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@ARTICLE{Eulitz:166794,
      author       = {Eulitz, S. and Sauer, Florian and Pelissier, M.-C. and
                      Boisguerin, P. and Molt, S. and Schuld, J. and Orfanos, Z.
                      and Kley, R. A. and Volkmer, R. and Wilmanns, M. and Kirfel,
                      G. and van der Ven, P. F. M. and Furst, D. O.},
      title        = {{I}dentification of {X}in-repeat proteins as novel ligands
                      of the {SH}3 domains of nebulin and nebulette and analysis
                      of their interaction during myofibril formation and
                      remodeling},
      journal      = {Molecular biology of the cell},
      volume       = {24},
      number       = {20},
      issn         = {1059-1524},
      address      = {Bethesda, Md.},
      publisher    = {American Society for Cell Biology},
      reportid     = {DESY-2014-01628},
      pages        = {3215 - 3226},
      year         = {2013},
      note         = {© Eulitz et al.},
      abstract     = {The Xin actin-binding repeat-containing proteins Xin and
                      XIRP2 are exclusively expressed in striated muscle cells,
                      where they are believed to play an important role in
                      development. In adult muscle, both proteins are concentrated
                      at attachment sites of myofibrils to the membrane. In
                      contrast, during development they are localized to immature
                      myofibrils together with their binding partner, filamin C,
                      indicating an involvement of both proteins in myofibril
                      assembly. We identify the SH3 domains of nebulin and
                      nebulette as novel ligands of proline-rich regions of Xin
                      and XIRP2. Precise binding motifs are mapped and shown to
                      bind both SH3 domains with micromolar affinity.
                      Cocrystallization of the nebulette SH3 domain with the
                      interacting XIRP2 peptide PPPTLPKPKLPKH reveals selective
                      interactions that conform to class II SH3 domain-binding
                      peptides. Bimolecular fluorescence complementation
                      experiments in cultured muscle cells indicate a temporally
                      restricted interaction of Xin-repeat proteins with
                      nebulin/nebulette during early stages of myofibril
                      development that is lost upon further maturation. In mature
                      myofibrils, this interaction is limited to longitudinally
                      oriented structures associated with myofibril development
                      and remodeling. These data provide new insights into the
                      role of Xin actin-binding repeat-containing proteins
                      (together with their interaction partners) in myofibril
                      assembly and after muscle damage.},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {DORIS Beamline K1.3 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-K1.3-20130405},
      experiment   = {EXP:(DE-H253)D-K1.3-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000328123800006},
      pubmed       = {pmid:23985323},
      doi          = {10.1091/mbc.E13-04-0202},
      url          = {https://bib-pubdb1.desy.de/record/166794},
}