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@ARTICLE{Ohhashi:858396,
      author       = {Ohhashi, Yumiko and Yamaguchi, Yoshiki and Kurahashi,
                      Hiroshi and Kamatari, Yuji O. and Sugiyama, Shinju and
                      Uluca, Boran and Piechatzek, Timo and Komi, Yusuke and
                      Shida, Toshinobu and Müller, Henrik and Hanashima, Shinya
                      and Heise, Henrike and Kuwata, Kazuo and Tanaka, Motomasa},
      title        = {{M}olecular basis for diversification of yeast prion strain
                      conformation},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {115},
      number       = {10},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2018-07282},
      pages        = {2389 - 2394},
      year         = {2018},
      abstract     = {Self-propagating β-sheet–rich fibrillar protein
                      aggregates, amyloidfibers, are often associated with
                      cellular dysfunction and disease.Distinct amyloid
                      conformations dictate different physiological
                      consequences,such as cellular toxicity. However, the origin
                      of the diversityof amyloid conformation remains unknown.
                      Here, we suggest thataltered conformational equilibrium in
                      natively disordered monomericproteins leads to the
                      adaptation of alternate amyloid conformationsthat have
                      different phenotypic effects. We performed acomprehensive
                      high-resolution structural analysis of Sup35NM, anN-terminal
                      fragment of the Sup35 yeast prion protein, and foundthat
                      monomeric Sup35NM harbored latent local compact
                      structuresdespite its overall disordered conformation. When
                      the hidden localmicrostructures were relaxed by genetic
                      mutations or solvent conditions,Sup35NM adopted a strikingly
                      different amyloid conformation,which redirected
                      chaperone-mediated fiber fragmentation and modulatedprion
                      strain phenotypes. Thus, dynamic conformational
                      fluctuationsin natively disordered monomeric proteins
                      represent aposttranslational mechanism for diversification
                      of aggregate structuresand cellular phenotypes.},
      cin          = {ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29467288},
      UT           = {WOS:000426671900066},
      doi          = {10.1073/pnas.1715483115},
      url          = {https://juser.fz-juelich.de/record/858396},
}