Bovine PrPC directly interacts with αB-crystalline

Citations of this article
Mendeley users who have this article in their library.


We used a bovine brain cDNA library to perform a yeast two-hybrid assay with bovine mature PrPC as bait. The screening result showed that αB-crystalline interacted with PrPC. The interaction was further evaluated both in vivo and in vitro with different methods, such as immunofluorescent colocalization, native polyacrylamide-gel electrophoresis, and IAsys biosensor assays. The results suggested that αB-crystalline may have the ability to refold denatured prion proteins, and provided first evidence that αB-crystalline is directly associated with prion protein. © 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.




Sun, G., Guo, M., Shen, A., Mei, F., Peng, X., Gong, R., … Xiao, G. (2005). Bovine PrPC directly interacts with αB-crystalline. FEBS Letters, 579(24), 5419–5424.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free