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| Content Provider | Springer Nature Link |
|---|---|
| Author | Wang, Gailing Wang, Mingcheng Li, Chuanfeng |
| Copyright Year | 2015 |
| Abstract | According to the “protein-only” hypothesis, the misfolding and conversion of host-derived cellular prion protein (PrP$^{C}$) into pathogenically misfolded PrP are believed to be the key procedure in the pathogenesis of prion diseases. Intermediate, soluble oligomeric prion protein (PrP) aggregates were considered a critical process for prion diseases. Several independent studies on PrP oligomers gained insights into oligomers’ formation, biophysical and biochemical characteristics, structure conversion, and neurotoxicity. PrP oligomers are rich in β-sheet structure and slightly resistant to proteinase K digestion. PrP oligomers exhibited more neurotoxicity and induced neuronal apoptosis in vivo and/or in vitro. In this review, we summarized recent studies regarding PrP oligomers and the relationship between misfolded PrP aggregates and neuronal death in the course of prion diseases. |
| Starting Page | 932 |
| Ending Page | 937 |
| Page Count | 6 |
| File Format | |
| ISSN | 08958696 |
| Journal | Journal of Molecular Neuroscience |
| Volume Number | 56 |
| Issue Number | 4 |
| e-ISSN | 15591166 |
| Language | English |
| Publisher | Springer US |
| Publisher Date | 2015-04-01 |
| Publisher Place | New York |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Prion diseases Prion protein Oligomers Neurotoxicity Neurosciences Neurochemistry Cell Biology Proteomics Neurology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Cellular and Molecular Neuroscience |
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