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@ARTICLE{Redecke:94625,
      author       = {Redecke, L. and Binder, S. and Elmallah, M. I. Y. and
                      Broadbent, R. and Tilkorn, C. and Schulz, B. and May, P. and
                      Goos, A. and Ruebhausen, M. and Betzel, C. and DESY},
      title        = {{UV} light induced conversion and aggregation of prion
                      proteins.},
      journal      = {Free radical biology and medicine},
      volume       = {46},
      issn         = {0891-5849},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-20359},
      pages        = {1353-1361},
      year         = {2009},
      note         = {© Elsevier Inc.},
      abstract     = {Increasing evidence suggests a central role for oxidative
                      stress in the pathology of prion diseases, a group of fatal
                      neurodegenerative disorders associated with structural
                      conversion of the prion protein (PrP). Because
                      UV-light-induced protein damage is mediated by direct
                      photo-oxidation and radical reactions, we investigated the
                      structural consequences of UVB radiation on recombinant
                      murine and human prion proteins at pH 7.4 and pH 5.0. As
                      revealed by circular dichroism and dynamic light scattering
                      measurements, the observed PrP aggregation follows two
                      independent pathways: (i) complete unfolding of the protein
                      structure associated with rapid precipitation or (ii)
                      specific structural conversion into distinct soluble
                      beta-oligomers. The choice of pathway was directly
                      attributed to the chromophoric properties of the PrP species
                      and the susceptibility to oxidation. Regarding size, the
                      oligomers characterized in this study share a high degree of
                      identity with oligomeric species formed after structural
                      destabilization induced by other triggers, which
                      significantly strengthens the theory that partly unfolded
                      intermediates represent initial precursor molecules
                      directing the pathway of PrP aggregation. Moreover, we
                      identified the first suitable photo-trigger capable of
                      inducing refolding of PrP, which has an important
                      biotechnological impact in terms of analyzing the conversion
                      process on small time scales.},
      keywords     = {Animals / Circular Dichroism / Humans / Mice /
                      Oxidation-Reduction / PrPC Proteins: chemistry / PrPC
                      Proteins: radiation effects / PrPSc Proteins: chemistry /
                      PrPSc Proteins: radiation effects / Prion Diseases: etiology
                      / Prion Diseases: physiopathology / Protein Conformation /
                      Protein Folding / Protein Multimerization / Protein
                      Processing, Post-Translational / Recombinant Proteins:
                      chemistry / Recombinant Proteins: radiation effects /
                      Solubility / Ultraviolet Rays / PrPC Proteins (NLM
                      Chemicals) / PrPSc Proteins (NLM Chemicals) / Recombinant
                      Proteins (NLM Chemicals)},
      cin          = {EMBL(-2012)},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline D1.2 (POF1-550)},
      pid          = {G:(DE-H253)POF1-D1.2-20130405},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19249347},
      UT           = {WOS:000267322900005},
      doi          = {10.1016/j.freeradbiomed.2009.02.013},
      url          = {https://bib-pubdb1.desy.de/record/94625},
}