This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes cryogenic electron microscopy data identifying the cryo-EM structure of CARD8-CARD filament. The main summary display for this entry includes information on the experimental method, validation and macromolecules in the deposit, as well as entry history and funding information. Data is provided...

This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes cryogenic electron microscopy data identifying the cryo-EM structure of CARD8-CARD filament. The main summary display for this entry includes information on the experimental method, validation and macromolecules in the deposit, as well as entry history and funding information. Data is provided...

This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes cryogenic electron microscopy data identifying the cryo-EM structure of the NLRP1-CARD filament. The main summary display for this entry includes information on the experimental method, validation and macromolecules in the deposit, as well as entry history and funding information. Data is provided...

Open Science Framework (OSF) is a repository with tools for data discovery, collection, storage and analysis, as well as study experiment design and publication. The Hao Wu Lab files are organized according to the publication they support. Available files include figures used in publications, PyMOL (.pse) and Chimera (.csx) session files which generate the 3D display of biological molecules and .pdb...

Summary from GEO: "We report the application of RNA-seq for profiling gene transcription upon treatment of methyl bestatin (MeBs, aminopeptidase inhibitor) or brefeldin A (BFA, ER-to-Golgi transport inhibitor), compared to DMSO control. We found MeBs and BFA similarly upregulated genes pertinent to proteotoxic stress." Overall design from GEO: "Examination of gene transcription levels upon treatment...

Inflammasomes are multiprotein complexes formed in response to pathogens. NLRP1 and CARD8 are related proteins that form inflammasomes, but the pathogen-associated signal(s) and the molecular mechanisms controlling their activation have not been established. Inhibitors of the serine dipeptidyl peptidases DPP8 and DPP9 (DPP8/9) were recently discovered to activate both NLRP1 and CARD8. Interestingly,...

Target identification of CQ31 using the photoreactive diazirine-alkyne probe, CQ73.

To find cellular protein binding partners of the NLRP1 inflammasome, FLAG-tagged full length NLRP1 (or a GFP-FLAG protein control) was ectopically expressed in HEK 293T cells and affinity purified from cell lysates (Note: the NLRP1-FLAG-containing lysate samples were affinity purified in the presence or absence of excess proline) before proteins were reduced, alkylated, and trypsinized before TMT...

Summary from GEO: "The danger signals that activate the NLRP1 inflammasome have yet to be firmly established. NLRP1 undergoes autoproteolysis to generate N-terminal (NT) and C-terminal (CT) fragment, which importantly, is a necessary step for its check-point regulation by the DPP9 ternary complex and the mechanistic activation of NLRP1 through functional degradation. Here, we report an added layer...

Summary from GEO: "The danger signals that activate the NLRP1 inflammasome have yet to be firmly established. NLRP1 undergoes autoproteolysis to generate N-terminal (NT) and C-terminal (CT) fragment, which importantly, is a necessary step for its check-point regulation by the DPP9 ternary complex and the mechanistic activation of NLRP1 through functional degradation. Here, we report an added layer...