A stretch of residues within the protease-resistant core is not necessary for prion structure and infectivity

Mapping out regions of PrP influencing prion conversion remains a challenging issue complicated by the lack of prion structure. The portion of PrP associated with infectivity contains the α-helical domain of the correctly folded protein and turns into a β-sheet-rich insoluble core in prions. Deletio...

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Detalhes bibliográficos
Publicado no:Prion
Main Authors: Munoz-Montesino, Carola, Sizun, Christina, Moudjou, Mohammed, Herzog, Laetitia, Reine, Fabienne, Igel-Egalon, Angelique, Barbereau, Clément, Chapuis, Jérôme, Ciric, Danica, Laude, Hubert, Béringue, Vincent, Rezaei, Human, Dron, Michel
Formato: Artigo
Idioma:Inglês
Publicado em: Taylor & Francis 2017
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC5360129/
https://ncbi.nlm.nih.gov/pubmed/28281924
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1080/19336896.2016.1274851
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