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@ARTICLE{Campaner:834627,
      author       = {Campaner, Elena and Rustighi, Alessandra and Zannini,
                      Alessandro and Cristiani, Alberto and Piazza, Silvano and
                      Ciani, Yari and Kalid, Ori and Golan, Gali and Baloglu,
                      Erkan and Shacham, Sharon and Valsasina, Barbara and Cucchi,
                      Ulisse and Pippione, Agnese Chiara and Lolli, Marco Lucio
                      and Giabbai, Barbara and Storici, Paola and Carloni, Paolo
                      and Rossetti, Giulia and Benvenuti, Federica and Bello, Ezia
                      and D’Incalci, Maurizio and Cappuzzello, Elisa and Rosato,
                      Antonio and Del Sal, Giannino},
      title        = {{A} covalent {PIN}1 inhibitor selectively targets cancer
                      cells by a dual mechanism of action},
      journal      = {Nature Communications},
      volume       = {8},
      issn         = {2041-1723},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2017-04535},
      pages        = {15772 -},
      year         = {2017},
      abstract     = {The prolyl isomerase PIN1, a critical modifier of multiple
                      signalling pathways, is overexpressed in the majority of
                      cancers and its activity strongly contributes to tumour
                      initiation and progression. Inactivation of PIN1 function
                      conversely curbs tumour growth and cancer stem cell
                      expansion, restores chemosensitivity and blocks metastatic
                      spread, thus providing the rationale for a therapeutic
                      strategy based on PIN1 inhibition. Notwithstanding, potent
                      PIN1 inhibitors are still missing from the arsenal of
                      anti-cancer drugs. By a mechanism-based screening, we have
                      identified a novel covalent PIN1 inhibitor, KPT-6566, able
                      to selectively inhibit PIN1 and target it for degradation.
                      We demonstrate that KPT-6566 covalently binds to the
                      catalytic site of PIN1. This interaction results in the
                      release of a quinone-mimicking drug that generates reactive
                      oxygen species and DNA damage, inducing cell death
                      specifically in cancer cells. Accordingly, KPT-6566
                      treatment impairs PIN1-dependent cancer phenotypes in vitro
                      and growth of lung metastasis in vivo.},
      cin          = {IAS-5 / INM-9 / JSC},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      I:(DE-Juel1)JSC-20090406},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511)},
      pid          = {G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000402967000001},
      pubmed       = {pmid:28598431},
      doi          = {10.1038/ncomms15772},
      url          = {https://juser.fz-juelich.de/record/834627},
}