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@ARTICLE{Marbach:150199,
      author       = {Marbach, Jendrik and Zentis, Peter and Ellinger, Philipp
                      and Müller, Henrik and Birkmann, Eva},
      title        = {{E}xpression and characterisation of fully
                      posttranslationally modified cellular prion protein in
                      {P}ichia pastoris},
      journal      = {Biological chemistry},
      volume       = {394},
      number       = {11},
      issn         = {1437-4315},
      address      = {Berlin [u.a.]},
      publisher    = {de Gruyter},
      reportid     = {FZJ-2014-00278},
      pages        = {1475-1483},
      year         = {2013},
      abstract     = {Prion 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.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000325717100011},
      doi          = {10.1515/hsz-2013-0180},
      url          = {https://juser.fz-juelich.de/record/150199},
}