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International Immunopharmacology, ISSN 1567-5769, 11/2013, Volume 17, Issue 3, pp. 638 - 650
Neutrophils play a critical role in the host defense against bacterial and fungal infections, but their inappropriate activation also contributes to tissue... 
Signaling | Receptors | Inflammation | Kinases | Neutrophils | ACTIVATED PROTEIN-KINASE | COLONY-STIMULATING FACTOR | LEUKOCYTE ADHESION DEFICIENCY | IMMUNOLOGY | SRC-FAMILY KINASES | HUMAN POLYMORPHONUCLEAR LEUKOCYTES | HIGH-AFFINITY RECEPTOR | TUMOR-NECROSIS-FACTOR | TOLL-LIKE RECEPTORS | PHARMACOLOGY & PHARMACY | BETA-GAMMA-SUBUNITS | NF-KAPPA-B | Signal Transduction - immunology | Animals | Receptors, Cell Surface - immunology | Humans | Neutrophils - immunology | Selectins - immunology | Mycoses | Lectins | Fc receptors | Integrins | FcR, Fc-receptor | GPI, glycosylphosphatidylinositol anchor | CLEC, C-type lectin | OSCAR, osteoclast-associated receptor | PKB, protein kinase B | DAG, diacyl-glycerol | Tyk2, tyrosine protein kinase 2 | VCAM-1, vascular cell adhesion molecule 1 | ICAM-1, intercellular adhesion molecule 1 | FADD, Fas-associated protein with death domain | IκB, inhibitor of NF-κB | GM-CSF, granulocyte | MyD88, myeloid differentiation protein 88 | TNF, tumor necrosis factor | LTβ, lymphotoxin β | TRADD, TNFR1-associated death domain protein | Abl, Abelson leukemia proto-oncogene | SLP-76, SH2 domain-containing leukocyte protein of 76 kDa | CALDAG-GEFI, calcium and DAG-regulated guanine nucleotide exchange factor I | IL, interleukin | Src, Rous sarcoma virus proto-oncogene | IRF, IFN regulatory factor | RIG, retinoic acid-inducible gene | PLC, phospholipase C | TCR, T-cell receptor | IKK, IκB kinase | ITAM, immunoreceptor tyrosine-based activation motif | CARD, caspase activation and recruitment domain | IP3, inositol-tris-phosphate | CHO, Chinese hamster ovary cells | MKK, MAP kinase kinase | fMLP, formly-Met-Leu-Phe | TRAF, TNF receptor-associated factor | MIP, macrophage inflammatory protein | Rac, Ras-related C3 botulinum toxin substrate | monocyte colony-stimulating factor | PIP3, phosphatidylinositol-3-phosphate | VLA-4, very late antigen 4 (α4β1 integrin) | PAF, platelet activating factor | STAT, signal transducer and activator of transcription | TAK, TGFβ-activated kinase 1 | Mac-1, macrophage antigen 1 (αMβ2 integrin) | FcRγ, Fc-receptor γ-chain | Asc, apoptosis-associated speck-like protein containing a CARD | cIAP, cellular inhibitor of apoptosis | BCR, B-cell receptor | Fgr, Gardner–Rasheed feline sarcoma proto-oncogene | VASP, vasodilator-stimulated phosphoprotein | Hck, hematopoietic cell kinase | TGFβ, transforming growth factor β | Rap, Ras-related protein | SHP-1, SH2 domain-containing protein tyrosine phosphatase 1 | Syk, spleen tyrosine kinase | GPCR, G protein-coupled receptor | G-CSF, granulocyte colony-stimulating factor | TREM, triggering receptor expressed on myeloid cells | DISC, death-inducing signaling complex | MDL-1, myeloid DAP12-associating lectin 1 | C3G, Crk SH3 domain-binding guanine nucleotide exchange factor (RapGEF1) | NF-κB, nuclear factor κB | ERM, ezrin-radixin-moesin | Epac1, exchange protein activated by cyclic AMP 1 | LTB4, leukotriene B4 | Mcl, macrophage C-type lectin | SAP130, Sin3A-associated protein of 130 kDa | SH2, Src-homology 2 domain | MAP kinase, mitogen-activated protein kinase | PSGL-1, P-selectin glycoprotein ligand | PI3K, phoshoinositide-3-kinase | ADAP, adhesion and degranulation promoting adapter protein (Fyb, SLAP-130) | NLRP3, NOD-like receptor family, pyrin domain containing 3 | MDA5, melanoma differentiation-associated protein 5 | TLR, Toll-like receptor | GRK, GPCR kinase | LAD, leukocyte adhesion deficiency | MAPKAP-kinase, MAP kinase-associated protein kinase | ZAP-70, ζ-chain-associated protein of 70 kDa | TRAIL, TNF-related apoptosis-inducing ligand | JNK, c-Jun N-terminal kinase | LFA-1, lymphocyte function-associated receptor 1 (αLβ2 integrin) | ROS, reactive oxygen species | RIP3, receptor-interacting serine-threonine protein kinase 3 | DAP12, DNAX activating protein 12 | IFN, interferon | PIR, paired immunoglobulin-like receptor | PKC, protein kinase C | PAK, p21-activated kinase | ESL-1, E-selectin ligand 1 | GAP, GTPase activating protein | ERK, extracellular signal-regulated kinase | SOCS, suppressor of cytokine signaling | JAK, Janus kinase | RANK, receptor activator of NF-κB | IRAK, IL-1 receptor-associated kinase | NOD, nucleotide-binding oligomerization domain containing protein | CEACAM3, carcinoembryonic antigen-related cell adhesion molecule 3 (CD66b)
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2016, Volume 64, Issue 2, pp. 236 - 250
Caspase-8 activation can be triggered by death receptor-mediated formation of the death-inducing signaling complex (DISC) and by the inflammasome adaptor ASC.... 
caspase-8 | DED | MC159 | cFLIP | DISC | Fas | death domain | FADD | vFLIP | filament | APOPTOSIS | ACTIVATION | IMMUNE-SYSTEM | INHIBITION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | UNIFIED MODEL | EFFECTOR DOMAIN | CELL-DEATH | CELL BIOLOGY | Death Domain Receptor Signaling Adaptor Proteins - chemistry | Apoptosis - drug effects | Cytoskeletal Proteins - genetics | Humans | Caspase 8 - metabolism | Caspase 8 - chemistry | CASP8 and FADD-Like Apoptosis Regulating Protein - chemistry | Death Domain Receptor Signaling Adaptor Proteins - genetics | Recombinant Fusion Proteins - metabolism | Viral Proteins - metabolism | Caspase 8 - genetics | Transfection | Cytoskeletal Proteins - metabolism | Protein Interaction Domains and Motifs | Binding Sites | CASP8 and FADD-Like Apoptosis Regulating Protein - metabolism | Death Effector Domain | Fas-Associated Death Domain Protein - genetics | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | CASP8 and FADD-Like Apoptosis Regulating Protein - genetics | Jurkat Cells | Viral Proteins - chemistry | Fas-Associated Death Domain Protein - metabolism | Viral Proteins - genetics | fas Receptor - pharmacology | Cytoskeletal Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Plasmids - metabolism | Fas-Associated Death Domain Protein - chemistry | Cryoelectron Microscopy | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | CARD Signaling Adaptor Proteins | Plasmids - chemistry | Protein Binding | Recombinant Fusion Proteins - genetics | Death Domain Receptor Signaling Adaptor Proteins - metabolism | Autoimmunity | Medical colleges | Skin diseases | Molecular biology | Analysis | Index Medicus
Journal Article
Cell, ISSN 0092-8674, 2003, Volume 114, Issue 2, pp. 181 - 190
Apoptosis induced by TNF-receptor I (TNFR1) is thought to proceed via recruitment of the adaptor FADD and caspase-8 to the receptor complex. TNFR1 signaling is... 
DEATH RECEPTORS | RECRUITMENT | TUMOR-NECROSIS-FACTOR | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | C-FLIP | FAS | FADD | NF-KAPPA-B | FLICE-INHIBITORY PROTEINS | REQUIREMENT | CELL BIOLOGY | Tumor Necrosis Factor-alpha - metabolism | Caspase 9 | Caspase 8 | Humans | Transcriptional Activation | Cytoplasm - metabolism | NF-kappa B - metabolism | RNA-Binding Proteins | fas Receptor - metabolism | TNF Receptor-Associated Factor 1 | Caspases - metabolism | Cell Membrane - metabolism | Tumor Cells, Cultured | Cell Survival - physiology | Receptors, Tumor Necrosis Factor - genetics | Receptors, Tumor Necrosis Factor - metabolism | Signal Transduction | Jurkat Cells | Nuclear Pore Complex Proteins - metabolism | Intracellular Signaling Peptides and Proteins | Fas-Associated Death Domain Protein | Caspase Inhibitors | Proteins - immunology | Proteins - genetics | Tumor Necrosis Factor-alpha - pharmacology | Adaptor Proteins, Signal Transducing | Carrier Proteins - metabolism | Proteins - metabolism | NF-kappa B - genetics | Models, Biological | CASP8 and FADD-Like Apoptosis Regulating Protein | Apoptosis - physiology | Receptors, Tumor Necrosis Factor - immunology | NF-kappa B - drug effects | Chemical inhibitors | Cell research | Cell death | Tumor necrosis factor | Analysis | Physiological aspects | Genetic aspects | Cytoplasm | Apoptosis | Cell Membrane | Antigens, CD95 | Proteins | Life Sciences | NF-kappa B | Carrier Proteins | Nuclear Pore Complex Proteins | Cell Survival | Biochemistry, Molecular Biology | Tumor Necrosis Factor-alpha | Receptors, Tumor Necrosis Factor | Caspases
Journal Article
Molecular Cell, ISSN 1097-2765, 08/2011, Volume 43, Issue 3, pp. 432 - 448
A better understanding of the mechanisms through which anticancer drugs exert their effects is essential to improve combination therapies. While studying how... 
CASPASE INHIBITORS | TUMOR-NECROSIS-FACTOR | LIGASE ACTIVITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | DNA-DAMAGE | ALPHA-DEPENDENT APOPTOSIS | TRAIL-INDUCED APOPTOSIS | TNF-ALPHA | CHEMOTHERAPEUTIC DRUGS | NF-KAPPA-B | CELL-DEATH | CELL BIOLOGY | CASP8 and FADD-Like Apoptosis Regulating Protein - physiology | Apoptosis - drug effects | Inhibitor of Apoptosis Proteins - genetics | Humans | Caspase 8 - metabolism | Nuclear Pore Complex Proteins - chemistry | Caspase 8 - chemistry | Inhibitor of Apoptosis Proteins - physiology | Nuclear Pore Complex Proteins - physiology | Antineoplastic Agents - pharmacology | CASP8 and FADD-Like Apoptosis Regulating Protein - metabolism | Fas-Associated Death Domain Protein - physiology | RNA-Binding Proteins - physiology | Signal Transduction | CASP8 and FADD-Like Apoptosis Regulating Protein - genetics | Nuclear Pore Complex Proteins - metabolism | RNA-Binding Proteins - chemistry | Fas-Associated Death Domain Protein - metabolism | Etoposide - pharmacology | Mitochondria - metabolism | Caspase 8 - physiology | Fas-Associated Death Domain Protein - chemistry | Cell Line, Tumor | Ligands | Apoptosis - physiology | DNA Damage | Enzyme Activation | RNA-Binding Proteins - metabolism | Ubiquitin | Green design | Oncology, Experimental | Internet service providers | Research | Sustainable development | Cancer
Journal Article
Molecular Cell, ISSN 1097-2765, 2005, Volume 20, Issue 6, pp. 939 - 949
The death-inducing signaling complex (DISC) comprising Fas, Fas-associated death domain (FADD), and caspase-8/10 is assembled via homotypic associations... 
RECEPTOR SIGNALS | APOPTOSIS | INDUCED-PROXIMITY MODEL | BIOCHEMISTRY & MOLECULAR BIOLOGY | NMR STRUCTURE | DEATH-EFFECTOR DOMAIN | CASPASE ACTIVATION | CONTAINING PROTEIN | SIGNALING COMPLEX DISC | CELL-DEATH | PYRIN DOMAIN | CELL BIOLOGY | Caspase 8 | Humans | Multiprotein Complexes | Molecular Sequence Data | Crystallography, X-Ray | Intracellular Signaling Peptides and Proteins - metabolism | fas Receptor - metabolism | Viral Proteins - metabolism | Death Domain Receptor Signaling Adaptor Proteins | Caspases - metabolism | Molluscum contagiosum virus - genetics | Caspase 10 | fas Receptor - genetics | Intracellular Signaling Peptides and Proteins - genetics | Amino Acid Sequence | Caspases - genetics | Viral Proteins - chemistry | Intracellular Signaling Peptides and Proteins - antagonists & inhibitors | Models, Molecular | Viral Proteins - genetics | Fas-Associated Death Domain Protein | Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - metabolism | Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - chemistry | Sequence Alignment | Animals | Intracellular Signaling Peptides and Proteins - chemistry | Adaptor Proteins, Signal Transducing - genetics | Molluscum contagiosum virus - chemistry | Protein Conformation | CASP8 and FADD-Like Apoptosis Regulating Protein | Apoptosis - physiology | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Proteins | Oligomers | Structure | Crystals
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2012, Volume 7, Issue 9, p. e46275
Escherichia coli FadR plays two regulatory roles in fatty acid metabolism. FadR represses the fatty acid degradation (fad) system and activates the unsaturated... 
DNA-BINDING | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | GROWTH | DEGRADATION | SYNTHETASE | EXCISION | RECEPTOR PROTEIN | REPRESSOR | TRANSCRIPTION FACTOR | ACYL-COENZYME | Protein Kinases - metabolism | Protein Kinases - genetics | Coenzyme A Ligases - genetics | Cyclic AMP Receptor Protein - genetics | Cyclic AMP Receptor Protein - metabolism | Oxygen - metabolism | Coenzyme A Ligases - metabolism | Regulon | Fatty Acid Transport Proteins - metabolism | Biological Transport | Escherichia coli - metabolism | Transcription, Genetic | Membrane Proteins - metabolism | Binding Sites | Cyclic AMP - metabolism | Fatty Acids - metabolism | Bacterial Outer Membrane Proteins - genetics | Repressor Proteins - metabolism | Promoter Regions, Genetic | Oxidation-Reduction | Signal Transduction | Membrane Proteins - genetics | Bacterial Proteins - genetics | Repressor Proteins - genetics | Escherichia coli Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Protein Binding | Bacterial Proteins - metabolism | Gene Expression Regulation, Bacterial | Fatty Acid Transport Proteins - genetics | Fatty acid metabolism | Crosstalk | Analysis | Escherichia coli | Physiological aspects | Cyclic adenylic acid | Research | Genetic transcription | Enzymes | Regulators | Transcription | Genes | Cyclic AMP | Chains | Biosynthesis | Glucose | Metabolism | Gene expression | Fatty acids | Flavin-adenine dinucleotide | Proteins | FADD protein | E coli | Plasmids | Oxidation | In vivo methods and tests | Transport | Binding sites
Journal Article
Journal Article
FEBS Letters, ISSN 0014-5793, 05/2015, Volume 589, Issue 12, pp. 1369 - 1375
The ubiquitin-editing enzyme A20 suppresses nuclear factor-κB (NF-κB) activation and tumor necrosis factor-α (TNF-α)-induced apoptosis in a deubiquitinating... 
Ubiquitin | Tumor necrosis factor-α | Nuclear factor-κB | Apoptosis | receptor-interacting protein | interleukin-1 | TRAF | TRADD | PARP | HOIP | IκB kinase | IκB | NF-κB | transforming growth factor-β-activated kinase 1 | heme-oxidized iron regulatory protein-2 ubiquitin ligase-1 | TAK1 | HOIL-1 | Fas-associated protein with death domain | TNF-related apoptosis-inducing ligand | cIAP | FADD | HOIL-1-interacting protein | TNF receptor-associated factor | Poly (ADP-ribose) polymerase | TNF receptor-associated death domain | TRAIL | IL-1 | IKK | cellular inhibitor of apoptosis | nuclear factor-κB | TNF-α | tumor necrosis factor-α | RIP | inhibitor of κB | Nuclear factor-kappa B | ACTIVATION | COMPLEX | LINEAR POLYUBIQUITIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CANCER | CELL-DEATH | CELL BIOLOGY | Tumor necrosis factor-alpha | TUMOR-NECROSIS-FACTOR | BIOPHYSICS | INFLAMMATION | NF-KAPPA-B | RIP1 | Cysteine Endopeptidases - chemistry | Tumor Necrosis Factor-alpha - metabolism | Apoptosis - drug effects | Humans | Tumor Necrosis Factor-alpha - genetics | Ubiquitin-Protein Ligases - antagonists & inhibitors | Interleukin-1alpha - metabolism | NF-kappa B - metabolism | Baculoviral IAP Repeat-Containing 3 Protein | Intracellular Signaling Peptides and Proteins - metabolism | DNA-Binding Proteins - metabolism | Cysteine Endopeptidases - metabolism | Inhibitor of Apoptosis Proteins - antagonists & inhibitors | Tumor Necrosis Factor alpha-Induced Protein 3 | Inhibitor of Apoptosis Proteins - metabolism | Interleukin-1alpha - genetics | Nuclear Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Recombinant Proteins - metabolism | Cell Line | Cell Survival - drug effects | NF-kappa B - antagonists & inhibitors | Zinc Fingers | Enzyme Inhibitors - pharmacology | Ubiquitin-Protein Ligases - metabolism | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Animals | Intracellular Signaling Peptides and Proteins - chemistry | Cysteine Endopeptidases - genetics | Mutant Proteins - chemistry | Mice | Amino Acid Substitution
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 12/2009, Volume 187, Issue 7, pp. 1037 - 1054
Journal Article