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@ARTICLE{Zielinski:1047078,
      author       = {Zielinski, Mara and Peralta Reyes, Fernanda S. and Gremer,
                      Lothar and Sommerhage, Simon and Pagnon de la Vega, María
                      and Röder, Christine and Heidler, Thomas V. and Syvänen,
                      Stina and Willbold, Dieter and Sehlin, Dag and Ingelsson,
                      Martin and Schröder, Gunnar F.},
      title        = {{C}ryo-{EM} studies of amyloid-β fibrils from human and
                      murine brains carrying the {U}ppsala {APP} mutation
                      (Δ690–695)},
      journal      = {Acta Neuropathologica Communications},
      volume       = {13},
      number       = {1},
      issn         = {2051-5960},
      address      = {London},
      publisher    = {Biomed Central},
      reportid     = {FZJ-2025-04104},
      pages        = {209},
      year         = {2025},
      abstract     = {Today, 13 intra-amyloid-β (Aβ) amyloid precursor protein
                      (APP) gene mutations are known to cause familial
                      Alzheimer’s disease (AD). Most of them are point mutations
                      causing an increased production or a change in the
                      conformation of Aβ. The Uppsala APP mutation (Δ690–695
                      in APP, Δ19–24 in Aβ) is the first known multi-codon
                      deletion causing autosomal dominant AD. Here, we applied
                      cryo-electron microscopy (cryo-EM) to investigate the
                      structure of Aβ fibrils with the Uppsala APP mutation from
                      tg-UppSwe mouse brain tissue. Murine AβUpp(1–42)Δ19–24
                      are made of two identical S-shaped protofilaments with an
                      ordered fibril core of S8-A42. The murine Aβ fold is almost
                      identical to previously described human type II filaments,
                      although the amino acid sequences differ considerably. In
                      addition, we report the cryo-EM structure of Aβ fibrils
                      from the temporal cortex of a patient with the Uppsala APP
                      mutation. The observed structure of the human Aβ fold
                      closely resembles previously described type I fibrils.
                      Structural modeling suggests that these fibrils are composed
                      of wild-type Aβ, which implies that AβUpp may be less
                      soluble and thus not readily accessible for cryo-EM image
                      processing and structure determination. Additionally, from
                      the human sample we determined the structures of tau paired
                      helical filaments and tau straight filaments, which are
                      identical to those found in sporadic AD cases. Finally, we
                      present the 3D cryo-EM structures of four dominant
                      AβUpp(1–42)Δ19–24 fibril polymorphs, formed in vitro.
                      All four polymorphs differ from the observed folds of
                      Uppsala Aβ in murine and human brain tissue, respectively.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1186/s40478-025-02120-x},
      url          = {https://juser.fz-juelich.de/record/1047078},
}