Cargando…
Characterization of Amyloid Cores in Prion Domains
Amyloids consist of repetitions of a specific polypeptide chain in a regular cross-β-sheet conformation. Amyloid propensity is largely determined by the protein sequence, the aggregation process being nucleated by specific and short segments. Prions are special amyloids that become self-perpetuating...
Autores principales: | Sant’Anna, Ricardo, Fernández, Maria Rosario, Batlle, Cristina, Navarro, Susanna, de Groot, Natalia S., Serpell, Louise, Ventura, Salvador |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5043269/ https://www.ncbi.nlm.nih.gov/pubmed/27686217 http://dx.doi.org/10.1038/srep34274 |
Ejemplares similares
-
Characterization of Soft Amyloid Cores in Human Prion-Like Proteins
por: Batlle, Cristina, et al.
Publicado: (2017) -
Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria
por: Macedo, Bruno, et al.
Publicado: (2015) -
Functionalized Prion-Inspired Amyloids for Biosensor
Applications
por: Díaz-Caballero, Marta, et al.
Publicado: (2021) -
Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis
por: Pallarès, Irantzu, et al.
Publicado: (2018) -
MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation
por: Batlle, Cristina, et al.
Publicado: (2021)