Propagation of PrPSc in mice reveals impact of aggregate composition on prion disease pathogenesis
Sheng Chun Chang, Samia Hannaoui, Maria Immaculata Arifin, Yuan-Hung Huang, Xinli Tang, Holger Wille, Sabine Gilch · 2023
Read Propagation of PrPSc in mice reveals impact of aggregate composition on prion disease pathogenesis by Sheng Chun Chang, Samia Hannaoui, Maria Immaculata Arifin, Yuan-Hung Huang, Xinli Tang, Holger Wille, Sabine Gilch (2023) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-10645910.txt.
Description
Infectious prions consist of PrPSc, a misfolded, aggregation-prone isoform of the host’s prion protein. PrPSc assemblies encode distinct biochemical and biological properties. They harbor a specific profile of PrPSc species, from small oligomers to fibrils in different ratios, where the highest infectivity aligns with oligomeric particles.
Catalog record
| CREATOR | Sheng Chun Chang, Samia Hannaoui, Maria Immaculata Arifin, Yuan-Hung Huang, Xinli Tang, Holger Wille, Sabine Gilch |
|---|---|
| YEAR | 2023 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 56 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |