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@ARTICLE{Hofmann:136874,
      author       = {Hofmann, Julia P and Denner, Philip and Nussbaum-Krammer,
                      Carmen and Kuhn, Peer-Hendrik and Suhre, Michael H and
                      Scheibel, Thomas and Lichtenthaler, Stefan F and Schätzl,
                      Hermann M and Bano, Daniele and Vorberg, Ina M},
      title        = {{C}ell-to-cell propagation of infectious cytosolic protein
                      aggregates.},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {110},
      number       = {15},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {DZNE-2020-03196},
      pages        = {5951-5956},
      year         = {2013},
      abstract     = {Prions are self-templating protein conformers that
                      replicate by recruitment and conversion of homotypic
                      proteins into growing protein aggregates. Originally
                      identified as causative agents of transmissible spongiform
                      encephalopathies, increasing evidence now suggests that
                      prion-like phenomena are more common in nature than
                      previously anticipated. In contrast to fungal prions that
                      replicate in the cytoplasm, propagation of mammalian prions
                      derived from the precursor protein PrP is confined to the
                      cell membrane or endocytic vesicles. Here we demonstrate
                      that cytosolic protein aggregates can also behave as
                      infectious entities in mammalian cells. When expressed in
                      the mammalian cytosol, protein aggregates derived from the
                      prion domain NM of yeast translation termination factor
                      Sup35 persistently propagate and invade neighboring cells,
                      thereby inducing a self-perpetuating aggregation state of
                      NM. Cell contact is required for efficient infection.
                      Aggregates can also be induced in primary astrocytes,
                      neurons, and organotypic cultures, demonstrating that this
                      phenomenon is not specific to immortalized cells. Our data
                      have important implications for understanding prion-like
                      phenomena of protein aggregates associated with human
                      diseases and for the growing number of amyloidogenic
                      proteins discovered in mammals.},
      keywords     = {Animals / Astrocytes: cytology / Cell Communication /
                      Coculture Techniques / Cytoplasm: metabolism / Cytosol:
                      metabolism / Green Fluorescent Proteins: metabolism /
                      Hippocampus: metabolism / Mice / Microscopy, Confocal /
                      Peptide Termination Factors: metabolism / Prion Diseases /
                      Prions: metabolism / Protein Conformation / Saccharomyces
                      cerevisiae: metabolism / Saccharomyces cerevisiae Proteins:
                      metabolism / Peptide Termination Factors (NLM Chemicals) /
                      Prions (NLM Chemicals) / SUP35 protein, S cerevisiae (NLM
                      Chemicals) / Saccharomyces cerevisiae Proteins (NLM
                      Chemicals) / Green Fluorescent Proteins (NLM Chemicals)},
      cin          = {AG Lichtenthaler / AG Bano / AG Salomoni / AG Vorberg /
                      LAT},
      ddc          = {500},
      cid          = {I:(DE-2719)1110006 / I:(DE-2719)1013003 /
                      I:(DE-2719)1013032 / I:(DE-2719)1013004 /
                      I:(DE-2719)1040190},
      pnm          = {341 - Molecular Signaling (POF3-341) / 342 - Disease
                      Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-341 / G:(DE-HGF)POF3-342},
      experiment   = {EXP:(DE-2719)LAT-20190308},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23509289},
      pmc          = {pmc:PMC3625284},
      doi          = {10.1073/pnas.1217321110},
      url          = {https://pub.dzne.de/record/136874},
}