Mechanism and application of molecular self-assembly in Sup35 prion domain of Saccharomyces cerevisiae / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 1401-1407, 2011.
Artículo
en Chino
| WPRIM
| ID: wpr-304563
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.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Conformación Proteica
/
Saccharomyces cerevisiae
/
Priones
/
Datos de Secuencia Molecular
/
Química
/
Factores de Terminación de Péptidos
/
Secuencia de Aminoácidos
/
Proteínas de Saccharomyces cerevisiae
/
Genética
/
Amiloide
Tipo de estudio:
Estudio pronóstico
Idioma:
Chino
Revista:
Chinese Journal of Biotechnology
Año:
2011
Tipo del documento:
Artículo
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