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Arteriosclerosis, Thrombosis, and Vascular Biology, ISSN 1079-5642, 04/2017, Volume 37, Issue 4, pp. 694 - 706
OBJECTIVE—Increasing evidence suggests that contractile dysfunction in smooth muscle cells (SMCs) plays a critical role in aortic biomechanical dysfunction and... 
Caspase 1 | Glyburide | Inflammasomes | Contractile proteins | Proteolysis | Aortic aneurysm | OXIDATIVE STRESS | ACTIVATION | glyburide | inflammasomes | FOCUS | INJURY | caspase 1 | DELETION | aortic aneurysm | PERIPHERAL VASCULAR DISEASE | MICE | MUTATIONS | ISCHEMIA-REPERFUSION | HEMATOLOGY | proteolysis | contractile proteins | Aneurysm, Dissecting - genetics | Aortic Aneurysm, Abdominal - prevention & control | Inflammasomes - metabolism | Humans | Middle Aged | Caspase 1 - metabolism | Male | Mice, 129 Strain | Aorta, Abdominal - drug effects | Aneurysm, Dissecting - physiopathology | Glyburide - pharmacology | Inflammasomes - antagonists & inhibitors | Myocytes, Smooth Muscle - drug effects | Aneurysm, Dissecting - prevention & control | Disease Models, Animal | Muscle, Smooth, Vascular - drug effects | Genetic Predisposition to Disease | Myocytes, Smooth Muscle - enzymology | NLR Family, Pyrin Domain-Containing 3 Protein - metabolism | Vasoconstriction - drug effects | Aortic Aneurysm, Thoracic - physiopathology | Mice, Knockout | Aorta, Thoracic - enzymology | Biomechanical Phenomena | Phenotype | Aortic Aneurysm, Abdominal - enzymology | Aortic Aneurysm, Abdominal - physiopathology | Caspase 1 - deficiency | Muscle, Smooth, Vascular - enzymology | Aortic Aneurysm, Thoracic - genetics | Aortic Aneurysm, Thoracic - prevention & control | Myocytes, Smooth Muscle - pathology | Muscle, Smooth, Vascular - physiopathology | NLR Family, Pyrin Domain-Containing 3 Protein - genetics | Aneurysm, Dissecting - enzymology | Muscle Proteins - metabolism | Female | Aorta, Abdominal - pathology | Aorta, Thoracic - drug effects | Angiotensin II | Aorta, Abdominal - physiopathology | Aorta, Thoracic - pathology | Aortic Aneurysm, Thoracic - enzymology | Mice, Inbred C57BL | Cells, Cultured | Aortic Aneurysm, Abdominal - genetics | Aorta, Thoracic - physiopathology | Aorta, Abdominal - enzymology | Inflammasomes - genetics | NLR Family, Pyrin Domain-Containing 3 Protein - deficiency | Muscle, Smooth, Vascular - pathology | Animals | Caspase 1 - genetics | Aged | aneurysm | cardiovascular diseases | contractility | vessels
Journal Article
Journal Article
Journal Article
Biochemical Journal, ISSN 0264-6021, 12/2004, Volume 384, Issue 2, pp. 201 - 232
The death morphology commonly known as apoptosis results from a post-translational pathway driven largely by specific limited proteolysis. In the last decade... 
Zymogen | Caspase | Inhibitor | Protease | Inhibitor of apoptosis protein (IAP) | Apoptosis | INDUCED-PROXIMITY MODEL | VIRAL SERPIN CRMA | X-LINKED INHIBITOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | inhibitor of apoptosis protein (IAP) | apoptosis | zymogen | caspase | INTERLEUKIN-1-BETA CONVERTING-ENZYME | protease | PROGRAMMED CELL-DEATH | TOLL-LIKE RECEPTOR-2 | inhibitor | ANTI-APOPTOTIC ACTIVITY | CYTOCHROME-C RELEASE | DEATH-EFFECTOR DOMAIN | SIGNALING COMPLEX DISC | Caspases - physiology | Enzyme Precursors - chemistry | Humans | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Amino Acid Sequence - physiology | Structure-Activity Relationship | Caspase Inhibitors | Enzyme Precursors - metabolism | Animals | Caspases - metabolism | Protein Conformation | Molecular Structure | Caspases - chemistry | Enzyme Activation - physiology | CAD, caspase-activated DNase | FLICE, FADD-like ICE | TNF, tumour necrosis factor | CARD, LRR and NACHT-containing protein | Rip, receptor-interacting protein | DRONC, Drosophila Nedd2-like caspase | CARD-containing ICE-associated kinase | Ipaf | ICAD, inhibitor of CAD | CED, cell death-defective | DFF, DNA fragmentation factor | CARD, caspase-recruitment domain | APAF-1, apoptotic protease activating factor-1 | CLARP, caspase-like apoptosis-regulatory protein | DIABLO, direct IAP-binding protein with low pI | CLAN, ICE-protease-activating factor | RAIDD, caspase-2 and RipK1 domain-containing adaptor with death domain | ICE, interleukin-1β-converting enzyme | NALP1, NACHT, LRR and Pyrin domain containing 1 | ALPS, autoimmune lymphoproliferative syndrome | LRR, leucine-rich repeat | PYD- and CARD-containing molecule | NOD, nucleotide-binding and oligomerization domain-containing protein | NACHT, NTPase-domain named after NAIP, CIITA, HET-E and TP1 | S1, S2, …Sn and S1′, S2′, …Sm′ refer to the cognate pockets on the protease that accept these side chains | PYCARD, apoptosis-associated speck-like protein containing a CARD | PARP, poly(ADP-ribose) polymerase | P1, P2, …Pn and P1′, P2′, …Pm′ designate the side chains in substrates and inhibitors in the N- and C-terminal direction respectively from the P1–P1′ scissile peptide bond | TFPI, tissue factor pathway inhibitor | TLR, Toll-like receptor | serpin, serine protease inhibitor | RING, really interesting new gene | XIAP | DED, death effector domain | Review | PIDD, p53-induced protein with a death domain | TRAIL, TNF-related apoptosis-inducing ligand | IAP, inhibitor of apoptosis protein | NBD, nucleotide-binding domain | ASC | TRAF, TNF receptor-associated factor | BIRC4, X-linked IAP | DD, death domain | Smac, second mitochondrial activator of caspases | DIAP1, Drosophila inhibitor of apoptosis 1 | BIR, baculoviral IAP repeat | IBM, IAP binding motif | TRADD, TNFRSF1A-associated via death domain | CRADD | DISC, death-inducing signalling complex | FADD, Fas (TNFRSF6)-associated via death domain | FLIP, FLICE inhibitory protein | NF-κB, nuclear factor-κB | CARP, caspase-associated RING protein | CrmA, cytokine response modifier A | CARDIAK, Rip-like interacting CLARP kinase | RICK | Rip-associated protein with a death domain | baculoviral IAP repeat-containing 4
Journal Article
Redox Biology, ISSN 2213-2317, 04/2015, Volume 4, Issue C, pp. 296 - 307
Journal Article
Journal of Allergy and Clinical Immunology, The, ISSN 0091-6749, 2017, Volume 140, Issue 4, pp. 1054 - 1067.e10
Background The Nod-like receptor NACHT, LRR, and PYD domain–containing protein 3 (NLRP3) and Bruton tyrosine kinase (BTK) are protagonists in innate and... 
Allergy and Immunology | ibrutinib | Bruton tyrosine kinase | IL-1 | inflammation | inflammasome | NLRP3 | macrophage | X-linked agammaglobulinemia | Muckle-Wells syndrome | Staphylococcus aureus | IMMUNITY | ACTIVATION | IMMUNOLOGY | MASS-SPECTROMETRY | NALP3 INFLAMMASOME | B-CELL | ALLERGY | IN-VIVO | BTK | CHRONIC LYMPHOCYTIC-LEUKEMIA | EXPRESSION | Inflammasomes - metabolism | Agammaglobulinemia - genetics | Protein-Tyrosine Kinases - metabolism | Humans | Leukocidins - immunology | Molecular Targeted Therapy | Protein-Tyrosine Kinases - genetics | Genetic Diseases, X-Linked - genetics | Bacterial Proteins - immunology | Adaptive Immunity | Cryopyrin-Associated Periodic Syndromes - genetics | Nigericin - immunology | Staphylococcal Infections - immunology | NLR Family, Pyrin Domain-Containing 3 Protein - metabolism | Mice, Inbred C57BL | Cells, Cultured | Immunity, Innate | Mice, Knockout | Adaptor Proteins, Signal Transducing | Animals | Apoptosis Regulatory Proteins | Pyrin Domain - genetics | Agammaglobulinaemia Tyrosine Kinase | Proteomics | Staphylococcus aureus - immunology | Mice | Receptors, Cytoplasmic and Nuclear - metabolism | Proteins | Tyrosine | Phenols | Cells | Immunodeficiency | Regulators | Identification methods | Activation | Arthritis | Kinases | Immunity | Caspase-1 | Genotype & phenotype | Bacteria | Protein-tyrosine kinase | Immune system | Cytokines | Secretion | Agammaglobulinemia | Neutrophils | Caspase | Pharmacology | Adaptive immunity | FDA approval | IL-1β | Patients | Ablation | Bruton's tyrosine kinase | Human subjects | Nigericin | Speck | Mutation | Leukocidin | Cancer | Apoptosis
Journal Article
Journal Article
Current Opinion in Structural Biology, ISSN 0959-440X, 04/2012, Volume 22, Issue 2, pp. 241 - 247
► Death domain oligomerization is facilitated by conserved interaction surfaces. ► Known death domain oligomers possess helical symmetry. ► Helical... 
COMPLEX | CRYSTAL-STRUCTURE | DIGITAL ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | NMR STRUCTURE | RECEPTOR | FADD | NF-KAPPA-B | SIGNALING PLATFORM | EFFECTOR DOMAIN | PYRIN DOMAIN | CELL BIOLOGY | Protein Structure, Tertiary | Animals | Proteins - metabolism | Signal Transduction | Humans | Protein Binding | Ligands | Proteins - chemistry | Oligomers
Journal Article
American Journal of Respiratory and Critical Care Medicine, ISSN 1073-449X, 08/2017, Volume 196, Issue 3, pp. 283 - 297
Journal Article