| First Author | Luo JC | Year | 2012 |
| Journal | FEBS Lett | Volume | 586 |
| Issue | 6 | Pages | 680-5 |
| PubMed ID | 22449963 | Mgi Jnum | J:201296 |
| Mgi Id | MGI:5512941 | Doi | 10.1016/j.febslet.2012.01.062 |
| Citation | Luo JC, et al. (2012) Formation of amyloid fibrils from beta-amylase. FEBS Lett 586(6):680-5 |
| abstractText | Fibril formation has been considered a significant feature of amyloid proteins. However, it has been proposed that fibril formation is a common property of many proteins under appropriate conditions. We studied the fibril formation of beta-amylase, a non-amyloid protein rich in alpha-helical structure, because the secondary structure of beta-amylase is similar to that of prions. With the conditions for the fibril formation of prions, beta-amylase proteins were converted into amyloid fibrils. The features of beta-amylase proteins and fibrils are compared to prion proteins and fibrils. Furthermore, the cause of neurotoxicity in amyloid diseases is discussed. |
