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.
CITATION STYLE
Fernández-Borges, N., Eraña, H., Elezgarai, S. R., Harrathi, C., Venegas, V., & Castilla, J. (2017). A quick method to evaluate the effect of the amino acid sequence in the misfolding proneness of the prion protein. In Methods in Molecular Biology (Vol. 1658, pp. 205–216). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7244-9_15
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