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@ARTICLE{Baranauskiene:140090,
      author       = {Baranauskiene, L. and Hilvo, M. and Matuliene, J. and
                      Golovenko, D. and Manakova, E. and Dudutiene, V. and
                      Michailoviene, V. and Torresan, J. and Jachno, J. and
                      Parkkila, S. and Maresca, A. and Supuran, C. and Grazulis,
                      S. and Matulis, D. and DESY},
      title        = {{I}nhibition and binding studies of carbonic anhydrase
                      isozymes {I}, {II} and {IX} with
                      benzimidazo[1,2-c][1,2,3]thiadiazole-7-sulphonamides},
      journal      = {Journal of enzyme inhibition and medicinal chemistry},
      volume       = {25},
      issn         = {1475-6374},
      address      = {London},
      publisher    = {Informa Healthcare},
      reportid     = {PHPPUBDB-24676},
      pages        = {863-870},
      year         = {2010},
      abstract     = {The binding and inhibition strength of a series of
                      benzimidazo[1,2-c][1,2,3]thiadiazole-7-sulphonamides were
                      determined for recombinant human carbonic anhydrase isoforms
                      I, II, and IX. The inhibition strength was determined by a
                      stop-flow method to measure carbon dioxide hydration.
                      Inhibitor-enzyme binding was determined by two biophysical
                      techniques--isothermal titration calorimetry and thermal
                      shift assay. The co-crystal structure was determined by
                      X-ray crystallography. Comparing the results obtained using
                      three different inhibition and binding methods increased the
                      accuracy of compound affinity ranking and the ability to
                      determine compound inhibitory specificity towards a
                      particular carbonic anhydrase isoform. In most cases, all
                      three methods yielded the same results despite using very
                      different approaches to measure the binding and inhibition
                      reactions. Some of the compounds studied are submicromolar
                      inhibitors of the isoform IX, a prominent cancer target.},
      keywords     = {Algorithms / Antigens, Neoplasm: genetics / Antigens,
                      Neoplasm: metabolism / Antineoplastic Agents: chemistry /
                      Antineoplastic Agents: metabolism / Antineoplastic Agents:
                      pharmacology / Benzimidazoles: chemistry / Benzimidazoles:
                      metabolism / Benzimidazoles: pharmacology / Calorimetry:
                      methods / Carbonic Anhydrase I: antagonists $\&$ inhibitors
                      / Carbonic Anhydrase I: genetics / Carbonic Anhydrase I:
                      metabolism / Carbonic Anhydrase II: antagonists $\&$
                      inhibitors / Carbonic Anhydrase II: chemistry / Carbonic
                      Anhydrase II: genetics / Carbonic Anhydrase II: metabolism /
                      Carbonic Anhydrase Inhibitors: chemistry / Carbonic
                      Anhydrase Inhibitors: metabolism / Carbonic Anhydrase
                      Inhibitors: pharmacology / Carbonic Anhydrases: genetics /
                      Carbonic Anhydrases: metabolism / Catalytic Domain: drug
                      effects / Crystallography, X-Ray / Humans / Kinetics /
                      Ligands / Molecular Conformation / Recombinant Proteins:
                      antagonists $\&$ inhibitors / Recombinant Proteins:
                      chemistry / Recombinant Proteins: metabolism / Sulfonamides:
                      chemistry / Sulfonamides: metabolism / Sulfonamides:
                      pharmacology / Thiadiazoles: chemistry / Thiadiazoles:
                      metabolism / Thiadiazoles: pharmacology / Antigens, Neoplasm
                      (NLM Chemicals) / Antineoplastic Agents (NLM Chemicals) /
                      Benzimidazoles (NLM Chemicals) / Carbonic Anhydrase
                      Inhibitors (NLM Chemicals) / Ligands (NLM Chemicals) /
                      Recombinant Proteins (NLM Chemicals) / Sulfonamides (NLM
                      Chemicals) / Thiadiazoles (NLM Chemicals) / Carbonic
                      Anhydrase I (NLM Chemicals) / Carbonic Anhydrase II (NLM
                      Chemicals) / CA9 protein, human (NLM Chemicals) / Carbonic
                      Anhydrases (NLM Chemicals)},
      cin          = {HASYLAB / EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$ /
                      $I:(DE-H253)EMBL_-2012_-20130307$},
      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:20166809},
      UT           = {WOS:000283939300016},
      doi          = {10.3109/14756360903571685},
      url          = {https://bib-pubdb1.desy.de/record/140090},
}