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@ARTICLE{Liu:259955,
      author       = {Liu, Shu and Heumueller, Stefanie-Elisabeth and Hossinger,
                      André and Müller, Stephan A and Buravlova, Oleksandra and
                      Lichtenthaler, Stefan F and Denner, Philip and Vorberg, Ina
                      M},
      title        = {{R}eactivated endogenous retroviruses promote protein
                      aggregate spreading.},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DZNE-2023-00808},
      pages        = {5034},
      year         = {2023},
      abstract     = {Prion-like spreading of protein misfolding is a
                      characteristic of neurodegenerative diseases, but the exact
                      mechanisms of intercellular protein aggregate dissemination
                      remain unresolved. Evidence accumulates that endogenous
                      retroviruses, remnants of viral germline infections that are
                      normally epigenetically silenced, become upregulated in
                      neurodegenerative diseases such as amyotrophic lateral
                      sclerosis and tauopathies. Here we uncover that activation
                      of endogenous retroviruses affects prion-like spreading of
                      proteopathic seeds. We show that upregulation of endogenous
                      retroviruses drastically increases the dissemination of
                      protein aggregates between cells in culture, a process that
                      can be inhibited by targeting the viral envelope protein or
                      viral protein processing. Human endogenous retrovirus
                      envelopes of four different clades also elevate
                      intercellular spreading of proteopathic seeds, including
                      pathological Tau. Our data support a role of endogenous
                      retroviruses in protein misfolding diseases and suggest that
                      antiviral drugs could represent promising candidates for
                      inhibiting protein aggregate spreading.},
      keywords     = {Humans / Endogenous Retroviruses: genetics / Protein
                      Aggregates / Amyotrophic Lateral Sclerosis / Antiviral
                      Agents / Prions / Protein Aggregates (NLM Chemicals) /
                      Antiviral Agents (NLM Chemicals) / Prions (NLM Chemicals)},
      cin          = {AG Vorberg / AG Fava / AG Lichtenthaler / LAT},
      ddc          = {500},
      cid          = {I:(DE-2719)1013004 / I:(DE-2719)1040000 /
                      I:(DE-2719)1110006 / I:(DE-2719)1040190},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      experiment   = {EXP:(DE-2719)LAT-20190308},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37596282},
      pmc          = {pmc:PMC10439213},
      doi          = {10.1038/s41467-023-40632-z},
      url          = {https://pub.dzne.de/record/259955},
}