SIAH2 antagonizes TYK2-STAT3 signaling in lung carcinoma cells. - Wikidata - wikimedia - TriplyDB

SIAH2 antagonizes TYK2-STAT3 signaling in lung carcinoma cells.

SIAH2 antagonizes TYK2-STAT3 signaling in lung carcinoma cells.

http://www.wikidata.org/entity/Q38994472

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A pan-cancer modular regulatory network analysis to identify common and cancer-specific network components.STAT3 inhibition suppresses proliferation of retinoblastoma through down-regulation of positive feedback loop of STAT3/miR-17-92 clusters.The Expression of the Ubiquitin Ligase SIAH2 (Seven In Absentia Homolog 2) Is Increased in Human Lung Cancer.The Steroidogenic Enzyme AKR1C3 Regulates Stability of the Ubiquitin Ligase Siah2 in Prostate Cancer Cells Global functional profiling of human ubiquitome identifies E3 ubiquitin ligase DCST1 as a novel negative regulator of Type-I interferon signaling Molecular targets of luteolin in cancer Clinical genomic profiling identifies TYK2 mutation and overexpression in patients with neurofibromatosis type 1-associated malignant peripheral nerve sheath tumors.Overriding TKI resistance of renal cell carcinoma by combination therapy with IL-6 receptor blockade.Inhibition of Siah2 Ubiquitin Ligase by Vitamin K3 Attenuates Chronic Myeloid Leukemia Chemo-Resistance in Hypoxic Microenvironment.Resveratrol selectively induces apoptosis in malignant cells with the JAK2V617F mutation by inhibiting the JAK2 pathway.

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SIAH2 antagonizes TYK2-STAT3 signaling in lung carcinoma cells.

http://www.wikidata.org/entity/Q38994472

description

2014 nî lūn-bûn

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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2014年论文

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2014年论文

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name

SIAH2 antagonizes TYK2-STAT3 signaling in lung carcinoma cells.

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type

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SIAH2 antagonizes TYK2-STAT3 signaling in lung carcinoma cells.

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SIAH2 antagonizes TYK2-STAT3 signaling in lung carcinoma cells.

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ONCOTARGET.1899

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SIAH2 antagonizes TYK2-STAT3 signaling in lung carcinoma cells.

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Alexander Schütz

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

Andrea Haitel

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Claude Haan

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Claudia Schäfer

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Iver Petersen

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Jana Klitzsch

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Karlheinz Friedrich

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Katharina Schmid

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

Lienhard M Schmitz

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

Marc Buchwald

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P2860

Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1.

Basal ubiquitin-independent internalization of interferon alpha receptor is prevented by Tyk2-mediated masking of a linear endocytic motif

Mutations in the EGFR kinase domain mediate STAT3 activation via IL-6 production in human lung adenocarcinomas

Oxidants and signaling by mitogen-activated protein kinases in lung epithelium

Catalytically active TYK2 is essential for interferon-beta-mediated phosphorylation of STAT3 and interferon-alpha receptor-1 (IFNAR-1) but not for activation of phosphoinositol 3-kinase

TYK2 kinase activity is required for functional type I interferon responses in vivo

JAK1 activates STAT3 activity in non-small-cell lung cancer cells and IL-6 neutralizing antibodies can suppress JAK1-STAT3 signaling

Should we continue to use the term non-small-cell lung cancer?

STAT3 is activated by JAK2 independent of key oncogenic driver mutations in non-small cell lung carcinoma.

A novel human p53 isoform is an essential element of the ATR-intra-S phase checkpoint.

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3184-3196

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10.18632/ONCOTARGET.1899

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10

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5

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Oliver H Krämer

Richard Moriggl

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2014-05-01T00:00:00Z

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262386319

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24833526

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4102802

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