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@ARTICLE{Seebahn:14601,
      author       = {Seebahn, A. and Dinkel, H. and Mohrlüder, J. and Hartmann,
                      R. and Vogel, N. and Becker, C.M. and Sticht, H. and Enz,
                      R.},
      title        = {{S}tructural characterization of intracellular {C}-terminal
                      domains of group {III} metabotropic glutamate receptors},
      journal      = {FEBS letters},
      volume       = {585},
      issn         = {0014-5793},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-14601},
      pages        = {511 - 516},
      year         = {2011},
      note         = {We thank Wei Xiang for help with mass spectrometry and
                      Dieter Willbold for helpful discussions. This work was
                      supported by the Deutsche Forschungsgemeinschaft [EN349/5-2,
                      EU-HEALTH-F4-2008-202088, SFB539, SFB796].},
      abstract     = {Metabotropic glutamate receptors (mGluRs) are regulated by
                      interacting proteins that mostly bind to their intracellular
                      C-termini. Here, we investigated if mGluR6, mGluR7a and
                      mGluR8a C-termini form predefined binding surfaces or if
                      they were rather unstructured. Limited tryptic digest of
                      purified peptides argued against the formation of stable
                      globular folds. Circular dichroism, (1)H NMR and (1)H(15)N
                      HSQC spectra indicated the absence of rigid secondary
                      structure elements. Furthermore, we localized short linear
                      binding motifs in the unstructured receptor domains. Our
                      data provide evidence that protein interactions of the
                      analyzed mGluR C-termini are mediated rather by short linear
                      motifs than by preformed folds.},
      keywords     = {Amino Acid Motifs / Animals / Circular Dichroism /
                      Computational Biology: methods / Nuclear Magnetic Resonance,
                      Biomolecular / Peptide Fragments: chemistry / Peptide
                      Fragments: metabolism / Protein Folding / Protein
                      Hydrolysates: chemistry / Protein Interaction Domains and
                      Motifs / Protein Isoforms: chemistry / Protein Isoforms:
                      metabolism / Protein Structure, Secondary / Rats /
                      Receptors, Metabotropic Glutamate: chemistry / Receptors,
                      Metabotropic Glutamate: genetics / Receptors, Metabotropic
                      Glutamate: metabolism / Recombinant Fusion Proteins:
                      chemistry / Recombinant Fusion Proteins: metabolism /
                      Spectrometry, Mass, Matrix-Assisted Laser
                      Desorption-Ionization / Peptide Fragments (NLM Chemicals) /
                      Protein Hydrolysates (NLM Chemicals) / Protein Isoforms (NLM
                      Chemicals) / Receptors, Metabotropic Glutamate (NLM
                      Chemicals) / Recombinant Fusion Proteins (NLM Chemicals) /
                      metabotropic glutamate receptor 6 (NLM Chemicals) /
                      metabotropic glutamate receptor 7 (NLM Chemicals) /
                      metabotropic glutamate receptor 8 (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung / NEUROCYPRES - Neurotransmitter
                      Cys-loop receptors: structure, function and disease
                      (202088)},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505 /
                      G:(EU-Grant)202088},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics / Cell
                      Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21219903},
      UT           = {WOS:000286657700011},
      doi          = {10.1016/j.febslet.2010.12.042},
      url          = {https://juser.fz-juelich.de/record/14601},
}