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@ARTICLE{Yokoyama:276228,
      author       = {Yokoyama, Takeshi and Mizuguchi, Mineyuki and Ostermann,
                      Andreas and Kusaka, Katsuhiro and Niimura, Nobuo and
                      Schrader, Tobias Erich and Tanaka, Ichiro},
      title        = {{P}rotonation {S}tate and {H}ydration of {B}isphosphonate
                      {B}ound to {F}arnesyl {P}yrophosphate {S}ynthase},
      journal      = {Journal of medicinal chemistry},
      volume       = {58},
      number       = {18},
      issn         = {1520-4804},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2015-06693},
      pages        = {7549 - 7556},
      year         = {2015},
      abstract     = {Farnesyl pyrophosphate synthase (FPPS) catalyzes the
                      condensation of isopentenyl pyrophosphate (IPP) and
                      dimethylallyl pyrophosphate to FPP and is known to be a
                      molecular target of osteoporosis drugs, such as risedronate
                      (RIS), which is a nitrogen-containing bisphosphonate. The
                      protonation states and hydration structure of RIS bound to
                      FPPS were determined by neutron protein crystallography,
                      which allows direct visualization of hydrogens and
                      deuteriums. The structure analysis revealed that the
                      phosphate groups of RIS were fully deprotonated with the
                      abnormally decreased pKa, and that the roles of E93 and D264
                      consisted of canceling the extra negative charges upon the
                      binding of ligands. Collectively, our neutron structures
                      provided insights into the physicochemical properties during
                      the bisphosphonate binding event.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000361921800033},
      doi          = {10.1021/acs.jmedchem.5b01147},
      url          = {https://juser.fz-juelich.de/record/276228},
}