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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Библиографические подробности

Опубликовано в::	EMBO J
Главные авторы:	Yedidia, Yifat, Horonchik, Lior, Tzaban, Salit, Yanai, Anat, Taraboulos, Albert
Формат:	Artigo
Язык:	Inglês
Опубликовано:	Nature Publishing Group 2001
Предметы:	Article
Online-ссылка:	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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