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Document type:
Journal Article; Research Support, Non-U.S. Gov't 
Author(s):
Nunziante, M; Ackermann, K; Dietrich, K; Wolf, H; Gädtke, L; Gilch, S; Vorberg, I; Groschup, M; Schätzl, HM 
Title:
Proteasomal dysfunction and endoplasmic reticulum stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of pathologic prion protein. 
Abstract:
A conformational change of the cellular prion protein (PrP(c)) underlies formation of PrP(Sc), which is closely associated with pathogenesis and transmission of prion diseases. The precise conformational prerequisites and the cellular environment necessary for this post-translational process remain to be completely elucidated. At steady state, glycosylated PrP(c) is found primarily at the cell surface, whereas a minor fraction of the population is disposed of by the ER-associated degradation-pro...    »
 
Journal title abbreviation:
J Biol Chem 
Year:
2011 
Journal volume:
286 
Journal issue:
39 
Pages contribution:
33942-53 
Language:
eng 
Fulltext / DOI:
Print-ISSN:
0021-9258 
TUM Institution:
Institut für Virologie