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@ARTICLE{Zielinski:1016976,
      author       = {Zielinski, Mara and Peralta Reyes, Fernanda and Gremer,
                      Lothar and Schemmert, Sarah and Frieg, Benedikt and
                      Schäfer, Luisa and Willuweit, Antje and Donner, Lili and
                      Elvers, Margitta and Nilsson, Lars N. G. and Syvänen, Stina
                      and Sehlin, Dag and Ingelsson, Martin and Willbold, Dieter
                      and Schröder, Gunnar},
      title        = {{C}ryo-{EM} of {A}β {F}ibrils from {M}ouse {M}odels find
                      tg-{APPA}rc{S}we fibrils resemble those found in sporadic
                      {A}lzheimer's disease patients},
      journal      = {Nature neuroscience},
      volume       = {26},
      issn         = {1097-6256},
      address      = {New York, NY},
      publisher    = {Nature America},
      reportid     = {FZJ-2023-03883},
      pages        = {2073-2080},
      year         = {2023},
      abstract     = {The use of transgenic mice displaying amyloid-β (Aβ)
                      brain pathology has been essential for the preclinical
                      assessment of new treatment strategies for Alzheimer's
                      disease. However, the properties of Aβ in such mice have
                      not been systematically compared to Aβ in the brains of
                      patients with Alzheimer's disease. Here, we determined the
                      structures of nine ex vivo Aβ fibrils from six different
                      mouse models by cryogenic-electron microscopy. We found
                      novel Aβ fibril structures in the APP/PS1, ARTE10 and
                      tg-SwDI models, whereas the human type II filament fold was
                      found in the ARTE10, tg-APPSwe and APP23 models. The
                      tg-APPArcSwe mice showed an Aβ fibril whose structure
                      resembles the human type I filament found in patients with
                      sporadic Alzheimer's disease. A detailed assessment of the
                      Aβ fibril structure is key to the selection of adequate
                      mouse models for the preclinical development of novel
                      plaque-targeting therapeutics and positron emission
                      tomography imaging tracers in Alzheimer's disease.},
      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},
      pubmed       = {37973869},
      UT           = {WOS:001106141500001},
      doi          = {10.1038/s41593-023-01484-4},
      url          = {https://juser.fz-juelich.de/record/1016976},
}