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Cunninghamia lanceolata plantations in China
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Tyrosine phosphorylation of insulin receptor β subunit activates the receptor tyrosine kinase in intact H-35 hepatoma cells


Tyrosine phosphorylation of insulin receptor β subunit activates the receptor tyrosine kinase in intact H-35 hepatoma cells



The Journal of Biological Chemistry 261(10): 4715-4722



ISSN/ISBN: 0021-9258


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(PDF emailed within 1 workday: $29.90)

Accession: 078666193

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Related references

Tyrosine phosphorylation of insulin receptor beta subunit activates the receptor tyrosine kinase in intact H-35 hepatoma cells. Journal of Biological Chemistry 261(10): 4715-4722, 1986

Tyrosine phosphorylation of insulin receptor b subunit activates the receptor tyrosine kinase in intact H-35 hepatoma cells. The Journal of Biological Chemistry 261: 15-22, 1986

Tyrosine phosphorylation of the insulin receptor beta subunit activates the receptor-associated tyrosine kinase activity. Journal of Biological Chemistry 259(8): 5277-5286, 1984

Tyrosine phosphorylation of the insulin receptor β subunit activates the receptor-associated tyrosine kinase activity. The Journal of Biological Chemistry 259(8): 5277-5286, 1984

Tyrosine phosphorylation of the insulin receptor b subunit activates the receptor-associated tyrosine kinase activity. The Journal of Biological Chemistry 259: 77-86, 1984

Hydrogen peroxide stimulates tyrosine phosphorylation of the insulin receptor and its tyrosine kinase activity in intact cells. Biochemical Journal 250(1): 95-101, 1988

Autoantibodies to the insulin receptor (B-10) can stimulate tyrosine phosphorylation of the β-subunit of the insulin receptor and a 185,000 molecular weight protein in rat hepatoma cells. The Journal of Clinical Endocrinology and Metabolism 68(4): 787-795, 1989

Autoantibodies to the insulin receptor (B-10) can stimulate tyrosine phosphorylation of the beta-subunit of the insulin receptor and a 185,000 molecular weight protein in rat hepatoma cells. Journal of Clinical Endocrinology and Metabolism 68(4): 787-795, 1989

G-protein and tyrosine kinase receptor cross-talk in rat aortic smooth muscle cells: thrombin- and angiotensin II-induced tyrosine phosphorylation of insulin receptor substrate-1 and insulin-like growth factor 1 receptor. Biochemical and Biophysical Research Communications 218(3): 934-939, 1996

Phosphorylation of insulin-like growth factor I receptor by insulin receptor tyrosine kinase in intact cultured skeletal muscle cells. Biochemistry 27(9): 3222-3228, 1988

Identification of the insulin receptor tyrosine residues undergoing insulin-stimulated phosphorylation in intact rat hepatoma cells. Journal of Biological Chemistry 263(1): 350-359, 1988

Two-dimensional phosphopeptide analysis of the autophosphorylation cascade of a soluble insulin receptor tyrosine kinase : the tyrosines phosphorylated are typical of those observed following phosphorylation of the heterotetrameric insulin receptor in intact cells. The Journal of Biological Chemistry 266(3): 1390-1395, 1991

Two-dimensional phosphopeptide analysis of the autophosphorylation cascade of a soluble insulin receptor tyrosine kinase. The tyrosines phosphorylated are typical of those observed following phosphorylation of the heterotetrameric insulin receptor in intact cells. Journal of Biological Chemistry 266(3): 1390-1395, 1991

An alpha-subunit mutation in the insulin receptor constitutively activates receptor tyrosine kinase, with no effect on cell growth or key signalling enzymes. Journal of Cellular Biochemistry Suppl 1994(18B): 280, 1994

Insulin stimulates tyrosine phosphorylation of its receptor -subunit in intact rat hepatocytes. Biochemical Journal 241(1): 99-104, 1987