Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2053109 | FEBS Letters | 2005 | 6 Pages |
Abstract
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.
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Authors
Guihong Sun, Mingxiong Guo, Ao Shen, Fanghua Mei, Xiaoxue Peng, Rui Gong, Deyin Guo, Jianguo Wu, Po Tien, Gengfu Xiao,