The native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro
Abstract The conversion of globular proteins into amyloid fibrils is associated with a wide variety of human diseases. One example is the prion protein (PrP), which adopts an α-helical structure in the native state but its amyloid form is implicated in the pathogenesis of prion diseases. Previous ev...
Guardado en:
Autores principales: | Ryo P. Honda, Kazuo Kuwata |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2017
|
Materias: | |
Acceso en línea: | https://doaj.org/article/8126e4635924452a844f306dd1a48911 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Canine D163-PrP polymorphic variant does not provide complete protection against prion infection in small ruminant PrP context
por: Alba Marín-Moreno, et al.
Publicado: (2021) -
PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.
por: Mourad Tayebi, et al.
Publicado: (2011) -
Paracrine diffusion of PrP(C) and propagation of prion infectivity by plasma membrane-derived microvesicles.
por: Vincenzo Mattei, et al.
Publicado: (2009) -
Propagation of RML prions in mice expressing PrP devoid of GPI anchor leads to formation of a novel, stable prion strain.
por: Sukhvir Paul Mahal, et al.
Publicado: (2012) -
Regulating factors of PrP glycosylation in Creutzfeldt-Jakob disease--implications for the dissemination and the diagnosis of human prion strains.
por: Etienne Levavasseur, et al.
Publicado: (2008)