A Mutant Form of Human Protein Farnesyltransferase Exhibits Increased Resistance to Farnesyltransferase Inhibitors*

@article{Villar1999AMF,
  title={A Mutant Form of Human Protein Farnesyltransferase Exhibits Increased Resistance to Farnesyltransferase Inhibitors*},
  author={K. Del Villar and J. Urano and L. Guo and F. Tamanoi},
  journal={The Journal of Biological Chemistry},
  year={1999},
  volume={274},
  pages={27010 - 27017}
}
Protein farnesyltransferase (FTase) is a key enzyme responsible for the lipid modification of a large and important number of proteins including Ras. Recent demonstrations that inhibitors of this enzyme block the growth of a variety of human tumors point to the importance of this enzyme in human tumor formation. In this paper, we report that a mutant form of human FTase, Y361L, exhibits increased resistance to farnesyltransferase inhibitors, particularly a tricyclic compound, SCH56582, which is… Expand
40 Citations
Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase.
Resistance to a Protein Farnesyltransferase Inhibitor in Plasmodium falciparum*
Molecular dynamics simulations on the critical states of the farnesyltransferase enzyme.
The Protein Farnesyltransferase Regulates HDAC6 Activity in a Microtubule-dependent Manner*
...
1
2
3
4
...

References

SHOWING 1-10 OF 40 REFERENCES
Novel Tricyclic Inhibitors of Farnesyl Protein Transferase
Mutant farnesyltransferase beta subunit of Saccharomyces cerevisiae that can substitute for geranylgeranyltransferase type I beta subunit.
Identification of Ras farnesyltransferase inhibitors by microbial screening.
  • M. Hara, K. Akasaka, +6 authors F. Tamanoi
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1993
Selective inhibition of farnesyl-protein transferase blocks ras processing in vivo.
...
1
2
3
4
...