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@ARTICLE{Elmallah:168223,
      author       = {Elmallah, Mohammed IY and Borgmeyer, Uwe and Betzel,
                      Christian and Redecke, Lars},
      title        = {{I}mpact of methionine oxidation as an initial event on the
                      pathway of human prion protein conversion},
      journal      = {Prion},
      volume       = {7},
      number       = {5},
      issn         = {1933-690X},
      address      = {Austin, Tex.},
      publisher    = {Landes Bioscience},
      reportid     = {DESY-2014-02424},
      pages        = {404 - 411},
      year         = {2013},
      note         = {© Landes Bioscience; Post referee fulltext in progress;
                      Embargo 12 months from publication},
      abstract     = {Prion diseases comprise a group of fatal neurodegenerative
                      disorders characterized by the autocatalytic conversion of
                      the cellular prion protein PrP(C) into the infectious
                      misfolded isoform PrP(Sc). Increasing evidence supports a
                      specific role of oxidative stress in the onset of
                      pathogenesis. Although the associated molecular mechanisms
                      remain to be elucidated in detail, several studies currently
                      suggest that methionine oxidation already detected in
                      misfolded PrP(Sc) destabilizes the native PrP fold as an
                      early event in the conversion pathway. To obtain more
                      insights about the specific impact of surface-exposed
                      methionine residues on the oxidative-induced conversion of
                      human PrP we designed, produced, and comparatively
                      investigated two new pseudosulfoxidation mutants of human
                      PrP 121-231 that comprises the well-folded C-terminal
                      domain. Applying circular dichroism spectroscopy and dynamic
                      light scattering techniques we showed that
                      pseudosulfoxidation of all surface exposed Met residues
                      formed a monomeric molten globule-like species with striking
                      similarities to misfolding intermediates recently reported
                      by other groups. However, individual pseudosulfoxidation at
                      the polymorphic M129 site did not significantly contribute
                      to the structural destabilization. Further metal-induced
                      oxidation of the partly unfolded pseudosulfoxidation mutant
                      resulted in the formation of an oligomeric state that shares
                      a comparable size and stability with PrP oligomers detected
                      after the application of different other triggers for
                      structural conversion, indicating a generic misfolding
                      pathway of PrP. The obtained results highlight the specific
                      importance of methionine oxidation at surface exposed
                      residues for PrP misfolding, strongly supporting the
                      hypothesis that increased oxidative stress could be one
                      causative event for sporadic prion diseases and other
                      neurodegenerative disorders.},
      cin          = {EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {FS Beamline without reference (POF2-544)},
      pid          = {G:(DE-H253)POF2-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000327383600007},
      pubmed       = {pmid:24121542},
      doi          = {10.4161/pri.26745},
      url          = {https://bib-pubdb1.desy.de/record/168223},
}