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@ARTICLE{Drnberger:140086,
      author       = {Dürnberger, Yvonne and Liu, Shu and Riemschoß, Katrin and
                      Paulsen, Lydia and Bester, Romina and Kuhn, Peer-Hendrik and
                      Schölling, Manuel and Lichtenthaler, Stefan F and Vorberg,
                      Ina},
      title        = {{P}rion {R}eplication in the {M}ammalian {C}ytosol:
                      {F}unctional {R}egions within a {P}rion {D}omain {D}riving
                      {I}nduction, {P}ropagation, and {I}nheritance.},
      journal      = {Molecular and cellular biology},
      volume       = {38},
      number       = {15},
      issn         = {0270-7306},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {DZNE-2020-06408},
      pages        = {e00111-18/mcb/38/15/e00111-18.atom},
      year         = {2018},
      abstract     = {Prions of lower eukaryotes are transmissible protein
                      particles that propagate by converting homotypic soluble
                      proteins into growing protein assemblies. Prion activity is
                      conferred by so-called prion domains, regions of low
                      complexity that are often enriched in glutamines and
                      asparagines (Q/N). The compositional similarity of fungal
                      prion domains with intrinsically disordered domains found in
                      many mammalian proteins raises the question of whether
                      similar sequence elements can drive prion-like phenomena in
                      mammals. Here, we define sequence features of the prototype
                      Saccharomyces cerevisiae Sup35 prion domain that govern
                      prion activities in mammalian cells by testing the ability
                      of deletion mutants to assemble into self-perpetuating
                      particles. Interestingly, the amino-terminal Q/N-rich tract
                      crucially important for prion induction in yeast was
                      dispensable for the prion life cycle in mammalian cells.
                      Spontaneous and template-assisted prion induction, growth,
                      and maintenance were preferentially driven by the
                      carboxy-terminal region of the prion domain that contains a
                      putative soft amyloid stretch recently proposed to act as a
                      nucleation site for prion assembly. Our data demonstrate
                      that preferred prion nucleation domains can differ between
                      lower and higher eukaryotes, resulting in the formation of
                      prions with strikingly different amyloid cores.},
      keywords     = {Amino Acid Sequence / Animals / Binding Sites / Cell Line /
                      Cytosol: metabolism / Mice / Models, Molecular / Mutation /
                      Peptide Termination Factors: biosynthesis / Peptide
                      Termination Factors: chemistry / Peptide Termination
                      Factors: genetics / Prion Proteins: biosynthesis / Prion
                      Proteins: chemistry / Prion Proteins: genetics / Prions:
                      biosynthesis / Prions: chemistry / Prions: genetics /
                      Protein Aggregates: genetics / Protein Aggregation,
                      Pathological: genetics / Protein Aggregation, Pathological:
                      metabolism / Protein Domains / Protein Folding / Recombinant
                      Proteins: biosynthesis / Recombinant Proteins: chemistry /
                      Recombinant Proteins: genetics / Saccharomyces cerevisiae
                      Proteins: biosynthesis / Saccharomyces cerevisiae Proteins:
                      chemistry / Saccharomyces cerevisiae Proteins: genetics /
                      Sequence Deletion / Peptide Termination Factors (NLM
                      Chemicals) / Prion Proteins (NLM Chemicals) / Prions (NLM
                      Chemicals) / Protein Aggregates (NLM Chemicals) /
                      Recombinant Proteins (NLM Chemicals) / SUP35 protein, S
                      cerevisiae (NLM Chemicals) / Saccharomyces cerevisiae
                      Proteins (NLM Chemicals)},
      cin          = {AG Vorberg / AG Lichtenthaler / IDAF},
      ddc          = {570},
      cid          = {I:(DE-2719)1013004 / I:(DE-2719)1110006 /
                      I:(DE-2719)1040200},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      experiment   = {EXP:(DE-2719)IDAF-20190308},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29784771},
      pmc          = {pmc:PMC6048315},
      doi          = {10.1128/MCB.00111-18},
      url          = {https://pub.dzne.de/record/140086},
}