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humans (569) 569
apoptosis (490) 490
animals (393) 393
fas-associated death domain protein (393) 393
adaptor proteins, signal transducing (300) 300
biochemistry & molecular biology (282) 282
index medicus (266) 266
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mice (246) 246
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fadd (136) 136
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induced apoptosis (70) 70
tumor-necrosis-factor (70) 70
tumor necrosis factor-alpha - pharmacology (69) 69
fas ligand protein (67) 67
receptor (67) 67
tumor cells, cultured (66) 66
article (65) 65
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caspase (64) 64
nf-kappa b - metabolism (64) 64
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cancer (58) 58
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rats (54) 54
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intracellular signaling peptides and proteins (53) 53
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protein binding (52) 52
tumor necrosis factor-alpha - metabolism (52) 52
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adaptor proteins, signal transducing - genetics (50) 50
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neurosciences (50) 50
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cytochrome-c (48) 48
cd95 (46) 46
mice, knockout (46) 46
mice, transgenic (46) 46
necrosis (46) 46
casp8 and fadd-like apoptosis regulating protein (45) 45
mice, inbred c57bl (45) 45
protein structure, tertiary (45) 45
proto-oncogene proteins c-bcl-2 - metabolism (45) 45
biophysics (44) 44
caspases - physiology (44) 44
gene expression (44) 44
cd95 fas/apo-1 (43) 43
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1. Full Text The Ripoptosome, a Signaling Platform that Assembles in Response to Genotoxic Stress and Loss of IAPs
by Tenev, Tencho and Bianchi, Katiuscia and Darding, Maurice and Broemer, Meike and Langlais, Claudia and Wallberg, Fredrik and Zachariou, Anna and Lopez, Juanita and MacFarlane, Marion and Cain, Kelvin and Meier, Pascal
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
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2. Full Text Death receptor signal transducers: nodes of coordination in immune signaling networks
by Ashkenazi, Avi and Dixit, Vishva and Wilson, Nicholas S
Nature Immunology, ISSN 1529-2908, 04/2009, Volume 10, Issue 4, pp. 348 - 355
Death receptors (DRs) are members of the tumor necrosis factor receptor superfamily that possess a cytoplasmic death domain (DD). DRs regulate important... 
TOLL-LIKE-RECEPTORS | CASPASE-8 ACTIVATION | TUMOR-NECROSIS-FACTOR | NATURAL-KILLER-CELLS | APOPTOSIS-INDUCING LIGAND | T-CELL-ACTIVATION | FAS-MEDIATED APOPTOSIS | IMMUNOLOGY | HELICASE ANTIVIRAL PATHWAY | NF-KAPPA-B | FLICE-INHIBITORY PROTEIN | Immunity, Active | Receptors, Death Domain - immunology | Humans | Receptors, Death Domain - physiology | Immunity, Innate | Receptors, Tumor Necrosis Factor - physiology | Adaptor Proteins, Signal Transducing - physiology | Fas-Associated Death Domain Protein - immunology | Animals | TNF Receptor-Associated Death Domain Protein - physiology | Adaptor Proteins, Signal Transducing - immunology | Signal Transduction - physiology | Apoptosis - physiology | TNF Receptor-Associated Death Domain Protein - immunology | Receptors, Tumor Necrosis Factor - immunology | Fas-Associated Death Domain Protein - physiology | Physiological aspects | Cell receptors | Cellular signal transduction | Research | Immune system
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3. Full Text Synchronized renal tubular cell death involves ferroptosis
by Andreas Linkermann and Rachid Skouta and Nina Himmerkus and Shrikant R. Mulay and Christin Dewitz and Federica De Zen and Agnes Prokai and Gabriele Zuchtriegel and Fritz Krombach and Patrick-Simon Welz and Ricardo Weinlich and Tom Vanden Berghe and Peter Vandenabeele and Manolis Pasparakis and Markus Bleich and Joel M. Weinberg and Christoph A. Reichel and Jan Hinrich Bräsen and Ulrich Kunzendorf and Hans-Joachim Anders and Brent R. Stockwell and Douglas R. Green and Stefan Krautwald and Vishva M. Dixit
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2014, Volume 111, Issue 47, pp. 16836 - 16841
Receptor-interacting protein kinase 3 (RIPK3)-mediated necroptosis is thought to be the pathophysiologically predominant pathway that leads to regulated... 
Cell death | Acute kidney injury | Plasma stability | Physiological regulation | Grants | Renal tubules | Reperfusion injury | Research universities | Necrosis | Apoptosis | Ferroptosis | Programmed cell death | Necroptosis | Regulated cell death | PATHWAYS | ferroptosis | REGULATED NECROSIS | MULTIDISCIPLINARY SCIENCES | apoptosis | regulated cell death | ISCHEMIA-REPERFUSION INJURY | INFLAMMATION | CASPASE-8 | MICE | TNF-ALPHA | FADD | programmed cell death | INHIBITOR | necroptosis | Caspase 8 - genetics | Fas-Associated Death Domain Protein - genetics | Kidney Tubules - cytology | Receptor-Interacting Protein Serine-Threonine Kinases - genetics | Animals | Body Weight | Reperfusion Injury - prevention & control | Mice | Caspase 8 - physiology | Fas-Associated Death Domain Protein - physiology | Receptor-Interacting Protein Serine-Threonine Kinases - physiology | Protein research | Ischemia | Physiological aspects | Research | Phosphotransferases | Health aspects | Biological Sciences
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4. Full Text Survival Function of the FADD-CASPASE-8-cFLIP(L) Complex
by Dillon, CP and Oberst, A and Weinlich, R and Janke, LJ and Kang, TB and Ben-Moshe, T and Mak, TW and Wallach, D and Green, DR
CELL REPORTS, ISSN 2211-1247, 05/2012, Volume 1, Issue 5, pp. 401 - 407
Caspase-8, the initiator caspase of the death receptor pathway of apoptosis, its adapter molecule, FADD, required for caspase-8 activation, and cFLIP(L), a... 
APOPTOSIS | ACTIVATION | NECROSIS | NECROPTOSIS | INFLAMMATION | IN-VIVO | CASPASE 8 | FADD | NF-KAPPA-B | CELL-DEATH | CELL BIOLOGY | Fas-Associated Death Domain Protein - genetics | CASP8 and FADD-Like Apoptosis Regulating Protein - physiology | CASP8 and FADD-Like Apoptosis Regulating Protein - genetics | CASP8 and FADD-Like Apoptosis Regulating Protein - deficiency | Embryonic Development - genetics | Embryonic Development - physiology | Fas-Associated Death Domain Protein - deficiency | Apoptosis - genetics | Signal Transduction - genetics | Caspase 8 - physiology | Receptor-Interacting Protein Serine-Threonine Kinases - physiology | Mice, Knockout | Caspase 8 - genetics | Receptor-Interacting Protein Serine-Threonine Kinases - genetics | Animals | Necrosis - physiopathology | Gene Deletion | Signal Transduction - physiology | Mice | Necrosis - genetics | Receptor-Interacting Protein Serine-Threonine Kinases - deficiency | Apoptosis - physiology | Fas-Associated Death Domain Protein - physiology
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5. Full Text Cutting edge: FAS (CD95) mediates noncanonical IL-1β and IL-18 maturation via caspase-8 in an RIP3-independent manner
by Bossaller, Lukas and Chiang, Ping-I and Schmidt-Lauber, Christian and Ganesan, Sandhya and Kaiser, William J and Rathinam, Vijay A. K and Mocarski, Edward S and Subramanian, Deepa and Green, Douglas R and Silverman, Neal and Fitzgerald, Katherine A and Marshak-Rothstein, Ann and Latz, Eicke
Journal of Immunology, ISSN 0022-1767, 12/2012, Volume 189, Issue 12, pp. 5508 - 5512
Fas, a TNF family receptor, is activated by the membrane protein Fas ligand expressed on various immune cells. Fas signaling triggers apoptosis and induces... 
APOPTOSIS | ACTIVATION | MACROPHAGES | INFLAMMASOME | ENGAGEMENT | LIGAND | RELEASE | IMMUNOLOGY | INHIBITOR | NF-KAPPA-B | EXPRESSION | Inflammasomes - metabolism | Dendritic Cells - immunology | Caspase 8 - metabolism | Enzyme Activation - immunology | Caspase 8 - genetics | Signal Transduction - immunology | Interleukin-1beta - biosynthesis | fas Receptor - physiology | Fas-Associated Death Domain Protein - physiology | Dendritic Cells - metabolism | Fas-Associated Death Domain Protein - genetics | Mice, Inbred C57BL | Macrophages, Peritoneal - enzymology | Fas-Associated Death Domain Protein - deficiency | Macrophages, Peritoneal - immunology | Mice, Transgenic | Signal Transduction - genetics | Caspase 8 - physiology | Receptor-Interacting Protein Serine-Threonine Kinases - physiology | Mice, Knockout | Inflammasomes - physiology | Interleukin-18 - biosynthesis | Receptor-Interacting Protein Serine-Threonine Kinases - genetics | Animals | Dendritic Cells - enzymology | Mice | Mice, Inbred BALB C | Receptor-Interacting Protein Serine-Threonine Kinases - deficiency | Macrophages, Peritoneal - metabolism
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6. Full Text Directing cancer cells to self-destruct with pro-apoptotic receptor agonists
by Ashkenazi, Avi
Nature Reviews Drug Discovery, ISSN 1474-1776, 2008, Volume 7, Issue 12, pp. 1001 - 1012
Each day, the human body eliminates billions of unwanted cells by apoptotic suicide. Apoptosis provides an important barrier against cancer; however, specific... 
DEATH RECEPTORS | TUMOR-NECROSIS-FACTOR | NATURAL-KILLER-CELLS | DECOY RECEPTORS | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | LIGAND-INDUCED APOPTOSIS | IN-VIVO | HUMAN MONOCLONAL-ANTIBODY | PHARMACOLOGY & PHARMACY | TRAIL-INDUCED APOPTOSIS | TUMORICIDAL ACTIVITY | MEDIATED CASPASE-8 ACTIVATION | Fas-Associated Death Domain Protein - drug effects | Apoptosis - drug effects | Humans | Receptors, Death Domain - physiology | Antineoplastic Agents - therapeutic use | Apoptosis Regulatory Proteins - drug effects | DNA, Neoplasm - drug effects | Neoplasms - drug therapy | Neoplasms - genetics | Drug Design | Signal Transduction - physiology | Receptors, Death Domain - drug effects | Cell Transformation, Neoplastic - drug effects | DNA, Neoplasm - genetics | Neoplasms - pathology | Fas-Associated Death Domain Protein - physiology | Physiological aspects | Causes of | Research | Properties | Drug therapy | Agonists (Biochemistry) | Apoptosis | Cancer
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7. Full Text FLIP and the death effector domain family
by Yu, J.W and Shi, Y
Oncogene, ISSN 0950-9232, 10/2008, Volume 27, Issue 48, pp. 6216 - 6227
Death effector domains (DEDs) are protein interaction modules found in a number of proteins known to regulate apoptosis from death receptors. The core DED... 
Caspase-8 | NF-κB | DED | Extrinsic cell death | FLIP | Apoptosis | caspase-8 | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | apoptosis | RECEPTOR-INDUCED APOPTOSIS | FAS-MEDIATED APOPTOSIS | CELL BIOLOGY | CASPASE-8 ACTIVATION | extrinsic cell death | T-CELL PROLIFERATION | NF-kappa B | APOPTOSIS-INDUCING LIGAND | ONCOLOGY | GENETICS & HEREDITY | REGULATES FAS/TNFR1-INDUCED APOPTOSIS | C-FLIPL | NF-KAPPA-B | SIGNALING COMPLEX DISC | Sequence Alignment | CASP8 and FADD-Like Apoptosis Regulating Protein - physiology | Humans | Models, Molecular | Apoptosis - physiology | Fas-Associated Death Domain Protein - physiology | Fas-Associated Death Domain Protein - chemistry | Genetic aspects | Cellular signal transduction | Research | Health aspects | Cancer cells | Proteins | Signal transduction | Oncology | Genetics
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8. Full Text Transforming Growth Factor β–Activated Kinase 1 Signaling Pathway Critically Regulates Myocardial Survival and Remodeling
by Li, Lei and Chen, Yi and Doan, Jessica and Murray, Jason and Molkentin, Jeffery D and Liu, Qinghang
Circulation, ISSN 0009-7322, 12/2014, Volume 130, Issue 24, pp. 2162 - 2172
BACKGROUND—Programmed necrosis (necroptosis) plays an important role in development, tissue homeostasis, and disease pathogenesis. The molecular mechanisms... 
ventricular remodeling | heart failure | myocytes, cardiac | apoptosis | necrosis | signal transduction | PRESSURE-OVERLOAD | CARDIAC & CARDIOVASCULAR SYSTEMS | HEART-FAILURE | PROGRAMMED NECROSIS | CELL-DEATH | CARDIOMYOCYTE DEATH | FAILING HEART | RECEPTOR-INTERACTING PROTEIN | CARDIAC-HYPERTROPHY | PERIPHERAL VASCULAR DISEASE | NF-KAPPA-B | SKIN INFLAMMATION | Cell Line | MAP Kinase Kinase Kinases - genetics | Heart Failure - physiopathology | Heart Failure - pathology | Ventricular Remodeling - physiology | Caspase 8 - physiology | Receptor-Interacting Protein Serine-Threonine Kinases - physiology | Mice, Knockout | Myocytes, Cardiac - pathology | Animals | MAP Kinase Kinase Kinases - deficiency | Necrosis - physiopathology | Myocytes, Cardiac - physiology | Homeostasis - physiology | MAP Kinase Kinase Kinases - physiology | Signal Transduction - physiology | Mice | Apoptosis - physiology | Fas-Associated Death Domain Protein - physiology | Disease Models, Animal | Heart Failure - mortality
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9. Full Text FADD and Caspase-8 Control the Outcome of Autophagic Signaling in Proliferating T Cells
by Bryan D. Bell and Sabrina Leverrier and Brian M. Weist and Ryan H. Newton and Adrian F. Arechiga and Keith A. Luhrs and Naomi S. Morrissette and Craig M. Walsh
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2008, Volume 105, Issue 43, pp. 16677 - 16682
Fas-associated death domain protein (FADD) and caspase-8 (casp8) are vital intermediaries in apoptotic signaling induced by tumor necrosis factor family... 
T lymphocytes | Cell growth | Cell death | B lymphocytes | Cell cycle | Cultured cells | Cellular immunity | Gene expression regulation | Organelles | Apoptosis | Caspases | FADD | Necroptosis | Autophagy | SURVIVAL | ACTIVATION | autophagy | INDUCED APOPTOSIS | MULTIDISCIPLINARY SCIENCES | apoptosis | KINASE RIP | CUTTING EDGE | C-FLIP | FAS | caspases | NF-KAPPA-B | DEATH DOMAIN PROTEIN | necroptosis | TRANSGENIC MICE | Fas-Associated Death Domain Protein - genetics | Cell Proliferation | Lymphocyte Activation | Mice, Transgenic | Caspase 8 - physiology | Caspase 8 - genetics | Signal Transduction - immunology | Feedback, Physiological | Animals | T-Lymphocytes - cytology | Mice | Fas-Associated Death Domain Protein - physiology | Evaluation | Cysteine proteinases | T cell proliferation | Properties | Necrosis | Immunological research | Biological Sciences
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10. Full Text A novel mitochondrial MAVS/caspase-8 platform links RNA virus-induced innate antiviral signaling to bax/bak-independent apoptosis
by Maadidi, Souhayla El and Faletti, Laura and Berg, Birgit and Wenzl, Christin and Wieland, Katrin and Chen, Zhijian J and Maurer, Ulrich and Borner, Christoph
Journal of Immunology, ISSN 0022-1767, 02/2014, Volume 192, Issue 3, pp. 1171 - 1183
Semliki Forest virus (SFV) requires RNA replication and Bax/Bak for efficient apoptosis induction. However, cells lacking Bax/Bak continue to die in a... 
CASPASE-8 ACTIVATION | DOUBLE-STRANDED-RNA | PROTEIN-KINASE PKR | HEPATITIS-C-VIRUS | RIG-I | SEMLIKI-FOREST-VIRUS | ENDOPLASMIC-RETICULUM | IMMUNOLOGY | NF-KAPPA-B | MAMMALIAN-CELLS | CELL-DEATH | Fibroblasts - virology | Mitochondria - enzymology | HeLa Cells - virology | Semliki forest virus - physiology | Signal Transduction | Humans | Caspase 3 - metabolism | Cytopathogenic Effect, Viral - physiology | Caspase 8 - physiology | HEK293 Cells - virology | Interferon-Induced Helicase, IFIH1 | Proto-Oncogene Proteins c-bcl-2 - metabolism | Adaptor Proteins, Signal Transducing - physiology | DEAD-box RNA Helicases - physiology | Animals | RNA, Viral - genetics | RNA Interference | Virus Replication | Mice | Apoptosis - physiology | Enzyme Activation | Mitochondria - physiology | bcl-X Protein - metabolism | Fas-Associated Death Domain Protein - physiology
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11. Full Text Chemotherapy‐induced apoptosis in hepatocellular carcinoma involves the p53 family and is mediated via the extrinsic and the intrinsic pathway
by Seitz, Sarah J and Schleithoff, Elisa Schulze and Koch, Andreas and Schuster, André and Teufel, Andreas and Staib, Frank and Stremmel, Wolfgang and Melino, Gerry and Krammer, Peter H and Schilling, Tobias and Müller, Martina
International Journal of Cancer, ISSN 0020-7136, 05/2010, Volume 126, Issue 9, pp. 2049 - 2066
We investigated the downstream mechanisms by which chemotherapeutic drugs elicit apoptosis in hepatocellular carcinoma (HCC). Genomic signatures of HCC cell... 
CD95 | TRAIL | apoptosis | chemosensitivity | p63 | p73 | p53 | Chemosensitivity | P63 | P73 | Apoptosis | P53 | CANCER-CELLS | DEATH RECEPTORS | PROTEIN | DNA-DAMAGE | MITOCHONDRIA | SORAFENIB | ONCOLOGY | GENE-EXPRESSION | Caspases - physiology | Prognosis | Oligonucleotide Array Sequence Analysis | Apoptosis - drug effects | Humans | Liver Neoplasms - drug therapy | Membrane Potential, Mitochondrial - drug effects | Hep G2 Cells | Tumor Suppressor Protein p53 - physiology | Carcinoma, Hepatocellular - drug therapy | Membrane Proteins - physiology | Carcinoma, Hepatocellular - pathology | Bleomycin - pharmacology | Liver Neoplasms - pathology | Fas-Associated Death Domain Protein - physiology
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12. Full Text FKHRL1-mediated expression of Noxa and Bim induces apoptosis via the mitochondria in neuroblastoma cells
by Obexer, P and Geiger, K and Ambros, P.F and Meister, B and Ausserlechner, M.J
Cell Death and Differentiation, ISSN 1350-9047, 03/2007, Volume 14, Issue 3, pp. 534 - 547
Protein kinase-B (PKB) and its target, the forkhead transcription factor like 1 (FKHRL1)/FoxO3a, have been suggested as regulators of neurotrophin-mediated... 
BCL-2 FAMILY-MEMBER | Akt/PKB | NEUROTROPHIC FACTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | Bim | FACTOR FKHR-L1 | GROWTH FACTOR-1-INDUCED PHOSPHORYLATION | Noxa | CELL BIOLOGY | CYTOCHROME-C | NEURONAL SURVIVAL | PI3K | BH3-ONLY PROTEINS PUMA | LEUKEMIA-CELLS | FACTOR FKHRL1 | programmed cell death | forkhead transcription factor | Puma | Humans | Gene Expression Regulation, Neoplastic | Phosphatidylinositol 3-Kinases - metabolism | Receptors, TNF-Related Apoptosis-Inducing Ligand - metabolism | fas Receptor - metabolism | Proto-Oncogene Proteins c-bcl-2 - metabolism | Caspases - metabolism | Bcl-2-Like Protein 11 | Forkhead Transcription Factors - metabolism | Cell Death | Apoptosis Regulatory Proteins - genetics | Membrane Proteins - metabolism | fas Receptor - physiology | Fas-Associated Death Domain Protein - physiology | 3-Phosphoinositide-Dependent Protein Kinases | Protein-Serine-Threonine Kinases - metabolism | Proto-Oncogene Proteins - metabolism | Peptide Fragments - metabolism | Transduction, Genetic | Signal Transduction | Membrane Proteins - genetics | Fas-Associated Death Domain Protein - metabolism | Proto-Oncogene Proteins - genetics | Mitochondria - metabolism | Forkhead Transcription Factors - genetics | Reverse Transcriptase Polymerase Chain Reaction | TNF-Related Apoptosis-Inducing Ligand - metabolism | Tamoxifen - analysis | Apoptosis Regulatory Proteins - metabolism | Models, Biological | Tamoxifen - pharmacology | Neuroblastoma - metabolism | Forkhead Box Protein O3 | Proto-Oncogene Proteins c-bcl-2 - genetics | Apoptosis
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