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Volumn 46, Issue 2, 2007, Pages 554-560

Time-dependent inhibition of isoprenylcysteine carboxyl methyltransferase by indole-based small molecules

Author keywords

[No Author keywords available]

Indexed keywords

CELL ACTIVE INHIBITORS; ISOPRENYLCYSTEINE CARBOXYL METHYLTRANSFERASE (ICMT); METHYLATION; PRENYLATED PROTEINS;

EID: 33846236895     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060344n     Document Type: Article
Times cited : (25)

References (33)
  • 1
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F. L., and Casey, P. J. (1996) Protein prenylation: Molecular mechanisms and functional consequences, Annu. Rev. Biochem. 65, 241-69.
    • (1996) Annu. Rev. Biochem , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 2
    • 0028170814 scopus 로고
    • Role of protein modification reactions in programming interactions between rasrelated GTPases and cell membranes
    • Glomset, J. A., and Farnsworth, C. C. (1994) Role of protein modification reactions in programming interactions between rasrelated GTPases and cell membranes, Annu. Rev. Cell Biol. 10, 181-205.
    • (1994) Annu. Rev. Cell Biol , vol.10 , pp. 181-205
    • Glomset, J.A.1    Farnsworth, C.C.2
  • 3
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • Casey, P. J., and Seabra, M. C. (1996) Protein prenyltransferases, J. Biol. Chem. 271, 5289-92.
    • (1996) J. Biol. Chem , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 4
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke, S. (1992) Protein isoprenylation and methylation at carboxyl-terminal cysteine residues, Annu. Rev. Biochem. 61, 355-86.
    • (1992) Annu. Rev. Biochem , vol.61 , pp. 355-386
    • Clarke, S.1
  • 5
    • 0032530150 scopus 로고    scopus 로고
    • Endoplasmic reticulum membrane localization of Rcelp and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage
    • Schmidt, W. K., Tam, A., Fujimura-Kamada, K., and Michaelis, S. (1998) Endoplasmic reticulum membrane localization of Rcelp and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage, Proc. Natl. Acad. Sci. U.S.A. 95, 11175-80.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 11175-11180
    • Schmidt, W.K.1    Tam, A.2    Fujimura-Kamada, K.3    Michaelis, S.4
  • 6
    • 0000081175 scopus 로고
    • Posttranslational modification of the Ha-ras oncogene protein: Evidence for a third class of protein carboxyl methyltransferases
    • Clarke, S., Vogel, J. P., Deschenes, R. J., and Stock, J. (1988) Posttranslational modification of the Ha-ras oncogene protein: Evidence for a third class of protein carboxyl methyltransferases, Proc. Natl. Acad. Sci. U.S.A. 85, 4643-7.
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 4643-4647
    • Clarke, S.1    Vogel, J.P.2    Deschenes, R.J.3    Stock, J.4
  • 7
    • 0031945668 scopus 로고    scopus 로고
    • CaaX converting enzymes
    • Ashby, M. N. (1998) CaaX converting enzymes, Curr. Opin. Lipidol. 9, 99-102.
    • (1998) Curr. Opin. Lipidol , vol.9 , pp. 99-102
    • Ashby, M.N.1
  • 8
    • 18344394166 scopus 로고    scopus 로고
    • Post-prenylation-processing enzymes as new targets in oncogenesis
    • Winter-Vann, A. M., and Casey, P. J. (2005) Post-prenylation-processing enzymes as new targets in oncogenesis, Nat. Rev. Cancer 5, 405-12.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 405-412
    • Winter-Vann, A.M.1    Casey, P.J.2
  • 9
    • 0037805547 scopus 로고    scopus 로고
    • RAS oncogenes: The first 30 years
    • Malumbres, M., and Barbacid, M. (2003) RAS oncogenes: The first 30 years, Nat. Rev. Cancer 3, 459-65.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 459-465
    • Malumbres, M.1    Barbacid, M.2
  • 10
    • 0027213688 scopus 로고
    • Inhibitors of Ras farnesyltransferases
    • Tamanoi, F. (1993) Inhibitors of Ras farnesyltransferases, Trends Biochem. Sci. 18, 349-53.
    • (1993) Trends Biochem. Sci , vol.18 , pp. 349-353
    • Tamanoi, F.1
  • 13
    • 0030968859 scopus 로고    scopus 로고
    • Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo
    • Rowell, C. A., Kowalczyk, J. J., Lewis, M. D., and Garcia, A. M. (1997) Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo, J. Biol. Chem. 272, 14093-7.
    • (1997) J. Biol. Chem , vol.272 , pp. 14093-14097
    • Rowell, C.A.1    Kowalczyk, J.J.2    Lewis, M.D.3    Garcia, A.M.4
  • 15
    • 0033605743 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian prenyl protein-specific protease
    • Otto, J. C., Kim, E., Young, S. G., and Casey, P. J. (1999) Cloning and characterization of a mammalian prenyl protein-specific protease, J. Biol. Chem. 274, 8379-82.
    • (1999) J. Biol. Chem , vol.274 , pp. 8379-8382
    • Otto, J.C.1    Kim, E.2    Young, S.G.3    Casey, P.J.4
  • 16
    • 0034625181 scopus 로고    scopus 로고
    • Targeted inactivation of the isoprenylcysteine carboxyl methyltransferase gene causes mislocalization of K-Ras in mammalian cells
    • Bergo, M. O., Leung, G. K., Ambroziak, P., Otto, J. C., Casey, P. J., and Young, S. G. (2000) Targeted inactivation of the isoprenylcysteine carboxyl methyltransferase gene causes mislocalization of K-Ras in mammalian cells, J. Biol. Chem. 275, 17605-10.
    • (2000) J. Biol. Chem , vol.275 , pp. 17605-17610
    • Bergo, M.O.1    Leung, G.K.2    Ambroziak, P.3    Otto, J.C.4    Casey, P.J.5    Young, S.G.6
  • 20
    • 14644417903 scopus 로고    scopus 로고
    • Analysis of the kinetic mechanism of recombinant human isoprenylcysteine carboxylmethyltransferase (Icmt)
    • Baron, R. A., and Casey, P. J. (2004) Analysis of the kinetic mechanism of recombinant human isoprenylcysteine carboxylmethyltransferase (Icmt), BMC Biochem. 5, 19.
    • (2004) BMC Biochem , vol.5 , pp. 19
    • Baron, R.A.1    Casey, P.J.2
  • 21
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison, J. F., and Walsh, C. T. (1988) The behavior and significance of slow-binding enzyme inhibitors, Adv. Enzymol. Relat. Areas Mol. Biol. 61, 201-301.
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 22
    • 0026630109 scopus 로고
    • Kinetic mechanism of isoprenylated protein methyltransferase
    • Shi, Y. Q., and Rando, R. R. (1992) Kinetic mechanism of isoprenylated protein methyltransferase, J. Biol. Chem. 267, 9547-51.
    • (1992) J. Biol. Chem , vol.267 , pp. 9547-9551
    • Shi, Y.Q.1    Rando, R.R.2
  • 23
    • 0003922525 scopus 로고
    • John Wiley & Sons, New York. 1982
    • Jain, M. (1982) Handbook of Enzyme Inhibitors (1965-1977), Vol. 24, John Wiley & Sons, New York.
    • (1965) Handbook of Enzyme Inhibitors , vol.24
    • Jain, M.1
  • 24
    • 0025870323 scopus 로고
    • Identifying the recognition unit for G protein methylation
    • Tan, E. W., Perez-Sala, D., Canada, F. J., and Rando, R. R. (1991) Identifying the recognition unit for G protein methylation, J. Biol. Chem. 266, 10719-22.
    • (1991) J. Biol. Chem , vol.266 , pp. 10719-10722
    • Tan, E.W.1    Perez-Sala, D.2    Canada, F.J.3    Rando, R.R.4
  • 25
    • 0026748625 scopus 로고
    • Prenylated protein methyltransferases do not distinguish between farnesylated and geranylgeranylated substrates
    • Perez-Sala, D., Gilbert, B. A., Tan, E. W., and Rando, R. R. (1992) Prenylated protein methyltransferases do not distinguish between farnesylated and geranylgeranylated substrates, Biochem. J. 284, 835-40.
    • (1992) Biochem. J , vol.284 , pp. 835-840
    • Perez-Sala, D.1    Gilbert, B.A.2    Tan, E.W.3    Rando, R.R.4
  • 26
    • 0001396685 scopus 로고
    • The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions
    • Morrison, J. F. (1982) The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions, Trends Biochem. Sci. 7, 102-4.
    • (1982) Trends Biochem. Sci , vol.7 , pp. 102-104
    • Morrison, J.F.1
  • 28
    • 23844534430 scopus 로고    scopus 로고
    • The isoprenoid substrate specificity of isoprenylcysteine carboxylmethyltransferase: Development of novel inhibitors
    • Anderson, J. L., Henriksen, B. S., Gibbs, R. A., and Hrycyna, C. A. (2005) The isoprenoid substrate specificity of isoprenylcysteine carboxylmethyltransferase: Development of novel inhibitors, J. Biol Chem. 280, 29454-61.
    • (2005) J. Biol Chem , vol.280 , pp. 29454-29461
    • Anderson, J.L.1    Henriksen, B.S.2    Gibbs, R.A.3    Hrycyna, C.A.4
  • 29
    • 33745713224 scopus 로고    scopus 로고
    • Amide-substituted farnesylcysteine analogs as inhibitors of human isoprenylcysteine carboxyl methyltransferase
    • Donelson, J. L., Hodges, H. B., Macdougall, D. D., Henriksen, B. S., Hrycyna, C. A., and Gibbs, R. A. (2006) Amide-substituted farnesylcysteine analogs as inhibitors of human isoprenylcysteine carboxyl methyltransferase, Bioorg. Med. Chem. Lett. 16, 4420-3.
    • (2006) Bioorg. Med. Chem. Lett , vol.16 , pp. 4420-4423
    • Donelson, J.L.1    Hodges, H.B.2    Macdougall, D.D.3    Henriksen, B.S.4    Hrycyna, C.A.5    Gibbs, R.A.6
  • 30
    • 0037342399 scopus 로고    scopus 로고
    • Isoprenylcysteine carboxyl methyltransferase activity modulates endothelial cell apoptosis
    • Kramer, K., Harrington, E. O., Lu, Q., Bellas, R., Newton, J., Sheahan, K. L., and Rounds, S. (2003) Isoprenylcysteine carboxyl methyltransferase activity modulates endothelial cell apoptosis, Mol. Biol. Cell 14, 848-57.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 848-857
    • Kramer, K.1    Harrington, E.O.2    Lu, Q.3    Bellas, R.4    Newton, J.5    Sheahan, K.L.6    Rounds, S.7
  • 31
    • 0030610589 scopus 로고    scopus 로고
    • Inhibition of growth and p21ras methylation in vascular endothelial cells by homocysteine but not cysteine
    • Wang, H., Yoshizumi, M., Lai, K., Tsai, J. C., Perrella, M. A., Haber, E., and Lee, M. E. (1997) Inhibition of growth and p21ras methylation in vascular endothelial cells by homocysteine but not cysteine, J. Biol. Chem. 272, 25380-5.
    • (1997) J. Biol. Chem , vol.272 , pp. 25380-25385
    • Wang, H.1    Yoshizumi, M.2    Lai, K.3    Tsai, J.C.4    Perrella, M.A.5    Haber, E.6    Lee, M.E.7


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