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@ARTICLE{Cukkemane:57477,
      author       = {Cukkemane, A. and Grüter, B. and Novak, K. and Gensch, T.
                      and Bönigk, W. and Gerharz, T. and Kaupp, U. B. and
                      Seifert, R.},
      title        = {{S}ubunits act independently in a cyclic
                      nucleotide-activated {K}+ channel},
      journal      = {EMBO reports},
      volume       = {8},
      issn         = {1469-221X},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {PreJuSER-57477},
      pages        = {749 - 755},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Ion channels gated by cyclic nucleotides have crucial roles
                      in neuronal excitability and signal transduction of sensory
                      neurons. Here, we studied ligand binding of a cyclic
                      nucleotide-activated K(+) channel from Mesorhizobium loti
                      and its isolated cyclic nucleotide-binding domain. The
                      channel and the binding domain alone bind cyclic AMP with
                      similar affinity in a non-cooperative manner. The cAMP
                      sensitivities of binding and activation coincide. Thus, each
                      subunit in the tetrameric channel acts independently of the
                      others. The binding and gating properties of the bacterial
                      channel are distinctively different from those of eukaryotic
                      cyclic nucleotide-gated channels.},
      keywords     = {Alphaproteobacteria: metabolism / Bacterial Proteins:
                      chemistry / Bacterial Proteins: genetics / Cyclic AMP:
                      chemistry / Cyclic Nucleotide-Gated Cation Channels:
                      chemistry / Cyclic Nucleotide-Gated Cation Channels:
                      genetics / Ligands / Potassium Channels: chemistry /
                      Potassium Channels: genetics / Protein Structure, Tertiary /
                      Protein Subunits: chemistry / Spectrometry, Fluorescence /
                      Bacterial Proteins (NLM Chemicals) / Cyclic Nucleotide-Gated
                      Cation Channels (NLM Chemicals) / Ligands (NLM Chemicals) /
                      Potassium Channels (NLM Chemicals) / Protein Subunits (NLM
                      Chemicals) / Cyclic AMP (NLM Chemicals) / J (WoSType)},
      cin          = {IBT-1 / INB-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB55 / I:(DE-Juel1)VDB804},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Cell Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17668006},
      pmc          = {pmc:PMC1978089},
      UT           = {WOS:000248447300011},
      doi          = {10.1038/sj.embor.7401025},
      url          = {https://juser.fz-juelich.de/record/57477},
}