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@PHDTHESIS{Debowski:1297,
      author       = {Debowski, Katharina},
      title        = {{I}dentifizierung und {C}harakterisierung eines neuen
                      {B}indeproteins für zyklische {N}ukleotide},
      volume       = {4260},
      issn         = {0944-2952},
      school       = {Univ. Köln},
      type         = {Dr. (Univ.)},
      address      = {Jülich},
      publisher    = {Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag},
      reportid     = {PreJuSER-1297, Juel-4260},
      series       = {Berichte des Forschungszentrums Jülich},
      pages        = {VII, 107 p},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012; Köln, Univ., Diss.,
                      2007},
      abstract     = {Cyclic adenosine monophosphate (cAMP) and cyclic guanosine
                      monophosphate are important intracellular messengers.
                      Binding of cyclic nucleotides controls the activity of
                      protein kinases, ion channels and
                      guanine-nucleotide-exchange factors in many cells. The SCNBP
                      (soluble cyclic nucleotide-binding protein) is a novel
                      uncharacterized protein predicted to comprise a cyclic
                      nucleotide-binding domain. This protein belongs to neither
                      of the known families of effector proteins for cyclic
                      nucleotides. Within 17 distinct species - from marine
                      invertebrates to humans - genes orthologous to the mouse
                      SCNBP are present. Hence, the SCNBP could belong to a novel
                      class of effector proteins for cyclic nucleotides. Northern
                      blot experiments with mouse tissue indicate that the mRNA of
                      SCNBP is expressed predominantly in the testis and by means
                      of in situ hybridization it was specifically detected in
                      spermatocytes. In the present study, SCNBP expression has
                      been analyzed in mouse testis utilizing specific antibodies.
                      I could provide evidence that two distinct SCNBP variants
                      are present in mouse testis. To approach the physiological
                      function of SCNBP, I identified by immunoprecipitation and
                      mass spectrometry proteins in mouse testis that potentially
                      interact with SCNBP. For a comprehensive biochemical study,
                      SCNBP was heterologously expressed in Chinese hamster ovary
                      (CHO) cells. Following fermentation of these cells in a
                      stirred tank bioreactor I purified SCNBP by affinity
                      chromatography.},
      cin          = {INB-1},
      cid          = {I:(DE-Juel1)VDB804},
      pnm          = {Grundlagen für zukünftige Informationstechnologien},
      pid          = {G:(DE-Juel1)FUEK412},
      typ          = {PUB:(DE-HGF)11 / PUB:(DE-HGF)3},
      url          = {https://juser.fz-juelich.de/record/1297},
}