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@ARTICLE{Friker:151661,
      author       = {Friker, Lea L. and Scheiblich, Hannah and Hochheiser, Inga
                      V. and Brinkschulte, Rebecca and Riedel, Dietmar and Latz,
                      Eicke and Geyer, Matthias and Heneka, Michael T.},
      title        = {β-{A}myloid {C}lustering around {ASC} {F}ibrils {B}oosts
                      {I}ts {T}oxicity in {M}icroglia},
      journal      = {Cell reports},
      volume       = {30},
      number       = {11},
      issn         = {2211-1247},
      address      = {[New York, NY]},
      publisher    = {Elsevier},
      reportid     = {DZNE-2020-01240},
      pages        = {3743 - 3754.e6},
      year         = {2020},
      abstract     = {Alzheimer’s disease is the world’s most common
                      neurodegenerative disorder. It is associated with
                      neuroinflammation involving activation of microglia by
                      β-amyloid (Aβ) deposits. Based on previous studies showing
                      apoptosis-associated speck-like protein containing a CARD
                      (ASC) binding and cross-seeding extracellular Aβ, we
                      investigate the propagation of ASC between primary microglia
                      and the effects of ASC-Aβ composites on microglial
                      inflammasomes and function. Indeed, ASC released by a
                      pyroptotic cell can be functionally built into the
                      neighboring microglia NOD-like receptor protein (NLRP3)
                      inflammasome. Compared with protein-only application,
                      exposure to ASC-Aβ composites amplifies the proinflammatory
                      response, resulting in pyroptotic cell death, setting free
                      functional ASC and inducing a feedforward stimulating
                      vicious cycle. Clustering around ASC fibrils also
                      compromises clearance of Aβ by microglia. Together, these
                      data enable a closer look at the turning point from acute to
                      chronic Aβ-related neuroinflammation through formation of
                      ASC-Aβ composites.},
      keywords     = {Amyloid beta-Peptides: metabolism / Amyloid beta-Peptides:
                      toxicity / Amyloid beta-Peptides: ultrastructure / Animals /
                      CARD Signaling Adaptor Proteins: metabolism / Caspase 1:
                      metabolism / Cells, Cultured / Humans / Inflammasomes:
                      metabolism / Interleukin-1beta: metabolism / Mice, Inbred
                      C57BL / Microglia: drug effects / Microglia: metabolism /
                      Microglia: pathology / Models, Biological / NLR Family,
                      Pyrin Domain-Containing 3 Protein: metabolism / Proteolysis:
                      drug effects / Pyroptosis: drug effects / Signal
                      Transduction: drug effects / Toll-Like Receptor 2:
                      metabolism / Toll-Like Receptor 4: metabolism},
      cin          = {AG Heneka ; AG Heneka},
      ddc          = {610},
      cid          = {I:(DE-2719)1011303},
      pnm          = {344 - Clinical and Health Care Research (POF3-344)},
      pid          = {G:(DE-HGF)POF3-344},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC8729885},
      pubmed       = {pmid:32187546},
      doi          = {10.1016/j.celrep.2020.02.025},
      url          = {https://pub.dzne.de/record/151661},
}