% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Brger:276620,
      author       = {Börger, Claudia and Schünke, Sven and Lecher, Justin and
                      Stoldt, Matthias and Winkhaus, Friederike and Kaupp, U.
                      Benjamin and Willbold, Dieter},
      title        = {{R}esonance assignment of the ligand-free cyclic
                      nucleotide-binding domain from the murine ion channel
                      {HCN}$_{2}$},
      journal      = {Biomolecular NMR assignments},
      volume       = {9},
      number       = {2},
      issn         = {1874-270X},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Netherlands},
      reportid     = {FZJ-2015-06965},
      pages        = {243 - 246},
      year         = {2015},
      abstract     = {Hyperpolarization activated and cyclic nucleotide-gated
                      (HCN) ion channels as well as cyclic nucleotide-gated (CNG)
                      ion channels are essential for the regulation of cardiac
                      cells, neuronal excitability, and signaling in sensory
                      cells. Both classes are composed of four subunits. Each
                      subunit comprises a transmembrane region, intracellular N-
                      and C-termini, and a C-terminal cyclic nucleotide-binding
                      domain (CNBD). Binding of cyclic nucleotides to the CNBD
                      promotes opening of both CNG and HCN channels. In case of
                      CNG channels, binding of cyclic nucleotides to the CNBD is
                      sufficient to open the channel. In contrast, HCN channels
                      open upon membrane hyperpolarization and their activity is
                      modulated by binding of cyclic nucleotides shifting the
                      activation potential to more positive values. Although
                      several high-resolution structures of CNBDs from HCN and CNG
                      channels are available, the gating mechanism for murine HCN2
                      channel, which leads to the opening of the channel pore, is
                      still poorly understood. As part of a structural
                      investigation, here, we report the complete backbone and
                      side chain resonance assignments of the murine HCN2 CNBD
                      with part of the C-linker.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000361440100005},
      doi          = {10.1007/s12104-014-9583-x},
      url          = {https://juser.fz-juelich.de/record/276620},
}