Dephosphorylation of human insulin-like growth factor I (IGF-I) receptors by membrane-associated tyrosine phosphatases.

@article{Peraldi1992DephosphorylationOH,
  title={Dephosphorylation of human insulin-like growth factor I (IGF-I) receptors by membrane-associated tyrosine phosphatases.},
  author={Pascal Peraldi and S Hauguel-de Mouzon and Franc Oise Alengrin and E Van Obberghen},
  journal={The Biochemical journal},
  year={1992},
  volume={285 ( Pt 1)},
  pages={71-8}
}
The insulin-like growth factor-I (IGF-I) receptor exhibits structural and functional similarities to the insulin receptor. Although the regulation of the insulin-receptor tyrosine kinase has been extensively investigated, the mechanisms involved in phosphorylation/dephosphorylation of the IGF-I receptor have received only little attention. To obtain a better understanding of the mode of IGF-I action, we have investigated the effects of protein phosphotyrosine phosphatases (PTPases) on the… CONTINUE READING

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