Ras farnesyltransferase

Waldmann H, Thutewohl M (2000) Ras-Farnesyltransferase-Inhibitors as Promising Anti-Tumor Drugs. 211 117-130 Wang G-X, see Chow H-F (2001) 217 1-50 Weil T, see Wiesler U-M (2001) 212 1-40... 

Waldmann H, Thutewohl M (2000) Ras-Farnesyltransferase-Inhibitors as Promising Anti-Tiimor Drugs. 211 117-130... 

Ras is strictly localized to the inner side of the plasma membrane. A lipid anchor covalently attached to the C-terminus of Ras penetrates into the lipid bilayer. This membrane anchorage is essential for the biological activity of Ras. Hence, the inhibition of anchor attachment has become an attractive pharmacological target [ 13]. See Waldmann H, Thutewohl M,Ras-Farnesyltransferase-inhibitors as promising anti-tumor drugs, this volume. 

Ras-Farnesyltransferase-Inhibitors as Promising Anti-Tumor Drugs... 

Reiss, Y., Seabra, M.C., Armstrong, S. A., Slaughter, C.A., Goldstein, J.L., and Brown, M. S. (1991). Nonidentical subunits of p21H-ras farnesyltransferase. Peptide binding and farnesyl pyrophosphate carrier functions. J Biol Chem 266 10672-10677. 

This technique has been successfully applied in those biological targets where the key structural amino acids of the native peptide for peptide recognition are known. Miscellaneous examples are found in glycoprotein Gbllb/IIIa inhibitors (33)that mimic the RGD sequence (64) or in Ras-farnesyltransferase inhibitors (34) that mimic the CAAX sequence (Fig. 15.15) (65). 

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