Cargando…
Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core
Self-templating assemblies of the human prion protein are clinically associated with transmissible spongiform encephalopathies. Here we present the cryo-EM structure of a denaturant- and protease-resistant fibril formed in vitro spontaneously by a 9.7kDa unglycosylated fragment of the human prion pr...
Autores principales: | Glynn, Calina, Sawaya, Michael R., Ge, Peng, Gallagher-Jones, Marcus, Short, Connor W., Bowman, Ronquiajah, Apostol, Marcin, Zhou, Z. Hong, Eisenberg, David, Rodriguez, Jose A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7338044/ https://www.ncbi.nlm.nih.gov/pubmed/32284600 http://dx.doi.org/10.1038/s41594-020-0403-y |
Ejemplares similares
-
Sub-ångstrom cryo-EM structure of a prion protofibril reveals a polar clasp
por: Gallagher-Jones, Marcus, et al.
Publicado: (2018) -
Cryo-EM Structures of Four Polymorphic TDP-43 Amyloid Cores
por: Cao, Qin, et al.
Publicado: (2019) -
Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils
por: Cao, Qin, et al.
Publicado: (2020) -
Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation
por: Abskharon, Romany, et al.
Publicado: (2022) -
Crystallographic Studies of Prion Protein (PrP) Segments Suggest How Structural Changes Encoded by Polymorphism at Residue 129 Modulate Susceptibility to Human Prion Disease
por: Apostol, Marcin I., et al.
Publicado: (2010)