Cargando…
Rabbit PrP Is Partially Resistant to in vitro Aggregation Induced by Different Biological Cofactors
Prion diseases have been described in humans and other mammals, including sheep, goats, cattle, and deer. Since mice, hamsters, and cats are susceptible to prion infection, they are often used to study the mechanisms of prion infection and conversion. Mammals, such as horses and dogs, however, do no...
Autores principales: | Angelli, Juliana N., Passos, Yulli M., Brito, Julyana M. A., Silva, Jerson L., Cordeiro, Yraima, Vieira, Tuane C. R. G. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8249948/ https://www.ncbi.nlm.nih.gov/pubmed/34220442 http://dx.doi.org/10.3389/fnins.2021.689315 |
Ejemplares similares
-
Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria
por: Macedo, Bruno, et al.
Publicado: (2015) -
Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids
por: Macedo, Bruno, et al.
Publicado: (2017) -
Phase separation of p53 precedes aggregation and is affected by oncogenic mutations and ligands
por: Petronilho, Elaine C., et al.
Publicado: (2021) -
PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions
por: Barron, Rona M., et al.
Publicado: (2016) -
Prion Protein Complexed to N2a Cellular RNAs through Its N-terminal Domain Forms Aggregates and Is Toxic to Murine Neuroblastoma Cells
por: Gomes, Mariana P. B., et al.
Publicado: (2008)