The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity.

Lignende værker

• Tyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatase.
  af: Autero, M, et al.
  Udgivet: (1994)
• Ras GTPase-activating protein: a substrate and a potential binding protein of the protein-tyrosine kinase p56lck.
  af: Amrein, K E, et al.
  Udgivet: (1992)
• The Src homology 2 domain of the protein-tyrosine kinase p56lck mediates both intermolecular and intramolecular interactions.
  af: Amrein, K E, et al.
  Udgivet: (1993)
• Activation of p56lck by p72syk through physical association and N-terminal tyrosine phosphorylation.
  af: Couture, C, et al.
  Udgivet: (1994)
• The SH2 domain is required for stable phosphorylation of p56lck at tyrosine 505, the negative regulatory site.
  af: Gervais, F G, et al.
  Udgivet: (1993)