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@ARTICLE{Zaccagnini:884076,
      author       = {Zaccagnini, Ludovica and Rossetti, Giulia and Tran, Thanh
                      Hoa and Salzano, Giulia and Gandini, Annachiara and Colini
                      Baldeschi, Arianna and Bolognesi, Maria Laura and Carloni,
                      Paolo and Legname, Giuseppe},
      title        = {{I}n silico/in vitro screening and hit evaluation
                      identified new phenothiazine anti-prion derivatives},
      journal      = {European journal of medicinal chemistry},
      volume       = {196},
      issn         = {0223-5234},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier71544},
      reportid     = {FZJ-2020-03077},
      pages        = {112295},
      year         = {2020},
      abstract     = {Prion diseases or transmissible spongiform encephalopathies
                      (TSEs) are a group of rare neurodegenerative disorders. TSEs
                      are characterized by the accumulation of prions (PrPSc) that
                      represent pathological isoforms of the physiological
                      cellular prion protein PrPC. Although the conversion of PrPC
                      to PrPSc is still not completely understood, blocking this
                      process may lead to develop new therapies. Here, we have
                      generated a pharmacophore model, based on anti-prion
                      molecules reported in literature to be effective in
                      phenotypic assay. The model was used to conduct a virtual
                      screen of commercial compound databases that selected a
                      small library of ten compounds. These molecules were then
                      screened in mouse neuroblastoma cell line chronically
                      infected with prions (ScN2a) after excluding neurotoxicity.
                      1 has been identified as the therapeutic hit on the basis of
                      the following evidence: chronic treatments of ScN2a cells
                      using 1 eliminate PrPSc loaded in both Western blotting
                      analysis and Real-Time Quaking-Induced Conversion (RT-QuIC)
                      assay. We also proposed the mechanism of action of 1 by
                      which it has the ability to bind PrPC and consequentially
                      blocks prion conversion. Herein we describe the results of
                      these efforts.},
      cin          = {IAS-5 / INM-9 / JSC},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      I:(DE-Juel1)JSC-20090406},
      pnm          = {574 - Theory, modelling and simulation (POF3-574) / 511 -
                      Computational Science and Mathematical Methods (POF3-511)},
      pid          = {G:(DE-HGF)POF3-574 / G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32325366},
      UT           = {WOS:000530224900004},
      doi          = {10.1016/j.ejmech.2020.112295},
      url          = {https://juser.fz-juelich.de/record/884076},
}