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...
保存先:
| 出版年: | EMBO J |
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| 主要な著者: | , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Nature Publishing Group
2001
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC125653/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11574470/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/emboj/20.19.5383 |
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