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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...

詳細記述

保存先:
書誌詳細
主要な著者: Yedidia, Yifat, Horonchik, Lior, Tzaban, Salit, Yanai, Anat, Taraboulos, Albert
フォーマット: Artigo
言語:Inglês
出版事項: Oxford University Press 2001
主題:
オンライン・アクセス: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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