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@ARTICLE{Yokoyama:872856,
      author       = {Yokoyama, Takeshi and Matsumoto, Kazunori and Ostermann,
                      Andreas and Schrader, Tobias E. and Nabeshima, Yuko and
                      Mizuguchi, Mineyuki},
      title        = {{S}tructural and thermodynamic characterization of the
                      binding of isoliquiritigenin to the first bromodomain of
                      {BRD}4},
      journal      = {The FEBS journal},
      volume       = {286},
      number       = {9},
      issn         = {1742-4658},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2020-00324},
      pages        = {1656 - 1667},
      year         = {2019},
      abstract     = {Bromodomain-containing protein 4 (BRD4) recognizes the
                      acetylated lysineof histone H4 via its bromodomains, leading
                      to the recruitment of positivetranscription elongation
                      factor b. Small molecules that inhibit BRD4 havepotential as
                      anticancer agents by leading to the downregulation of
                      specificoncogenes. Using X-ray crystallographic screening,
                      we identified the BRD4inhibitory activity of
                      isoliquiritigenin (ISL), a natural chalcone found
                      inlicorice. Structural analysis revealed that ISL bound to
                      BRD4 with a novelbinding mode and squeezed out one of the
                      six conserved water moleculesthat form a strong hydrogen
                      bond network. The thermodynamic analysisrevealed that the
                      binding of ISL is enthalpy driven, suggesting that
                      stronghydrogen bonds would compensate for the desolvation
                      penalty. Neutronprotein crystallography further suggested
                      that the favorable bindingenthalpy originates from the
                      stabilization and optimization of the hydrogenbond network
                      of the conserved water molecules. Here, we describe the
                      noveltyand potential of ISL as a template for new BRD4
                      inhibitors.},
      cin          = {JCNS-FRM-II / JCNS-1 / MLZ},
      ddc          = {610},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15) / 6215 - Soft Matter,
                      Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15 /
                      G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30565859},
      UT           = {WOS:000467253400005},
      doi          = {10.1111/febs.14736},
      url          = {https://juser.fz-juelich.de/record/872856},
}