Chapter title |
A Quick Method to Evaluate the Effect of the Amino Acid Sequence in the Misfolding Proneness of the Prion Protein
|
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Chapter number | 15 |
Book title |
Prions
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Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-7244-9_15 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7242-5, 978-1-4939-7244-9
|
Authors |
Natalia Fernández-Borges, Hasier Eraña, Saioa R. Elezgarai, Chafik Harrathi, Vanesa Venegas, Joaquín Castilla, Fernández-Borges, Natalia, Eraña, Hasier, Elezgarai, Saioa R., Harrathi, Chafik, Venegas, Vanesa, Castilla, Joaquín |
Abstract |
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. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Unknown | 5 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 2 | 40% |
Researcher | 2 | 40% |
Unknown | 1 | 20% |
Readers by discipline | Count | As % |
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Biochemistry, Genetics and Molecular Biology | 2 | 40% |
Immunology and Microbiology | 1 | 20% |
Neuroscience | 1 | 20% |
Unknown | 1 | 20% |