Effect of basic polycations and proteins on purified insulin receptor. Insulin-independent activation of the receptor tyrosine-specific protein kinase by poly(L-lysine).

Lignende værker

• Tyrosine-specific phosphorylation of calmodulin by the insulin receptor kinase purified from human placenta.
  af: Sacks, D B, et al.
  Udgivet: (1989)
• Tyrosine-specific protein kinase activity is associated with the purified insulin receptor.
  af: Kasuga, M, et al.
  Udgivet: (1983)
• 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.
  af: Fujita-Yamaguchi, Y, et al.
  Udgivet: (1985)
• 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.
  af: Fujita-Yamaguchi, Y, et al.
  Udgivet: (1989)
• Binding of isolated rheumatoid factors to histone proteins and basic polycations.
  af: Hobbs, R N, et al.
  Udgivet: (1983)