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@ARTICLE{Mayans:390618,
      author       = {Mayans, O. and van der Ven, P. F. and Wilm, M. and Mues, A.
                      and Young, P. and Fürst, D. O. and Wilmanns, M. and Gautel,
                      M.},
      title        = {{S}tructural basis for activation of the titin kinase
                      domain during myofibrillogenesis.},
      journal      = {Nature},
      volume       = {395},
      number       = {6705},
      issn         = {0028-0836},
      address      = {London [u.a.]},
      publisher    = {Nature Publ. Group},
      reportid     = {PUBDB-2017-09675},
      pages        = {863 - 869},
      year         = {1998},
      note         = {F-Bereich; EMBL},
      abstract     = {The giant muscle protein titin (connectin) is essential in
                      the temporal and spatial control of the assembly of the
                      highly ordered sarcomeres (contractile units) of striated
                      muscle. Here we present the crystal structure of titin's
                      only catalytic domain, an autoregulated serine kinase (titin
                      kinase). The structure shows how the active site is
                      inhibited by a tyrosine of the kinase domain. We describe a
                      dual mechanism of activation of titin kinase that consists
                      of phosphorylation of this tyrosine and binding of
                      calcium/calmodulin to the regulatory tail. The serine kinase
                      domain of titin is the first known non-arginine-aspartate
                      kinase to be activated by phosphorylation. The
                      phosphorylated tyrosine is not located in the activation
                      segment, as in other kinases, but in the P + 1 loop,
                      indicating that this tyrosine is a binding partner of the
                      titin kinase substrate. Titin kinase phosphorylates the
                      muscle protein telethonin in early differentiating myocytes,
                      indicating that this kinase may act in myofibrillogenesis.},
      keywords     = {Connectin (NLM Chemicals) / Muscle Proteins (NLM Chemicals)
                      / Protein Kinase Inhibitors (NLM Chemicals) / Recombinant
                      Proteins (NLM Chemicals) / TCAP protein, human (NLM
                      Chemicals) / TTN protein, human (NLM Chemicals) / Tyrosine
                      (NLM Chemicals) / Protein Kinases (NLM Chemicals)},
      cin          = {DESY(-2012)},
      ddc          = {070},
      cid          = {$I:(DE-H253)DESY_-2012_-20170516$},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:9804419},
      UT           = {WOS:00},
      doi          = {10.1038/27603},
      url          = {https://bib-pubdb1.desy.de/record/390618},
}