Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase - Wikidata - wikimedia - TriplyDB

Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase

Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase

http://www.wikidata.org/entity/Q42141824

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Intermolecular transphosphorylation between insulin receptors and EGF-insulin receptor chimerae.Functional reconstitution of the canalicular bile salt transport system of rat liver Insulin rapidly stimulates phosphorylation of a 46-kDa membrane protein on tyrosine residues as well as phosphorylation of several soluble proteins in intact fat cells.Insulin stimulates phosphorylation of a 120-kDa glycoprotein substrate (pp120) for the receptor-associated protein kinase in intact H-35 hepatoma cells.The insulin receptor: signalling mechanism and contribution to the pathogenesis of insulin resistance.Role of kinases in insulin stimulation of glucose transport.The regulation of glucose transport in insulin-sensitive cells.Insulin resistance: a look at the role of insulin receptor kinase.Protein kinase activity of the insulin receptor Regulation of the protein kinase activity of the human insulin receptor.Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein Regulation of glucose carrier activity by AlCl3 and phospholipase C in fat-cells.Epidermal growth factor, but not insulin, stimulates tyrosine phosphorylation of an endogenous protein of Mr 95,000 in triton extracts of human placental syncytiotrophoblast membranes.Sustained signalling from the insulin receptor after stimulation with insulin analogues exhibiting increased mitogenic potency Tyrosine-specific phosphorylation of calmodulin by the insulin receptor kinase purified from human placenta.Activation of mitogen-activated protein kinase and phosphatidylinositol 3'-kinase is not sufficient for the hormonal stimulation of glucose uptake, lipogenesis, or glycogen synthesis in 3T3-L1 adipocytes.An Mr 180,000 protein is an endogenous substrate for the insulin-receptor-associated tyrosine kinase in human placenta.Tyrosine phosphorylation of two cytosolic proteins of 50 kDa and 35 kDa in rat liver by insulin-receptor kinase in vitro.Evidence that α5β1 integrins mediate Leydig cell binding to fibronectin and enhance Leydig cell proliferation stimulated by a Sertoli cell-secreted mitogenic factor in vitro.

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P2860

Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase

http://www.wikidata.org/entity/Q42141824

description

1985 nî lūn-bûn

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1985年の論文

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1985年論文

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1985年論文

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1985年論文

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1985年論文

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1985年論文

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1985年论文

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1985年论文

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1985年论文

@zh-cn

name

Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase

@en

Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase

@nl

type

label

Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase

@en

Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase

@nl

prefLabel

Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase

@en

Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase

@nl

P1433

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P1433

Biochemical Journal

P1476

Identification of a cellular 110 000-Da protein substrate for the insulin-receptor kinase

@en

P2093

Ballotti R

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Debant A

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Fehlmann M

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Peyron JF

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Sadoul JL

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Van Obberghen E

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P2860

Insulin receptor: evidence that it is a protein kinase

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

The role of protein phosphorylation in neural and hormonal control of cellular activity

Transforming gene product of Rous sarcoma virus phosphorylates tyrosine

Biosynthetic labeling of insulin receptor: studies of subunits in cultured human IM-9 lymphocytes

Insulin receptor is an insulin-dependent tyrosine protein kinase: copurification of insulin-binding activity and protein kinase activity to homogeneity from human placenta

Insulin activates a tyrosine-specific protein kinase in extracts of 3T3-L1 adipocytes and human placenta.

Insulin-induced receptor loss in cultured human lymphocytes is due to accelerated receptor degradation.

Receptor-mediated phosphorylation of the hepatic insulin receptor: evidence that the Mr 95,000 receptor subunit is its own kinase

Tyrosine-specific protein kinase activity is associated with the purified insulin receptor.

P304

887-892

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10.1042/BJ2270887

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3

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227

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2988507

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1144918

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