Misfolded PrP impairs the UPS by interaction with the 20S proteasome and inhibition of substrate entry

Prion diseases are associated with the conversion of cellular prion protein (PrP(C)) to toxic β-sheet isoforms (PrP(Sc)), which are reported to inhibit the ubiquitin-proteasome system (UPS). Accordingly, UPS substrates accumulate in prion-infected mouse brains, suggesting impairment of the 26S prote...

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Bibliographic Details
Main Authors:	Deriziotis, Pelagia, André, Ralph, Smith, David M, Goold, Rob, Kinghorn, Kerri J, Kristiansen, Mark, Nathan, James A, Rosenzweig, Rina, Krutauz, Dasha, Glickman, Michael H, Collinge, John, Goldberg, Alfred L, Tabrizi, Sarah J
Format:	Artigo
Language:	Inglês
Published:	Nature Publishing Group 2011
Subjects:	Article
Online Access:	https://ncbi.nlm.nih.gov/pmc/articles/PMC3160194/ https://ncbi.nlm.nih.gov/pubmed/21743439 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/emboj.2011.224
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Misfolded PrP impairs the UPS by interaction with the 20S proteasome and inhibition of substrate entry

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