Low Density Subcellular Fractions Enhance Disease-specific Prion Protein Misfolding
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference45 articles.
1. Nobel Lecture: Prions
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4. Recombinant prion protein induces a new transmissible prion disease in wild-type animals
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1. PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions;Acta Neuropathologica;2016-07-04
2. Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein;Scientific Reports;2015-10-22
3. The Glycosylation Status of PrPCIs a Key Factor in Determining Transmissible Spongiform Encephalopathy Transmission between Species;Journal of Virology;2015-02-11
4. Lysine hydroxylation and O-glycosylation in the globular, C-terminal region of mammalian-expressed, recombinant PrP;International Journal of Mass Spectrometry;2013-07
5. The PrPC C1 fragment derived from the ovine A136R154R171 PRNP allele is highly abundant in sheep brain and inhibits fibrillisation of full-length PrPC protein in vitro;Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease;2013-06
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