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@ARTICLE{Pellegrini:856112,
      author       = {Pellegrini, E. and Desfosses, A. and Wallmann, A. and
                      Schulze, W. M. and Rehbein, K. and Mas, P. and Signor, L.
                      and Gaudon, S. and Zenkeviciute, G. and Hons, M. and Malet,
                      H. and Gutsche, I. and Sachse, Carsten and Schoehn, G. and
                      Oschkinat, H. and Cusack, S.},
      title        = {{RIP}2 filament formation is required for {NOD}2 dependent
                      {NF}-κ{B} signalling},
      journal      = {Nature Communications},
      volume       = {9},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2018-05758},
      pages        = {4043},
      year         = {2018},
      abstract     = {Activation of the innate immune pattern recognition
                      receptor NOD2 by the bacterial muramyl-dipeptide
                      peptidoglycan fragment triggers recruitment of the
                      downstream adaptor kinase RIP2, eventually leading to NF-κB
                      activation and proinflammatory cytokine production. Here we
                      show that full-length RIP2 can form long filaments mediated
                      by its caspase recruitment domain (CARD), in common with
                      other innate immune adaptor proteins. We further show that
                      the NOD2 tandem CARDs bind to one end of the RIP2 CARD
                      filament, suggesting a mechanism for polar filament
                      nucleation by activated NOD2. We combine X-ray
                      crystallography, solid-state NMR and high-resolution
                      cryo-electron microscopy to determine the atomic structure
                      of the helical RIP2 CARD filament, which reveals the
                      intermolecular interactions that stabilize the assembly.
                      Using structure-guided mutagenesis, we demonstrate the
                      importance of RIP2 polymerization for the activation of
                      NF-κB signalling by NOD2. Our results could be of use to
                      develop new pharmacological strategies to treat inflammatory
                      diseases characterised by aberrant NOD2 signalling.},
      cin          = {ER-C-3},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30279485},
      UT           = {WOS:000446017000011},
      doi          = {10.1038/s41467-018-06451-3},
      url          = {https://juser.fz-juelich.de/record/856112},
}