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@ARTICLE{Gerresheim:890029,
      author       = {Gerresheim, Else F. and Herring, Arne and Gremer, Lothar
                      and Müller‐Schiffmann, Andreas and Keyvani, Kathy and
                      Korth, Carsten},
      title        = {{T}he interaction of insoluble {A}myloid‐β with soluble
                      {A}myloid‐β dimers decreases {A}myloid‐β plaque
                      numbers},
      journal      = {Neuropathology $\&$ applied neurobiology},
      volume       = {47},
      number       = {5},
      issn         = {1365-2990},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2021-00623},
      pages        = {603-610},
      year         = {2021},
      abstract     = {ObjectivesThe heterogeneity of Amyloid‐beta (Aβ) plaque
                      load in patients with Alzheimer's disease (AD) has puzzled
                      neuropathology. Since brain Aβ plaque load does not
                      correlate with cognitive decline, neurotoxic soluble Aβ
                      oligomers have been championed as disease‐causing agents
                      in early AD. So far, investigating molecular interactions
                      between soluble oligomeric Aβ and insoluble Aβ in vivo has
                      been difficult because of the abundance of Aβ oligomer
                      species and the kinetic equilibrium in which they coexist.
                      Here, we investigated whether Aβ plaque heterogeneity
                      relates to interactions of different Aβ
                      conformers.Materials and MethodsWe took advantage of
                      transgenic mice that generate exclusively Aβ dimers
                      (tgDimer mice) but do not develop Aβ plaques or
                      neuroinflammation during their lifetime, crossed them to the
                      transgenic CRND8 mice that develop plaques after 90 days and
                      measured Aβ plaque load using immunohistochemical and
                      biochemical assays. Furthermore, we performed in vitro
                      thioflavin T (ThT) aggregation assays titrating synthetic
                      Aβ42‐S8C dimers into fibril‐forming synthetic
                      Aβ42.ResultsWe observed a lower number of Aβ plaques in
                      the brain of double transgenic mice compared to tgCRND8 mice
                      alone while the average plaque size remained unaltered.
                      Corroborating these in vivo findings, synthetic Aβ‐S8C
                      dimers inhibited fibril formation of wild‐type Aβ also in
                      vitro, seen by an increased half‐time in the ThT
                      assay.ConclusionsOur study indicates that Aβ dimers
                      directly interfere with Aβ fibril formation in vivo and in
                      vitro. The variable interaction of Aβ dimers with insoluble
                      Aβ seeds could thus contribute to the heterogeneity of Aβ
                      plaque load in AD patients.},
      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       = {33338256},
      UT           = {WOS:000605339600001},
      doi          = {10.1111/nan.12685},
      url          = {https://juser.fz-juelich.de/record/890029},
}