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Journal Article
Nature medicine, ISSN 1078-8956, 10/2017, Volume 23, Issue 10, p. 1241
This corrects the article DOI: 10.1038/nm.4290. 
FADD protein | Primates | Apoptosis
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
JOURNAL OF PSYCHOPHARMACOLOGY, ISSN 0269-8811, 02/2018, Volume 32, Issue 2, pp. 248 - 255
The cell fate regulator Fas-associated death domain (FADD) balances cell death with non-apoptotic actions via its phosphorylated form. A recent study... 
ageing | cognition | hippocampus | FADD PROTEIN | BRAIN CORTEX | PSYCHIATRY | FRONTAL-CORTEX | DOWN-REGULATION | Brimonidine | Fas-associated death domain (FADD) | COCAINE | NEUROSCIENCES | PREFRONTAL CORTEX | CLINICAL NEUROLOGY | RECEPTOR SUBTYPES | P-FADD/FADD | PHARMACOLOGY & PHARMACY | YOUNG-ADULT | ALPHA-2-ADRENERGIC AGONIST
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
Journal of Clinical Investigation, ISSN 0021-9738, 11/2012, Volume 122, Issue 11, pp. 4094 - 4104
TNF, an inflammatory cytokine that is enriched in the tumor microenvironment, promotes tumor growth and subverts innate immune responses to cancer cells. We... 
MEDICINE, RESEARCH & EXPERIMENTAL | TUMOR-NECROSIS-FACTOR | INHIBITION | INFLAMMATION | MACROPHAGES | DEATH | EXPRESSION | CANCER | ANTITUMOR | T-CELLS | FACTOR-ALPHA | Neoplasms - metabolism | Tumor Necrosis Factor-alpha - metabolism | Neoplasm Transplantation | Tumor Escape | Receptors, Tumor Necrosis Factor, Type I - immunology | Tumor Necrosis Factor-alpha - genetics | Caspase 8 - metabolism | Graft Rejection - metabolism | Receptors, Tumor Necrosis Factor, Type I - metabolism | Receptors, Tumor Necrosis Factor, Type II - immunology | Caspase 8 - genetics | Signal Transduction - immunology | Neoplasms - genetics | T-Lymphocytes - metabolism | Myeloid Cells - immunology | Receptors, Tumor Necrosis Factor, Type II - metabolism | Tumor Necrosis Factor-alpha - immunology | T-Lymphocytes - pathology | Graft Rejection - pathology | CASP8 and FADD-Like Apoptosis Regulating Protein - genetics | Signal Transduction - genetics | Receptors, Tumor Necrosis Factor, Type I - genetics | CASP8 and FADD-Like Apoptosis Regulating Protein - biosynthesis | Receptors, Tumor Necrosis Factor, Type II - genetics | Mice, Knockout | Caspase 8 - immunology | Animals | Neoplasms - immunology | Cell Line, Tumor | Myeloid Cells - metabolism | T-Lymphocytes - immunology | Mice | Mice, Inbred BALB C | CASP8 and FADD-Like Apoptosis Regulating Protein - immunology | Graft Rejection - immunology | Myeloid Cells - pathology | Graft Rejection - genetics | Neoplasms - pathology | Tumor necrosis factor | Genetic aspects | Cellular signal transduction | Research | Properties | Gene expression | Apoptosis
Journal Article
Journal Article
CELL, ISSN 0092-8674, 07/2003, 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
Neurochemistry International, ISSN 0197-0186, 01/2019, Volume 122, pp. 59 - 72
Midazolam and ketamine-induced anesthesia were recently shown to induce a disruption of MEK/ERK sequential phosphorylation with parallel upregulation of p-FADD... 
MEK-ERK | p-FADD/FADD | Other anesthetic agents | Mouse brain | Pentobarbital | Isoflurane | PATHWAYS | DEATH DOMAIN FADD | SLEEP | PROTEIN | PHOSPHORYLATION | GABA-A RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | PEA-15 | NEUROSCIENCES | PREFRONTAL CORTEX | RAT-BRAIN | MIDAZOLAM-INDUCED HYPNOSIS | Physiological aspects | Anesthesia | Sleep | Chloral hydrate
Journal Article