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...
Main Authors: | Michael B Miller, James C Geoghegan, Surachai Supattapone |
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Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2011-07-01
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Series: | PLoS Pathogens |
Online Access: | http://europepmc.org/articles/PMC3136465?pdf=render |
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