% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Kroth:136651,
      author       = {Kroth, Heiko and Ansaloni, Annalisa and Varisco, Yvan and
                      Jan, Asad and Sreenivasachary, Nampally and Rezaei-Ghaleh,
                      Nasrollah and Giriens, Valérie and Lohmann, Sophie and
                      López-Deber, María Pilar and Adolfsson, Oskar and
                      Pihlgren, Maria and Paganetti, Paolo and Froestl, Wolfgang
                      and Nagel-Steger, Luitgard and Willbold, Dieter and
                      Schrader, Thomas and Zweckstetter, Markus and Pfeifer,
                      Andrea and Lashuel, Hilal A and Muhs, Andreas},
      title        = {{D}iscovery and structure activity relationship of small
                      molecule inhibitors of toxic β-amyloid-42 fibril
                      formation.},
      journal      = {The journal of biological chemistry},
      volume       = {287},
      number       = {41},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.60645},
      reportid     = {DZNE-2020-02973},
      pages        = {34786-34800},
      year         = {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.},
      keywords     = {Amyloid beta-Peptides: antagonists $\&$ inhibitors /
                      Amyloid beta-Peptides: chemistry / Cell Line, Tumor /
                      Cytotoxins: antagonists $\&$ inhibitors / Cytotoxins:
                      chemistry / Humans / Hydrogen Bonding / Hydrophobic and
                      Hydrophilic Interactions / Peptide Fragments: antagonists
                      $\&$ inhibitors / Peptide Fragments: chemistry / Protein
                      Structure, Secondary / Pyrazoles: chemistry /
                      Structure-Activity Relationship / 3-aminopyrazole (NLM
                      Chemicals) / Amyloid beta-Peptides (NLM Chemicals) /
                      Cytotoxins (NLM Chemicals) / Peptide Fragments (NLM
                      Chemicals) / Pyrazoles (NLM Chemicals) / amyloid
                      beta-protein (1-42) (NLM Chemicals)},
      cin          = {AG Zweckstetter},
      ddc          = {540},
      cid          = {I:(DE-2719)1410001},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22891248},
      pmc          = {pmc:PMC3464581},
      doi          = {10.1074/jbc.M112.357665},
      url          = {https://pub.dzne.de/record/136651},
}