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@ARTICLE{Bolognesi:201270,
      author       = {Bolognesi, Maria Laura and Ai Tran, Hoang Ngoc and
                      Staderini, Matteo and Monaco, Alessandra and
                      López-Cobeñas, Alberto and Bongarzone, Salvatore and
                      Biarnés, Xevi and López-Alvarado, Pilar and Cabezas,
                      Nieves and Caramelli, Maria and Carloni, Paolo and
                      Menéndez, J. Carlos and Legname, Giuseppe},
      title        = {{D}iscovery of a {C}lass of {D}iketopiperazines as
                      {A}ntiprion {C}ompounds},
      journal      = {ChemMedChem},
      volume       = {5},
      number       = {8},
      issn         = {1860-7179},
      address      = {Weinheim [u.a.]},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2015-03575},
      pages        = {1324 - 1334},
      year         = {2010},
      abstract     = {Prion diseases are fatal neurodegenerative and infectious
                      disorders for which effective pharmacological tools are not
                      yet available. This unmet challenge and the recently
                      proposed interplay between prion diseases and Alzheimer's
                      have led to a more urgent demand for new antiprion agents.
                      Herein, we report the identification of a novel bifunctional
                      diketopiperazine (DKP) derivative 1 d, which exhibits
                      activity in the low micromolar range against prion
                      replication in ScGT1 cells, while showing low cytotoxicity.
                      Supported by properly addressed molecular modeling studies,
                      we hypothesized that a planar conformation is the major
                      determinant for activity in this class of compounds.
                      Moreover, studies aimed at assessing the mechanism-of-action
                      at the molecular level showed that 1 d might interact
                      directly with recombinant prion protein (recPrP) to prevent
                      its conversion to the pathogenic misfolded prion protein
                      (PrPSc)-like form. This investigation suggests that DKP
                      based antiprion compounds can serve as a promising lead
                      scaffold in developing new drugs to combat prion diseases},
      cin          = {GRS / IAS-5},
      ddc          = {540},
      cid          = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {899 - ohne Topic (POF2-899)},
      pid          = {G:(DE-HGF)POF2-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000281061300017},
      doi          = {10.1002/cmdc.201000133},
      url          = {https://juser.fz-juelich.de/record/201270},
}