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@ARTICLE{Kroth:23050,
      author       = {Kroth, H. and Ansaloni, A. and Varisco, Y. and Jan, A. and
                      Sreenivasachary, N. and Rezaei-Ghaleh, N. and Giriens, V.
                      and Lohmann, S. and Pilar López-Deber, M. and Adolfsson, O.
                      and Pihlgren, M. and Paganetti, P. and Froestl, W. and
                      Nagel-Steger, L. and Willbold, D and Schrader, T and
                      Zweckstetter, M. and Pfeifer, A. and Lashuel, H.A. and Muhs,
                      A.},
      title        = {{D}iscovery and structure activity relationship of small
                      molecule inhibitors of toxic-ß--amyloid-42 fibril
                      formation},
      journal      = {The journal of biological chemistry},
      volume       = {287},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-23050},
      pages        = {34786 - 34800},
      year         = {2012},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Increasing evidence implicates Aβ peptides self-assembly
                      and fibril formation as crucial events in the pathogenesis
                      of Alzheimer disease. Thus, inhibiting Aβ aggregation,
                      among others, has emerged as a potential therapeutic
                      intervention for this disorder. Herein, we employed
                      3-aminopyrazole as a key fragment in our design of non-dye
                      compounds capable of interacting with Aβ42 via a
                      donor-acceptor-donor hydrogen bond pattern complementary to
                      that of the β-sheet conformation of Aβ42. The initial
                      design of the compounds was based on connecting two
                      3-aminopyrazole moieties via a linker to identify suitable
                      scaffold molecules. Additional aryl substitutions on the two
                      3-aminopyrazole moieties were also explored to enhance π-π
                      stacking/hydrophobic interactions with amino acids of Aβ42.
                      The efficacy of these compounds on inhibiting Aβ fibril
                      formation and toxicity in vitro was assessed using a
                      combination of biophysical techniques and viability assays.
                      Using structure activity relationship data from the in vitro
                      assays, we identified compounds capable of preventing
                      pathological self-assembly of Aβ42 leading to decreased
                      cell toxicity.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22891248},
      pmc          = {pmc:PMC3464581},
      UT           = {WOS:000309654200078},
      doi          = {10.1074/jbc.M112.357665},
      url          = {https://juser.fz-juelich.de/record/23050},
}