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  • Title: [Mechanism and application of molecular self-assembly in Sup35 prion domain of Saccharomyces cerevisiae].
    Author: Yin W, He J, Yu Z, Wang J.
    Journal: Sheng Wu Gong Cheng Xue Bao; 2011 Oct; 27(10):1401-7. PubMed ID: 22260056.
    Abstract:
    Sup35 in its native state is a translation termination factor in Saccharomyces cerevisiae. The prion domain of Sup35p can form amyloid-like proteinaceous fibrils in vitro and in vivo. Furthermore, the in-register cross beta-sheet structure of Sup35p amyloid fibrils is similar to those formed in other species. Therefore, studies on mechanism of Sup35p self-assembly can be an appropriate model to study protein misfolding-related diseases and prion biology. Because of its ability to self-assemble into nanowires, the prion domain of Sup35p has been widely used in biotechnology and nanotechnology.
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