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Inflammasome sensor NLRP1 disease variant M1184V promotes autoproteolysis and DPP9 complex formation by stabilizing the FIIND domain.
Moecking, Jonas; Laohamonthonkul, Pawat; Mese, Kubilay; Hagelueken, Gregor; Steiner, Annemarie; Harapas, Cassandra R; Sandow, Jarrod J; Graves, Jonathan D; Masters, Seth L; Geyer, Matthias.
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  • Moecking J; Institute of Structural Biology, Medical Faculty, University of Bonn, Bonn, Germany.
  • Laohamonthonkul P; Inflammation Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, Australia; Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.
  • Mese K; Institute of Structural Biology, Medical Faculty, University of Bonn, Bonn, Germany.
  • Hagelueken G; Institute of Structural Biology, Medical Faculty, University of Bonn, Bonn, Germany.
  • Steiner A; Institute of Structural Biology, Medical Faculty, University of Bonn, Bonn, Germany; Inflammation Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, Australia; Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.
  • Harapas CR; Inflammation Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, Australia; Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.
  • Sandow JJ; Inflammation Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, Australia; Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.
  • Graves JD; IFM Therapeutics, Boston, Massachusetts, USA.
  • Masters SL; Inflammation Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, Australia; Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.
  • Geyer M; Institute of Structural Biology, Medical Faculty, University of Bonn, Bonn, Germany. Electronic address: matthias.geyer@uni-bonn.de.
J Biol Chem ; 298(12): 102645, 2022 12.
Article en En | MEDLINE | ID: mdl-36309085
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Enfermedades Autoinmunes / Dipeptidil-Peptidasas y Tripeptidil-Peptidasas / Inflamasomas / Proteínas NLR Límite: Humans Idioma: En Revista: J Biol Chem Año: 2022 Tipo del documento: Article País de afiliación: Alemania
Texto completo
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Enfermedades Autoinmunes / Dipeptidil-Peptidasas y Tripeptidil-Peptidasas / Inflamasomas / Proteínas NLR Límite: Humans Idioma: En Revista: J Biol Chem Año: 2022 Tipo del documento: Article País de afiliación: Alemania