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@ARTICLE{Pickhardt:140512,
      author       = {Pickhardt, Marcus and Tassoni, Michele and Denner, Philip
                      and Kurkowsky, Birgit and Kitanovic, Ana and Möhl,
                      Christoph and Fava, Eugenio and Mandelkow, Eckhard},
      title        = {{S}creening of a neuronal cell model of tau pathology for
                      therapeutic compounds.},
      journal      = {Neurobiology of aging},
      volume       = {76},
      issn         = {0197-4580},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {DZNE-2020-06834},
      pages        = {24-34},
      year         = {2019},
      abstract     = {We have developed a cell-based phenotypic automated
                      high-content screening approach for N2a cells expressing the
                      pro-aggregant repeat domain of tau protein (tauRDΔK), which
                      allows analysis of a chemogenomic library of 1649 compounds
                      for their effect on the inhibition or stimulation of
                      intracellular tau aggregation. We identified several
                      inhibitors and stimulators of aggregation and achieved a
                      screening reproducibility $>85\%$ for all data. We
                      identified 18 potential inhibitors (= $1.1\%$ of the
                      library) and 10 stimulators (= $0.6\%$ of the library) of
                      tau aggregation in this cell model of tau pathology. The
                      results provide insights into the regulation of cellular tau
                      aggregation and the pathways involved in this process (e.g.,
                      involving signaling via p38 mitogen-activated protein
                      kinase, histone deacetylases, vascular endothelial growth
                      factor, rho/ROCK). For example, inhibitors of protein
                      kinases (e.g., p38) can reduce tau aggregation, whereas
                      inhibitors of deacetylases (histone deacetylases) can
                      enhance aggregation. These observations are compatible with
                      reports that phosphorylated or acetylated tau promotes
                      pathology.},
      keywords     = {Cell Line / Drug Evaluation, Preclinical: methods / Enzyme
                      Inhibitors: pharmacology / Histone Deacetylase Inhibitors /
                      Histone Deacetylases: pharmacology / Humans / Models,
                      Biological / Protein Aggregation, Pathological: genetics /
                      Protein Aggregation, Pathological: metabolism / Signal
                      Transduction: genetics / Signal Transduction: physiology /
                      Tauopathies: drug therapy / Tauopathies: genetics /
                      Tauopathies: metabolism / p38 Mitogen-Activated Protein
                      Kinases: antagonists $\&$ inhibitors / tau Proteins:
                      metabolism / Enzyme Inhibitors (NLM Chemicals) / Histone
                      Deacetylase Inhibitors (NLM Chemicals) / tau Proteins (NLM
                      Chemicals) / p38 Mitogen-Activated Protein Kinases (NLM
                      Chemicals) / Histone Deacetylases (NLM Chemicals)},
      cin          = {AG Mandelkow 1 / AG Fava 1 / LAT / IDAF},
      ddc          = {610},
      cid          = {I:(DE-2719)1013014 / I:(DE-2719)1013016 /
                      I:(DE-2719)1040190 / I:(DE-2719)1040200},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30640040},
      doi          = {10.1016/j.neurobiolaging.2018.11.026},
      url          = {https://pub.dzne.de/record/140512},
}