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Sheng Wu Gong Cheng Xue Bao. 2011 Oct;27(10):1401-7.

[Mechanism and application of molecular self-assembly in Sup35 prion domain of Saccharomyces cerevisiae].

[Article in Chinese]

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State Key Laboratory ofAgricultural Microbiology, National Engineering Research Center of Microbial Pesticides, Huazhong Agricultural University, Wuhan 430070, China.


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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