Phosphorylation Activates the Insulin Receptor Tyrosine Protein Kinase

Preparations of insulin receptor from cultured 3T3-L1 adipocytes and human placenta previously was found to catalyze the phosphorylation of the 90,000-dalton component of the insulin receptor on tyrosine residues. This insulin-dependent phosphorylation has now been shown to coincide with the generat...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1983-06, Vol.80 (11), p.3237-3240
Hauptverfasser:	Rosen, Ora M., Herrera, Roman, Olowe, Yetunde, Petruzzelli, Lilli M., Cobb, Melanie H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Adipocytes Adipose Tissue - metabolism Animals Biochemistry Cations, Divalent Cell Differentiation Cells, Cultured Enzyme Activation Enzymes Female Gels Histones Humans Insulin Kinetics Mice Phosphorylation Placenta Placenta - metabolism Pregnancy Protein Kinases - metabolism Protein-Tyrosine Kinases Receptor, Insulin - metabolism Receptors Ungulates
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