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@ARTICLE{Chatziefthimiou:603747,
      author       = {Chatziefthimiou, Spyros D. and Hornburg, Philipp and Sauer,
                      Florian and Mueller, Simone and Ugurlar, Deniz and Xu,
                      Emma-Ruoqi and Wilmanns, Matthias},
      title        = {{S}tructural diversity in the atomic resolution 3{D}
                      fingerprint of the titin {M}-band segment},
      journal      = {PLOS ONE},
      volume       = {14},
      number       = {12},
      issn         = {1932-6203},
      address      = {San Francisco, California, US},
      publisher    = {PLOS},
      reportid     = {PUBDB-2024-00932},
      pages        = {e0226693 -},
      year         = {2019},
      abstract     = {In striated muscles, molecular filaments are largely
                      composed of long protein chains with extensive arrays of
                      identically folded domains, referred to as
                      “beads-on-a-string”. It remains a largely unresolved
                      question how these domains have developed a unique molecular
                      profile such that each carries out a distinct function
                      without false-positive readout. This study focuses on the
                      M-band segment of the sarcomeric protein titin, which
                      comprises ten identically folded immunoglobulin domains.
                      Comparative analysis of high-resolution structures of six of
                      these domains ‒ M1, M3, M4, M5, M7, and M10 ‒ reveals
                      considerable structural diversity within three distinct
                      loops and a non-conserved pattern of exposed cysteines. Our
                      data allow to structurally interpreting distinct
                      pathological readouts that result from
                      titinopathy-associated variants. Our findings support
                      general principles that could be used to identify individual
                      structural/functional profiles of hundreds of identically
                      folded protein domains within the sarcomere and other
                      densely crowded cellular environments.},
      cin          = {EMBL},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)D-K1.3-20150101 /
                      EXP:(DE-H253)D-K1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {31856237},
      UT           = {WOS:000534249400059},
      doi          = {10.1371/journal.pone.0226693},
      url          = {https://bib-pubdb1.desy.de/record/603747},
}