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Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
Prion diseases propagate by converting a normal glycoprotein of the host, PrP(C), into a pathogenic ‘prion’ conformation. Several misfolding mutants of PrP(C) are degraded through the ER-associated degradation (ERAD)–proteasome pathway. In their infectious form, prion diseases such as bovine spongif...
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| Hauptverfasser: | , , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
Oxford University Press
2001
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC125653/ https://ncbi.nlm.nih.gov/pubmed/11574470 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/20.19.5383 |
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