Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation. - Test2 - elhamkhani - TriplyDB

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

http://www.wikidata.org/entity/Q34785695

about

Systems biology of the microvasculature Quantitative characterization of cellular membrane-receptor heterogeneity through statistical and computational modeling Analytical reduction of combinatorial complexity arising from multiple protein modification sites.Computational systems biology approaches to anti-angiogenic cancer therapeutics.Site-Specific Phosphorylation of VEGFR2 Is Mediated by Receptor Trafficking: Insights from a Computational Model Gab2 facilitates epithelial-to-mesenchymal transition via the MEK/ERK/MMP signaling in colorectal cancer Compartment model predicts VEGF secretion and investigates the effects of VEGF trap in tumor-bearing mice.Computational model of VEGFR2 pathway to ERK activation and modulation through receptor trafficking.Effects of endothelial cell proliferation and migration rates in a computational model of sprouting angiogenesis.Quantitative fluorescent profiling of VEGFRs reveals tumor cell and endothelial cell heterogeneity in breast cancer xenografts.Integrative meta-modeling identifies endocytic vesicles, late endosome and the nucleus as the cellular compartments primarily directing RTK signaling.VEGFR1 promotes cell migration and proliferation through PLCγ and PI3K pathways.Computer Simulation of TSP1 Inhibition of VEGF-Akt-eNOS: An Angiogenesis Triple Threat.Computational modeling of synergistic interaction between αVβ3 integrin and VEGFR2 in endothelial cells: Implications for the mechanism of action of angiogenesis-modulating integrin-binding peptides

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P2860

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

http://www.wikidata.org/entity/Q34785695

description

2013 nî lūn-bûn

@nan

2013 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հունիսին 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

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

@ast

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

@en

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

@nl

type

label

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

@ast

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

@en

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

@nl

prefLabel

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

@ast

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

@en

Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation.

@nl

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JOURNAL.PONE.0067438

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Computational Model of Gab1/2-Dependent VEGFR2 Pathway to Akt Activation

@en

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Feilim Mac Gabhann

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

Wan Hua Tan

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

P2860

Universally sloppy parameter sensitivities in systems biology models

Function, regulation and pathological roles of the Gab/DOS docking proteins

Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization

Increased proliferation and altered growth factor dependence of human mammary epithelial cells overexpressing the Gab2 docking protein

Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF

Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein

New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival

PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2.

Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules

Modeling HER2 effects on cell behavior from mass spectrometry phosphotyrosine data

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e67438

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scholarly article

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10.1371/JOURNAL.PONE.0067438

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6

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8

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Aleksander S. Popel

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2013-06-21T00:00:00Z

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242334635

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23805312

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3689841

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