Selectivity at the cleavage/attachment site of phosphatidylinositol-glycan anchored membrane proteins is enzymatically determined.

Lignende værker

• Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase.
  af: Micanovic, R, et al.
  Udgivet: (1990)
• Biosynthesis of phosphatidylinositol-glycan (PI-G)-anchored membrane proteins in cell-free systems: cleavage of the nascent protein and addition of the PI-G moiety depend on the size of the COOH-terminal signal peptide.
  af: Kodukula, K, et al.
  Udgivet: (1992)
• Characterization of the phosphatidylinositol-glycan membrane anchor of human placental alkaline phosphatase.
  af: Howard, A D, et al.
  Udgivet: (1987)
• Phosphatidylinositol-glycan (PI-G)-anchored membrane proteins: requirement of ATP and GTP for translation-independent COOH-terminal processing.
  af: Amthauer, R, et al.
  Udgivet: (1992)
• Conversion of placental alkaline phosphatase from a phosphatidylinositol-glycan-anchored protein to an integral transmembrane protein.
  af: Berger, J, et al.
  Udgivet: (1989)