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• W2992534356 abstract "Significance Inflammasomes are cytosolic protein complexes that detect the presence of pathogens and damages to elicit immune responses, and dysregulation in inflammasome signaling is associated with many human diseases. As the unified downstream effector of canonical inflammasomes, caspase-1 is recruited though CARD–CARD interactions with the adaptor proteins ASC or NLRC4. We have determined the cryo-EM structures of ASC CARD and NLRC4 CARD filaments. Using multidisciplinary methods, we reveal a common mechanism of caspase-1 CARD nucleation, assembly, and activation by equivalent assembly patterns in ASC and NLRC4. Collectively, our data provide insights into inflammasome assembly and activation and afford structural platforms for modulating these CARD–CARD interactions in potential therapeutic applications." @default.
• W2992534356 created "2019-12-13" @default.
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• W2992534356 date "2018-10-02" @default.
• W2992534356 modified "2023-09-26" @default.
• W2992534356 title "Cryo-EM structures of ASC and NLRC4 CARD filaments reveal a unified mechanism of nucleation and activation of caspase-1" @default.
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• W2992534356 doi "https://doi.org/10.1073/pnas.1810524115" @default.
• W2992534356 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6205419" @default.
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