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@ARTICLE{Ribeiro:207413,
      author       = {Ribeiro, Euripedes de Almeida and Pinotsis, Nikos and
                      Ghisleni, Andrea and Salmazo, Anita and Konarev, Petr and
                      Kostan, Julius and Sjöblom, Björn and Schreiner, Claudia
                      and Polyansky, Anton A. and Gkougkoulia, Eirini A. and
                      Holt, Mark R. and Aachmann, Finn L. and Žagrović, Bojan
                      and Bordignon, Enrica and Pirker, Katharina F. and Svergun,
                      Dmitri and Gautel, Mathias and Djinović-Carugo, Kristina},
      title        = {{T}he {S}tructure and {R}egulation of {H}uman {M}uscle
                      $\alpha$-{A}ctinin},
      journal      = {Cell},
      volume       = {159},
      number       = {6},
      issn         = {0092-8674},
      address      = {[Cambridge, Mass.]},
      publisher    = {Cell Press},
      reportid     = {PUBDB-2015-01323},
      pages        = {1447 - 1460},
      year         = {2014},
      note         = {OA},
      abstract     = {The spectrin superfamily of proteins plays key roles in
                      assembling the actin cytoskeleton in various cell types,
                      crosslinks actin filaments, and acts as scaffolds for the
                      assembly of large protein complexes involved in structural
                      integrity and mechanosensation, as well as cell signaling.
                      α-actinins in particular are the major actin crosslinkers
                      in muscle Z-disks, focal adhesions, and actin stress fibers.
                      We report a complete high-resolution structure of the 200
                      kDa α-actinin-2 dimer from striated muscle and explore its
                      functional implications on the biochemical and cellular
                      level. The structure provides insight into the
                      phosphoinositide-based mechanism controlling its interaction
                      with sarcomeric proteins such as titin, lays a foundation
                      for studying the impact of pathogenic mutations at molecular
                      resolution, and is likely to be broadly relevant for the
                      regulation of spectrin-like proteins},
      cin          = {EMBL / EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)EMBL-User-20120814},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13) / BIOSTRUCT-X -
                      Transnational access and enhancement of integrated
                      Biological Structure determination at synchrotron X-ray
                      radiation facilities (283570)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405 / G:(EU-Grant)283570},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000346652900021},
      pubmed       = {pmid:25433700},
      doi          = {10.1016/j.cell.2014.10.056},
      url          = {https://bib-pubdb1.desy.de/record/207413},
}