Cargando…
In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells
Yeast prion [PSI(+)] is caused by aggregated structures of the Sup35 protein. Although Sup35 forms typical amyloid fibrils in vitro, there is no direct evidence for the fibrillar structures of Sup35 in vivo. We analyzed [PSI(+)] cells in which Sup35 fused with green fluorescent protein (GFP) formed...
Autores principales: | Kawai-Noma, Shigeko, Pack, Chan-Gi, Kojidani, Tomoko, Asakawa, Haruhiko, Hiraoka, Yasushi, Kinjo, Masataka, Haraguchi, Tokuko, Taguchi, Hideki, Hirata, Aiko |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2930275/ https://www.ncbi.nlm.nih.gov/pubmed/20643880 http://dx.doi.org/10.1083/jcb.201002149 |
Ejemplares similares
-
Biased assembly of the nuclear pore complex is required for somatic and germline nuclear differentiation in Tetrahymena
por: Iwamoto, Masaaki, et al.
Publicado: (2015) -
Heterogeneous interaction network of yeast prions and remodeling factors detected in live cells
por: Pack, Chan-Gi, et al.
Publicado: (2017) -
Visualization of secretory cargo transport within the Golgi apparatus
por: Kurokawa, Kazuo, et al.
Publicado: (2019) -
Reconstruction of the kinetochore: a prelude to meiosis
por: Asakawa, Haruhiko, et al.
Publicado: (2007) -
Physical breakdown of the nuclear envelope is not necessary for breaking its barrier function
por: Asakawa, Haruhiko, et al.
Publicado: (2011)