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@ARTICLE{Quy:186054,
      author       = {Quy, Vo and Carnevale, Vincenzo and Manganaro, Lara and
                      Lusic, Marina and Rossetti, Giulia and Leone, Vanessa and
                      Fenollar-Ferrer, Cristina and Raugei, Simone and Sal,
                      Giannino and Giacca, Mauro and Carloni, Paolo},
      title        = {{HIV}-1 {I}ntegrase {B}inding to its {C}ellular {P}artners:
                      {A} {P}erspective from {C}omputational {B}iology},
      journal      = {Current pharmaceutical design},
      volume       = {20},
      number       = {21},
      issn         = {1381-6128},
      address      = {Hilversum},
      publisher    = {Bentham Science Publ.},
      reportid     = {FZJ-2015-00155},
      pages        = {3412 - 3421},
      year         = {2014},
      abstract     = {Viral DNA integration into the infected cell genome is an
                      essential step in the HIV-1 life cycle. Hence, the viral
                      integrase enzyme has become an important target for
                      antiviral therapy. The integrase's activity action relies on
                      the binding to its cellular partners, therefore the
                      knowledge of the structural determinants is very important
                      from a therapeutic perspective. Here we first review
                      published computer-aided structural predictions of HIV-1
                      integrase in complex with its interactors. These include DNA
                      and the human HAT protein. Next, we present a prediction of
                      the complex between HIV-1 integrase with the human
                      prolyl-isomerase-1 (hPin1) enzyme. Interaction with hPin1 is
                      crucial for efficient HIV-1 infection and it increases
                      integrase stability (Manganaro et. al 2010, Nat. Med. 16,
                      329). The modeling presented here, which is validated
                      against experimental data, provides a rationale for a
                      variety of viral protein's mutations which impair protein
                      function and HIV-1 virus replication in vivo without
                      significantly affecting enzymatic activity.},
      cin          = {JSC / IAS-5 / INM-9},
      ddc          = {610},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)IAS-5-20120330 /
                      I:(DE-Juel1)INM-9-20140121},
      pnm          = {411 - Computational Science and Mathematical Methods
                      (POF2-411)},
      pid          = {G:(DE-HGF)POF2-411},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:24001231},
      UT           = {WOS:000337899300004},
      doi          = {10.2174/13816128113199990631},
      url          = {https://juser.fz-juelich.de/record/186054},
}