Investigating the conformational stability of prion strains through a kinetic replication model.
Prion proteins are known to misfold into a range of different aggregated forms, showing different phenotypic and pathological states. Understanding strain specificities is an important problem in the field of prion disease. Little is known about which PrP(Sc) structural properties and molecular mech...
Guardado en:
Autores principales: | Mattia Zampieri, Giuseppe Legname, Claudio Altafini |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2009
|
Materias: | |
Acceso en línea: | https://doaj.org/article/02b61d6446504e58aa83389939e67aa5 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.
por: Florent Laferrière, et al.
Publicado: (2013) -
Continuous quinacrine treatment results in the formation of drug-resistant prions.
por: Sina Ghaemmaghami, et al.
Publicado: (2009) -
Artificial strain of human prions created in vitro
por: Chae Kim, et al.
Publicado: (2018) -
Alteration of Prion Strain Emergence by Nonhost Factors
por: Sara A. M. Holec, et al.
Publicado: (2019) -
Prion strains depend on different endocytic routes for productive infection
por: Andrea Fehlinger, et al.
Publicado: (2017)