cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination - Wikidata - wikimedia - TriplyDB

cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination

cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination

http://www.wikidata.org/entity/Q28284721

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An atypical E3 ligase zinc finger protein 91 stabilizes and activates NF-kappaB-inducing kinase via Lys63-linked ubiquitination Smac mimetic bypasses apoptosis resistance in FADD- or caspase-8-deficient cells by priming for tumor necrosis factor α-induced necroptosis RIP1 is required for IAP inhibitor-mediated sensitization of childhood acute leukemia cells to chemotherapy-induced apoptosis Cellular inhibitor of apoptosis protein-1 (cIAP1) can regulate E2F1 transcription factor-mediated control of cyclin transcription Ubiquitin-specific protease 4 promotes TNF-α-induced apoptosis by deubiquitination of RIP1 in head and neck squamous cell carcinoma cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms ARTS and Siah collaborate in a pathway for XIAP degradation A novel role for the apoptosis inhibitor ARC in suppressing TNFα-induced regulated necrosis The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2 Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase TRAF2 OTUB1 modulates c-IAP1 stability to regulate signalling pathways Pellino3 targets RIP1 and regulates the pro-apoptotic effects of TNF-α cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4)Many stimuli pull the necrotic trigger, an overview Emerging role of Lys-63 ubiquitination in protein kinase and phosphatase activation and cancer development Necroptosis in tumorigenesis, activation of anti-tumor immunity, and cancer therapy Post-translational modifications as key regulators of TNF-induced necroptosis Molecular crosstalk between apoptosis, necroptosis, and survival signaling Poly-ubiquitination in TNFR1-mediated necroptosis API2-MALT1 oncoprotein promotes lymphomagenesis via unique program of substrate ubiquitination and proteolysis Know the enemy as well as the weapons in hand: the aberrant death pathways and therapeutic agents in chronic lymphocytic leukemia Regulation of Cell Death by IAPs and Their Antagonists DED or alive: assembly and regulation of the death effector domain complexes Fueling the flames: Mammalian programmed necrosis in inflammatory diseases The two faces of receptor interacting protein kinase-1 Small-molecule SMAC mimetics as new cancer therapeutics NOD-Like Receptors: Master Regulators of Inflammation and Cancer IAPs: a central element in the NF-κB activating signaling pathway Viral infection and the evolution of caspase 8-regulated apoptotic and necrotic death pathways Non-Canonical NF-κB Signaling Initiated by BAFF Influences B Cell Biology at Multiple Junctures RIPK-dependent necrosis and its regulation by caspases: a mystery in five acts Programmed necrosis in the cross talk of cell death and inflammation Structural Basis for the Lack of E2 Interaction in the RING Domain of TRAF2 Crystal Structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 Complexes: Affinity, Specificity, and Regulation Discovery of a Potent Small-Molecule Antagonist of Inhibitor of Apoptosis (IAP) Proteins and Clinical Candidate for the Treatment of Cancer (GDC-0152)The FP domains of PI31 and Fbxo7 have the same protein fold but very different modes of protein-protein interaction UBXD Proteins: A Family of Proteins with Diverse Functions in Cancer Molecular basis for specificity of the Met1-linked polyubiquitin signal Linear ubiquitination in immunity Targeting Non-proteolytic Protein Ubiquitination for the Treatment of Diffuse Large B Cell Lymphoma

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cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination

http://www.wikidata.org/entity/Q28284721

description

2008 nî lūn-bûn

@nan

2008 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

cIAP1 and cIAP2 facilitate can ...... at promote RIP1 ubiquitination

@ast

cIAP1 and cIAP2 facilitate can ...... at promote RIP1 ubiquitination

@en

cIAP1 and cIAP2 facilitate can ...... at promote RIP1 ubiquitination

@nl

type

label

cIAP1 and cIAP2 facilitate can ...... at promote RIP1 ubiquitination

@ast

cIAP1 and cIAP2 facilitate can ...... at promote RIP1 ubiquitination

@en

cIAP1 and cIAP2 facilitate can ...... at promote RIP1 ubiquitination

@nl

prefLabel

cIAP1 and cIAP2 facilitate can ...... at promote RIP1 ubiquitination

@ast

cIAP1 and cIAP2 facilitate can ...... at promote RIP1 ubiquitination

@en

cIAP1 and cIAP2 facilitate can ...... at promote RIP1 ubiquitination

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P3181

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J.MOLCEL.2008.05.014

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P1476

cIAP1 and cIAP2 facilitate can ...... at promote RIP1 ubiquitination

@en

P2093

Alain Boudreault

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

James B Jaquith

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

John W Gillard

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

Jon Durkin

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

Kathleen M Dickson

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

Philip A Barker

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

Snezana Milutinovic

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

Stephen J Morris

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

Wai Chi Ho

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

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689-700

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scholarly article

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2383319

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10.1016/J.MOLCEL.2008.05.014

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P433

6

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30

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Mathieu Jm Bertrand

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2008-06-01T00:00:00Z

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5285408

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18570872

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P921

protein ubiquitination