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Volumn 42, Issue 8, 1999, Pages 1333-1340

Potent, highly selective, and non-thiol inhibitors of protein geranylgeranyltransferase-I

Author keywords

[No Author keywords available]

Indexed keywords

4 [[N (1H IMIDAZOL 2 YL)METHYLENEAMINO] 2 (1 NAPHTHYL)BENZOYL]LEUCINE METHYL ESTER; 4 NITRO 2 (1 NAPHTHYL)BENZOIC ACID METHYL ESTER; ANTINEOPLASTIC AGENT; ENZYME INHIBITOR; GERANYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 0033594336     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm9900873     Document Type: Article
Times cited : (79)

References (26)
  • 1
    • 0030935249 scopus 로고    scopus 로고
    • Yeast protein geranylgeranyltransferase type-I: Steady-state kinetics and substrate binding
    • Sirtan, W. G.; Poulter, C. D. Yeast protein geranylgeranyltransferase type-I: steady-state kinetics and substrate binding. Biochemistry 1997, 36, 4552-4557. Yokoyama, K.; McGeady, P.; Gelb, M. H. Mammalian protein geranylgeranyltransferase-I: substrate specificity, kinetic mechanism, metal requirements, and affinity labeling. Biochemistry 1995, 34, 1344-1354. Sirtan, W. G.; Poulter, C. D. Yeast protein geranylgeranyltransferase type-I: overproduction, purification, and characterization. Arch. Biochem. Biophys. 1995, 321, 182-190. Zhang, F. L.; Moomaw, J. F.; Casey, P. J. Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type-I. J. Biol. Chem. 1994, 269, 23465-23470.
    • (1997) Biochemistry , vol.36 , pp. 4552-4557
    • Sirtan, W.G.1    Poulter, C.D.2
  • 2
    • 0028988427 scopus 로고
    • Mammalian protein geranylgeranyltransferase-I: Substrate specificity, kinetic mechanism, metal requirements, and affinity labeling
    • Sirtan, W. G.; Poulter, C. D. Yeast protein geranylgeranyltransferase type-I: steady-state kinetics and substrate binding. Biochemistry 1997, 36, 4552-4557. Yokoyama, K.; McGeady, P.; Gelb, M. H. Mammalian protein geranylgeranyltransferase-I: substrate specificity, kinetic mechanism, metal requirements, and affinity labeling. Biochemistry 1995, 34, 1344-1354. Sirtan, W. G.; Poulter, C. D. Yeast protein geranylgeranyltransferase type-I: overproduction, purification, and characterization. Arch. Biochem. Biophys. 1995, 321, 182-190. Zhang, F. L.; Moomaw, J. F.; Casey, P. J. Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type-I. J. Biol. Chem. 1994, 269, 23465-23470.
    • (1995) Biochemistry , vol.34 , pp. 1344-1354
    • Yokoyama, K.1    McGeady, P.2    Gelb, M.H.3
  • 3
    • 0029159923 scopus 로고
    • Yeast protein geranylgeranyltransferase type-I: Overproduction, purification, and characterization
    • Sirtan, W. G.; Poulter, C. D. Yeast protein geranylgeranyltransferase type-I: steady-state kinetics and substrate binding. Biochemistry 1997, 36, 4552-4557. Yokoyama, K.; McGeady, P.; Gelb, M. H. Mammalian protein geranylgeranyltransferase-I: substrate specificity, kinetic mechanism, metal requirements, and affinity labeling. Biochemistry 1995, 34, 1344-1354. Sirtan, W. G.; Poulter, C. D. Yeast protein geranylgeranyltransferase type-I: overproduction, purification, and characterization. Arch. Biochem. Biophys. 1995, 321, 182-190. Zhang, F. L.; Moomaw, J. F.; Casey, P. J. Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type-I. J. Biol. Chem. 1994, 269, 23465-23470.
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 182-190
    • Sirtan, W.G.1    Poulter, C.D.2
  • 4
    • 0027933505 scopus 로고
    • Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type-I
    • Sirtan, W. G.; Poulter, C. D. Yeast protein geranylgeranyltransferase type-I: steady-state kinetics and substrate binding. Biochemistry 1997, 36, 4552-4557. Yokoyama, K.; McGeady, P.; Gelb, M. H. Mammalian protein geranylgeranyltransferase-I: substrate specificity, kinetic mechanism, metal requirements, and affinity labeling. Biochemistry 1995, 34, 1344-1354. Sirtan, W. G.; Poulter, C. D. Yeast protein geranylgeranyltransferase type-I: overproduction, purification, and characterization. Arch. Biochem. Biophys. 1995, 321, 182-190. Zhang, F. L.; Moomaw, J. F.; Casey, P. J. Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type-I. J. Biol. Chem. 1994, 269, 23465-23470.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23465-23470
    • Zhang, F.L.1    Moomaw, J.F.2    Casey, P.J.3
  • 5
    • 0027050783 scopus 로고
    • Biochemistry of protein prenylation
    • Casey, P. J. Biochemistry of protein prenylation. J. Lipid Res. 1992, 33, 1731-1740.
    • (1992) J. Lipid Res. , vol.33 , pp. 1731-1740
    • Casey, P.J.1
  • 6
    • 0029839489 scopus 로고    scopus 로고
    • Yeast geranylgeranyltransferase type-II: Steady state kinetic studies of the recombinant enzyme
    • Witter, D. J.; Poulter, C. D. Yeast geranylgeranyltransferase type-II: steady state kinetic studies of the recombinant enzyme. Biochemistry 1996, 35, 925-932.
    • (1996) Biochemistry , vol.35 , pp. 925-932
    • Witter, D.J.1    Poulter, C.D.2
  • 7
    • 0028331587 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic
    • Gibbs, J, B.; Oliff, A.; Kohl, N. E. Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic. Cell 1994, 77, 175-178. Buss, J. E.; Marsters, J. C. Farnesyltransferase inhibitors: the successes and suprises of a new class of potential cancer chemotherapeutics. Chem. Biol. 1995, 2, 787-791. Sebti, S. M.; Hamilton, A. D. Inhibition of Ras prenylation: a novel approach to cancer chemotherapy. Pharmacol. Ther. 1997, 71, 1-12.
    • (1994) Cell , vol.77 , pp. 175-178
    • Gibbs, J.B.1    Oliff, A.2    Kohl, N.E.3
  • 8
    • 0029613291 scopus 로고
    • Farnesyltransferase inhibitors: The successes and suprises of a new class of potential cancer chemotherapeutics
    • Gibbs, J, B.; Oliff, A.; Kohl, N. E. Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic. Cell 1994, 77, 175-178. Buss, J. E.; Marsters, J. C. Farnesyltransferase inhibitors: the successes and suprises of a new class of potential cancer chemotherapeutics. Chem. Biol. 1995, 2, 787-791. Sebti, S. M.; Hamilton, A. D. Inhibition of Ras prenylation: a novel approach to cancer chemotherapy. Pharmacol. Ther. 1997, 71, 1-12.
    • (1995) Chem. Biol. , vol.2 , pp. 787-791
    • Buss, J.E.1    Marsters, J.C.2
  • 9
    • 0028331587 scopus 로고    scopus 로고
    • Inhibition of Ras prenylation: A novel approach to cancer chemotherapy
    • Gibbs, J, B.; Oliff, A.; Kohl, N. E. Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic. Cell 1994, 77, 175-178. Buss, J. E.; Marsters, J. C. Farnesyltransferase inhibitors: the successes and suprises of a new class of potential cancer chemotherapeutics. Chem. Biol. 1995, 2, 787-791. Sebti, S. M.; Hamilton, A. D. Inhibition of Ras prenylation: a novel approach to cancer chemotherapy. Pharmacol. Ther. 1997, 71, 1-12.
    • (1997) Pharmacol. Ther. , vol.71 , pp. 1-12
    • Sebti, S.M.1    Hamilton, A.D.2
  • 10
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac and Cdc42 GTPases in cell cycle progression through G1
    • Olson, M. F.; Ashworth, A.; Hall, A. An essential role for Rho, Rac and Cdc42 GTPases in cell cycle progression through G1. Science 1995, 269, 1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 11
    • 0029857638 scopus 로고    scopus 로고
    • Protein geranylgeranylation, not farnesylation, is required for G1 to S phase transition in mouse fibroblasts
    • Vogt, A.; Qian, Y.; McGuire, T. F.; Blaskovich, M. A.; Hamilton, A. D.; Sebti, S. M. Protein geranylgeranylation, not farnesylation, is required for G1 to S phase transition in mouse fibroblasts. Oncogene 1996, 13, 1991-1999.
    • (1996) Oncogene , vol.13 , pp. 1991-1999
    • Vogt, A.1    Qian, Y.2    McGuire, T.F.3    Blaskovich, M.A.4    Hamilton, A.D.5    Sebti, S.M.6
  • 12
    • 0032546264 scopus 로고    scopus 로고
    • Both farnesyltransferase and geranylgeranyltransferase are required for inhibition of oncogenic K-Ras prenylation but each alone is sufficient to supress human tumor growth in nude mouse xenografts
    • Sun, J.; Qian, Y.; Hamilton, A. D.; Sebti, S. M. Both farnesyltransferase and geranylgeranyltransferase are required for inhibition of oncogenic K-Ras prenylation but each alone is sufficient to supress human tumor growth in nude mouse xenografts. Oncogene 1998, 16, 1467-1473.
    • (1998) Oncogene , vol.16 , pp. 1467-1473
    • Sun, J.1    Qian, Y.2    Hamilton, A.D.3    Sebti, S.M.4
  • 14
    • 0030999565 scopus 로고    scopus 로고
    • Inhibition of protein geranylgeranylation causes a superinduction of nitric oxide synthase by IL-1β in artery smooth muscle cells
    • Finder, J. D.; Litz, J. L.; Blaskovich, M. A.; McGuire, T. F.; Qian, Y.; Hamilton, A. D.; Davies, P.; Sebti, S. M. Inhibition of protein geranylgeranylation causes a superinduction of nitric oxide synthase by IL-1β in artery smooth muscle cells. J. Biol. Chem. 1997, 272, 13484-13488.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13484-13488
    • Finder, J.D.1    Litz, J.L.2    Blaskovich, M.A.3    McGuire, T.F.4    Qian, Y.5    Hamilton, A.D.6    Davies, P.7    Sebti, S.M.8
  • 15
    • 0345098267 scopus 로고    scopus 로고
    • Peptidomimetic inhibitors of farnesyltransferase: An approach to new antitumor agents
    • Abell, A., Ed.; Jai Press: Greenwich, CT
    • Qian, Y.; Sebti, S. M.; Hamilton, A. D. Peptidomimetic inhibitors of farnesyltransferase: An approach to new antitumor agents. In Advances in Peptidomimetic Chemistry; Abell, A., Ed.; Jai Press: Greenwich, CT, 1997; Vol. 1, pp 165-192.
    • (1997) Advances in Peptidomimetic Chemistry , vol.1 , pp. 165-192
    • Qian, Y.1    Sebti, S.M.2    Hamilton, A.D.3
  • 16
    • 0030952552 scopus 로고    scopus 로고
    • Inhibition of the prenylation of K-Ras, but not H- or N-Ras, is highly resisitant to CAAX peptidomimetics and requires both a farnesyltransferase and a geranylgeranyltranferase I inhibitor in human cell lines
    • Lerner, E. C.; Zhang, T. T.; Knowles, D.; Qian, Y.; Hamilton, A. D.; Sebti, S. M. Inhibition of the prenylation of K-Ras, but not H- or N-Ras, is highly resisitant to CAAX peptidomimetics and requires both a farnesyltransferase and a geranylgeranyltranferase I inhibitor in human cell lines. Oncogene 1997, 15, 1283-1288.
    • (1997) Oncogene , vol.15 , pp. 1283-1288
    • Lerner, E.C.1    Zhang, T.T.2    Knowles, D.3    Qian, Y.4    Hamilton, A.D.5    Sebti, S.M.6
  • 17
    • 0029833497 scopus 로고    scopus 로고
    • Synthesis of protein farnesyltransferase and protein geranylgeranyltransferase inhibitors: Rapid access to chaetomellic acid A and its analogues
    • Ratemi, E. S.; Dolence, J. M.; Poulter, C. D.; Veders, J. C. Synthesis of protein farnesyltransferase and protein geranylgeranyltransferase inhibitors: rapid access to chaetomellic acid A and its analogues. J. Org. Chem. 1996, 61, 6296-6301. Macchia, M.; Jannitti, N.; Gervasi, G.; Danesi, R. Geranylgeranyl diphosphate-based inhibitors of post-translational geranylgeranylation of cellular proteins. J. Med. Chem. 1996, 39, 1352-1356.
    • (1996) J. Org. Chem. , vol.61 , pp. 6296-6301
    • Ratemi, E.S.1    Dolence, J.M.2    Poulter, C.D.3    Veders, J.C.4
  • 18
    • 0029938011 scopus 로고    scopus 로고
    • Geranylgeranyl diphosphate-based inhibitors of post-translational geranylgeranylation of cellular proteins
    • Ratemi, E. S.; Dolence, J. M.; Poulter, C. D.; Veders, J. C. Synthesis of protein farnesyltransferase and protein geranylgeranyltransferase inhibitors: rapid access to chaetomellic acid A and its analogues. J. Org. Chem. 1996, 61, 6296-6301. Macchia, M.; Jannitti, N.; Gervasi, G.; Danesi, R. Geranylgeranyl diphosphate-based inhibitors of post-translational geranylgeranylation of cellular proteins. J. Med. Chem. 1996, 39, 1352-1356.
    • (1996) J. Med. Chem. , vol.39 , pp. 1352-1356
    • Macchia, M.1    Jannitti, N.2    Gervasi, G.3    Danesi, R.4
  • 19
    • 0028973293 scopus 로고
    • Ras CAAX peptidomimetic FTI277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras/ Raf complexes
    • Lerner, E. C.; Qian, Y.; Blaskovitch, M.; Fossum, R.; Vogt, A.; Sun, J.; Cox, A. D.; Der, C. J.; Hamilton, A. D.; Sebti, S. M. Ras CAAX peptidomimetic FTI277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras/ Raf complexes. J. Biol. Chem. 1995, 270, 26802-26806. Qian, Y.; Vogt, A.; Sebti, S. M.; Hamilton, A. D. Design and synthesis of non-peptide Ras CAAX mimetics as potent farnesyltransferases inhibitors. J. Med. Chem. 1996, 39, 217-223.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26802-26806
    • Lerner, E.C.1    Qian, Y.2    Blaskovitch, M.3    Fossum, R.4    Vogt, A.5    Sun, J.6    Cox, A.D.7    Der, C.J.8    Hamilton, A.D.9    Sebti, S.M.10
  • 20
    • 0030046735 scopus 로고    scopus 로고
    • Design and synthesis of non-peptide Ras CAAX mimetics as potent farnesyltransferases inhibitors
    • Lerner, E. C.; Qian, Y.; Blaskovitch, M.; Fossum, R.; Vogt, A.; Sun, J.; Cox, A. D.; Der, C. J.; Hamilton, A. D.; Sebti, S. M. Ras CAAX peptidomimetic FTI277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras/ Raf complexes. J. Biol. Chem. 1995, 270, 26802-26806. Qian, Y.; Vogt, A.; Sebti, S. M.; Hamilton, A. D. Design and synthesis of non-peptide Ras CAAX mimetics as potent farnesyltransferases inhibitors. J. Med. Chem. 1996, 39, 217-223.
    • (1996) J. Med. Chem. , vol.39 , pp. 217-223
    • Qian, Y.1    Vogt, A.2    Sebti, S.M.3    Hamilton, A.D.4
  • 21
    • 0028810275 scopus 로고
    • Disruption of oncogenic K-Ras4B processing and signaling by a potent geranylgeranyltransferase inhibitor
    • (a) Lerner, E. C.; Qian, Y.; McGuire, T. F.; Hamilton, A. D.; Sebti, S. M. Disruption of oncogenic K-Ras4B processing and signaling by a potent geranylgeranyltransferase inhibitor. J. Biol. Chem. 1995, 270, 26770-26773.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26770-26773
    • Lerner, E.C.1    Qian, Y.2    McGuire, T.F.3    Hamilton, A.D.4    Sebti, S.M.5
  • 22
    • 0031894821 scopus 로고    scopus 로고
    • Selective inhibition of type-I geranylgeranyltransferase in vitro and in whole cells by CAAL peptidomimetics
    • (b) Qian, Y.; Vogt, A.; Vasudevan, A.; Sebti, S.; Hamilton, A. D. Selective inhibition of type-I geranylgeranyltransferase in vitro and in whole cells by CAAL peptidomimetics. Bioorg. Med. Chem. 1998, 6, 293-299.
    • (1998) Bioorg. Med. Chem. , vol.6 , pp. 293-299
    • Qian, Y.1    Vogt, A.2    Vasudevan, A.3    Sebti, S.4    Hamilton, A.D.5
  • 23
    • 0030470834 scopus 로고    scopus 로고
    • Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I
    • Zhang, F. L.; Casey, P. J. Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I. Biochem. J. 1996, 320, 925-932.
    • (1996) Biochem. J. , vol.320 , pp. 925-932
    • Zhang, F.L.1    Casey, P.J.2
  • 24
    • 0021887747 scopus 로고
    • Imidazolyl derivatives of enalapril as potential angiotensin converting enzyme inhibitors
    • Cecchi, R.; Ciabatti, R.; Favara, D.; Barone, D.; Baldoli, E. Imidazolyl derivatives of enalapril as potential angiotensin converting enzyme inhibitors. Farmaco Ed. Sci. 1985, 40, 541-554.
    • (1985) Farmaco Ed. Sci. , vol.40 , pp. 541-554
    • Cecchi, R.1    Ciabatti, R.2    Favara, D.3    Barone, D.4    Baldoli, E.5
  • 26
    • 0344667413 scopus 로고    scopus 로고
    • The exceptions were ethers 13 and 14 and aminomethylenes 11 and 12 which were prepared from the corresponding 4-hydroxy-and 4-cyanobenzoic acid derivatives, respectively
    • The exceptions were ethers 13 and 14 and aminomethylenes 11 and 12 which were prepared from the corresponding 4-hydroxy-and 4-cyanobenzoic acid derivatives, respectively.


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