bao = Chinese journal of virology [Bing Du Xue Bao] 2009 May; Vol. 25 (3), pp. 208-12. |
| Abstrakt: |
The molecular interaction between PrP and 14-3-3 beta and the possible interactional domain between two proteins were studied by co-immunoprecipitation, pull down and FRET assays. The results showed that PrP protein could interact with 14-3-3 beta in vitro and in vivo. The domain which responded for the interaction was located at C-terminal of PrP (amino acid residues 106 to 126). This study of the interaction between PrP and 14-3-3 protein further provided the insight into the potential role of 14-3-3 in the biological function of PrP and the pathogenesis of prion disease. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
