Dissociation of Infectivity from Seeding Ability in Prions with Alternate Docking Mechanism

Previous studies identified two mammalian prion protein (PrP) polybasic domains that bind the disease-associated conformer PrP(Sc), suggesting that these domains of cellular prion protein (PrP(C)) serve as docking sites for PrP(Sc) during prion propagation. To examine the role of polybasic domains i...

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Detalles Bibliográficos
Autores principales: Miller, Michael B., Geoghegan, James C., Supattapone, Surachai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3136465/
https://www.ncbi.nlm.nih.gov/pubmed/21779169
http://dx.doi.org/10.1371/journal.ppat.1002128

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3136465/
https://www.ncbi.nlm.nih.gov/pubmed/21779169
http://dx.doi.org/10.1371/journal.ppat.1002128

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