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@ARTICLE{Elfrink:340,
      author       = {Elfrink, K. and Ollesch, J. and Stoehr, J. and Willbold, D.
                      and Riesner, D. and Gerwert, K.},
      title        = {{S}tructural changes of membrane-anchored native {P}r{P}c},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {105},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PreJuSER-340},
      pages        = {10815 - 10819},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Misfolding and subsequent aggregation of endogenous
                      proteins constitute essential steps in many human disorders,
                      including Alzheimer and prion diseases. In most prion
                      protein-folding studies, the posttranslational
                      modifications, the lipid anchor in particular, were lacking.
                      Here, we studied a fully posttranslationally modified
                      cellular prion protein, carrying two N-glycosylations and
                      the natural GPI anchor. We used time-resolved FTIR to study
                      the prion protein secondary structure changes when binding
                      to a raft-like lipid membrane via its GPI anchor. We
                      observed that membrane anchoring above a threshold
                      concentration induced refolding of the prion protein to
                      intermolecular beta-sheets. Such transition is not observed
                      in solution and is membrane specific. Excessive membrane
                      anchoring, analyzed with molecular sensitivity, is thought
                      to be a crucial event in the development of prion diseases.},
      keywords     = {Animals / Cricetinae / Membrane Proteins: genetics /
                      Mesocricetus / Models, Molecular / PrPC Proteins: genetics /
                      Protein Conformation / Protein Folding / Spectroscopy,
                      Fourier Transform Infrared / Membrane Proteins (NLM
                      Chemicals) / PrPC Proteins (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {000},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18669653},
      pmc          = {pmc:PMC2504809},
      UT           = {WOS:000258308500036},
      doi          = {10.1073/pnas.0804721105},
      url          = {https://juser.fz-juelich.de/record/340},
}