Insulin stimulates phosphorylation of a 120-kDa glycoprotein substrate (pp120) for the receptor-associated protein kinase in intact H-35 hepatoma cells.

Ítems similars

• Tyrosine phosphorylation of two cytosolic proteins of 50 kDa and 35 kDa in rat liver by insulin-receptor kinase in vitro.
  per: Kwok, Y C, et al.
  Publicat: (1987)
• Identification of pp120, an endogenous substrate for the hepatocyte insulin receptor tyrosine kinase, as an integral membrane glycoprotein of the bile canalicular domain.
  per: Margolis, R N, et al.
  Publicat: (1988)
• Insulin rapidly stimulates phosphorylation of a 46-kDa membrane protein on tyrosine residues as well as phosphorylation of several soluble proteins in intact fat cells.
  per: Häring, H U, et al.
  Publicat: (1987)
• Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein.
  per: Guan, J L, et al.
  Publicat: (1991)
• Derived protein sequence, oligosaccharides, and membrane insertion of the 120-kDa lysosomal membrane glycoprotein (lgp120): identification of a highly conserved family of lysosomal membrane glycoproteins.
  per: Howe, C L, et al.
  Publicat: (1988)