Mutations alter RNA-mediated conversion of human prions
| Autor: | Ulrich H. E. Hansmann, Izra D. Lodangco, Erik J. Alred, Jennifer Gallaher |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Initial Seed General Chemical Engineering animal diseases Scrapie Biology 010402 general chemistry 01 natural sciences Article lcsh:Chemistry 03 medical and health sciences 0103 physical sciences medicine 030304 developmental biology Sequence (medicine) Fatal familial insomnia 0303 health sciences 010304 chemical physics RNA General Chemistry medicine.disease 0104 chemical sciences nervous system diseases 3. Good health Cell biology 030104 developmental biology lcsh:QD1-999 Protein folding |
| Zdroj: | ACS Omega ACS Omega, Vol 3, Iss 4, Pp 3936-3944 (2018) |
| DOI: | 10.1101/235879 |
| Popis: | Prion diseases are connected with self-replication and self-propagation of mis-folded proteins. The rate-limiting factor is the formation of the initial seed. We have recently studied early stages in the conversion between functional PrPC and the infectious scrapie PrPSC form, triggered by the binding of RNA. Here, we study how this process is modulated by the prion sequence. We focus on residues 129 and 178, which are connected to the hereditary neurodegenerative disease Fatal Familial Insomnia. |
| Databáze: | OpenAIRE |
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