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@ARTICLE{Mangels:6512,
      author       = {Mangels, C. and Frank, A.O. and Ziegler, J. and
                      Klingenstein, R. and Schweimer, K. and Willbold, D. and
                      Korth, C. and Rösch, P. and Schwarzinger, S.},
      title        = {{B}inding of {TCA} to the prion protein: mechanism,
                      implication for therapy, and application as probe for
                      complex formation of bio-macromolecules},
      journal      = {Journal of biomolecular structure $\&$ dynamics},
      volume       = {27},
      issn         = {0739-1102},
      address      = {Guilderland, NY},
      publisher    = {Adenine Press},
      reportid     = {PreJuSER-6512},
      pages        = {163 - 170},
      year         = {2009},
      note         = {We thank Dr. Vilma Martins for providing a plasmid with the
                      human PRNP-gene. Financial support from the Bavarian Prion
                      Research Platform (ForPrion) and the Volkswagen-Stiftung
                      (1/79968) is gratefully acknowledged.},
      abstract     = {Tricyclic aromatic compounds (TCA) are promising candidates
                      for treatment of transmissible spongiform encephalopathies.
                      Direct binding to the cellular prion protein (PrPC) has been
                      proposed as anti-prion active mechanism. We here show by
                      means of NMR-spectroscopy that binding of TCA occurs with
                      millimolar affinity to motifs consisting of two neighboring
                      aromatic residues (Ar-Ar motif). It is independent of the
                      secondary structure of this motif and of the side chain
                      attached to the TCA and it is not specific to PrPC. Because
                      biologically inactive 9-aminoacridine (9-aa) binds with
                      similar K-D as anti-prion active quinacrine, direct
                      interaction with PrPC as mechanism of action appears highly
                      unlikely. However, binding of 9-aa to Ar-Ar-motifs in
                      proteins can be used as reporter for biological
                      macromolecule interactions, by measuring changes in T-1-NMR
                      relaxation times of 9-aa.},
      keywords     = {J (WoSType)},
      cin          = {ISB-3 / JARA-HPC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000270000500006},
      url          = {https://juser.fz-juelich.de/record/6512},
}