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@ARTICLE{Lu:153359,
      author       = {Lu, Alvin and Magupalli, Venkat Giri and Ruan, Jianbin and
                      Yin, Qian and Atianand, Maninjay K. and Vos, Matthijn R. and
                      Schröder, Gunnar F. and Fitzgerald, Katherine A. and Wu,
                      Hao and Egelman, Edward H.},
      title        = {{U}nified {P}olymerization {M}echanism for the {A}ssembly
                      of {ASC}-{D}ependent {I}nflammasomes},
      journal      = {Cell},
      volume       = {156},
      number       = {6},
      issn         = {0092-8674},
      address      = {[Cambridge, Mass.]},
      publisher    = {Cell Press},
      reportid     = {FZJ-2014-02990},
      pages        = {1193 - 1206},
      year         = {2014},
      note         = {Bitte ändern Sie "Schröder, Gunnar" in "Schröder, Gunnar
                      F." um.},
      abstract     = {Inflammasomes elicit host defense inside cells by
                      activating caspase-1 for cytokine maturation and cell death.
                      AIM2 and NLRP3 are representative sensor proteins in two
                      major families of inflammasomes. The adaptor protein ASC
                      bridges the sensor proteins and caspase-1 to form ternary
                      inflammasome complexes, achieved through pyrin domain (PYD)
                      interactions between sensors and ASC and through caspase
                      activation and recruitment domain (CARD) interactions
                      between ASC and caspase-1. We found that PYD and CARD both
                      form filaments. Activated AIM2 and NLRP3 nucleate PYD
                      filaments of ASC, which, in turn, cluster the CARD of ASC.
                      ASC thus nucleates CARD filaments of caspase-1, leading to
                      proximity-induced activation. Endogenous NLRP3 inflammasome
                      is also filamentous. The cryoelectron microscopy structure
                      of ASCPYD filament at near-atomic resolution provides a
                      template for homo- and hetero-PYD/PYD associations, as
                      confirmed by structure-guided mutagenesis. We propose that
                      ASC-dependent inflammasomes in both families share a unified
                      assembly mechanism that involves two successive steps of
                      nucleation-induced polymerization.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000332945100010},
      pubmed       = {pmid:24630722},
      doi          = {10.1016/j.cell.2014.02.008},
      url          = {https://juser.fz-juelich.de/record/153359},
}