Ubiquitin Ligase gp78 Targets Unglycosylated Prion Protein PrP for Ubiquitylation and Degradation

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Shao, Jia; Choe, Vitnary; Cheng, Haili; Tsai, Yien Che; Weissman, Allan M.; Luo, Shiwen; Rao, Hai;
  • Publisher: Public Library of Science
  • Journal: PLoS ONE,volume 9,issue 4 (issn: 1932-6203, eissn: 1932-6203)
  • Publisher copyright policies & self-archiving
  • Related identifiers: pmc: PMC3979651, doi: 10.1371/journal.pone.0092290
  • Subject: Cellular Stress Responses | Research Article | Biology and Life Sciences | Molecular Cell Biology | Veterinary Science | Protein Metabolism | Veterinary Diseases | Infectious Diseases | Cell Growth | Zoonoses | Medicine | Cell Processes | Q | R | Cell Biology | Prion Diseases | Science | Biochemistry | Metabolism | Medicine and Health Sciences | Veterinary Prion Diseases
    mesheuropmc: nervous system diseases | animal diseases

Prion protein PrP is a central player in several devastating neurodegenerative disorders, including mad cow disease and Creutzfeltd-Jacob disease. Conformational alteration of PrP into an aggregation-prone infectious form PrPSc can trigger pathogenic events. How levels ... View more
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