Published January 1, 2017
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A Quick Method to Evaluate the Effect of the Amino Acid Sequence in the Misfolding Proneness of the Prion Protein
- 1. CIC bioGUNE, Parque Tecnológico de Bizkaia, Derio, 48160, Bizkaia, Spain.
- 2. CIC bioGUNE, Parque Tecnológico de Bizkaia, Derio, 48160, Bizkaia, Spain
- 3. CIC bioGUNE, Parque Tecnológico de Bizkaia, Derio, 48160, Bizkaia, Spain. IKERBASQUE, Basque Foundation for Science, Bilbao, 48013, Bizkaia, Spain.
Description
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.
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