Purification of a mammalian protein geranylgeranyltransferase. Formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex.

This publication has 29 references indexed in Scilit:

• PROTEIN ISOPRENYLATION AND METHYLATION AT CARBOXYL-TERMINAL CYSTEINE RESIDUES
  Annual Review of Biochemistry, 1992
• cDNA cloning and expression of the peptide-binding β subunit of rat p21rasfarnesyltransferase, the counterpart of yeast DPR1/RAM1
  Cell, 1991
• C terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester.
  Proceedings of the National Academy of Sciences, 1991
• Protein farnesyltransferase and geranylgeranyltransferase share a common α subunit
  Cell, 1991
• The prenylation of proteins
  Current Opinion in Lipidology, 1991
• A geranylgeranyltransferase for rhoA p21 distinct from the farnesyltransferase for ras p21A
  Biochemical and Biophysical Research Communications, 1991
• Mutants of Saccharomyces cerevisiae defective in the farnesylation of Ras proteins.
  Proceedings of the National Academy of Sciences, 1990
• Enzymatic Coupling of Cholesterol Intermediates to a Mating Pheromone Precursor and to the Ras Protein
  Science, 1990
• Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides
  Cell, 1990
• Protein contaminants of sodium dodecyl sulfate-polyacrylamide gels
  Analytical Biochemistry, 1983