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@ARTICLE{Lyu:859286,
      author       = {Lyu, , Wenping and Arnesano, Fabio and Carloni, Paolo and
                      Natile, Giovanni and Rossetti, Giulia},
      title        = {{E}ffect of in vivo post-translational modifications of the
                      {HMGB}1 protein upon binding to platinated {DNA}: a
                      molecular simulation study},
      journal      = {Nucleic acids symposium series},
      volume       = {46},
      number       = {22},
      issn         = {1362-4962},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {FZJ-2019-00158},
      pages        = {11687 - 11697},
      year         = {2018},
      abstract     = {Cisplatin is one of the most widely used anticancer drugs.
                      Its efficiency is unfortunately severely hampered by
                      resistance. The High Mobility Group Box (HMGB) proteins may
                      sensitize tumor cells to cisplatin by specifically binding
                      to platinated DNA (PtDNA) lesions. In vivo, the HMGB/PtDNA
                      binding is regulated by multisite post-translational
                      modifications (PTMs). The impact of PTMs on the HMGB/PtDNA
                      complex at atomistic level is here investigated by enhanced
                      sampling molecular simulations. The PTMs turn out to affect
                      the structure of the complex, the mobility of several
                      regions (including the platinated site), and the nature of
                      the protein/PtDNA non-covalent interactions. Overall, the
                      multisite PTMs increase significantly the apparent synchrony
                      of all the contacts between the protein and PtDNA.
                      Consequently, the hydrophobic anchoring of the side chain of
                      F37 between the two cross-linked guanines at the platinated
                      site—a key element of the complexes formation - is more
                      stable than in the complex without PTM. These differences
                      can account for the experimentally measured greater affinity
                      for PtDNA of the protein isoforms with PTMs. The collective
                      behavior of multisite PTMs, as revealed here by the
                      synchrony of contacts, may have a general significance for
                      the modulation of intermolecular recognitions occurring in
                      vivo.},
      cin          = {IAS-5 / INM-9 / JARA-HPC / JSC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      $I:(DE-82)080012_20140620$ / 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},
      pubmed       = {pmid:30407547},
      UT           = {WOS:000456714000009},
      doi          = {10.1093/nar/gky1082},
      url          = {https://juser.fz-juelich.de/record/859286},
}