Targeting of the protein interaction site between FAK and IGF-1R. - Wikidata - awgldk - TriplyDB

Targeting of the protein interaction site between FAK and IGF-1R.

Targeting of the protein interaction site between FAK and IGF-1R.

http://www.wikidata.org/entity/Q37344395

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FAK and paxillin, two potential targets in pancreatic cancer Multifaceted role of insulin-like growth factors and mammalian target of rapamycin in skeletal muscle Inhibiting the interaction of cMET and IGF-1R with FAK effectively reduces growth of pancreatic cancer cells in vitro and in vivo DOT2: Macromolecular docking with improved biophysical models.FAK activation is required for IGF1R-mediated regulation of EMT, migration, and invasion in mesenchymal triple negative breast cancer cells Focal adhesion kinase-promoted tumor glucose metabolism is associated with a shift of mitochondrial respiration to glycolysis.Thioredoxin reductase linked to cytoskeleton by focal adhesion kinase reverses actin S-nitrosylation and restores neutrophil β(2) integrin function Disruption of the protein interaction between FAK and IGF-1R inhibits melanoma tumor growth.Focal adhesion kinase regulation of mechanotransduction and its impact on endothelial cell functions.Oncogenic Receptor Tyrosine Kinases Directly Phosphorylate Focal Adhesion Kinase (FAK) as a Resistance Mechanism to FAK-Kinase Inhibitors.An activity-based probe reveals dynamic protein-protein interactions mediating IGF-1R transactivation by the GABA(B) receptor.Nitric-oxide synthase-2 linkage to focal adhesion kinase in neutrophils influences enzyme activity and β2 integrin function Dual targeting of the insulin-like growth factor and collateral pathways in cancer: combating drug resistance.Targeting Focal Adhesion Kinase Using Inhibitors of Protein-Protein Interactions

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P2860

Targeting of the protein interaction site between FAK and IGF-1R.

http://www.wikidata.org/entity/Q37344395

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 05 August 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Targeting of the protein interaction site between FAK and IGF-1R.

@en

Targeting of the protein interaction site between FAK and IGF-1R.

@nl

type

label

Targeting of the protein interaction site between FAK and IGF-1R.

@en

Targeting of the protein interaction site between FAK and IGF-1R.

@nl

prefLabel

Targeting of the protein interaction site between FAK and IGF-1R.

@en

Targeting of the protein interaction site between FAK and IGF-1R.

@nl

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J.BBRC.2009.07.156

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Biochemical and Biophysical Research Communications

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Targeting of the protein interaction site between FAK and IGF-1R.

@en

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Andrew Magis

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

David Ostrov

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

Deniz Ucar

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

Donghang Zheng

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

Elena Kurenova

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

Steven N Hochwald

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

Vita Golubovskaya

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

William G Cance

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P2860

Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases

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

Structural basis for the autoinhibition of focal adhesion kinase

Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain

Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity

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

Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation

FAK regulates biological processes important for the pathogenesis of cancer

Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility

Transmembrane crosstalk between the extracellular matrix--cytoskeleton crosstalk

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301-305

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scholarly article

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10.1016/J.BBRC.2009.07.156

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2009-08-05T00:00:00Z

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