c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis - Wikidata - wikimedia - TriplyDB

c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis

c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis

http://www.wikidata.org/entity/Q39644966

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Antioxidant c-FLIP inhibits Fas ligand-induced NF-kB activation in a phosphatidylinositol 3-kinase/Akt-dependent manner The Fas death signaling pathway connecting reactive oxygen species generation and FLICE inhibitory protein down-regulation Involvement of caspase 8 and c-FLIPL in the proangiogenic effects of the tumour necrosis factor-related apoptosis-inducing ligand (TRAIL)Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling The PAAD/PYRIN-family protein ASC is a dual regulator of a conserved step in nuclear factor kappaB activation pathways Caspases: pharmacological manipulation of cell death Elevated NF-kappaB responses and FLIP levels in leukemic but not normal lymphocytes: reduction by salicylate allows TNF-induced apoptosis Onto better TRAILs for cancer treatment FLIP the Switch: Regulation of Apoptosis and Necroptosis by cFLIP DDX3, a potential target for cancer treatment Molecular targets of TRAIL-sensitizing agents in colorectal cancer Marine Drugs Regulating Apoptosis Induced by Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand (TRAIL)Regulation of cell death by transfer RNA Getting TRAIL back on track for cancer therapy Mechanism of procaspase-8 activation by c-FLIPL Cell apoptosis, autophagy and necroptosis in osteosarcoma treatment Molecular architecture of the DED chains at the DISC: regulation of procaspase-8 activation by short DED proteins c-FLIP and procaspase-8 prodomain FLIP and the death effector domain family Hyperthermia enhances mapatumumab-induced apoptotic death through ubiquitin-mediated degradation of cellular FLIP(long) in human colon cancer cells Raf-1 sets the threshold of Fas sensitivity by modulating Rok-alpha signaling TIPE2, a negative regulator of innate and adaptive immunity that maintains immune homeostasis Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis N-terminal fragment of c-FLIP(L) processed by caspase 8 specifically interacts with TRAF2 and induces activation of the NF-kappaB signaling pathway Dual regulation by apurinic/apyrimidinic endonuclease-1 inhibits gastric epithelial cell apoptosis during Helicobacter pylori infection Fas-associated protein with death domain (FADD)-independent recruitment of c-FLIPL to death receptor 5.Functional genetic screening reveals the role of mitochondrial cytochrome b as a mediator of FAS-induced apoptosis.Protein kinase Cbeta modulates ligand-induced cell surface death receptor accumulation: a mechanistic basis for enzastaurin-death ligand synergy.Constitutive expression of murine c-FLIPR causes autoimmunity in aged mice Induction of apoptosis by Shiga toxins.Modeling the TNFα-induced apoptosis pathway in hepatocytes.Induction of the apoptosis inhibitor ARC by Ras in human cancers A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death.Model-based dissection of CD95 signaling dynamics reveals both a pro- and antiapoptotic role of c-FLIPL.c-Fos as a proapoptotic agent in TRAIL-induced apoptosis in prostate cancer cells Hepatocyte death: a clear and present danger.The many roles of FAS receptor signaling in the immune system The caspase-8 dimerization/dissociation balance is a highly potent regulator of caspase-8, -3, -6 signaling Gene expression analysis implicates a death receptor pathway in schizophrenia pathology Activation of caspases-8 and -10 by FLIP(L).The domains of apoptosis: a genomics perspective.

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c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis

http://www.wikidata.org/entity/Q39644966

description

2002 nî lūn-bûn

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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2002年论文

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2002年论文

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name

c-FLIP

@nl

c-FLIP(L) is a dual function r ...... on and CD95-mediated apoptosis

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type

label

c-FLIP

@nl

c-FLIP(L) is a dual function r ...... on and CD95-mediated apoptosis

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prefLabel

c-FLIP

@nl

c-FLIP(L) is a dual function r ...... on and CD95-mediated apoptosis

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The EMBO Journal

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c-FLIP(L) is a dual function r ...... on and CD95-mediated apoptosis

@en

P2093

Alicia Algeciras-Schimnich

http://www.w3.org/2001/XMLSchema#string

Bryan C Barnhart

http://www.w3.org/2001/XMLSchema#string

David W Chang

http://www.w3.org/2001/XMLSchema#string

Marcus E Peter

http://www.w3.org/2001/XMLSchema#string

Shoshanit Yaish-Ohad

http://www.w3.org/2001/XMLSchema#string

Xiaolu Yang

http://www.w3.org/2001/XMLSchema#string

Yi Pan

http://www.w3.org/2001/XMLSchema#string

Zheng Xing

http://www.w3.org/2001/XMLSchema#string

P2860

Caspase-10 is an initiator caspase in death receptor signaling

Casper is a FADD- and caspase-related inducer of apoptosis

Inhibition of death receptor signals by cellular FLIP

FLICE-inhibitory proteins: regulators of death receptor-mediated apoptosis

Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor

MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death

Redesigning an FKBP-ligand interface to generate chemical dimerizers with novel specificity

Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8

Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex

FLICE is activated by association with the CD95 death-inducing signaling complex (DISC).

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3704-3714

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10.1093/EMBOJ/CDF356

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14

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21

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2002-07-01T00:00:00Z

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11267148

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12110583

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125398

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