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.

Eitemau Tebyg

• Tyrosine-specific phosphorylation of calmodulin by the insulin receptor kinase purified from human placenta.
  gan: Sacks, D B, et al.
  Cyhoeddwyd: (1989)
• Effect of basic polycations and proteins on purified insulin receptor. Insulin-independent activation of the receptor tyrosine-specific protein kinase by poly(L-lysine).
  gan: Fujita-Yamaguchi, Y, et al.
  Cyhoeddwyd: (1989)
• Phosphorylation of tyrosine residues of calmodulin in Rous sarcoma virus-transformed cells.
  gan: Fukami, Y, et al.
  Cyhoeddwyd: (1986)
• The monomeric alpha beta form of the insulin receptor exhibits much higher insulin-dependent tyrosine-specific protein kinase activity than the intact alpha 2 beta 2 form of the receptor.
  gan: Fujita-Yamaguchi, Y, et al.
  Cyhoeddwyd: (1985)
• Tyrosine phosphorylation of RAS by ABL allosterically enhances effector binding
  gan: Ting, Pamela Y., et al.
  Cyhoeddwyd: (2015)