메뉴 건너뛰기




Volumn 4, Issue 3, 2013, Pages 476-492

Prenyltransferase inhibitors: Treating human ailments from cancer to parasitic infections

Author keywords

[No Author keywords available]

Indexed keywords

2 HYDROXY 2 PHOSPHONO 3 (3 PYRIDINYL)PROPANOIC ACID; 3 BENZYL 7 CYANO 2,3,4,5 TETRAHYDRO 1 (1H IMIDAZOL 4 YLMETHYL) 4 (2 THIENYLSULFONYL) 1H 1,4 BENZODIAZEPINE; BISPHOSPHONIC ACID DERIVATIVE; DIMETHYLALLYLTRANSFERASE; GGTI 2154; GGTI 2418; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; IMIDAZOLE DERIVATIVE; ISOPRENOID; ISOPRENOID DERIVATIVE; L 778123; LONAFARNIB; N [2 [2 (2 AMINO 3 MERCAPTOPROPYLAMINO) 3 METHYLPENTYLOXY] 3 PHENYLPROPIONYL]METHIONINE SULFONE; N [[5 [(2 AMINO 3 MERCAPTOPROPYL)AMINO][1,1' BIPHENYL] 2 YL]CARBONYL]METHIONINE; PRAVASTATIN; PRENYLTRANSFERASE INHIBITOR; RAS PROTEIN; RISEDRONIC ACID; SCH 211618; TIPIFARNIB; TRANSFERASE INHIBITOR; UNCLASSIFIED DRUG; ZOLEDRONIC ACID;

EID: 84874505210     PISSN: 20402503     EISSN: 20402511     Source Type: Journal    
DOI: 10.1039/c2md20299a     Document Type: Review
Times cited : (56)

References (146)
  • 2
    • 0025020641 scopus 로고
    • Identification of geranylgeranyl-modified proteins in HeLa cells
    • C. C. Farnsworth M. H. Gelb J. A. Glomset Identification of geranylgeranyl-modified proteins in HeLa cells Science 1990 247 320 322
    • (1990) Science , vol.247 , pp. 320-322
    • Farnsworth, C.C.1    Gelb, M.H.2    Glomset, J.A.3
  • 3
    • 33750730629 scopus 로고    scopus 로고
    • Protein prenylation: An (almost) comprehensive overview on discovery history, enzymology, and significance in physiology and disease
    • W. Benetka M. Koranda F. Eisenhaber Protein prenylation: an (almost) comprehensive overview on discovery history, enzymology, and significance in physiology and disease Monatsh. Chem. 2006 137 1241 1281
    • (2006) Monatsh. Chem. , vol.137 , pp. 1241-1281
    • Benetka, W.1    Koranda, M.2    Eisenhaber, F.3
  • 4
    • 0027050783 scopus 로고
    • Biochemistry of protein prenylation
    • P. J. Casey Biochemistry of protein prenylation J. Lipid Res. 1992 33 1731 1740
    • (1992) J. Lipid Res. , vol.33 , pp. 1731-1740
    • Casey, P.J.1
  • 5
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • S. Clarke Protein isoprenylation and methylation at carboxyl-terminal cysteine residues Annu. Rev. Biochem. 1992 61 355 386
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 355-386
    • Clarke, S.1
  • 6
    • 80054866000 scopus 로고    scopus 로고
    • Targeting protein prenylation for cancer therapy
    • N. Berndt A. D. Hamilton S. M. Sebti Targeting protein prenylation for cancer therapy Nat. Rev. Cancer 2011 11 775 791
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 775-791
    • Berndt, N.1    Hamilton, A.D.2    Sebti, S.M.3
  • 7
    • 70450224430 scopus 로고    scopus 로고
    • Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities
    • J. L. Hougland K. A. Hicks H. L. Hartman R. A. Kelly T. J. Watt C. A. Fierke Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities J. Mol. Biol. 2010 395 176 190
    • (2010) J. Mol. Biol. , vol.395 , pp. 176-190
    • Hougland, J.L.1    Hicks, K.A.2    Hartman, H.L.3    Kelly, R.A.4    Watt, T.J.5    Fierke, C.A.6
  • 10
    • 27744520682 scopus 로고    scopus 로고
    • Rab proteins, connecting transport and vesicle fusion
    • I. Jordens M. Marsman C. Kuijl J. Neefjes Rab proteins, connecting transport and vesicle fusion Traffic 2005 6 1070 1077
    • (2005) Traffic , vol.6 , pp. 1070-1077
    • Jordens, I.1    Marsman, M.2    Kuijl, C.3    Neefjes, J.4
  • 14
    • 0344874683 scopus 로고    scopus 로고
    • Structure of mammalian protein geranylgeranyltransferase type-I
    • J. S. Taylor T. S. Reid K. L. Terry P. J. Casey L. S. Beese Structure of mammalian protein geranylgeranyltransferase type-I EMBO J. 2003 22 5963 5974
    • (2003) EMBO J. , vol.22 , pp. 5963-5974
    • Taylor, J.S.1    Reid, T.S.2    Terry, K.L.3    Casey, P.J.4    Beese, L.S.5
  • 16
    • 0029127725 scopus 로고
    • Binding of prenylated and polybasic peptides to membranes: Affinities and intervesicle exchange
    • F. Ghomashchi X. Zhang L. Liu M. H. Gelb Binding of prenylated and polybasic peptides to membranes: affinities and intervesicle exchange Biochemistry 1995 34 11910 11918
    • (1995) Biochemistry , vol.34 , pp. 11910-11918
    • Ghomashchi, F.1    Zhang, X.2    Liu, L.3    Gelb, M.H.4
  • 17
    • 0031970317 scopus 로고    scopus 로고
    • Membrane association and targeting of prenylated Ras-like GTPases
    • M. C. Seabra Membrane association and targeting of prenylated Ras-like GTPases Cell. Signalling 1998 10 167 172
    • (1998) Cell. Signalling , vol.10 , pp. 167-172
    • Seabra, M.C.1
  • 19
    • 0037470819 scopus 로고    scopus 로고
    • Protein prenylation: A pivotal posttranslational process
    • R. Roskoski Jr Protein prenylation: a pivotal posttranslational process Biochem. Biophys. Res. Commun. 2003 303 1 7
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 1-7
    • Roskoski Jr., R.1
  • 22
    • 0030909826 scopus 로고    scopus 로고
    • Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution
    • H.-W. Park S. R. Boduluri J. F. Moomaw P. J. Casey L. S. Beese Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution Science 1997 275 1800 1805
    • (1997) Science , vol.275 , pp. 1800-1805
    • Park, H.-W.1    Boduluri, S.R.2    Moomaw, J.F.3    Casey, P.J.4    Beese, L.S.5
  • 23
    • 0031017064 scopus 로고    scopus 로고
    • 2+-farnesyltransferase indicates metal coordination of the substrate thiolate
    • 2+- farnesyltransferase indicates metal coordination of the substrate thiolate J. Biol. Chem. 1997 272 20 23
    • (1997) J. Biol. Chem. , vol.272 , pp. 20-23
    • Huang, C.-C.1    Casey, P.J.2    Fierke, C.A.3
  • 24
    • 0032847980 scopus 로고    scopus 로고
    • as of peptide substrates bound as zinc thiolates
    • as of peptide substrates bound as zinc thiolates Biochemistry 1999 38 13138 13146
    • (1999) Biochemistry , vol.38 , pp. 13138-13146
    • Rozema, D.B.1    Poulter, C.D.2
  • 25
    • 0035799332 scopus 로고    scopus 로고
    • Stereochemical analysis of the reaction catalyzed by human protein geranylgeranyl transferase
    • V. A. Clausen R. L. Edelstein M. D. Distefano Stereochemical analysis of the reaction catalyzed by human protein geranylgeranyl transferase Biochemistry 2001 40 3920 3930
    • (2001) Biochemistry , vol.40 , pp. 3920-3930
    • Clausen, V.A.1    Edelstein, R.L.2    Distefano, M.D.3
  • 26
    • 0000950803 scopus 로고    scopus 로고
    • Stereochemical analysis of the reaction catalyzed by yeast protein farnesyltransferase
    • R. L. Edelstein V. A. Weller M. D. Distefano J. S. Tung Stereochemical analysis of the reaction catalyzed by yeast protein farnesyltransferase J. Org. Chem. 1998 63 5298 5299
    • (1998) J. Org. Chem. , vol.63 , pp. 5298-5299
    • Edelstein, R.L.1    Weller, V.A.2    Distefano, M.D.3    Tung, J.S.4
  • 27
    • 0029007293 scopus 로고
    • A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase
    • J. M. Dolence C. D. Poulter A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase Proc. Natl. Acad. Sci. U. S. A. 1995 92 5008 5011
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 5008-5011
    • Dolence, J.M.1    Poulter, C.D.2
  • 28
    • 0029983874 scopus 로고    scopus 로고
    • On the stereochemical course of human protein-farnesyl transferase
    • Y. Mu C. A. Omer R. A. Gibbs On the stereochemical course of human protein-farnesyl transferase J. Am. Chem. Soc. 1996 118 1817 1823
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1817-1823
    • Mu, Y.1    Omer, C.A.2    Gibbs, R.A.3
  • 30
    • 33845210617 scopus 로고    scopus 로고
    • Measurement of the α-secondary kinetic isotope effect for the reaction catalyzed by mammalian protein farnesyltransferase
    • J. E. Pais K. E. Bowers C. A. Fierke Measurement of the α-secondary kinetic isotope effect for the reaction catalyzed by mammalian protein farnesyltransferase J. Am. Chem. Soc. 2006 128 15086 15087
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15086-15087
    • Pais, J.E.1    Bowers, K.E.2    Fierke, C.A.3
  • 31
    • 67650066252 scopus 로고    scopus 로고
    • Unraveling the catalytic pathway of metalloenzyme farnesyltransferase through QM/MM computation
    • M.-H. Ho V. M. De P. M. Dal M. L. Klein Unraveling the catalytic pathway of metalloenzyme farnesyltransferase through QM/MM computation J. Chem. Theory Comput. 2009 5 1657 1666
    • (2009) J. Chem. Theory Comput. , vol.5 , pp. 1657-1666
    • Ho, M.-H.1    De, V.M.2    Dal, P.M.3    Klein, M.L.4
  • 33
    • 84862908683 scopus 로고    scopus 로고
    • Insights into the mechanistic dichotomy of the protein farnesyltransferase peptide substrates CVIM and CVLS
    • Y. Yang B. Wang M. N. Ucisik G. Cui C. A. Fierke K. M. Merz Insights into the mechanistic dichotomy of the protein farnesyltransferase peptide substrates CVIM and CVLS J. Am. Chem. Soc. 2012 134 820 823
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 820-823
    • Yang, Y.1    Wang, B.2    Ucisik, M.N.3    Cui, G.4    Fierke, C.A.5    Merz, K.M.6
  • 34
    • 79960241386 scopus 로고    scopus 로고
    • Organization and function of the rab prenylation and recycling machinery
    • ed. C. A. H. Fuyuhiko Tamanoi and O. B. Martin, Academic Press
    • K. Alexandrov, Y. Wu, W. Blankenfeldt, H. Waldmann and R. S. Goody, Organization and function of the rab prenylation and recycling machinery, in Enzymes, ed., C. A. H. Fuyuhiko Tamanoi, and, O. B. Martin, Academic Press, 2011, vol. 29, pp. 147-162
    • (2011) Enzymes , vol.29 , pp. 147-162
    • Alexandrov, K.1    Wu, Y.2    Blankenfeldt, W.3    Waldmann, H.4    Goody, R.S.5
  • 37
    • 84864204194 scopus 로고    scopus 로고
    • Solid-phase synthesis of C-terminal peptide libraries for studying the specificity of enzymatic protein prenylation
    • Y.-C. Wang M. D. Distefano Solid-phase synthesis of C-terminal peptide libraries for studying the specificity of enzymatic protein prenylation Chem. Commun. 2012 48 8228 8230
    • (2012) Chem. Commun. , vol.48 , pp. 8228-8230
    • Wang, Y.-C.1    Distefano, M.D.2
  • 38
    • 0345269998 scopus 로고    scopus 로고
    • Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase
    • T. C. Turek-Etienne C. L. Strickland M. D. Distefano Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase Biochemistry 2003 42 3716 3724
    • (2003) Biochemistry , vol.42 , pp. 3716-3724
    • Turek-Etienne, T.C.1    Strickland, C.L.2    Distefano, M.D.3
  • 41
    • 0027213688 scopus 로고
    • Inhibitors of ras farnesyltransferases
    • F. Tamanoi Inhibitors of ras farnesyltransferases Trends Biochem. Sci. 1993 18 349 353
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 349-353
    • Tamanoi, F.1
  • 44
    • 0037137175 scopus 로고    scopus 로고
    • Isoprenoids influence expression of Ras and Ras-related proteins
    • S. A. Holstein C. L. Wohlford-Lenane R. J. Hohl Isoprenoids influence expression of Ras and Ras-related proteins Biochemistry 2002 41 13698 13704
    • (2002) Biochemistry , vol.41 , pp. 13698-13704
    • Holstein, S.A.1    Wohlford-Lenane, C.L.2    Hohl, R.J.3
  • 45
    • 0035988617 scopus 로고    scopus 로고
    • Structure based design of benzophenone-based non-thiol farnesyltransferase inhibitors
    • M. Schlitzer Structure based design of benzophenone-based non-thiol farnesyltransferase inhibitors Curr. Pharm. Des. 2002 8 1713 1722
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 1713-1722
    • Schlitzer, M.1
  • 49
    • 0037607008 scopus 로고    scopus 로고
    • Inhibitors of farnesyltransferase and geranylgeranyltransferase-I for antitumor therapy: Substrate-based design, conformational constraint and biological activity
    • C. J. Dinsmore I. M. Bell Inhibitors of farnesyltransferase and geranylgeranyltransferase-I for antitumor therapy: substrate-based design, conformational constraint and biological activity Curr. Top. Med. Chem. 2003 3 1075 1093
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 1075-1093
    • Dinsmore, C.J.1    Bell, I.M.2
  • 50
    • 0034820134 scopus 로고    scopus 로고
    • Non-peptidic prenyltransferase inhibitors: Diverse structural classes and surprising anti-cancer mechanisms
    • R. A. Gibbs T. J. Zahn J. S. Sebolt-Leopold Non-peptidic prenyltransferase inhibitors: diverse structural classes and surprising anti-cancer mechanisms Curr. Med. Chem. 2001 8 1437 1465
    • (2001) Curr. Med. Chem. , vol.8 , pp. 1437-1465
    • Gibbs, R.A.1    Zahn, T.J.2    Sebolt-Leopold, J.S.3
  • 52
    • 0028912593 scopus 로고
    • A non-peptide mimetic of Ras-CAAX: Selective inhibition of farnesyltransferase and Ras processing
    • A. Vogt Y. Qian M. A. Blaskovich R. D. Fossum A. D. Hamilton S. M. Sebti A non-peptide mimetic of Ras-CAAX: selective inhibition of farnesyltransferase and Ras processing J. Biol. Chem. 1995 270 660 664
    • (1995) J. Biol. Chem. , vol.270 , pp. 660-664
    • Vogt, A.1    Qian, Y.2    Blaskovich, M.A.3    Fossum, R.D.4    Hamilton, A.D.5    Sebti, S.M.6
  • 54
    • 0028973293 scopus 로고
    • Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complexes
    • E. C. Lerner Y. Qian M. A. Blaskovich R. D. Fossum A. Vogt J. Sun A. D. Cox C. J. Der A. D. Hamilton S. M. Sebti Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complexes J. Biol. Chem. 1995 270 26802 26806
    • (1995) J. Biol. Chem. , vol.270 , pp. 26802-26806
    • Lerner, E.C.1    Qian, Y.2    Blaskovich, M.A.3    Fossum, R.D.4    Vogt, A.5    Sun, J.6    Cox, A.D.7    Der, C.J.8    Hamilton, A.D.9    Sebti, S.M.10
  • 55
    • 0028810275 scopus 로고
    • Disruption of oncogenic K-Ras4B processing and signaling by a potent geranylgeranyltransferase i inhibitor
    • E. C. Lerner Y. Qian A. D. Hamilton S. M. Sebti Disruption of oncogenic K-Ras4B processing and signaling by a potent geranylgeranyltransferase I inhibitor J. Biol. Chem. 1995 270 26770 26773
    • (1995) J. Biol. Chem. , vol.270 , pp. 26770-26773
    • Lerner, E.C.1    Qian, Y.2    Hamilton, A.D.3    Sebti, S.M.4
  • 61
    • 0033214457 scopus 로고    scopus 로고
    • Antitumor efficacy of a novel class of non-thiol-containing peptidomimetic inhibitors of farnesyltransferase and geranylgeranyltransferase i
    • J. Sun M. A. Blaskovich D. Knowles Y. Qian J. Ohkanda R. D. Bailey A. D. Hamilton S. M. Sebti Antitumor efficacy of a novel class of non-thiol-containing peptidomimetic inhibitors of farnesyltransferase and geranylgeranyltransferase I Cancer Res. 1999 59 4919 4926
    • (1999) Cancer Res. , vol.59 , pp. 4919-4926
    • Sun, J.1    Blaskovich, M.A.2    Knowles, D.3    Qian, Y.4    Ohkanda, J.5    Bailey, R.D.6    Hamilton, A.D.7    Sebti, S.M.8
  • 62
  • 63
    • 44349178715 scopus 로고    scopus 로고
    • Inhibitors of protein geranylgeranyltransferase i and Rab geranylgeranyltransferase identified from a library of allenoate-derived compounds
    • M. Watanabe H. D. G. Fiji L. Guo L. Chan S. S. Kinderman D. J. Slamon O. Kwon F. Tamanoi Inhibitors of protein geranylgeranyltransferase I and Rab geranylgeranyltransferase identified from a library of allenoate-derived compounds J. Biol. Chem. 2008 283 9571 9579
    • (2008) J. Biol. Chem. , vol.283 , pp. 9571-9579
    • Watanabe, M.1    Fiji, H.D.G.2    Guo, L.3    Chan, L.4    Kinderman, S.S.5    Slamon, D.J.6    Kwon, O.7    Tamanoi, F.8
  • 65
    • 84866163433 scopus 로고    scopus 로고
    • Differential expression of Rab27A/B correlates with clinical outcome in hepatocellular carcinoma
    • W.-W. Dong Q. Mou J. Chen J.-T. Cui W.-M. Li W.-H. Xiao Differential expression of Rab27A/B correlates with clinical outcome in hepatocellular carcinoma World J. Gastroenterol. 2012 18 1806 1813
    • (2012) World J. Gastroenterol. , vol.18 , pp. 1806-1813
    • Dong, W.-W.1    Mou, Q.2    Chen, J.3    Cui, J.-T.4    Li, W.-M.5    Xiao, W.-H.6
  • 67
    • 0036727151 scopus 로고    scopus 로고
    • Bisphosphonate mechanism of action
    • G. A. Rodan A. A. Reszka Bisphosphonate mechanism of action Curr. Mol. Med. 2002 2 571 577
    • (2002) Curr. Mol. Med. , vol.2 , pp. 571-577
    • Rodan, G.A.1    Reszka, A.A.2
  • 69
    • 4344677917 scopus 로고    scopus 로고
    • Nitrogen-containing bisphosphonate mechanism of action
    • A. A. Reszka G. A. Rodan Nitrogen-containing bisphosphonate mechanism of action Mini-Rev. Med. Chem. 2004 4 711 719
    • (2004) Mini-Rev. Med. Chem. , vol.4 , pp. 711-719
    • Reszka, A.A.1    Rodan, G.A.2
  • 70
    • 23844443254 scopus 로고    scopus 로고
    • Phosphonocarboxylate inhibitors of Rab geranylgeranyl transferase disrupt the prenylation and membrane localization of Rab proteins in osteoclasts in vitro and in vivo
    • F. P. Coxon F. H. Ebetino E. H. Mules M. C. Seabra C. E. McKenna M. J. Rogers Phosphonocarboxylate inhibitors of Rab geranylgeranyl transferase disrupt the prenylation and membrane localization of Rab proteins in osteoclasts in vitro and in vivo Bone 2005 37 349 358
    • (2005) Bone , vol.37 , pp. 349-358
    • Coxon, F.P.1    Ebetino, F.H.2    Mules, E.H.3    Seabra, M.C.4    McKenna, C.E.5    Rogers, M.J.6
  • 71
    • 33646383590 scopus 로고    scopus 로고
    • Recent advances in understanding the mechanism of action of bisphosphonates
    • F. P. Coxon K. Thompson M. J. Rogers Recent advances in understanding the mechanism of action of bisphosphonates Curr. Opin. Pharmacol. 2006 6 307 312
    • (2006) Curr. Opin. Pharmacol. , vol.6 , pp. 307-312
    • Coxon, F.P.1    Thompson, K.2    Rogers, M.J.3
  • 75
    • 0024316475 scopus 로고
    • Genetic and pharmacological suppression of oncogenic mutations in ras genes of yeast and humans
    • W. R. Schafer R. Kim R. Sterne J. Thorner S. H. Kim J. Rine Genetic and pharmacological suppression of oncogenic mutations in ras genes of yeast and humans Science 1989 245 379 385
    • (1989) Science , vol.245 , pp. 379-385
    • Schafer, W.R.1    Kim, R.2    Sterne, R.3    Thorner, J.4    Kim, S.H.5    Rine, J.6
  • 76
    • 0024376173 scopus 로고
    • Ras oncogenes in human cancer: A review
    • J. L. Bos Ras oncogenes in human cancer: a review Cancer Res. 1989 49 4682 4689
    • (1989) Cancer Res. , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 77
    • 0025194466 scopus 로고
    • Inhibition of purified p21ras farnesylprotein transferase by Cys-AAX tetrapeptides
    • Y. Reiss J. L. Goldstein M. C. Seabra P. J. Casey M. S. Brown Inhibition of purified p21ras farnesylprotein transferase by Cys-AAX tetrapeptides Cell 1990 62 81 88
    • (1990) Cell , vol.62 , pp. 81-88
    • Reiss, Y.1    Goldstein, J.L.2    Seabra, M.C.3    Casey, P.J.4    Brown, M.S.5
  • 78
    • 0030952552 scopus 로고    scopus 로고
    • Inhibition of the prenylation of K-Ras, but not H- or N-Ras, is highly resistant to CAAX peptidomimetics and requires both a farnesyltransferase and a geranylgeranyltransferase i inhibitor in human tumor cell lines
    • E. C. Lerner T.-T. Zhang D. B. Knowles Y. Qian A. D. Hamilton S. M. Sebti Inhibition of the prenylation of K-Ras, but not H- or N-Ras, is highly resistant to CAAX peptidomimetics and requires both a farnesyltransferase and a geranylgeranyltransferase I inhibitor in human tumor cell lines Oncogene 1997 15 1283 1288
    • (1997) Oncogene , vol.15 , pp. 1283-1288
    • Lerner, E.C.1    Zhang, T.-T.2    Knowles, D.B.3    Qian, Y.4    Hamilton, A.D.5    Sebti, S.M.6
  • 79
    • 0030968859 scopus 로고    scopus 로고
    • Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo
    • C. A. Rowell J. J. Kowalczyk M. D. Lewis A. M. Garcia Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo J. Biol. Chem. 1997 272 14093 14097
    • (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
  • 80
    • 0032546264 scopus 로고    scopus 로고
    • Both farnesyltransferase and geranylgeranyltransferase i inhibitors are required for inhibition of oncogenic K-Ras prenylation but each alone is sufficient to suppress human tumor growth in nude mouse xenografts
    • J. Sun Y. Qian A. D. Hamilton S. M. Sebti Both farnesyltransferase and geranylgeranyltransferase I inhibitors are required for inhibition of oncogenic K-Ras prenylation but each alone is sufficient to suppress 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
  • 84
    • 0029586503 scopus 로고
    • Et al., 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 R. Doll G. Njoroge J. Catino J. Schwartz et al., Novel tricyclic inhibitors of farnesyl protein transferase. Biochemical characterization and inhibition of Ras modification in transfected Cos cells J. Biol. Chem. 1995 270 30611 30618
    • (1995) J. Biol. Chem. , vol.270 , pp. 30611-30618
    • Bishop, W.R.1    Bond, R.2    Petrin, J.3    Wang, L.4    Patton, R.5    Doll, R.6    Njoroge, G.7    Catino, J.8    Schwartz, J.9
  • 86
    • 0035282792 scopus 로고    scopus 로고
    • High-performance liquid chromatography/mass spectrometry characterization of Ki4B-Ras in PSN-1 cells treated with the prenyltransferase inhibitor L-778,123
    • C. A. Buser C. J. Dinsmore C. Fernandes I. Greenberg K. Hamilton S. D. Mosser E. S. Walsh T. M. Williams K. S. Koblan High-performance liquid chromatography/mass spectrometry characterization of Ki4B-Ras in PSN-1 cells treated with the prenyltransferase inhibitor L-778,123 Anal. Biochem. 2001 290 126 137
    • (2001) Anal. Biochem. , vol.290 , pp. 126-137
    • Buser, C.A.1    Dinsmore, C.J.2    Fernandes, C.3    Greenberg, I.4    Hamilton, K.5    Mosser, S.D.6    Walsh, E.S.7    Williams, T.M.8    Koblan, K.S.9
  • 87
    • 84874491385 scopus 로고    scopus 로고
    • Clinical trials using farnesyltransferase inhibitors, accessed July 2012
    • Clinical trials using farnesyltransferase inhibitors, http://www.clinicaltrials.gov, accessed July 2012
  • 88
    • 80054936061 scopus 로고    scopus 로고
    • Inhibition of Ras for cancer treatment: The search continues
    • A. T. Baines D. Xu C. J. Der Inhibition of Ras for cancer treatment: the search continues Future Med. Chem. 2011 3 1787 1808
    • (2011) Future Med. Chem. , vol.3 , pp. 1787-1808
    • Baines, A.T.1    Xu, D.2    Der, C.J.3
  • 90
    • 0028835253 scopus 로고
    • A peptidomimetic inhibitor of farnesylprotein transferase blocks the anchorage-dependent and -independent growth of human tumor cell lines
    • L. Sepp-Lorenzino Z. Ma E. Rands N. E. Kohl J. B. Gibbs A. Oliff N. Rosen A peptidomimetic inhibitor of farnesylprotein transferase blocks the anchorage-dependent and -independent growth of human tumor cell lines Cancer Res. 1995 55 5302 5309
    • (1995) Cancer Res. , vol.55 , pp. 5302-5309
    • Sepp-Lorenzino, L.1    Ma, Z.2    Rands, E.3    Kohl, N.E.4    Gibbs, J.B.5    Oliff, A.6    Rosen, N.7
  • 92
    • 78650092789 scopus 로고    scopus 로고
    • Alkynyl-farnesol reporters for detection of protein S-prenylation in cells
    • G. Charron L. K. Tsou W. Maguire J. S. Yount H. C. Hang Alkynyl-farnesol reporters for detection of protein S-prenylation in cells Mol. BioSyst. 2011 7 67 73
    • (2011) Mol. BioSyst. , vol.7 , pp. 67-73
    • Charron, G.1    Tsou, L.K.2    Maguire, W.3    Yount, J.S.4    Hang, H.C.5
  • 95
    • 77950666952 scopus 로고    scopus 로고
    • A tagging-via-substrate approach to detect the farnesylated proteome using two-dimensional electrophoresis coupled with Western blotting
    • F. O. Onono M. A. Morgan H. P. Spielmann D. A. Andres T. Subramanian A. Ganser C. W. M. Reuter A tagging-via-substrate approach to detect the farnesylated proteome using two-dimensional electrophoresis coupled with Western blotting Mol. Cell. Proteomics 2010 9 742 751
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 742-751
    • Onono, F.O.1    Morgan, M.A.2    Spielmann, H.P.3    Andres, D.A.4    Subramanian, T.5    Ganser, A.6    Reuter, C.W.M.7
  • 98
    • 81355146839 scopus 로고    scopus 로고
    • Lamin A, farnesylation and aging
    • S. Reddy L. Comai Lamin A, farnesylation and aging Exp. Cell Res. 2012 318 1 7
    • (2012) Exp. Cell Res. , vol.318 , pp. 1-7
    • Reddy, S.1    Comai, L.2
  • 99
    • 33845269544 scopus 로고    scopus 로고
    • Hutchinson-Gilford progeria syndrome: Review of the phenotype
    • R. C. M. Hennekam Hutchinson-Gilford progeria syndrome: review of the phenotype Am. J. Med. Genet., Part A 2006 140 2603 2624
    • (2006) Am. J. Med. Genet., Part A , vol.140 , pp. 2603-2624
    • Hennekam, R.C.M.1
  • 102
    • 77949498915 scopus 로고    scopus 로고
    • Prelamin A prenylation and the treatment of progeria
    • H. J. Worman Prelamin A prenylation and the treatment of progeria J. Lipid Res. 2010 51 223 225
    • (2010) J. Lipid Res. , vol.51 , pp. 223-225
    • Worman, H.J.1
  • 103
    • 79960219823 scopus 로고    scopus 로고
    • Farnesyl transferase inhibitors: From targeted cancer therapeutic to a potential treatment for progeria
    • W. R. Bishop, R. Doll and P. Kirschmeier, Farnesyl transferase inhibitors: from targeted cancer therapeutic to a potential treatment for progeria, in Enzymes, 2011, vol. 29, pp. 275-303
    • (2011) Enzymes , vol.29 , pp. 275-303
    • Bishop, W.R.1    Doll, R.2    Kirschmeier, P.3
  • 104
    • 68849119046 scopus 로고    scopus 로고
    • Laminopathies and the long strange trip from basic cell biology to therapy
    • H. J. Worman L. G. Fong A. Muchir S. G. Young Laminopathies and the long strange trip from basic cell biology to therapy J. Clin. Invest. 2009 119 1825 1836
    • (2009) J. Clin. Invest. , vol.119 , pp. 1825-1836
    • Worman, H.J.1    Fong, L.G.2    Muchir, A.3    Young, S.G.4
  • 106
    • 33645060977 scopus 로고    scopus 로고
    • A protein farnesyltransferase inhibitor ameliorates disease in a mouse model of Progeria
    • L. G. Fong D. Frost M. Meta X. Qiao S. H. Yang C. Coffinier S. G. Young A protein farnesyltransferase inhibitor ameliorates disease in a mouse model of Progeria Science 2006 311 1621 1623
    • (2006) Science , vol.311 , pp. 1621-1623
    • Fong, L.G.1    Frost, D.2    Meta, M.3    Qiao, X.4    Yang, S.H.5    Coffinier, C.6    Young, S.G.7
  • 109
    • 39049111972 scopus 로고    scopus 로고
    • Treatment with a farnesyltransferase inhibitor improves survival in mice with a Hutchinson-Gilford progeria syndrome mutation
    • S. H. Yang X. Qiao L. G. Fong S. G. Young Treatment with a farnesyltransferase inhibitor improves survival in mice with a Hutchinson-Gilford progeria syndrome mutation Biochim. Biophys. Acta 2008 1781 36 39
    • (2008) Biochim. Biophys. Acta , vol.1781 , pp. 36-39
    • Yang, S.H.1    Qiao, X.2    Fong, L.G.3    Young, S.G.4
  • 110
    • 77949527805 scopus 로고    scopus 로고
    • Assessing the efficacy of protein farnesyltransferase inhibitors in mouse models of progeria
    • S. H. Yang S. Y. Chang D. A. Andres H. P. Spielmann S. G. Young L. G. Fong Assessing the efficacy of protein farnesyltransferase inhibitors in mouse models of progeria J. Lipid Res. 2010 51 400 405
    • (2010) J. Lipid Res. , vol.51 , pp. 400-405
    • Yang, S.H.1    Chang, S.Y.2    Andres, D.A.3    Spielmann, H.P.4    Young, S.G.5    Fong, L.G.6
  • 114
    • 84874451612 scopus 로고    scopus 로고
    • Phase II trial of lonafarnib (a farnesyltransferase inhibitor) for progeria, accessed July 2012
    • Phase II trial of lonafarnib (a farnesyltransferase inhibitor) for progeria, http://www.clinicaltrials.gov, accessed July 2012
  • 116
    • 84874506571 scopus 로고    scopus 로고
    • Study of zoledronic acid, pravastatin, and lonafarnib for patients with progeria, accessed July 2012
    • Study of zoledronic acid, pravastatin, and lonafarnib for patients with progeria, http://www.clinicaltrials.gov, accessed July 2012
  • 117
    • 84857774169 scopus 로고    scopus 로고
    • Targeting protein kinases in the malaria parasite: Update of an antimalarial drug target
    • V. M. Zhang M. Chavchich N. C. Waters Targeting protein kinases in the malaria parasite: update of an antimalarial drug target Curr. Top. Med. Chem. 2012 12 456 472
    • (2012) Curr. Top. Med. Chem. , vol.12 , pp. 456-472
    • Zhang, V.M.1    Chavchich, M.2    Waters, N.C.3
  • 120
    • 0030581643 scopus 로고    scopus 로고
    • Characterisation of protein isoprenylation in procyclic form Trypanosoma brucei
    • H. Field I. Blench S. Croft M. C. Field Characterisation of protein isoprenylation in procyclic form Trypanosoma brucei Mol. Biochem. Parasitol. 1996 82 67 80
    • (1996) Mol. Biochem. Parasitol. , vol.82 , pp. 67-80
    • Field, H.1    Blench, I.2    Croft, S.3    Field, M.C.4
  • 121
    • 0034791773 scopus 로고    scopus 로고
    • Identification and characterisation of Toxoplasma gondii protein farnesyltransferase
    • M. Ibrahim N. Azzouz P. Gerold R. T. Schwarz Identification and characterisation of Toxoplasma gondii protein farnesyltransferase Int. J. Parasitol. 2001 31 1489 1497
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1489-1497
    • Ibrahim, M.1    Azzouz, N.2    Gerold, P.3    Schwarz, R.T.4
  • 122
    • 0346457089 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a protein farnesyltransferase from the enteric protozoan parasite Entamoeba histolytica
    • M. Kumagai A. Makioka T. Takeuchi T. Nozaki Molecular cloning and characterization of a protein farnesyltransferase from the enteric protozoan parasite Entamoeba histolytica J. Biol. Chem. 2004 279 2316 2323
    • (2004) J. Biol. Chem. , vol.279 , pp. 2316-2323
    • Kumagai, M.1    Makioka, A.2    Takeuchi, T.3    Nozaki, T.4
  • 127
  • 128
    • 51849137409 scopus 로고    scopus 로고
    • Potent, plasmodium-selective farnesyltransferase inhibitors that arrest the growth of malaria parasites: Structure-activity relationships of ethylenediamine-analogue scaffolds and homology model validation
    • S. Fletcher C. G. Cummings K. Rivas W. P. Katt C. Horney F. S. Buckner D. Chakrabarti S. M. Sebti M. H. Gelb V. W. C. Van A. D. Hamilton Potent, plasmodium-selective farnesyltransferase inhibitors that arrest the growth of malaria parasites: structure-activity relationships of ethylenediamine-analogue scaffolds and homology model validation J. Med. Chem. 2008 51 5176 5197
    • (2008) J. Med. Chem. , vol.51 , pp. 5176-5197
    • Fletcher, S.1    Cummings, C.G.2    Rivas, K.3    Katt, W.P.4    Horney, C.5    Buckner, F.S.6    Chakrabarti, D.7    Sebti, S.M.8    Gelb, M.H.9    Van, V.W.C.10    Hamilton, A.D.11
  • 129
    • 80053400607 scopus 로고    scopus 로고
    • Structures of Cryptococcus neoformans protein farnesyltransferase reveal strategies for developing inhibitors that target fungal pathogens
    • M. A. Hast C. B. Nichols S. M. Armstrong S. M. Kelly H. W. Hellinga J. A. Alspaugh L. S. Beese Structures of Cryptococcus neoformans protein farnesyltransferase reveal strategies for developing inhibitors that target fungal pathogens J. Biol. Chem. 2011 286 35149 35162
    • (2011) J. Biol. Chem. , vol.286 , pp. 35149-35162
    • Hast, M.A.1    Nichols, C.B.2    Armstrong, S.M.3    Kelly, S.M.4    Hellinga, H.W.5    Alspaugh, J.A.6    Beese, L.S.7
  • 132
    • 39149093700 scopus 로고    scopus 로고
    • 2-Oxotetrahydroquinoline-based antimalarials with high potency and metabolic stability
    • V. J. Bulbule K. Rivas C. L. M. J. Verlinde V. W. C. Van M. H. Gelb 2-Oxotetrahydroquinoline-based antimalarials with high potency and metabolic stability J. Med. Chem. 2008 51 384 387
    • (2008) J. Med. Chem. , vol.51 , pp. 384-387
    • Bulbule, V.J.1    Rivas, K.2    Verlinde, C.L.M.J.3    Van, V.W.C.4    Gelb, M.H.5
  • 134
    • 76449101336 scopus 로고    scopus 로고
    • Towards the synthesis of bisubstrate inhibitors of protein farnesyltransferase: Synthesis and biological evaluation of new farnesylpyrophosphate analogues
    • S. Duez L. Coudray E. Mouray P. Grellier J. Dubois Towards the synthesis of bisubstrate inhibitors of protein farnesyltransferase: synthesis and biological evaluation of new farnesylpyrophosphate analogues Bioorg. Med. Chem. 2010 18 543 556
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 543-556
    • Duez, S.1    Coudray, L.2    Mouray, E.3    Grellier, P.4    Dubois, J.5
  • 136
    • 84862227635 scopus 로고    scopus 로고
    • Intrinsically unstructured domain 3 of hepatitis C virus NS5A forms a fuzzy complex with VAPB-MSP domain which carries ALS-causing mutations
    • G. Gupta H. Qin J. Song Intrinsically unstructured domain 3 of hepatitis C virus NS5A forms a fuzzy complex with VAPB-MSP domain which carries ALS-causing mutations PLoS One 2012 7 e39261
    • (2012) PLoS One , vol.7 , pp. 39261
    • Gupta, G.1    Qin, H.2    Song, J.3
  • 138
    • 0346103657 scopus 로고    scopus 로고
    • Disruption of hepatitis C virus RNA replication through inhibition of host protein geranylgeranylation
    • J. Ye C. Wang R. Sumpter M. S. Brown J. L. Goldstein M. Gale Disruption of hepatitis C virus RNA replication through inhibition of host protein geranylgeranylation Proc. Natl. Acad. Sci. U. S. A. 2003 100 15865 15870
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 15865-15870
    • Ye, J.1    Wang, C.2    Sumpter, R.3    Brown, M.S.4    Goldstein, J.L.5    Gale, M.6
  • 140
    • 0029965270 scopus 로고    scopus 로고
    • The hepatitis delta virus large antigen is farnesylated both in vitro and in animal cells
    • J. C. Otto P. J. Casey The hepatitis delta virus large antigen is farnesylated both in vitro and in animal cells J. Biol. Chem. 1996 271 4569 4572
    • (1996) J. Biol. Chem. , vol.271 , pp. 4569-4572
    • Otto, J.C.1    Casey, P.J.2
  • 142
    • 0031664153 scopus 로고    scopus 로고
    • Use of a prenylation inhibitor as a novel antiviral agent
    • J. S. Glenn J. C. Marsters, Jr H. B. Greenberg Use of a prenylation inhibitor as a novel antiviral agent J. Virol. 1998 72 9303 9306
    • (1998) J. Virol. , vol.72 , pp. 9303-9306
    • Glenn, J.S.1    Marsters Jr., J.C.2    Greenberg, H.B.3
  • 143
    • 0037090093 scopus 로고    scopus 로고
    • Inhibition of Rho GTPases with protein prenyltransferase inhibitors prevents leukocyte recruitment to the central nervous system and attenuates clinical signs of disease in an animal model of multiple sclerosis
    • C. E. Walters G. Pryce D. J. R. Hankey S. M. Sebti A. D. Hamilton D. Baker J. Greenwood P. Adamson Inhibition of Rho GTPases with protein prenyltransferase inhibitors prevents leukocyte recruitment to the central nervous system and attenuates clinical signs of disease in an animal model of multiple sclerosis J. Immunol. 2002 168 4087 4094
    • (2002) J. Immunol. , vol.168 , pp. 4087-4094
    • Walters, C.E.1    Pryce, G.2    Hankey, D.J.R.3    Sebti, S.M.4    Hamilton, A.D.5    Baker, D.6    Greenwood, J.7    Adamson, P.8
  • 144
    • 0033930168 scopus 로고    scopus 로고
    • Protein geranylgeranylation is required for osteoclast formation, function, and survival: Inhibition by bisphosphonates and GGTI-298
    • F. P. Coxon M. H. Helfrich H. R. Van't S. Sebti S. H. Ralston A. Hamilton M. J. Rogers Protein geranylgeranylation is required for osteoclast formation, function, and survival: Inhibition by bisphosphonates and GGTI-298 J. Bone Miner. Res. 2000 15 1467 1476
    • (2000) J. Bone Miner. Res. , vol.15 , pp. 1467-1476
    • Coxon, F.P.1    Helfrich, M.H.2    Van'T, H.R.3    Sebti, S.4    Ralston, S.H.5    Hamilton, A.6    Rogers, M.J.7
  • 145
    • 3142752754 scopus 로고    scopus 로고
    • The RAM1 gene encoding a protein-farnesyltransferase α-subunit homologue is essential in Cryptococcus neoformans
    • M. A. Vallim L. Fernandes J. A. Alspaugh The RAM1 gene encoding a protein-farnesyltransferase α-subunit homologue is essential in Cryptococcus neoformans Microbiology 2004 150 1925 1935
    • (2004) Microbiology , vol.150 , pp. 1925-1935
    • Vallim, M.A.1    Fernandes, L.2    Alspaugh, J.A.3
  • 146
    • 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 C. L. Wainwright Short-term local delivery of an inhibitor of Ras farnesyltransferase prevents neointima formation in vivo after porcine coronary balloon angioplasty Circulation 2001 104 1538 1543
    • (2001) Circulation , vol.104 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.