메뉴 건너뛰기




Volumn 70, Issue 12, 2005, Pages 1735-1743

Isothiazole dioxide derivative 6n inhibits vascular smooth muscle cell proliferation and protein farnesylation

Author keywords

Atherosclerosis; Cell proliferation; Farnesol; Farnesyl transferase inhibitor; Farnesylation; Smooth muscle cell

Indexed keywords

FARNESOL; ISOTHIAZOLE DERIVATIVE; PROTEIN FARNESYLTRANSFERASE; PROTEIN FARNESYLTRANSFERASE INHIBITOR; THYMIDINE;

EID: 27744443732     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2005.09.022     Document Type: Article
Times cited : (7)

References (46)
  • 1
    • 0033552883 scopus 로고    scopus 로고
    • Atherosclerosis - An inflammatory disease
    • R. Ross Atherosclerosis - an inflammatory disease N Engl J Med 340 2 1999 115 126
    • (1999) N Engl J Med , vol.340 , Issue.2 , pp. 115-126
    • Ross, R.1
  • 2
    • 0027534090 scopus 로고
    • Smooth muscle cells and the pathogenesis of the lesions of atherosclerosis
    • E.W. Raines, and R. Ross Smooth muscle cells and the pathogenesis of the lesions of atherosclerosis Br Heart J 69 1 Suppl 1993 S30 S37
    • (1993) Br Heart J , vol.69 , Issue.1 SUPPL.
    • Raines, E.W.1    Ross, R.2
  • 3
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • M.F. Olson, A. Ashworth, and A. Hall An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1 Science 269 5228 1995 1270 1272
    • (1995) Science , vol.269 , Issue.5228 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 4
    • 0021970413 scopus 로고
    • Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells
    • L.S. Mulcahy, M.R. Smith, and D.W. Stacey Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells Nature 313 5999 1985 241 243
    • (1985) Nature , vol.313 , Issue.5999 , pp. 241-243
    • Mulcahy, L.S.1    Smith, M.R.2    Stacey, D.W.3
  • 5
    • 0028170814 scopus 로고
    • Role of protein modification reactions in programming interactions between ras-related GTPases and cell membranes
    • J.A. Glomset, and C.C. Farnsworth Role of protein modification reactions in programming interactions between ras-related GTPases and cell membranes Annu Rev Cell Biol 10 1994 181 205
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 181-205
    • Glomset, J.A.1    Farnsworth, C.C.2
  • 6
    • 0034644537 scopus 로고    scopus 로고
    • Ras and Rho GTPases: A family reunion
    • D. Bar-Sagi, and A. Hall Ras and Rho GTPases: a family reunion Cell 103 2 2000 227 238
    • (2000) Cell , vol.103 , Issue.2 , pp. 227-238
    • Bar-Sagi, D.1    Hall, A.2
  • 7
    • 0021719520 scopus 로고
    • Microinjection of the oncogene form of the human H-ras (T-24) protein results in rapid proliferation of quiescent cells
    • J.R. Feramisco, M. Gross, T. Kamata, M. Rosenberg, and R.W. Sweet Microinjection of the oncogene form of the human H-ras (T-24) protein results in rapid proliferation of quiescent cells Cell 38 1 1984 109 117
    • (1984) Cell , vol.38 , Issue.1 , pp. 109-117
    • Feramisco, J.R.1    Gross, M.2    Kamata, T.3    Rosenberg, M.4    Sweet, R.W.5
  • 8
    • 0031005738 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of a dominant-negative H-ras suppresses neointimal formation in balloon-injured arteries in vivo
    • H. Ueno, H. Yamamoto, S. Ito, J.J. Li, and A. Takeshita Adenovirus-mediated transfer of a dominant-negative H-ras suppresses neointimal formation in balloon-injured arteries in vivo Arterioscler Thromb Vasc Biol 17 5 1997 898 904
    • (1997) Arterioscler Thromb Vasc Biol , vol.17 , Issue.5 , pp. 898-904
    • Ueno, H.1    Yamamoto, H.2    Ito, S.3    Li, J.J.4    Takeshita, A.5
  • 9
    • 0029073183 scopus 로고
    • Inhibition of cellular ras prevents smooth muscle cell proliferation after vascular injury in vivo
    • C. Indolfi, E.V. Avvedimento, A. Rapacciuolo, E. Di Lorenzo, G. Esposito, and E. Stabile Inhibition of cellular ras prevents smooth muscle cell proliferation after vascular injury in vivo Nat Med 1 6 1995 541 545
    • (1995) Nat Med , vol.1 , Issue.6 , pp. 541-545
    • Indolfi, C.1    Avvedimento, E.V.2    Rapacciuolo, A.3    Di Lorenzo, E.4    Esposito, G.5    Stabile, E.6
  • 10
    • 0037150157 scopus 로고    scopus 로고
    • Functional inhibition of Ras by S-trans,trans-farnesyl thiosalicylic acid attenuates atherosclerosis in apolipoprotein e knockout mice
    • J. George, A. Afek, P. Keren, I. Herz, I. Goldberg, and R. Haklai Functional inhibition of Ras by S-trans,trans-farnesyl thiosalicylic acid attenuates atherosclerosis in apolipoprotein E knockout mice Circulation 105 20 2002 2416 2422
    • (2002) Circulation , vol.105 , Issue.20 , pp. 2416-2422
    • George, J.1    Afek, A.2    Keren, P.3    Herz, I.4    Goldberg, I.5    Haklai, R.6
  • 12
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • P.J. Casey, and M.C. Seabra Protein prenyltransferases J Biol Chem 271 10 1996 5289 5292
    • (1996) J Biol Chem , vol.271 , Issue.10 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 13
    • 0027416643 scopus 로고
    • Purification of a mammalian protein geranylgeranyltransferase. Formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex
    • K. Yokoyama, and M.H. Gelb Purification of a mammalian protein geranylgeranyltransferase. Formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex J Biol Chem 268 6 1993 4055 4060
    • (1993) J Biol Chem , vol.268 , Issue.6 , pp. 4055-4060
    • Yokoyama, K.1    Gelb, M.H.2
  • 14
    • 0032613078 scopus 로고    scopus 로고
    • Incorporation of radiolabeled prenyl alcohols and their analogs into mammalian cell proteins. a useful tool for studying protein prenylation
    • A. Corsini, C.C. Farnsworth, P. McGeady, M.H. Gelb, and J.A. Glomset Incorporation of radiolabeled prenyl alcohols and their analogs into mammalian cell proteins. A useful tool for studying protein prenylation Meth Mol Biol 116 1999 125 144
    • (1999) Meth Mol Biol , vol.116 , pp. 125-144
    • Corsini, A.1    Farnsworth, C.C.2    McGeady, P.3    Gelb, M.H.4    Glomset, J.A.5
  • 15
    • 4644362784 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors as anticancer agents: Critical crossroads
    • R.J. Doll, P. Kirschmeier, and W.R. Bishop Farnesyltransferase inhibitors as anticancer agents: critical crossroads Curr Opin Drug Discov Devel 7 4 2004 478 486
    • (2004) Curr Opin Drug Discov Devel , vol.7 , Issue.4 , pp. 478-486
    • Doll, R.J.1    Kirschmeier, P.2    Bishop, W.R.3
  • 16
    • 0036876188 scopus 로고    scopus 로고
    • Ras as a target in cancer therapy
    • R.S. Midgley, and D.J. Kerr Ras as a target in cancer therapy Crit Rev Oncol Hematol 44 2 2002 109 120
    • (2002) Crit Rev Oncol Hematol , vol.44 , Issue.2 , pp. 109-120
    • Midgley, R.S.1    Kerr, D.J.2
  • 17
    • 0031814992 scopus 로고    scopus 로고
    • Inhibiting geranylgeranylation blocks growth and promotes apoptosis in pulmonary vascular smooth muscle cells
    • W.W. Stark Jr., M.A. Blaskovich, B.A. Johnson, Y. Qian, A. Vasudevan, and B. Pitt Inhibiting geranylgeranylation blocks growth and promotes apoptosis in pulmonary vascular smooth muscle cells Am J Physiol 275 1 Pt 1 1998 L55 L63
    • (1998) Am J Physiol , vol.275 , Issue.1 PART 1
    • Stark Jr., W.W.1    Blaskovich, M.A.2    Johnson, B.A.3    Qian, Y.4    Vasudevan, A.5    Pitt, B.6
  • 18
    • 0035894057 scopus 로고    scopus 로고
    • Effect of S(-) perillic acid on protein prenylation and arterial smooth muscle cell proliferation
    • N. Ferri, L. Arnaboldi, A. Orlandi, K. Yokoyama, R. Gree, and A. Granata Effect of S(-) perillic acid on protein prenylation and arterial smooth muscle cell proliferation Biochem Pharmacol 62 12 2001 1637 1645
    • (2001) Biochem Pharmacol , vol.62 , Issue.12 , pp. 1637-1645
    • Ferri, N.1    Arnaboldi, L.2    Orlandi, A.3    Yokoyama, K.4    Gree, R.5    Granata, A.6
  • 19
    • 0037349211 scopus 로고    scopus 로고
    • Ajoene, a garlic compound, inhibits protein prenylation and arterial smooth muscle cell proliferation
    • N. Ferri, K. Yokoyama, M. Sadilek, R. Paoletti, R. Apitz-Castro, and M.H. Gelb Ajoene, a garlic compound, inhibits protein prenylation and arterial smooth muscle cell proliferation Br J Pharmacol 138 5 2003 811 818
    • (2003) Br J Pharmacol , vol.138 , Issue.5 , pp. 811-818
    • Ferri, N.1    Yokoyama, K.2    Sadilek, M.3    Paoletti, R.4    Apitz-Castro, R.5    Gelb, M.H.6
  • 20
    • 0037136025 scopus 로고    scopus 로고
    • Isothiazole dioxides: Synthesis and inhibition of Trypanosoma brucei protein farnesyltransferase
    • F. Clerici, M.L. Gelmi, K. Yokoyama, D. Pocar, W.C. Van Voorhis, and F.S. Buckner Isothiazole dioxides: synthesis and inhibition of Trypanosoma brucei protein farnesyltransferase Bioorg Med Chem Lett 12 16 2002 2217 2220
    • (2002) Bioorg Med Chem Lett , vol.12 , Issue.16 , pp. 2217-2220
    • Clerici, F.1    Gelmi, M.L.2    Yokoyama, K.3    Pocar, D.4    Van Voorhis, W.C.5    Buckner, F.S.6
  • 21
    • 0034698159 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and distinct substrate specificity of protein farnesyltransferase from Trypanosoma brucei
    • F.S. Buckner, K. Yokoyama, L. Nguyen, A. Grewal, H. Erdjument-Bromage, and P. Tempst Cloning, heterologous expression, and distinct substrate specificity of protein farnesyltransferase from Trypanosoma brucei J Biol Chem 275 29 2000 21870 21876
    • (2000) J Biol Chem , vol.275 , Issue.29 , pp. 21870-21876
    • Buckner, F.S.1    Yokoyama, K.2    Nguyen, L.3    Grewal, A.4    Erdjument-Bromage, H.5    Tempst, P.6
  • 22
    • 0033548013 scopus 로고    scopus 로고
    • Isothiazoles. Part IX. An efficient synthetic route to 5-substitute-3-amino-4-aryl-isothiazole 1,1-dioxides and their 4,5-dihydro derivatives
    • E.M. Beccalli, F. Clerici, and M.L. Gelmi Isothiazoles. Part IX. An efficient synthetic route to 5-substitute-3-amino-4-aryl-isothiazole 1,1-dioxides and their 4,5-dihydro derivatives Tetrahedron 55 1999 2001 2012
    • (1999) Tetrahedron , vol.55 , pp. 2001-2012
    • Beccalli, E.M.1    Clerici, F.2    Gelmi, M.L.3
  • 23
    • 0026549588 scopus 로고
    • N-sulfonylamidines. Part IV. Intramolecular cyclization of N-sulfonylamidines of 2-oxoacides: A new synthesis of 3-aminoisothiazoles S,S-dioxides
    • F. Clerici, G. Marazzi, and M. Taglietti N-sulfonylamidines. Part IV. Intramolecular cyclization of N-sulfonylamidines of 2-oxoacides: a new synthesis of 3-aminoisothiazoles S,S-dioxides Tetrahedron 48 1992 3227 3238
    • (1992) Tetrahedron , vol.48 , pp. 3227-3238
    • Clerici, F.1    Marazzi, G.2    Taglietti, M.3
  • 24
    • 0030783965 scopus 로고    scopus 로고
    • Isothiazoles. Part VII. An efficient palladium catalyzed functionalization of 3-amino-4-aryl-isothiazole 1,1-dioxides with organostannanes
    • F. Clerici, E. Erba, M.L. Gelmi, and M. Valle Isothiazoles. Part VII. An efficient palladium catalyzed functionalization of 3-amino-4-aryl-isothiazole 1,1-dioxides with organostannanes Tetrahedron 53 1997 15859 15866
    • (1997) Tetrahedron , vol.53 , pp. 15859-15866
    • Clerici, F.1    Erba, E.2    Gelmi, M.L.3    Valle, M.4
  • 25
    • 0032505225 scopus 로고    scopus 로고
    • Isothiazoles. Part VIII. Thermal rearrangement to a,b-unsaturated nitriles of cycloadducts from 3-diethylamino-4-(4-methoxyphenyl)-5-vinyl- isothiazole 1,1-dioxide with nitrile oxides and munchnones
    • F. Clerici, M.L. Gelmi, R. Soave, and M. Valle Isothiazoles. Part VIII. Thermal rearrangement to a,b-unsaturated nitriles of cycloadducts from 3-diethylamino-4-(4-methoxyphenyl)-5-vinyl-isothiazole 1,1-dioxide with nitrile oxides and munchnones Tetrahedron 54 1998 11285 11296
    • (1998) Tetrahedron , vol.54 , pp. 11285-11296
    • Clerici, F.1    Gelmi, M.L.2    Soave, R.3    Valle, M.4
  • 26
    • 0028925536 scopus 로고
    • Effects of 26-aminocholesterol, 27-hydroxycholesterol, and 25-hydroxycholesterol on proliferation and cholesterol homeostasis in arterial myocytes
    • A. Corsini, D. Verri, M. Raiteri, P. Quarato, R. Paoletti, and R. Fumagalli Effects of 26-aminocholesterol, 27-hydroxycholesterol, and 25-hydroxycholesterol on proliferation and cholesterol homeostasis in arterial myocytes Arterioscler Thromb Vasc Biol 15 3 1995 420 428
    • (1995) Arterioscler Thromb Vasc Biol , vol.15 , Issue.3 , pp. 420-428
    • Corsini, A.1    Verri, D.2    Raiteri, M.3    Quarato, P.4    Paoletti, R.5    Fumagalli, R.6
  • 27
    • 0027185879 scopus 로고
    • Relationship between mevalonate pathway and arterial myocyte proliferation: In vitro studies with inhibitors of HMG-CoA reductase
    • A. Corsini, M. Mazzotti, M. Raiteri, M.R. Soma, G. Gabbiani, and R. Fumagalli Relationship between mevalonate pathway and arterial myocyte proliferation: in vitro studies with inhibitors of HMG-CoA reductase Atherosclerosis 101 1 1993 117 125
    • (1993) Atherosclerosis , vol.101 , Issue.1 , pp. 117-125
    • Corsini, A.1    Mazzotti, M.2    Raiteri, M.3    Soma, M.R.4    Gabbiani, G.5    Fumagalli, R.6
  • 28
    • 0031055466 scopus 로고    scopus 로고
    • Differential prenyl pyrophosphate binding to mammalian protein geranylgeranyltransferase-I and protein farnesyltransferase and its consequence on the specificity of protein prenylation
    • K. Yokoyama, K. Zimmerman, J. Scholten, and M.H. Gelb Differential prenyl pyrophosphate binding to mammalian protein geranylgeranyltransferase-I and protein farnesyltransferase and its consequence on the specificity of protein prenylation J Biol Chem 272 7 1997 3944 3952
    • (1997) J Biol Chem , vol.272 , Issue.7 , pp. 3944-3952
    • Yokoyama, K.1    Zimmerman, K.2    Scholten, J.3    Gelb, M.H.4
  • 29
    • 0026001936 scopus 로고
    • A protein geranylgeranyltransferase from bovine brain: Implications for protein prenylation specificity
    • K. Yokoyama, G.W. Goodwin, F. Ghomashchi, J.A. Glomset, and M.H. Gelb A protein geranylgeranyltransferase from bovine brain: implications for protein prenylation specificity Proc Natl Acad Sci USA 88 12 1991 5302 5306
    • (1991) Proc Natl Acad Sci USA , vol.88 , Issue.12 , pp. 5302-5306
    • Yokoyama, K.1    Goodwin, G.W.2    Ghomashchi, F.3    Glomset, J.A.4    Gelb, M.H.5
  • 30
    • 0033963644 scopus 로고    scopus 로고
    • Inhibition of RAS-targeted prenylation: Protein farnesyl transferase inhibitors revisited
    • B.T. Hill, D. Perrin, and A. Kruczynski Inhibition of RAS-targeted prenylation: protein farnesyl transferase inhibitors revisited Crit Rev Oncol Hematol 33 1 2000 7 23
    • (2000) Crit Rev Oncol Hematol , vol.33 , Issue.1 , pp. 7-23
    • Hill, B.T.1    Perrin, D.2    Kruczynski, A.3
  • 31
    • 0033578751 scopus 로고    scopus 로고
    • A mutant form of human protein farnesyltransferase exhibits increased resistance to farnesyltransferase inhibitors
    • K. Del Villar, J. Urano, L. Guo, and F. Tamanoi A mutant form of human protein farnesyltransferase exhibits increased resistance to farnesyltransferase inhibitors J Biol Chem 274 38 1999 27010 27017
    • (1999) J Biol Chem , vol.274 , Issue.38 , pp. 27010-27017
    • Del Villar, K.1    Urano, J.2    Guo, L.3    Tamanoi, F.4
  • 32
    • 0029586503 scopus 로고
    • Novel tricyclic inhibitors of farnesyl protein transferase. Biochemical characterization and inhibition of Ras modification in transfected Cos cells
    • W.R. Bishop, R. Bond, J. Petrin, L. Wang, R. Patton, and R. Doll Novel tricyclic inhibitors of farnesyl protein transferase. Biochemical characterization and inhibition of Ras modification in transfected Cos cells J Biol Chem 270 51 1995 30611 30618
    • (1995) J Biol Chem , vol.270 , Issue.51 , pp. 30611-30618
    • Bishop, W.R.1    Bond, R.2    Petrin, J.3    Wang, L.4    Patton, R.5    Doll, R.6
  • 33
    • 0030749464 scopus 로고    scopus 로고
    • Inhibition of Ras prenylation: A novel approach to cancer chemotherapy
    • S.M. Sebti, and A.D. Hamilton Inhibition of Ras prenylation: a novel approach to cancer chemotherapy Pharmacol Ther 74 1 1997 103 114
    • (1997) Pharmacol Ther , vol.74 , Issue.1 , pp. 103-114
    • Sebti, S.M.1    Hamilton, A.D.2
  • 34
    • 0032493641 scopus 로고    scopus 로고
    • A farnesyl-protein transferase inhibitor induces p21 expression and G1 block in p53 wild type tumor cells
    • L. Sepp-Lorenzino, and N. Rosen A farnesyl-protein transferase inhibitor induces p21 expression and G1 block in p53 wild type tumor cells J Biol Chem 273 32 1998 20243 20251
    • (1998) J Biol Chem , vol.273 , Issue.32 , pp. 20243-20251
    • Sepp-Lorenzino, L.1    Rosen, N.2
  • 35
    • 15644376974 scopus 로고    scopus 로고
    • Pharmacological control of the mevalonate pathway: Effect on arterial smooth muscle cell proliferation
    • M. Raiteri, L. Arnaboldi, P. McGeady, M.H. Gelb, D. Verri, and C. Tagliabue Pharmacological control of the mevalonate pathway: effect on arterial smooth muscle cell proliferation J Pharmacol Exp Ther 281 3 1997 1144 1153
    • (1997) J Pharmacol Exp Ther , vol.281 , Issue.3 , pp. 1144-1153
    • Raiteri, M.1    Arnaboldi, L.2    McGeady, P.3    Gelb, M.H.4    Verri, D.5    Tagliabue, C.6
  • 36
    • 0032898892 scopus 로고    scopus 로고
    • Inhibition of human smooth muscle cell proliferation in culture by farnesyl pyrophosphate analogues, inhibitors of in vitro protein: Farnesyl transferase
    • L.H. Cohen, E. Pieterman, R.E. van Leeuwen, J. Du, P. Negre-Aminou, and A.R. Valentijn Inhibition of human smooth muscle cell proliferation in culture by farnesyl pyrophosphate analogues, inhibitors of in vitro protein: farnesyl transferase Biochem Pharmacol 57 4 1999 365 373
    • (1999) Biochem Pharmacol , vol.57 , Issue.4 , pp. 365-373
    • Cohen, L.H.1    Pieterman, E.2    Van Leeuwen, R.E.3    Du, J.4    Negre-Aminou, P.5    Valentijn, A.R.6
  • 37
    • 0029980255 scopus 로고    scopus 로고
    • Effect of the new HMG-CoA reductase inhibitor cerivastatin (BAY W 6228) on migration, proliferation and cholesterol synthesis in arterial myocytes
    • A. Corsini, L. Arnaboldi, M. Raiteri, P. Quarato, A. Faggiotto, and R. Paoletti Effect of the new HMG-CoA reductase inhibitor cerivastatin (BAY W 6228) on migration, proliferation and cholesterol synthesis in arterial myocytes Pharmacol Res 33 1 1996 55 61
    • (1996) Pharmacol Res , vol.33 , Issue.1 , pp. 55-61
    • Corsini, A.1    Arnaboldi, L.2    Raiteri, M.3    Quarato, P.4    Faggiotto, A.5    Paoletti, R.6
  • 38
    • 0037155865 scopus 로고    scopus 로고
    • Consequences of mevalonate depletion. Differential transcriptional, translational, and post-translational up-regulation of Ras, Rap1a, RhoA, and RhoB
    • S.A. Holstein, C.L. Wohlford-Lenane, and R.J. Hohl Consequences of mevalonate depletion. Differential transcriptional, translational, and post-translational up-regulation of Ras, Rap1a, RhoA, AND RhoB J Biol Chem 277 12 2002 10678 10682
    • (2002) J Biol Chem , vol.277 , Issue.12 , pp. 10678-10682
    • Holstein, S.A.1    Wohlford-Lenane, C.L.2    Hohl, R.J.3
  • 39
    • 0034811763 scopus 로고    scopus 로고
    • Dominant negative farnesyltransferase alpha-subunit inhibits insulin mitogenic effects
    • C.S. Solomon, and M.L. Goalstone Dominant negative farnesyltransferase alpha-subunit inhibits insulin mitogenic effects Biochem Biophys Res Commun 285 2 2001 161 166
    • (2001) Biochem Biophys Res Commun , vol.285 , Issue.2 , pp. 161-166
    • Solomon, C.S.1    Goalstone, M.L.2
  • 40
    • 0035949639 scopus 로고    scopus 로고
    • Short-term local delivery of an inhibitor of Ras farnesyltransferase prevents neointima formation in vivo after porcine coronary balloon angioplasty
    • L.M. Work, A.R. McPhaden, N.J. Pyne, S. Pyne, R.M. Wadsworth, and C.L. Wainwright Short-term local delivery of an inhibitor of Ras farnesyltransferase prevents neointima formation in vivo after porcine coronary balloon angioplasty Circulation 104 13 2001 1538 1543
    • (2001) Circulation , vol.104 , Issue.13 , pp. 1538-1543
    • Work, L.M.1    McPhaden, A.R.2    Pyne, N.J.3    Pyne, S.4    Wadsworth, R.M.5    Wainwright, C.L.6
  • 41
    • 0142211304 scopus 로고    scopus 로고
    • High affinity for farnesyltransferase and alternative prenylation contribute individually to K-Ras4B resistance to farnesyltransferase inhibitors
    • J.J. Fiordalisi, R.L. Johnson 2nd, C.A. Weinbaum, K. Sakabe, Z. Chen, and P.J. Casey High affinity for farnesyltransferase and alternative prenylation contribute individually to K-Ras4B resistance to farnesyltransferase inhibitors J Biol Chem 278 43 2003 41718 41727
    • (2003) J Biol Chem , vol.278 , Issue.43 , pp. 41718-41727
    • Fiordalisi, J.J.1    Johnson III, R.L.2    Weinbaum, C.A.3    Sakabe, K.4    Chen, Z.5    Casey, P.J.6
  • 42
    • 0036117985 scopus 로고    scopus 로고
    • Fluvastatin reduces tissue factor expression and macrophage accumulation in carotid lesions of cholesterol-fed rabbits in the absence of lipid lowering
    • R. Baetta, M. Camera, C. Comparato, C. Altana, M.D. Ezekowitz, and E. Tremoli Fluvastatin reduces tissue factor expression and macrophage accumulation in carotid lesions of cholesterol-fed rabbits in the absence of lipid lowering Arterioscler Thromb Vasc Biol 22 4 2002 692 698
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , Issue.4 , pp. 692-698
    • Baetta, R.1    Camera, M.2    Comparato, C.3    Altana, C.4    Ezekowitz, M.D.5    Tremoli, E.6
  • 43
    • 0034646238 scopus 로고    scopus 로고
    • Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state
    • C. Huang, K.E. Hightower, and C.A. Fierke Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state Biochemistry 39 10 2000 2593 2602
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2593-2602
    • Huang, C.1    Hightower, K.E.2    Fierke, C.A.3
  • 44
    • 0037057707 scopus 로고    scopus 로고
    • Reaction path of protein farnesyltransferase at atomic resolution
    • S.B. Long, P.J. Casey, and L.S. Beese Reaction path of protein farnesyltransferase at atomic resolution Nature 419 6907 2002 645 650
    • (2002) Nature , vol.419 , Issue.6907 , pp. 645-650
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 45
    • 0037143497 scopus 로고    scopus 로고
    • Modulation of the zinc(II) center in protein farnesyltransferase by mutagenesis of the zinc(II) ligands
    • C.M. Harris, A.M. Derdowski, and C.D. Poulter Modulation of the zinc(II) center in protein farnesyltransferase by mutagenesis of the zinc(II) ligands Biochemistry 41 33 2002 10554 10562
    • (2002) Biochemistry , vol.41 , Issue.33 , pp. 10554-10562
    • Harris, C.M.1    Derdowski, A.M.2    Poulter, C.D.3
  • 46
    • 12444283656 scopus 로고    scopus 로고
    • A novel metal-chelating inhibitor of protein farnesyltransferase
    • A. Hamasaki, H. Naka, F. Tamanoi, K. Umezawa, and M. Otsuka A novel metal-chelating inhibitor of protein farnesyltransferase Bioorg Med Chem Lett 13 9 2003 1523 1526
    • (2003) Bioorg Med Chem Lett , vol.13 , Issue.9 , pp. 1523-1526
    • Hamasaki, A.1    Naka, H.2    Tamanoi, F.3    Umezawa, K.4    Otsuka, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.