% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Chandramowlishwaran:139830,
      author       = {Chandramowlishwaran, Pavithra and Sun, Meng and Casey,
                      Kristin L and Romanyuk, Andrey V and Grizel, Anastasiya V
                      and Sopova, Julia V and Rubel, Aleksandr A and
                      Nussbaum-Krammer, Carmen and Vorberg, Ina M and Chernoff,
                      Yury O},
      title        = {{M}ammalian amyloidogenic proteins promote prion nucleation
                      in yeast.},
      journal      = {The journal of biological chemistry},
      volume       = {293},
      number       = {9},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.60645},
      reportid     = {DZNE-2020-06152},
      pages        = {3436-3450},
      year         = {2018},
      abstract     = {Fibrous cross-β aggregates (amyloids) and their
                      transmissible forms (prions) cause diseases in mammals
                      (including humans) and control heritable traits in yeast.
                      Initial nucleation of a yeast prion by transiently
                      overproduced prion-forming protein or its (typically,
                      QN-rich) prion domain is efficient only in the presence of
                      another aggregated (in most cases, QN-rich) protein. Here,
                      we demonstrate that a fusion of the prion domain of yeast
                      protein Sup35 to some non-QN-rich mammalian proteins,
                      associated with amyloid diseases, promotes nucleation of
                      Sup35 prions in the absence of pre-existing aggregates. In
                      contrast, both a fusion of the Sup35 prion domain to a
                      multimeric non-amyloidogenic protein and the expression of a
                      mammalian amyloidogenic protein that is not fused to the
                      Sup35 prion domain failed to promote prion nucleation,
                      further indicating that physical linkage of a mammalian
                      amyloidogenic protein to the prion domain of a yeast protein
                      is required for the nucleation of a yeast prion. Biochemical
                      and cytological approaches confirmed the nucleation of
                      protein aggregates in the yeast cell. Sequence alterations
                      antagonizing or enhancing amyloidogenicity of human
                      amyloid-β (associated with Alzheimer's disease) and mouse
                      prion protein (associated with prion diseases),
                      respectively, antagonized or enhanced nucleation of a yeast
                      prion by these proteins. The yeast-based prion nucleation
                      assay, developed in our work, can be employed for mutational
                      dissection of amyloidogenic proteins. We anticipate that it
                      will aid in the identification of chemicals that influence
                      initial amyloid nucleation and in searching for new
                      amyloidogenic proteins in a variety of proteomes.},
      keywords     = {Amyloid: metabolism / Amyloid beta-Peptides: metabolism /
                      Humans / Peptide Fragments: metabolism / Peptide Termination
                      Factors: chemistry / Peptide Termination Factors: metabolism
                      / Protein Aggregates / Protein Domains / Saccharomyces
                      cerevisiae Proteins: chemistry / Saccharomyces cerevisiae
                      Proteins: metabolism / Amyloid (NLM Chemicals) / Amyloid
                      beta-Peptides (NLM Chemicals) / Peptide Fragments (NLM
                      Chemicals) / Peptide Termination Factors (NLM Chemicals) /
                      Protein Aggregates (NLM Chemicals) / SUP35 protein, S
                      cerevisiae (NLM Chemicals) / Saccharomyces cerevisiae
                      Proteins (NLM Chemicals) / amyloid beta-protein (1-40) (NLM
                      Chemicals) / amyloid beta-protein (1-42) (NLM Chemicals)},
      cin          = {AG Vorberg},
      ddc          = {540},
      cid          = {I:(DE-2719)1013004},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29330303},
      pmc          = {pmc:PMC5836139},
      doi          = {10.1074/jbc.M117.809004},
      url          = {https://pub.dzne.de/record/139830},
}