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@ARTICLE{Huang:140705,
      author       = {Huang, Chaolie and Wagner-Valladolid, Sara and Stephens,
                      Amberley D and Jung, Raimund and Poudel, Chetan and Sinnige,
                      Tessa and Lechler, Marie C and Schlörit, Nicole and Lu,
                      Meng and Laine, Romain F and Michel, Claire H and
                      Vendruscolo, Michele and Kaminski, Clemens F and Kaminski
                      Schierle, Gabriele S and David, Della C},
      title        = {{I}ntrinsically aggregation-prone proteins form
                      amyloid-like aggregates and contribute to tissue aging in
                      {C}aenorhabditis elegans.},
      journal      = {eLife},
      volume       = {8},
      issn         = {2050-084X},
      address      = {Cambridge},
      publisher    = {eLife Sciences Publications},
      reportid     = {DZNE-2020-07027},
      pages        = {e43059},
      year         = {2019},
      abstract     = {Reduced protein homeostasis leading to increased protein
                      instability is a common molecular feature of aging, but it
                      remains unclear whether this is a cause or consequence of
                      the aging process. In neurodegenerative diseases and other
                      amyloidoses, specific proteins self-assemble into amyloid
                      fibrils and accumulate as pathological aggregates in
                      different tissues. More recently, widespread protein
                      aggregation has been described during normal aging. Until
                      now, an extensive characterization of the nature of
                      age-dependent protein aggregation has been lacking. Here, we
                      show that age-dependent aggregates are rapidly formed by
                      newly synthesized proteins and have an amyloid-like
                      structure resembling that of protein aggregates observed in
                      disease. We then demonstrate that age-dependent protein
                      aggregation accelerates the functional decline of different
                      tissues in C. elegans. Together, these findings imply that
                      amyloid-like aggregates contribute to the aging process and
                      therefore could be important targets for strategies designed
                      to maintain physiological functions in the late stages of
                      life.},
      keywords     = {Aging / Amyloid: metabolism / Animals / Caenorhabditis
                      elegans: physiology / Caenorhabditis elegans Proteins:
                      metabolism / Protein Aggregates},
      cin          = {AG David},
      ddc          = {600},
      cid          = {I:(DE-2719)1210004},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31050339},
      pmc          = {pmc:PMC6524967},
      doi          = {10.7554/eLife.43059},
      url          = {https://pub.dzne.de/record/140705},
}