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Prion protein insertional mutations increase aggregation propensity but not fiber stability
BACKGROUND: Mutations in the PRNP gene account for ~15% of all prion disease cases. Little is understood about the mechanism of how some of these mutations in PRNP cause the protein to aggregate into amyloid fibers or cause disease. We have taken advantage of a chimeric protein system to study the o...
| Autores principales: | , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
BioMed Central
2008
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2276218/ https://www.ncbi.nlm.nih.gov/pubmed/18366654 http://dx.doi.org/10.1186/1471-2091-9-7 |