[HTML][HTML] Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B: possible facilitation by the formation of a …
BJ Goldstein, A Bittner-Kowalczyk, MF White… - Journal of Biological …, 2000 - ASBMB
Regulation of the steady-state tyrosine phosphorylation of the insulin receptor and its
postreceptor substrates are essential determinants of insulin signal transduction. However,
little is known regarding the molecular interactions that influence the balance of these
processes, especially the phosphorylation state of postinsulin receptor substrates, such as
insulin receptor substrate-1 (IRS-1). The specific activity of four candidate protein-tyrosine
phosphatases (protein-tyrosine phosphatase 1B (PTP1B), SH2 domain-containing PTPase …
postreceptor substrates are essential determinants of insulin signal transduction. However,
little is known regarding the molecular interactions that influence the balance of these
processes, especially the phosphorylation state of postinsulin receptor substrates, such as
insulin receptor substrate-1 (IRS-1). The specific activity of four candidate protein-tyrosine
phosphatases (protein-tyrosine phosphatase 1B (PTP1B), SH2 domain-containing PTPase …