Tyrosine-specific phosphorylation of calmodulin by the insulin receptor kinase purified from human placenta.

Samankaltaisia teoksia

• Effect of basic polycations and proteins on purified insulin receptor. Insulin-independent activation of the receptor tyrosine-specific protein kinase by poly(L-lysine).
  Tekijä: Fujita-Yamaguchi, Y, et al.
  Julkaistu: (1989)
• Tyrosine-specific protein kinase activity is associated with the purified insulin receptor.
  Tekijä: Kasuga, M, et al.
  Julkaistu: (1983)
• In vitro tyrosine phosphorylation studies on RAS proteins and calmodulin suggest that polylysine-like basic peptides or domains may be involved in interactions between insulin receptor kinase and its substrate.
  Tekijä: Fujita-Yamaguchi, Y, et al.
  Julkaistu: (1989)
• Insulin-stimulated phosphorylation of calmodulin.
  Tekijä: Sacks, D B, et al.
  Julkaistu: (1992)
• Phosphorylation by casein kinase II alters the biological activity of calmodulin.
  Tekijä: Sacks, D B, et al.
  Julkaistu: (1992)