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• W2023252383 endingPage "13442" @default.
• W2023252383 startingPage "13439" @default.
• W2023252383 abstract "ABSTRACT Prions are composed mainly, if not entirely, of PrP Sc , an infectious misfolded isoform of PrP C , the normal isoform of the prion protein. Here we show that protein misfolding cyclic amplification (PMCA)-generated hypertransmissible mink encephalopathy (HY TME) PrP Sc is highly infectious and has a titer that is similar, if not identical, to that associated with brain tissue from animals infected with the HY TME agent that are in the terminal stage of disease. These data demonstrate that PMCA efficiently replicates the prion agent and provide further support for the hypothesis that in vitro -generated prions are bona fide and are not due to contamination." @default.
• W2023252383 created "2016-06-24" @default.
• W2023252383 creator A5049941183 @default.
• W2023252383 creator A5080657235 @default.
• W2023252383 date "2011-12-15" @default.
• W2023252383 modified "2023-10-18" @default.
• W2023252383 title "<i>In Vitro</i> Generation of High-Titer Prions" @default.
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• W2023252383 doi "https://doi.org/10.1128/jvi.06134-11" @default.
• W2023252383 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3233131" @default.
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• W2023252383 hasPublicationYear "2011" @default.
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