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@ARTICLE{Rder:864649,
      author       = {Röder, Christine and Vettore, Nicola and Mangels, Lena N.
                      and Gremer, Lothar and Ravelli, Raimond B. G. and Willbold,
                      Dieter and Hoyer, Wolfgang and Buell, Alexander K. and
                      Schröder, Gunnar},
      title        = {{A}tomic structure of {PI}3-kinase {SH}3 amyloid fibrils by
                      cryo-electron microscopy},
      journal      = {Nature Communications},
      volume       = {10},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2019-04351},
      pages        = {3754},
      year         = {2019},
      abstract     = {High resolution structural information on amyloid fibrils
                      is crucial for the understanding of their formation
                      mechanisms and for the rational design of amyloid inhibitors
                      in the context of protein misfolding diseases. The
                      Src-homology 3 domain of phosphatidyl-inositol-3-kinase
                      (PI3K-SH3) is a model amyloid system that plays a pivotal
                      role in our basic understanding of protein misfolding and
                      aggregation. Here, we present the atomic model of the
                      PI3K-SH3 amyloid fibril with a resolution determined to
                      3.4 Å by cryo-electron microscopy (cryo-EM). The fibril
                      is composed of two intertwined protofilaments that create an
                      interface spanning 13 residues from each monomer. The model
                      comprises residues 1–77 out of 86 amino acids in total,
                      with the missing residues located in the highly flexible
                      C-terminus. The fibril structure allows us to rationalise
                      the effects of chemically conservative point mutations as
                      well as of the previously reported sequence perturbations on
                      PI3K-SH3 fibril formation and growth.},
      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:31434882},
      UT           = {WOS:000482004000006},
      doi          = {10.1038/s41467-019-11320-8},
      url          = {https://juser.fz-juelich.de/record/864649},
}