Cargando…
Qualitative and Quantitative Multiplexed Proteomic Analysis of Complex Yeast Protein Fractions That Modulate the Assembly of the Yeast Prion Sup35p
BACKGROUND: The aggregation of the baker's yeast prion Sup35p is at the origin of the transmissible [PSI(+)] trait. We and others have shown that molecular chaperones modulate Sup35p aggregation. However, other protein classes might be involved in [PSI(+)] formation. RESULTS: We designed a func...
Autores principales: | Redeker, Virginie, Hughes, Chris, Savistchenko, Jimmy, Vissers, Johannes P. C., Melki, Ronald |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3172207/ https://www.ncbi.nlm.nih.gov/pubmed/21931608 http://dx.doi.org/10.1371/journal.pone.0023659 |
Ejemplares similares
-
In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells
por: Kawai-Noma, Shigeko, et al.
Publicado: (2010) -
The 26S Proteasome Degrades the Soluble but Not the Fibrillar Form of the Yeast Prion Ure2p In Vitro
por: Wang, Kai, et al.
Publicado: (2015) -
Nonsense Mutations in the Yeast SUP35 Gene Affect the [PSI(+)] Prion Propagation
por: Trubitsina, Nina P., et al.
Publicado: (2020) -
Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants
por: Dergalev, Alexander A., et al.
Publicado: (2019) -
Sup35p in Its Soluble and Prion States Is Packaged inside Extracellular Vesicles
por: Kabani, Mehdi, et al.
Publicado: (2015)