A Quick Method to Evaluate the Effect of the Amino Acid Sequence in the Misfolding Proneness of the Prion Protein.
Prion diseases or transmissible spongiform encephalopathies (TSEs) are a group of neurodegenerative diseases where the misfolding of the prion protein (PrP) is a crucial event. Based on studies in TSE-affected humans and the generation of transgenic mouse models overexpressing different mutated versions of the PrP, we conclude that both wild-type and mutated PrPs exhibit differential propensity to misfold in vivo. Here, we describe a new method in vitro to assess and quantify the PrP misfolding phenomenon in order to better understand the molecular mechanisms involved in this process.
['Fernández-Borges|Natalia|N|', 'Eraña|Hasier|H|', 'Elezgarai|Saioa R|SR|', 'Harrathi|Chafik|C|', 'Venegas|Vanesa|V|', 'Castilla|Joaquín|J|']
D000595:Amino Acid Sequence D000818:Animals D001681:Biological Assay D001921:Brain D001923:Brain Chemistry D003956:Dialysis D019286:Endopeptidase K D015870:Gene Expression D051379:Mice D018345:Mice, Knockout D018621:PrPC Proteins D018620:PrPSc Proteins D000072757:Protein Conformation, beta-Strand D017510:Protein Folding D011994:Recombinant Proteins D013010:Sonication
In vitro prion propagation PMCA Protein misfolding Spontaneous recombinant prion recPMCA