Inhibition of FAK and VEGFR-3 binding decreases tumorigenicity in neuroblastoma. - Wikidata - wikimedia - TriplyDB

Inhibition of FAK and VEGFR-3 binding decreases tumorigenicity in neuroblastoma.

Inhibition of FAK and VEGFR-3 binding decreases tumorigenicity in neuroblastoma.

http://www.wikidata.org/entity/Q35207881

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Cell Proliferation in Neuroblastoma Pharmacokinetic analysis of the FAK scaffold inhibitor C4 in dogs Focal adhesion kinase and p53 synergistically decrease neuroblastoma cell survival.Targeting focal adhesion kinase renders pancreatic cancers responsive to checkpoint immunotherapy.SASH1 mediates sensitivity of breast cancer cells to chloropyramine and is associated with prognosis in breast cancer.Annexin A2 could enhance multidrug resistance by regulating NF-κB signaling pathway in pediatric neuroblastoma.Targeting CXCR4 and FAK reverses doxorubicin resistance and suppresses invasion in non-small cell lung carcinoma.

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Inhibition of FAK and VEGFR-3 binding decreases tumorigenicity in neuroblastoma.

http://www.wikidata.org/entity/Q35207881

description

2013 nî lūn-bûn

@nan

2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Inhibition of FAK and VEGFR-3 binding decreases tumorigenicity in neuroblastoma.

@ast

Inhibition of FAK and VEGFR-3 binding decreases tumorigenicity in neuroblastoma.

@en

type

label

Inhibition of FAK and VEGFR-3 binding decreases tumorigenicity in neuroblastoma.

@ast

Inhibition of FAK and VEGFR-3 binding decreases tumorigenicity in neuroblastoma.

@en

prefLabel

Inhibition of FAK and VEGFR-3 binding decreases tumorigenicity in neuroblastoma.

@ast

Inhibition of FAK and VEGFR-3 binding decreases tumorigenicity in neuroblastoma.

@en

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P1433

Molecular Carcinogenesis

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Inhibition of FAK and VEGFR-3 binding decreases tumorigenicity in neuroblastoma

@en

P2093

Elena V Kurenova

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

Hugh Nabers

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

Jerry E Stewart

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

Michael Megison

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

William G Cance

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

Xiaojie Ma

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

P2860

Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53

pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.

Disruption of epithelial cell-matrix interactions induces apoptosis

In vivo activation of the p53 pathway by small-molecule antagonists of MDM2

FAK integrates growth-factor and integrin signals to promote cell migration

FAK regulates biological processes important for the pathogenesis of cancer

Amplification of N-myc in untreated human neuroblastomas correlates with advanced disease stage

Cancer. Addiction to oncogenes--the Achilles heal of cancer

Control of adhesion-dependent cell survival by focal adhesion kinase

Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion.

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9-23

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scholarly article

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10.1002/MC.22070

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1

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54

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Elizabeth A. Beierle

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2013-07-19T00:00:00Z

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23868727

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4370318

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