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000150199 1001_ $$0P:(DE-HGF)0$$aMarbach, Jendrik$$b0
000150199 245__ $$aExpression and characterisation of fully posttranslationally modified cellular prion protein in Pichia pastoris
000150199 260__ $$aBerlin [u.a.]$$bde Gruyter$$c2013
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000150199 520__ $$aPrion diseases are fatal neurodegenerative diseases which occur as sporadic, genetic, and transmissible disorders. A molecular hallmark of prion diseases is the conformational conversion of the host-encoded cellular form of the prion protein (PrPC) into its misfolded pathogenic isoform (PrPSc). PrPSc is the main component of the pathological and infectious prion agent. The study of the conversion mechanism from PrPC to PrPSc is a major field in prion research. PrPC is glycosylated and attached to the plasma membrane via its glycosyl phosphatidyl inositol (GPI)-anchor. In this study we established and characterised the expression of fully posttranslationally modified mammalian Syrian golden hamster PrPC in the yeast Pichia pastoris using native PrPC-specific N- and C-terminal signal sequences. In vivo as well as in vitro-studies demonstrated that the signal sequences controlled posttranslational processing and trafficking of native PrPC, resulting in PrPC localised in the plasma membrane of P. pastoris. In addition, the glycosylation pattern of native PrPC could be confirmed.
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000150199 7001_ $$0P:(DE-HGF)0$$aZentis, Peter$$b1
000150199 7001_ $$0P:(DE-HGF)0$$aEllinger, Philipp$$b2
000150199 7001_ $$0P:(DE-Juel1)132017$$aMüller, Henrik$$b3$$ufzj
000150199 7001_ $$0P:(DE-Juel1)131992$$aBirkmann, Eva$$b4$$eCorresponding author$$ufzj
000150199 773__ $$0PERI:(DE-600)1466062-3$$a10.1515/hsz-2013-0180$$gVol. 394, no. 11$$n11$$p1475-1483$$tBiological chemistry$$v394$$x1437-4315$$y2013
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