Thrombin Stimulates Phosphorylation of Insulin-like Growth Factor-1 Receptor, Insulin Receptor Substrate-1, and Phospholipase C-γ1 in Rat Aortic Smooth Muscle Cells (Q57908184)

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scientific article published in Journal of Biological Chemistry

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English	Thrombin Stimulates Phosphorylation of Insulin-like Growth Factor-1 Receptor, Insulin Receptor Substrate-1, and Phospholipase C-γ1 in Rat Aortic Smooth Muscle Cells	scientific article published in Journal of Biological Chemistry

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7499260%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

Thrombin stimulates phosphorylation of insulin-like growth factor-1 receptor, insulin receptor substrate-1, and phospholipase C-gamma 1 in rat aortic smooth muscle cells (English)

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19 October 2019

phosphorylation

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Patrice Delafontaine

2

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19 October 2019

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G N Rao

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19 October 2019

M S Runge

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19 October 2019

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1 November 1995

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19 October 2019

Journal of Biological Chemistry

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19 October 2019

270

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19 October 2019

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19 October 2019

27871-27875

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19 October 2019

The pathogenesis of atherosclerosis: a perspective for the 1990s

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Synthetic alpha-thrombin receptor peptides activate G protein-coupled signaling pathways but are unable to induce mitogenesis

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Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation

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Insulin-stimulated microtubule-associated protein kinase is phosphorylated on tyrosine and threonine in vivo

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The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product

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Raf-1 activates MAP kinase-kinase

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Reconstitution of the Raf-1-MEK-ERK signal transduction pathway in vitro

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A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf

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ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase, Raf-1, and RSK

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Epidermal growth factor induces phosphorylation of extracellular signal-regulated kinase 2 via multiple pathways

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SH2/SH3 signaling proteins

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Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity.

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Tyrosine kinase inhibition: an approach to drug development

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Phenotypic change from transformed to normal induced by benzoquinonoid ansamycins accompanies inactivation of p60src in rat kidney cells infected with Rous sarcoma virus

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Substrate affinity of the protein tyrosine kinase pp60c-src is increased on thrombin stimulation of human platelets

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A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos.

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An SH3-SH2-SH3 protein is required for p21Ras1 activation and binds to sevenless and Sos proteins in vitro

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Binding of the Ras activator son of sevenless to insulin receptor substrate-1 signaling complexes

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Phosphorylation of transcription factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter

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Identifiers

10.1074/JBC.270.46.27871

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7499260%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7499260%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

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