A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing. - Wikidata - awgldk - TriplyDB

A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing.

A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing.

http://www.wikidata.org/entity/Q42555606

about

Converging roles of caspases in inflammasome activation, cell death and innate immunity DED or alive: assembly and regulation of the death effector domain complexes Necroptosis: The Trojan horse in cell autonomous antiviral host defense The intersection of cell death and inflammasome activation Deletion of FADD in macrophages and granulocytes results in RIP3- and MyD88-dependent systemic inflammation Caspase-8 as an Effector and Regulator of NLRP3 Inflammasome Signaling The Mitochondrial Phosphatase PGAM5 Is Dispensable for Necroptosis but Promotes Inflammasome Activation in Macrophages.Border Security: The Role of RIPK3 in Epithelium Homeostasis.RIPK1 and RIPK3 Kinases Promote Cell-Death-Independent Inflammation by Toll-like Receptor 4.Necroptosis Promotes Staphylococcus aureus Clearance by Inhibiting Excessive Inflammatory Signaling.Mycobacterium tuberculosis Zinc Metalloprotease-1 Assists Mycobacterial Dissemination in Zebrafish.RIPK3 deficiency or catalytically inactive RIPK1 provides greater benefit than MLKL deficiency in mouse models of inflammation and tissue injury.ZBP1/DAI is an innate sensor of influenza virus triggering the NLRP3 inflammasome and programmed cell death pathways.Caspase-8: not so silently deadly.Distinct Kinase-Independent Role of RIPK3 in CD11c+ Mononuclear Phagocytes in Cytokine-Induced Tissue Repair The diverse role of RIP kinases in necroptosis and inflammation.Emerging Roles for RIPK1 and RIPK3 in Pathogen-Induced Cell Death and Host Immunity.Induction of type I interferon through a non-canonical Toll-like receptor 7 pathway during Yersinia pestis infection Induction of necroptotic cell death by viral activation of the RIG-I or STING pathway.Generation of small molecules to interfere with regulated necrosis.Necroptosis-independent signaling by the RIP kinases in inflammation.Post-translational control of RIPK3 and MLKL mediated necroptotic cell death.RIPK3 Restricts Viral Pathogenesis via Cell Death-Independent Neuroinflammation.The Inflammatory Signal Adaptor RIPK3: Functions Beyond Necroptosis.Complex Pathologic Roles of RIPK1 and RIPK3: Moving Beyond Necroptosis.RIPK3 in cell death and inflammation: the good, the bad, and the ugly.Caspase-8: regulating life and death.The small molecule that packs a punch: ubiquitin-mediated regulation of RIPK1/FADD/caspase-8 complexes.Kinase Activities of RIPK1 and RIPK3 Can Direct IFN-β Synthesis Induced by Lipopolysaccharide.RIP3 deficiency ameliorates inflammatory response in mice infected with influenza H7N9 virus infection.Necroptosis: Mechanisms and Relevance to Disease.K45A mutation of RIPK1 results in poor necroptosis and cytokine signaling in macrophages, which impacts inflammatory responses in vivo.MLKL Activation Triggers NLRP3-Mediated Processing and Release of IL-1β Independently of Gasdermin-D.Cell death is not essential for caspase-1-mediated interleukin-1β activation and secretion Caspase-1 Engagement and TLR-Induced c-FLIP Expression Suppress ASC/Caspase-8-Dependent Apoptosis by Inflammasome Sensors NLRP1b and NLRC4.RIP3 deficiency exacerbates inflammation in dextran sodium sulfate-induced ulcerative colitis mice model.Combination therapy with proteasome inhibitors and TLR agonists enhances tumour cell death and IL-1β production.LRRK2 and the "LRRKtosome" at the Crossroads of Programmed Cell Death: Clues from RIP Kinase Relatives.The Receptor Interacting Protein Kinases in the Liver.RIPK3 promotes sepsis-induced acute kidney injury via mitochondrial dysfunction.

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P2860

A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing.

http://www.wikidata.org/entity/Q42555606

description

2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing.

@en

A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing.

@nl

type

label

A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing.

@en

A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing.

@nl

prefLabel

A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing.

@en

A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing.

@nl

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JIMMUNOL.1402167

P1433

Journal of Immunology

P1476

A RIPK3-caspase 8 complex mediates atypical pro-IL-1β processing.

@en

P2093

John Bertin

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

Kenta Moriwaki

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

Peter J Gough

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

P2860

Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis

The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis

Dectin-1 is an extracellular pathogen sensor for the induction and processing of IL-1β via a noncanonical caspase-8 inflammasome

cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms

Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation

Interleukin-1 in the pathogenesis and treatment of inflammatory diseases

RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition

Caspase-8 and RIP kinases regulate bacteria-induced innate immune responses and cell death.

Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3.

RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation.

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1938-1944

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10.4049/JIMMUNOL.1402167

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4

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194

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Francis Ka-Ming Chan

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2015-01-07T00:00:00Z

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25567679

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4324020

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