% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Kopp:618906,
      author       = {Kopp, Anja and Hagelueken, Gregor and Jamitzky, Isabell and
                      Moecking, Jonas and Schiffelers, Lisa D. J. and Schmidt,
                      Florian I. and Geyer, Matthias},
      title        = {{P}yroptosis inhibiting nanobodies block {G}asdermin {D}
                      pore formation},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2024-07228},
      pages        = {7923},
      year         = {2023},
      abstract     = {Human Gasdermin D (GSDMD) is a key mediator of pyroptosis,
                      a pro-inflammatory form of cell death occurring downstream
                      of inflammasome activation as part of the innate immune
                      defence. Upon cleavage by inflammatory caspases in the
                      cytosol, the N-terminal domain of GSDMD forms pores in the
                      plasma membrane resulting in cytokine release and eventually
                      cell death. Targeting GSDMD is an attractive way to dampen
                      inflammation. In this study, six GSDMD targeting nanobodies
                      are characterized in terms of their binding affinity,
                      stability, and effect on GSDMD pore formation. Three of the
                      nanobodies inhibit GSDMD pore formation in a liposome
                      leakage assay, although caspase cleavage was not perturbed.
                      We determine the crystal structure of human GSDMD in complex
                      with two nanobodies at 1.9 Å resolution, providing
                      detailed insights into the GSDMD–nanobody interactions and
                      epitope binding. The pore formation is sterically blocked by
                      one of the nanobodies that binds to the oligomerization
                      interface of the N-terminal domain in the multi-subunit pore
                      assembly. Our biochemical and structural findings provide
                      tools for studying inflammasome biology and build a
                      framework for the design of GSDMD targeting drugs.},
      cin          = {EMBL-User},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project
                      G:(GEPRIS)390873048 - EXC 2151: ImmunoSensation2 - the
                      immune sensory system (390873048) / GRK 2168 -
                      Internationales Graduiertenkolleg 2168 – Myeloid antigen
                      presenting cells and the induction of adaptive immunity
                      (GRK-2168-20170406)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)390873048 /
                      G:(DE-Juel1)GRK-2168-20170406},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38040708},
      UT           = {WOS:001113452500033},
      doi          = {10.1038/s41467-023-43707-z},
      url          = {https://bib-pubdb1.desy.de/record/618906},
}