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@ARTICLE{Rehders:94432,
      author       = {Rehders, D. and Claasen, B. and Redecke, L. and Buschke, A.
                      and Reibe, C. and Jehmlich, N. and von Bergen, M. and
                      Betzel, C. and Meyer, B. and DESY},
      title        = {{P}eptide {NMHRYPNQ} of the cellular prion protein
                      ({P}r{P}({C})) inhibits aggregation and is a potential key
                      for understanding prion-prion interactions.},
      journal      = {Journal of molecular biology},
      volume       = {392},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-19404},
      pages        = {198-207},
      year         = {2009},
      note         = {© Elsevier Ltd.; Post referee fulltext in progress 2;
                      Embargo 12 months from publication},
      abstract     = {Pathogenesis of transmissible spongiform encephalopathies
                      is correlated with a conversion of the normal cellular form
                      of the prion protein (PrP(C)) into the abnormal isoform
                      (scrapie form of PrP). Contact of the normal PrP with its
                      abnormal isoform, the scrapie form of PrP, induces the
                      transformation. Knowledge of molecules that inhibit such
                      contacts leads to an understanding of the mechanism of the
                      aggregation, and these molecules may serve as leads for
                      drugs against transmissible spongiform encephalopathies.
                      Therefore, we screened a synthetic octapeptide library of
                      the globular domain of the human PrP(C) for binding affinity
                      to PrP(C). Two fragments with binding affinity,
                      149YYRENMHR156 and 153NMHRYPNQ160, were identified with K(d)
                      values of 21 and 25 microM, respectively. A 10-fold excess
                      of peptide 153NMHRYPNQ160 inhibits aggregation of the PrP by
                      $99\%.$ NMR and mass spectrometry showed that the binding
                      region of the peptide 153NMHRYPNQ160 is located at helix 3
                      of the PrP.},
      keywords     = {Drug Evaluation, Preclinical / Humans / Kinetics / Magnetic
                      Resonance Spectroscopy / Mass Spectrometry / Models,
                      Molecular / Peptide Library / Peptides: pharmacology /
                      Prions: antagonists $\&$ inhibitors / Prions: metabolism /
                      Protein Binding / Protein Structure, Tertiary / Peptide
                      Library (NLM Chemicals) / Peptides (NLM Chemicals) / Prions
                      (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:19607841},
      UT           = {WOS:000270123600016},
      doi          = {10.1016/j.jmb.2009.07.014},
      url          = {https://bib-pubdb1.desy.de/record/94432},
}