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@ARTICLE{Clemen:126273,
      author       = {C. S. Clemen and F. Stöckigt and K.-H. Strucksberg and F.
                      Chevessier and L. Winter and J. Schütz and R. Bauer and
                      J.-M. Thorweihe and D. Wenzel and U. Schlötzer-Schrehardt
                      and V. Rasche and P. Krsmanovic$^*$ and H. A. Katus and W.
                      Rottbauer and S. Just and O. J. Müller and O. Friedrich and
                      R. Meyer and H. Herrmann$^*$ and J. W. Schrickel and R.
                      Schröder},
      title        = {{T}he toxic effect of {R}350{P} mutant desmin in striated
                      muscle of man and mouse.},
      journal      = {Acta neuropathologica},
      volume       = {129},
      number       = {2},
      issn         = {1432-0533},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {DKFZ-2017-02388},
      pages        = {297 - 315},
      year         = {2015},
      abstract     = {Mutations of the human desmin gene on chromosome 2q35 cause
                      autosomal dominant, autosomal recessive and sporadic forms
                      of protein aggregation myopathies and cardiomyopathies. We
                      generated R349P desmin knock-in mice, which harbor the
                      ortholog of the most frequently occurring human desmin
                      missense mutation R350P. These mice develop age-dependent
                      desmin-positive protein aggregation pathology, skeletal
                      muscle weakness, dilated cardiomyopathy, as well as cardiac
                      arrhythmias and conduction defects. For the first time, we
                      report the expression level and subcellular distribution of
                      mutant versus wild-type desmin in our mouse model as well as
                      in skeletal muscle specimens derived from human R350P
                      desminopathies. Furthermore, we demonstrate that the
                      missense-mutant desmin inflicts changes of the subcellular
                      localization and turnover of desmin itself and of direct
                      desmin-binding partners. Our findings unveil a novel
                      principle of pathogenesis, in which not the presence of
                      protein aggregates, but disruption of the extrasarcomeric
                      intermediate filament network leads to increased mechanical
                      vulnerability of muscle fibers. These structural defects
                      elicited at the myofiber level finally impact the entire
                      organ and subsequently cause myopathy and cardiomyopathy.},
      keywords     = {Desmin (NLM Chemicals) / RNA, Messenger (NLM Chemicals) /
                      Recombinant Proteins (NLM Chemicals)},
      cin          = {B065},
      ddc          = {610},
      cid          = {I:(DE-He78)B065-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25394388},
      pmc          = {pmc:PMC4309020},
      doi          = {10.1007/s00401-014-1363-2},
      url          = {https://inrepo02.dkfz.de/record/126273},
}