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@ARTICLE{Capkauskaite:140131,
      author       = {Capkauskaite, E. and Zubriene, A. and Baranauskiene, L. and
                      Tamulaitiene, G. and Manakova, E. and Kairys, V. and
                      Grazulis, S. and Tumkevicius, S. and Matulis, D. and DESY},
      title        = {{D}esign of [(2-pyrimidinylthio)acetyl]benzenesulfonamides
                      as inhibitors of human carbonic anhydrases.},
      journal      = {European journal of medicinal chemistry},
      volume       = {51},
      issn         = {0223-5234},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PHPPUBDB-24637},
      pages        = {259-70},
      year         = {2012},
      abstract     = {A series of [(2-pyrimidinylthio)acetyl]benzenesulfonamides
                      were designed and synthesized. Their binding affinities as
                      inhibitors of several recombinant human carbonic anhydrase
                      (CA) isozymes were determined by isothermal titration
                      calorimetry (ITC) and thermal shift assay (TSA). A group of
                      compounds containing a chlorine atom in the
                      benzenesulfonamide ring were found to exhibit higher
                      selectivity but lower binding affinity toward tested CAs.
                      The crystal structures of selected compounds in complex with
                      CA II were determined to atomic resolution. Docking studies
                      were performed to compare the binding modes of
                      experimentally determined crystallographic structures with
                      computational prediction of the pyrimidine derivative
                      binding to CA II. Several compounds bound to select CAs with
                      single-digit nanomolar affinities and could be used as leads
                      for inhibitor development toward a select CA isozyme.},
      keywords     = {Carbonic Anhydrase Inhibitors: chemical synthesis /
                      Carbonic Anhydrase Inhibitors: chemistry / Carbonic
                      Anhydrase Inhibitors: pharmacology / Carbonic Anhydrases:
                      chemistry / Carbonic Anhydrases: metabolism / Catalytic
                      Domain / Drug Design / Humans / Models, Molecular /
                      Sulfonamides: chemical synthesis / Sulfonamides: chemistry /
                      Sulfonamides: pharmacology / Carbonic Anhydrase Inhibitors
                      (NLM Chemicals) / Sulfonamides (NLM Chemicals) /
                      benzenesulfonamide (NLM Chemicals) / Carbonic Anhydrases
                      (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {610},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {FS Beamline without reference (POF2-544)},
      pid          = {G:(DE-H253)POF2-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22440859},
      UT           = {WOS:000304291900026},
      UT           = {WOS:000304291900026},
      doi          = {10.1016/j.ejmech.2012.02.050},
      url          = {https://bib-pubdb1.desy.de/record/140131},
}