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@ARTICLE{Schtzmann:904323,
      author       = {Schützmann, Marie P. and Hasecke, Filip and Bachmann,
                      Sarah and Zielinski, Mara and Hänsch, Sebastian and
                      Schröder, Gunnar F. and Zempel, Hans and Hoyer, Wolfgang},
      title        = {{E}ndo-lysosomal {A}β concentration and p{H} trigger
                      formation of {A}β oligomers that potently induce {T}au
                      missorting},
      journal      = {Nature Communications},
      volume       = {12},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2021-05893},
      pages        = {4634},
      year         = {2021},
      abstract     = {Amyloid-β peptide (Aβ) forms metastable oligomers >50
                      kDa, termed AβOs, that are more effective than Aβ amyloid
                      fibrils at triggering Alzheimer’s disease-related
                      processes such as synaptic dysfunction and Tau pathology,
                      including Tau mislocalization. In neurons, Aβ accumulates
                      in endo-lysosomal vesicles at low pH. Here, we show that the
                      rate of AβO assembly is accelerated 8,000-fold upon pH
                      reduction from extracellular to endo-lysosomal pH, at the
                      expense of amyloid fibril formation. The pH-induced
                      promotion of AβO formation and the high endo-lysosomal Aβ
                      concentration together enable extensive AβO formation of
                      Aβ42 under physiological conditions. Exploiting the
                      enhanced AβO formation of the dimeric Aβ variant dimAβ we
                      furthermore demonstrate targeting of AβOs to dendritic
                      spines, potent induction of Tau missorting, a key factor in
                      tauopathies, and impaired neuronal activity. The results
                      suggest that the endosomal/lysosomal system is a major site
                      for the assembly of pathomechanistically relevant AβOs.},
      cin          = {IBI-7},
      ddc          = {500},
      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       = {pmid:34330900},
      UT           = {WOS:000684302900001},
      doi          = {10.1038/s41467-021-24900-4},
      url          = {https://juser.fz-juelich.de/record/904323},
}