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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...
Autores principales: | Miller, Michael B., Geoghegan, James C., Supattapone, Surachai |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2011
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Materias: | |
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 |
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