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@ARTICLE{Benltifa:90093,
      author       = {Benltifa, M. and Hayes, J. M. and Vidal, S. and Gueyrard,
                      D. and Goekjian, P. G. and Praly, J.-P. and Kizilis, G. and
                      Tiraidis, C. and Alexacou, K.-M. and Chrysina, E. D. and
                      Zographos, S. E. and Leonidas, D. D. and Archontis, G. and
                      Oikonomakos, N. G. and DESY},
      title        = {{G}lucose-based spiro-isoxazolines: {A} new family of
                      potent glycogen phosphorylase inhibitors},
      journal      = {Bioorganic $\&$ medicinal chemistry},
      volume       = {17},
      issn         = {0968-0896},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-11918},
      pages        = {7368-7380},
      year         = {2009},
      note         = {© Elsevier Ltd.},
      abstract     = {A series of glucopyranosylidene-spiro-isoxazolines was
                      prepared through regio- and stereoselective
                      [3+2]-cycloaddition between the methylene acetylated
                      exo-glucal and aromatic nitrile oxides. The deprotected
                      cycloadducts were evaluated as inhibitors of muscle glycogen
                      phosphorylase b. The carbohydrate-based family of five
                      inhibitors displays K(i) values ranging from 0.63 to 92.5
                      microM. The X-ray structures of the enzyme-ligand complexes
                      show that the inhibitors bind preferentially at the
                      catalytic site of the enzyme retaining the less active
                      T-state conformation. Docking calculations with GLIDE in
                      extra-precision (XP) mode yielded excellent agreement with
                      experiment, as judged by comparison of the predicted binding
                      modes of the five ligands with the crystallographic
                      conformations and the good correlation between the docking
                      scores and the experimental free binding energies. Use of
                      docking constraints on the well-defined positions of the
                      glucopyranose moiety in the catalytic site and redocking of
                      GLIDE-XP poses using electrostatic potential fit-determined
                      ligand partial charges in quantum polarized ligand docking
                      (QPLD) produced the best results in this regard.},
      keywords     = {Crystallography, X-Ray / Enzyme Inhibitors: chemistry /
                      Enzyme Inhibitors: pharmacology / Glucose: chemistry /
                      Glycogen Phosphorylase: antagonists $\&$ inhibitors /
                      Glycogen Phosphorylase: metabolism / Kinetics / Magnetic
                      Resonance Spectroscopy / Models, Molecular / Oxazoles:
                      chemistry / Oxazoles: pharmacology / Spectrometry, Mass,
                      Electrospray Ionization / Enzyme Inhibitors (NLM Chemicals)
                      / Oxazoles (NLM Chemicals) / Glucose (NLM Chemicals) /
                      Glycogen Phosphorylase (NLM Chemicals)},
      cin          = {EMBL(-2012)},
      ddc          = {540},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {FS Beamline without reference (POF1-550) / DORIS Beamline
                      K1.1 (POF1-550)},
      pid          = {G:(DE-H253)POF1-No-Ref-20130405 /
                      G:(DE-H253)POF1-K1.1-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101 /
                      EXP:(DE-H253)D-K1.1-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19781947},
      UT           = {WOS:000270434000031},
      doi          = {10.1016/j.bmc.2009.08.060},
      url          = {https://bib-pubdb1.desy.de/record/90093},
}