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Volumn 47, Issue 1, 2006, Pages 15-31

Farnesyl transferase inhibitors

Author keywords

BMS 214662; CENP; HDJ; Iamin; Ionafarnib; L 778123; Ras; Rheb; RhoB; Tipifarnib

Indexed keywords

3 BENZYL 7 CYANO 2,3,4,5 TETRAHYDRO 1 (1H IMIDAZOL 4 YLMETHYL) 4 (2 THIENYLSULFONYL) 1H 1,4 BENZODIAZEPINE; L 778123; LONAFARNIB; PROTEIN FARNESYLTRANSFERASE INHIBITOR; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; RAS PROTEIN; RHOB GUANINE NUCLEOTIDE BINDING PROTEIN; TIPIFARNIB; ANTINEOPLASTIC AGENT; ENZYME INHIBITOR; FARNESYL TRANS TRANSFERASE;

EID: 30844467746     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.R500012-JLR200     Document Type: Review
Times cited : (276)

References (220)
  • 1
  • 2
    • 0026001936 scopus 로고
    • A protein geranylgeranyltransferase from bovine brain: Implications for protein prenylation specificity
    • Yokoyama, K., G. W. Goodwin, F. Ghomashchi, J. A. Glomset, and M. H. Gelb. 1991. A protein geranylgeranyltransferase from bovine brain: implications for protein prenylation specificity. Proc. Natl. Acad. Sci. USA. 88: 5302-5306.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5302-5306
    • Yokoyama, K.1    Goodwin, G.W.2    Ghomashchi, F.3    Glomset, J.A.4    Gelb, M.H.5
  • 4
    • 0023917971 scopus 로고    scopus 로고
    • Evidence for modification of lamin B by a product of mevalonic acid
    • Wolda, S. L., and J. A. Glomset. 1998. Evidence for modification of laminBby a product of mevalonic acid. J. Biol. Chem. 263: 5997-6000.
    • (1998) J. Biol. Chem. , vol.263 , pp. 5997-6000
    • Wolda, S.L.1    Glomset, J.A.2
  • 5
    • 0026686468 scopus 로고
    • Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae
    • Caplan, A. J., J. Tsai, P. J. Casey, and M. G. Douglas. 1992. Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae. J. Biol. Chem. 267: 18890-18895.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18890-18895
    • Caplan, A.J.1    Tsai, J.2    Casey, P.J.3    Douglas, M.G.4
  • 6
    • 0037195808 scopus 로고    scopus 로고
    • The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis
    • Wang, J., C. E. Kirby, and R. Herbst. 2002. The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis. J. Biol. Chem. 277: 46659-46668.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46659-46668
    • Wang, J.1    Kirby, C.E.2    Herbst, R.3
  • 7
    • 0026640530 scopus 로고
    • Post-translational modifications of p21rho proteins
    • Adamson, P., C. J. Marshall, A. Hall, and P. A. Tilbrook. 1992. Post-translational modifications of p21rho proteins. J. Biol. Chem. 267: 20033-20038.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20033-20038
    • Adamson, P.1    Marshall, C.J.2    Hall, A.3    Tilbrook, P.A.4
  • 8
    • 0030888163 scopus 로고    scopus 로고
    • The Ras-related protein Rheb is farnesylated and antagonizes Ras signaling and transformation
    • Clark, G. J., M. S. Kinch, K. Rogers-Graham, S. M. Sebti, A. D. Hamilton, and C. J. Der. 1997. The Ras-related protein Rheb is farnesylated and antagonizes Ras signaling and transformation. J. Biol. Chem. 272: 10608-10615.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10608-10615
    • Clark, G.J.1    Kinch, M.S.2    Rogers-Graham, K.3    Sebti, S.M.4    Hamilton, A.D.5    Der, C.J.6
  • 9
    • 0034730625 scopus 로고    scopus 로고
    • Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules
    • Ashar, H. R., L. James, K. Gray, D. Carr, S. Black, L. Armstrong, W. R. Bishop, and P. Kirschmeier. 2000. Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules. J. Biol. Chem. 275: 30451-30457.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30451-30457
    • Ashar, H.R.1    James, L.2    Gray, K.3    Carr, D.4    Black, S.5    Armstrong, L.6    Bishop, W.R.7    Kirschmeier, P.8
  • 10
    • 0030051303 scopus 로고    scopus 로고
    • Mechanism of digeranylgeranylation of Rab proteins. Formation of a complex between monogeranylgeranyl-Rab and Rab escort protein
    • Shen, F., and M. Seabra. 1996. Mechanism of digeranylgeranylation of Rab proteins. Formation of a complex between monogeranylgeranyl-Rab and Rab escort protein. J. Biol. Chem. 271: 3692-3698.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3692-3698
    • Shen, F.1    Seabra, M.2
  • 11
    • 0025819073 scopus 로고
    • Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit
    • Seabra, M. C., Y. Reiss, P. J. Casey, M. S. Brown, and J. L. Goldstein. 1991. Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit. Cell. 65: 429-434.
    • (1991) Cell , vol.65 , pp. 429-434
    • Seabra, M.C.1    Reiss, Y.2    Casey, P.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 12
    • 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. 272: 20-23.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20-23
    • Huang, C.C.1    Casey, P.J.2    Fierke, C.A.3
  • 13
    • 0029007105 scopus 로고
    • Protein farnesyltransferase: Kinetics of farnesyl pyrophosphate binding and product release
    • Furfine, E. S., J. J. Leban, A. Landavazo, J. F. Moomaw, and P. J. Casey. 1995. Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. Biochemistry. 34: 6857-6862.
    • (1995) Biochemistry , vol.34 , pp. 6857-6862
    • Furfine, E.S.1    Leban, J.J.2    Landavazo, A.3    Moomaw, J.F.4    Casey, P.J.5
  • 14
    • 3142781361 scopus 로고    scopus 로고
    • Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes
    • Reid, T. S., S. B. Long, and L. S. Beese. 2004. Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes. Biochemistry. 43: 9000-9008.
    • (2004) Biochemistry , vol.43 , pp. 9000-9008
    • Reid, T.S.1    Long, S.B.2    Beese, L.S.3
  • 15
    • 4644370323 scopus 로고    scopus 로고
    • Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity
    • Reid, T. S., K. L. Terry, P. J. Casey, and L. S. Beese. 2004. Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. J. Mol. Biol. 343: 417-433.
    • (2004) J. Mol. Biol. , vol.343 , pp. 417-433
    • Reid, T.S.1    Terry, K.L.2    Casey, P.J.3    Beese, L.S.4
  • 16
    • 0035818587 scopus 로고    scopus 로고
    • The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics
    • Long, S. B., P. J. Hancock, A. M. Kral, H. W. Hellinga, and L. S. Beese. 2001. The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. Proc. Natl. Acad. Sci. USA. 98: 12948-12953.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12948-12953
    • Long, S.B.1    Hancock, P.J.2    Kral, A.M.3    Hellinga, H.W.4    Beese, L.S.5
  • 18
    • 0032493317 scopus 로고    scopus 로고
    • Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate
    • Long, S. B., P. J. Casey, and L. S. Beese. 1998. Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. Biochemistry. 37: 9612-9618.
    • (1998) Biochemistry , vol.37 , pp. 9612-9618
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 19
    • 0024376173 scopus 로고
    • ras oncogenes in human cancer: A review
    • Bos, J. L. 1989. ras oncogenes in human cancer: a review. Cancer Res. 49: 4682-4689.
    • (1989) Cancer Res. , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 20
    • 0025194466 scopus 로고
    • Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides
    • Reiss, Y., J. L. Goldstein, M. C. Seabra, P. J. Casey, and M. S. Brown. 1990. Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides. Cell. 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
  • 21
    • 0026667497 scopus 로고
    • Tetrapeptide inhibitors of protein farnesyltransferase: Amino-terminal substitution in phenylalanine-containing tetrapeptides restores farnesylation
    • Brown, M. S., J. L. Goldstein, K. J. Paris, J. P. Burnier, and J. C. Marsters, Jr. 1992. Tetrapeptide inhibitors of protein farnesyltransferase: amino-terminal substitution in phenylalanine-containing tetrapeptides restores farnesylation. Proc. Natl. Acad. Sci. USA. 89: 8313-8316.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8313-8316
    • Brown, M.S.1    Goldstein, J.L.2    Paris, K.J.3    Burnier, J.P.4    Marsters Jr., J.C.5
  • 22
  • 24
    • 0028352281 scopus 로고
    • Design and structural requirements of potent peptidomimetic inhibitors of p21ras farnesyltransferase
    • Qian, Y., M. A. Blaskovich, M. Saleem, C. M. Seong, S. P. Wathen, A. D. Hamilton, and S. M. Sebti. 1994. Design and structural requirements of potent peptidomimetic inhibitors of p21ras farnesyltransferase. J. Biol. Chem. 269: 12410-12413.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12410-12413
    • Qian, Y.1    Blaskovich, M.A.2    Saleem, M.3    Seong, C.M.4    Wathen, S.P.5    Hamilton, A.D.6    Sebti, S.M.7
  • 25
    • 0028912593 scopus 로고
    • A non-peptide mimetic of Ras-CAAX: Selective inhibition of farnesyltransferase and Ras processing
    • Vogt, A., Y. Qian, M. A. Blaskovich, R. D. Fossum, A. D. Hamilton, and S. M. Sebti. 1995. A non-peptide mimetic of Ras-CAAX: selective inhibition of farnesyltransferase and Ras processing. J. Biol. Chem. 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
  • 26
    • 0027522046 scopus 로고
    • Potent inhibition of human tumor p21ras farnesyltransferase by A1A2-lacking p21ras CA1A2X peptidomimetics
    • Nigam, M., C. M. Seong, Y. Qian, A. D. Hamilton, and S. M. Sebti. 1993. Potent inhibition of human tumor p21ras farnesyltransferase by A1A2-lacking p21ras CA1A2X peptidomimetics. J. Biol. Chem. 268: 20695-20698.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20695-20698
    • Nigam, M.1    Seong, C.M.2    Qian, Y.3    Hamilton, A.D.4    Sebti, S.M.5
  • 30
    • 0029586503 scopus 로고
    • Novel tricyclic inhibitors of farnesyl protein transferase. Biochemical characterization and inhibition of Ras modification in transfected Cos cells
    • Bishop, W. R., R. Bond, J. Petrin, L. Wang, R. Patton, R. Doll, G. Njoroge, J. Catino, J. Schwartz, W. Windsor, et al. 1995. Novel tricyclic inhibitors of farnesyl protein transferase. Biochemical characterization and inhibition of Ras modification in transfected Cos cells. J. Biol. Chem. 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    Windsor, W.10
  • 31
    • 7844233665 scopus 로고    scopus 로고
    • (1)-4-[2-[4-(8-Chloro-3,10-dibromo-6,11-dihydro-5H-benzo[5, 6]cyclohepta[1,2-b]- pyridin-11(R)-yl)-1-piperidinyl]-2-oxo-ethyl]-1- piperidinecarboxamide (SCH-66336): A very potent farnesyl protein transferase inhibitor as a novel antitumor agent
    • Njoroge, F. G., A. G. Taveras, J. Kelly, S. Remiszewski, A. K. Mallams, R. Wolin, A. Afonso, A. B. Cooper, D. F. Rane, Y. T. Liu, et al. 1998. (1)-4-[2-[4-(8-Chloro-3,10-dibromo-6,11-dihydro-5H-benzo[5, 6]cyclohepta[1,2-b]- pyridin-11(R)-yl)-1-piperidinyl]-2-oxo-ethyl]-1-piperidinecarboxamide (SCH-66336): a very potent farnesyl protein transferase inhibitor as a novel antitumor agent. J. Med. Chem. 41: 4890-4902.
    • (1998) J. Med. Chem. , vol.41 , pp. 4890-4902
    • Njoroge, F.G.1    Taveras, A.G.2    Kelly, J.3    Remiszewski, S.4    Mallams, A.K.5    Wolin, R.6    Afonso, A.7    Cooper, A.B.8    Rane, D.F.9    Liu, Y.T.10
  • 32
    • 0035132538 scopus 로고    scopus 로고
    • Characterization of the antitumor effects of the selective farnesyl protein transferase inhibitor R115777 in vivo and in vitro
    • End, D. W., G. Smets, A. V. Todd, T. L. Applegate, C. J. Fuery, P. Angibaud, M. Venet, G. Sanz, H. Poignet, S. Skrzat, et al. 2001. Characterization of the antitumor effects of the selective farnesyl protein transferase inhibitor R115777 in vivo and in vitro. Cancer Res. 61: 131-137.
    • (2001) Cancer Res. , vol.61 , pp. 131-137
    • End, D.W.1    Smets, G.2    Todd, A.V.3    Applegate, T.L.4    Fuery, C.J.5    Angibaud, P.6    Venet, M.7    Sanz, G.8    Poignet, H.9    Skrzat, S.10
  • 33
    • 0034609805 scopus 로고    scopus 로고
    • Discovery of (R)-7-cyano-2,3,4,5-tetrahydro-1-(1H-imidazol-4-ylmethyl)-3- (phenylmethyl)-4-(2-thienylsulfonyl)-1H-1,4-benzodiazepine (BMS-214662), a farnesyltransferase inhibitor with potent preclinical antitumor activity
    • Hunt, J. T., C. Z. Ding, R. Batorsky, M. Bednarz, R. Bhide, Y. Cho, S. Chong, S. Chao, J. Gullo-Brown, P. Guo, et al. 2000. Discovery of (R)-7-cyano-2,3,4,5-tetrahydro-1-(1H-imidazol-4-ylmethyl)-3-(phenylmethyl) -4-(2-thienylsulfonyl)-1H-1,4-benzodiazepine (BMS-214662), a farnesyltransferase inhibitor with potent preclinical antitumor activity. J. Med. Chem. 43: 3587-3595.
    • (2000) J. Med. Chem. , vol.43 , pp. 3587-3595
    • Hunt, J.T.1    Ding, C.Z.2    Batorsky, R.3    Bednarz, M.4    Bhide, R.5    Cho, Y.6    Chong, S.7    Chao, S.8    Gullo-Brown, J.9    Guo, P.10
  • 35
    • 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
    • Buser, C. A., C. J. Dinsmore, C. Fernandes, I. Greenberg, K. Hamilton, S. D. Mosser, E. S. Walsh, T. M. Williams, and K. S. Koblan. 2001. High-performance liquid chromatography/mass spectrometry characterization of Ki4B-Ras in PSN-1 cells treated with the prenyltransferase inhibitor L-778,123. Anal. Biochem. 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
  • 36
    • 0021970413 scopus 로고
    • Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells
    • Mulcahy, L. S., M. R. Smith, and D. W. Stacey. 1985. Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells. Nature. 313: 241-243.
    • (1985) Nature , vol.313 , pp. 241-243
    • Mulcahy, L.S.1    Smith, M.R.2    Stacey, D.W.3
  • 37
    • 0026336517 scopus 로고
    • Dominant inhibitory Ras mutants demonstrate the requirement for Ras activity in the action of tyrosine kinase oncogenes
    • Stacey, D. W., M. Roudebush, R. Day, S. D. Mosser, J. B. Gibbs, and L. A. Feig. 1991. Dominant inhibitory Ras mutants demonstrate the requirement for Ras activity in the action of tyrosine kinase oncogenes. Oncogene. 6: 2297-2304.
    • (1991) Oncogene , vol.6 , pp. 2297-2304
    • Stacey, D.W.1    Roudebush, M.2    Day, R.3    Mosser, S.D.4    Gibbs, J.B.5    Feig, L.A.6
  • 38
    • 0027905014 scopus 로고
    • Altered growth of human colon cancer cell lines disrupted at activated Ki-ras
    • Shirasawa, S., M. Furuse, N. Yokoyama, and T. Sasazuki. 1993. Altered growth of human colon cancer cell lines disrupted at activated Ki-ras. Science. 260: 85-88.
    • (1993) Science , vol.260 , pp. 85-88
    • Shirasawa, S.1    Furuse, M.2    Yokoyama, N.3    Sasazuki, T.4
  • 39
    • 0027910431 scopus 로고
    • Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
    • Egan, S. E., B. W. Giddings, M. W. Brooks, L. Buday, A. M. Sizeland, and R. A. Weinberg. 1993. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature. 363: 45-51.
    • (1993) Nature , vol.363 , pp. 45-51
    • Egan, S.E.1    Giddings, B.W.2    Brooks, M.W.3    Buday, L.4    Sizeland, A.M.5    Weinberg, R.A.6
  • 41
    • 0028241533 scopus 로고
    • Activation of Raf as a result of recruitment to the plasma membrane
    • Stokoe, D., S. G. Macdonald, K. Cadwallader, M. Symons, and J. F. Hancock. 1994. Activation of Raf as a result of recruitment to the plasma membrane. Science. 264: 1463-1467.
    • (1994) Science , vol.264 , pp. 1463-1467
    • Stokoe, D.1    Macdonald, S.G.2    Cadwallader, K.3    Symons, M.4    Hancock, J.F.5
  • 42
    • 0028272507 scopus 로고
    • Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
    • Leevers, S. J., H. F. Paterson, and C. J. Marshall. 1994. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature. 369: 411-414.
    • (1994) Nature , vol.369 , pp. 411-414
    • Leevers, S.J.1    Paterson, H.F.2    Marshall, C.J.3
  • 43
    • 0026743949 scopus 로고
    • Purification of a murine protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product: Relationship to the fission yeast byr1 gene product
    • Crews, C. M., and R. L. Erikson. 1992. Purification of a murine protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product: relationship to the fission yeast byr1 gene product. Proc. Natl. Acad. Sci. USA. 89: 8205-8209.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8205-8209
    • Crews, C.M.1    Erikson, R.L.2
  • 44
    • 0027237273 scopus 로고
    • A dominant-negative mutant of raf blocks mitogen-activated protein kinase activation by growth factors and oncogenic p21ras
    • Schaap, D., J. van der Wal, L. R. Howe, C. J. Marshall, and W. J. van Blitterswijk. 1993. A dominant-negative mutant of raf blocks mitogen-activated protein kinase activation by growth factors and oncogenic p21ras. J. Biol. Chem. 268: 20232-20236.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20232-20236
    • Schaap, D.1    Van Der Wal, J.2    Howe, L.R.3    Marshall, C.J.4    Van Blitterswijk, W.J.5
  • 45
    • 0027297647 scopus 로고
    • The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain
    • Marais, R., J. Wynne, and R. Treisman. 1993. The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain. Cell. 73: 381-393.
    • (1993) Cell , vol.73 , pp. 381-393
    • Marais, R.1    Wynne, J.2    Treisman, R.3
  • 46
    • 0030022174 scopus 로고    scopus 로고
    • Ral-GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation
    • Urano, T., R. Emkey, and L. A. Feig. 1996. Ral-GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation. EMBO J. 15: 810-816.
    • (1996) EMBO J. , vol.15 , pp. 810-816
    • Urano, T.1    Emkey, R.2    Feig, L.A.3
  • 47
  • 48
    • 0024465343 scopus 로고
    • Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis
    • Gutierrez, L., A. I. Magee, C. J. Marshall, and J. F. Hancock. 1989. Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis. EMBO J. 8: 1093-1098.
    • (1989) EMBO J. , vol.8 , pp. 1093-1098
    • Gutierrez, L.1    Magee, A.I.2    Marshall, C.J.3    Hancock, J.F.4
  • 49
  • 50
    • 0028196986 scopus 로고
    • Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers
    • Silvius, J. R., and F. l'Heureux. 1994. Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers. Biochemistry. 33: 3014-3022.
    • (1994) Biochemistry , vol.33 , pp. 3014-3022
    • Silvius, J.R.1    L'Heureux, F.2
  • 51
    • 0026021456 scopus 로고
    • Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B)
    • Hancock, J. F., K. Cadwallader, and C. J. Marshall. 1991. Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B). EMBO J. 10: 641-646.
    • (1991) EMBO J. , vol.10 , pp. 641-646
    • Hancock, J.F.1    Cadwallader, K.2    Marshall, C.J.3
  • 53
    • 0034625181 scopus 로고    scopus 로고
    • Targeted inactivation of the isoprenylcysteine carboxyl methyltransferase gene causes mislocalization of K-Ras in mammalian cells
    • Bergo, M. O., G. K. Leung, P. Ambroziak, J. C. Otto, P. J. Casey, and S. G. Young. 2000. Targeted inactivation of the isoprenylcysteine carboxyl methyltransferase gene causes mislocalization of K-Ras in mammalian cells. J. Biol. Chem. 275: 17605-17610.
    • (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
  • 54
    • 15044352445 scopus 로고    scopus 로고
    • Fatty acylation and prenylation of proteins: What's hot in fat
    • Magee, T., and M. C. Seabra. 2005. Fatty acylation and prenylation of proteins: what's hot in fat. Curr. Opin. Cell Biol. 17: 190-196.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 190-196
    • Magee, T.1    Seabra, M.C.2
  • 55
    • 0028958919 scopus 로고
    • Polylysine and CVIM sequences of K-RasB dictate specificity of prenylation and confer resistance to benzodiazepine peptidomimetic in vitro
    • James, G. L., J. L. Goldstein, and M. S. Brown. 1995. Polylysine and CVIM sequences of K-RasB dictate specificity of prenylation and confer resistance to benzodiazepine peptidomimetic in vitro. J. Biol. Chem. 270: 6221-6226.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6221-6226
    • James, G.L.1    Goldstein, J.L.2    Brown, M.S.3
  • 56
    • 0030943198 scopus 로고    scopus 로고
    • Characterization of Ha-ras, N-ras, Ki-Ras4A, and Ki-Ras4B as in vitro substrates for farnesyl protein transferase and geranylgeranyl protein transferase type I
    • Zhang, F. L., P. Kirschmeier, D. Carr, L. James, R. W. Bond, L. Wang, R. Patton, W. T. Windsor, R. Syto, R. Zhang, et al. 1997. Characterization of Ha-ras, N-ras, Ki-Ras4A, and Ki-Ras4B as in vitro substrates for farnesyl protein transferase and geranylgeranyl protein transferase type I. J. Biol. Chem. 272: 10232-10239.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10232-10239
    • Zhang, F.L.1    Kirschmeier, P.2    Carr, D.3    James, L.4    Bond, R.W.5    Wang, L.6    Patton, R.7    Windsor, W.T.8    Syto, R.9    Zhang, R.10
  • 60
    • 0033582455 scopus 로고    scopus 로고
    • Inhibition of DNA synthesis by a farnesyltransferase inhibitor involves inhibition of the p70(s6k) pathway
    • Law, B. K., P. Norgaard, L. Gnudi, B. B. Kahn, H. S. Poulson, and H. L. Moses. 1999. Inhibition of DNA synthesis by a farnesyltransferase inhibitor involves inhibition of the p70(s6k) pathway. J. Biol. Chem. 274: 4743-4748.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4743-4748
    • Law, B.K.1    Norgaard, P.2    Gnudi, L.3    Kahn, B.B.4    Poulson, H.S.5    Moses, H.L.6
  • 61
    • 0035991542 scopus 로고    scopus 로고
    • The use of molecular markers in farnesyltransferase inhibitor (FTI) therapy of breast cancer
    • Moasser, M. M., and N. Rosen. 2002. The use of molecular markers in farnesyltransferase inhibitor (FTI) therapy of breast cancer. Breast Cancer Res. Treat. 73: 135-144.
    • (2002) Breast Cancer Res. Treat. , vol.73 , pp. 135-144
    • Moasser, M.M.1    Rosen, N.2
  • 62
  • 63
    • 0032521211 scopus 로고    scopus 로고
    • Antitumor effect of a farnesyl protein transferase inhibitor in mammary and lymphoid tumors overexpressing N-ras in transgenic mice
    • Mangues, R., T. Corral, N. E. Kohl, W. F. Symmans, S. Lu, M. Malumbres, J. B. Gibbs, A. Oliff, and A. Pellicer. 1998. Antitumor effect of a farnesyl protein transferase inhibitor in mammary and lymphoid tumors overexpressing N-ras in transgenic mice. Cancer Res. 58: 1253-1259.
    • (1998) Cancer Res. , vol.58 , pp. 1253-1259
    • Mangues, R.1    Corral, T.2    Kohl, N.E.3    Symmans, W.F.4    Lu, S.5    Malumbres, M.6    Gibbs, J.B.7    Oliff, A.8    Pellicer, A.9
  • 64
    • 0027998986 scopus 로고
    • The CAAX peptidomimetic compound B581 specifically blocks farnesylated, but not geranylgeranylated or myristylated, oncogenic ras signaling and transformation
    • Cox, A. D., A. M. Garcia, J. K. Westwick, J. J. Kowalczyk, M. D. Lewis, D. A. Brenner, and C. J. Der. 1994. The CAAX peptidomimetic compound B581 specifically blocks farnesylated, but not geranylgeranylated or myristylated, oncogenic ras signaling and transformation. J. Biol. Chem. 269: 19203-19206.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19203-19206
    • Cox, A.D.1    Garcia, A.M.2    Westwick, J.K.3    Kowalczyk, J.J.4    Lewis, M.D.5    Brenner, D.A.6    Der, C.J.7
  • 65
    • 0030916369 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB
    • Lebowitz, P. F., P. J. Casey, G. C. Prendergast, and J. A. Thissen. 1997. Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB. J. Biol. Chem. 272: 15591-15594.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15591-15594
    • Lebowitz, P.F.1    Casey, P.J.2    Prendergast, G.C.3    Thissen, J.A.4
  • 66
    • 0028892646 scopus 로고
    • Evidence that farnesyltransferase inhibitors suppress Ras transformation by interfering with Rho activity
    • Lebowitz, P. F., J. P. Davide, and G. C. Prendergast. 1995. Evidence that farnesyltransferase inhibitors suppress Ras transformation by interfering with Rho activity. Mol. Cell. Biol. 15: 6613-6622.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6613-6622
    • Lebowitz, P.F.1    Davide, J.P.2    Prendergast, G.C.3
  • 67
    • 0020037868 scopus 로고
    • Identification of a precursor in the biosynthesis of the p21 transforming protein of harvey murine sarcoma virus
    • Shih, T. Y., M. O. Weeks, P. Gruss, R. Dhar, S. Oroszlan, and E. M. Scolnick. 1982. Identification of a precursor in the biosynthesis of the p21 transforming protein of harvey murine sarcoma virus. J. Virol. 42: 253-261.
    • (1982) J. Virol. , vol.42 , pp. 253-261
    • Shih, T.Y.1    Weeks, M.O.2    Gruss, P.3    Dhar, R.4    Oroszlan, S.5    Scolnick, E.M.6
  • 68
    • 0033016719 scopus 로고    scopus 로고
    • Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB
    • Du, W., P. F. Lebowitz, and G. C. Prendergast. 1999. Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB. Mol. Cell. Biol. 19: 1831-1840.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1831-1840
    • Du, W.1    Lebowitz, P.F.2    Prendergast, G.C.3
  • 70
    • 8544270926 scopus 로고    scopus 로고
    • Cyclin B1 is a critical target of RhoB in the cell suicide program triggered by farnesyl transferase inhibition
    • Kamasani, U., M. Huang, J. B. Duhadaway, E. V. Prochownik, P. S. Donover, and G. C. Prendergast. 2004. Cyclin B1 is a critical target of RhoB in the cell suicide program triggered by farnesyl transferase inhibition. Cancer Res. 64: 8389-8396.
    • (2004) Cancer Res. , vol.64 , pp. 8389-8396
    • Kamasani, U.1    Huang, M.2    Duhadaway, J.B.3    Prochownik, E.V.4    Donover, P.S.5    Prendergast, G.C.6
  • 71
    • 0034674417 scopus 로고    scopus 로고
    • Both farnesylated and geranylgeranylated RhoB inhibit malignant transformation and suppress human tumor growth in nude mice
    • Chen, Z., J. Sun, A. Pradines, G. Favre, J. Adnane, and S. M. Sebti. 2000. Both farnesylated and geranylgeranylated RhoB inhibit malignant transformation and suppress human tumor growth in nude mice. J. Biol. Chem. 275: 17974-17978.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17974-17978
    • Chen, Z.1    Sun, J.2    Pradines, A.3    Favre, G.4    Adnane, J.5    Sebti, S.M.6
  • 72
    • 21444433243 scopus 로고    scopus 로고
    • Palmitoylated cysteine 192 is required for RhoB tumor-suppressive and apoptotic activities
    • Wang, D. A., and S. M. Sebti. 2005. Palmitoylated cysteine 192 is required for RhoB tumor-suppressive and apoptotic activities. J. Biol. Chem. 280: 19243-19249.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19243-19249
    • Wang, D.A.1    Sebti, S.M.2
  • 73
    • 0030774573 scopus 로고    scopus 로고
    • The geranylgeranyltransferase-I inhibitor GGTI-298 arrests human tumor cells in G0/G1 and induces p21(WAF1/CIP1/SDI1) in a p53-independent manner
    • Vogt, A., J. Sun, Y. Qian, A. D. Hamilton, and S. M. Sebti. 1997. The geranylgeranyltransferase-I inhibitor GGTI-298 arrests human tumor cells in G0/G1 and induces p21(WAF1/CIP1/SDI1) in a p53-independent manner. J. Biol. Chem. 272: 27224-27229.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27224-27229
    • Vogt, A.1    Sun, J.2    Qian, Y.3    Hamilton, A.D.4    Sebti, S.M.5
  • 74
    • 0033860183 scopus 로고    scopus 로고
    • RhoB alteration is necessary for apoptotic and antineoplastic responses to farnesyltransferase inhibitors
    • Liu, A., W. Du, J. P. Liu, T. M. Jessell, and G. C. Prendergast. 2000. RhoB alteration is necessary for apoptotic and antineoplastic responses to farnesyltransferase inhibitors. Mol. Cell. Biol. 20: 6105-6113.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6105-6113
    • Liu, A.1    Du, W.2    Liu, J.P.3    Jessell, T.M.4    Prendergast, G.C.5
  • 75
    • 0028237671 scopus 로고
    • rheb, a growth factor- and synaptic activity-regulated gene, encodes a novel Ras-related protein
    • Yamagata, K., L. K. Sanders, W. E. Kaufmann, W. Yee, C. A. Barnes, D. Nathans, and P. F. Worley. 1994. rheb, a growth factor- and synaptic activity-regulated gene, encodes a novel Ras-related protein. J. Biol. Chem. 269: 16333-16339.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16333-16339
    • Yamagata, K.1    Sanders, L.K.2    Kaufmann, W.E.3    Yee, W.4    Barnes, C.A.5    Nathans, D.6    Worley, P.F.7
  • 76
    • 0029560416 scopus 로고
    • A novel approach for expression cloning of small GTPases: Identification, tissue distribution and chromosome mapping of the human homolog of rheb
    • Gromov, P. S., P. Madsen, N. Tomerup, and J. E. Celis. 1995. A novel approach for expression cloning of small GTPases: identification, tissue distribution and chromosome mapping of the human homolog of rheb. FEBS Lett. 377: 221-226.
    • (1995) FEBS Lett. , vol.377 , pp. 221-226
    • Gromov, P.S.1    Madsen, P.2    Tomerup, N.3    Celis, J.E.4
  • 77
    • 24744465206 scopus 로고    scopus 로고
    • The farnesyl transferase inhibitor (FTI) SCH66336 (lonafarnib) inhibits Rheb farnesylation and mTOR signaling. Role in FTI enhancement of taxane and tamoxifen antitumor activity
    • Basso, A. D., A. Mirza, G. Liu, B. J. Long, W. R. Bishop, and P. Kirschmeier. 2005. The farnesyl transferase inhibitor (FTI) SCH66336 (lonafarnib) inhibits Rheb farnesylation and mTOR signaling. Role in FTI enhancement of taxane and tamoxifen antitumor activity. J. Biol. Chem. 280: 31101-31108.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31101-31108
    • Basso, A.D.1    Mirza, A.2    Liu, G.3    Long, B.J.4    Bishop, W.R.5    Kirschmeier, P.6
  • 78
    • 0042701991 scopus 로고    scopus 로고
    • Tuberous sclerosis complex gene products, tuberin and hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb
    • Tee, A. R., B. D. Manning, P. P. Roux, L. C. Cantley, and J. Blenis. 2003. Tuberous sclerosis complex gene products, tuberin and hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr. Biol. 13: 1259-1268.
    • (2003) Curr. Biol. , vol.13 , pp. 1259-1268
    • Tee, A.R.1    Manning, B.D.2    Roux, P.P.3    Cantley, L.C.4    Blenis, J.5
  • 79
    • 0043127125 scopus 로고    scopus 로고
    • Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
    • Inoki, K., Y. Li, T. Xu, and K. L. Guan. 2003. Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev. 17: 1829-1834.
    • (2003) Genes Dev. , vol.17 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3    Guan, K.L.4
  • 81
    • 0038141979 scopus 로고    scopus 로고
    • Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins
    • Zhang, Y., X. Gao, L. J. Saucedo, B. Ru, B. A. Edgar, and D. Pan. 2003. Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins. Nat. Cell Biol. 5: 578-581.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 578-581
    • Zhang, Y.1    Gao, X.2    Saucedo, L.J.3    Ru, B.4    Edgar, B.A.5    Pan, D.6
  • 82
    • 0027770784 scopus 로고
    • Identification and characterization of the tuberous sclerosis gene on chromosome 16
    • The European Chromosome 16 Tuberous Sclerosis Consortium. 1993. Identification and characterization of the tuberous sclerosis gene on chromosome 16. Cell. 75: 1305-1315.
    • (1993) Cell , vol.75 , pp. 1305-1315
  • 84
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • Inoki, K., Y. Li, T. Zhu, J. Wu, and K. L. Guan. 2002. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat. Cell Biol. 4: 648-657.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 85
    • 0037160104 scopus 로고    scopus 로고
    • Regulation of TSC2 by 14-3-3 binding
    • Li, Y., K. Inoki, R. Yeung, and K. L. Guan. 2002. Regulation of TSC2 by 14-3-3 binding. J. Biol. Chem. 277: 44593-44596.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44593-44596
    • Li, Y.1    Inoki, K.2    Yeung, R.3    Guan, K.L.4
  • 86
    • 0036714127 scopus 로고    scopus 로고
    • Akt regulates growth by directly phosphorylating Tsc2
    • Potter, C. J., L. G. Pedraza, and T. Xu. 2002. Akt regulates growth by directly phosphorylating Tsc2. Nat. Cell Biol. 4: 658-665.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 658-665
    • Potter, C.J.1    Pedraza, L.G.2    Xu, T.3
  • 87
    • 0037112527 scopus 로고    scopus 로고
    • 14-3-3 Interacts with the tumor suppressor tuberin at Akt phosphorylation site(s)
    • Liu, M. Y., S. Cai, A. Espejo, M. T. Bedford, and C. L. Walker. 2002. 14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation site(s). Cancer Res. 62: 6475-6480.
    • (2002) Cancer Res. , vol.62 , pp. 6475-6480
    • Liu, M.Y.1    Cai, S.2    Espejo, A.3    Bedford, M.T.4    Walker, C.L.5
  • 88
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway
    • Manning, B. D., A. R. Tee, M. N. Logsdon, J. Blenis, and L. C. Cantley. 2002. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol. Cell. 10: 151-162.
    • (2002) Mol. Cell. , vol.10 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Logsdon, M.N.3    Blenis, J.4    Cantley, L.C.5
  • 90
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki, K., T. Zhu, and K. L. Guan. 2003. TSC2 mediates cellular energy response to control cell growth and survival. Cell. 115: 577-590.
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 93
    • 0041356888 scopus 로고    scopus 로고
    • Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner
    • Castro, A. F., J. F. Rebhun, G. J. Clark, and L. A. Quilliam. 2003. Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner. J. Biol. Chem. 278: 32493-32496.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32493-32496
    • Castro, A.F.1    Rebhun, J.F.2    Clark, G.J.3    Quilliam, L.A.4
  • 94
    • 0141925647 scopus 로고    scopus 로고
    • Identification of dominant negative mutants of Rheb GTPase and their use to implicate the involvement of human Rheb in the activation of p70S6K
    • Tabancay, A. P., Jr., C. L. Gau, I. M. Machado, E. J. Uhlmann, D. H. Gutmann, L. Guo, and F. Tamanoi. 2003. Identification of dominant negative mutants of Rheb GTPase and their use to implicate the involvement of human Rheb in the activation of p70S6K. J. Biol. Chem. 278: 39921-39930.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39921-39930
    • Tabancay Jr., A.P.1    Gau, C.L.2    Machado, I.M.3    Uhlmann, E.J.4    Gutmann, D.H.5    Guo, L.6    Tamanoi, F.7
  • 95
    • 21244480367 scopus 로고    scopus 로고
    • The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses
    • Smith, E. M., S. G. Finn, A. R. Tee, G. J. Browne, and C. G. Proud. 2005. The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses. J. Biol. Chem. 280: 18717-18727.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18717-18727
    • Smith, E.M.1    Finn, S.G.2    Tee, A.R.3    Browne, G.J.4    Proud, C.G.5
  • 98
    • 0038643484 scopus 로고    scopus 로고
    • Rheb promotes cell growth as a component of the insulin/TOR signalling network
    • Saucedo, L. J., X. Gao, D. A. Chiarelli, L. Li, D. Pan, and B. A. Edgar. 2003. Rheb promotes cell growth as a component of the insulin/TOR signalling network. Nat. Cell Biol. 5: 566-571.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 566-571
    • Saucedo, L.J.1    Gao, X.2    Chiarelli, D.A.3    Li, L.4    Pan, D.5    Edgar, B.A.6
  • 100
    • 21344470906 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors reverse altered growth and distribution of actin filaments in Tsc-deficient cells via inhibition of both rapamycin-sensitive and -insensitive pathways
    • Gau, C. L., J. Kato-Stankiewicz, C. Jiang, S. Miyamoto, L. Guo, and F. Tamanoi. 2005. Farnesyltransferase inhibitors reverse altered growth and distribution of actin filaments in Tsc-deficient cells via inhibition of both rapamycin-sensitive and -insensitive pathways. Mol. Cancer Ther. 4: 918-926.
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 918-926
    • Gau, C.L.1    Kato-Stankiewicz, J.2    Jiang, C.3    Miyamoto, S.4    Guo, L.5    Tamanoi, F.6
  • 101
    • 0030838179 scopus 로고    scopus 로고
    • The microtubule-dependent motor centromere-associated protein E (CENP-E) is an integral component of kinetochore corona fibers that link centromeres to spindle microtubules
    • Yao, X., K. L. Anderson, and D. W. Cleveland. 1997. The microtubule-dependent motor centromere-associated protein E (CENP-E) is an integral component of kinetochore corona fibers that link centromeres to spindle microtubules. J. Cell Biol. 139: 435-447.
    • (1997) J. Cell Biol. , vol.139 , pp. 435-447
    • Yao, X.1    Anderson, K.L.2    Cleveland, D.W.3
  • 102
    • 0030665077 scopus 로고    scopus 로고
    • CENP-E is a plus end-directed kinetochore motor required for metaphase chromosome alignment
    • Wood, K. W., R. Sakowicz, L. S. Goldstein, and D. W. Cleveland. 1997. CENP-E is a plus end-directed kinetochore motor required for metaphase chromosome alignment. Cell. 91: 357-366.
    • (1997) Cell , vol.91 , pp. 357-366
    • Wood, K.W.1    Sakowicz, R.2    Goldstein, L.S.3    Cleveland, D.W.4
  • 103
    • 0029096822 scopus 로고
    • CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis
    • Liao, H., R. J. Winkfein, G. Mack, J. B. Rattner, and T. J. Yen. 1995. CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis. J. Cell Biol. 130: 507-518.
    • (1995) J. Cell Biol. , vol.130 , pp. 507-518
    • Liao, H.1    Winkfein, R.J.2    Mack, G.3    Rattner, J.B.4    Yen, T.J.5
  • 104
    • 0035844247 scopus 로고    scopus 로고
    • The farnesyltransferase inhibitor, FTI-2153, blocks bipolar spindle formation and chromosome alignment and causes prometaphase accumulation during mitosis of human lung cancer cells
    • Crespo, N. C., J. Ohkanda, T. J. Yen, A. D. Hamilton, and S. M. Sebti. 2001. The farnesyltransferase inhibitor, FTI-2153, blocks bipolar spindle formation and chromosome alignment and causes prometaphase accumulation during mitosis of human lung cancer cells. J. Biol. Chem. 276: 16161-16167.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16161-16167
    • Crespo, N.C.1    Ohkanda, J.2    Yen, T.J.3    Hamilton, A.D.4    Sebti, S.M.5
  • 105
    • 0036714596 scopus 로고    scopus 로고
    • Farnesylation of Cenp-F is required for G2/M progression and degradation after mitosis
    • Hussein, D., and S. S. Taylor. 2002. Farnesylation of Cenp-F is required for G2/M progression and degradation after mitosis. J. Cell Sci. 115: 3403-3414.
    • (2002) J. Cell Sci. , vol.115 , pp. 3403-3414
    • Hussein, D.1    Taylor, S.S.2
  • 108
    • 0034647510 scopus 로고    scopus 로고
    • Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome
    • Zeng, Q., X. Si, H. Horstmann, Y. Xu, W. Hong, and C. J. Pallen. 2000. Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome. J. Biol. Chem. 275: 21444-21452.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21444-21452
    • Zeng, Q.1    Si, X.2    Horstmann, H.3    Xu, Y.4    Hong, W.5    Pallen, C.J.6
  • 109
    • 0032510812 scopus 로고    scopus 로고
    • Mammalian cytosolic DnaJ homologues affect the hsp70 chaperone-substrate reaction cycle, but do not interact directly with nascent or newly synthesized proteins
    • Nagata, H., W. J. Hansen, B. Freeman, and W. J. Welch. 1998. Mammalian cytosolic DnaJ homologues affect the hsp70 chaperone-substrate reaction cycle, but do not interact directly with nascent or newly synthesized proteins. Biochemistry. 37: 6924-6938.
    • (1998) Biochemistry , vol.37 , pp. 6924-6938
    • Nagata, H.1    Hansen, W.J.2    Freeman, B.3    Welch, W.J.4
  • 110
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K., J. Marszalek, D. Ang, C. Georgopoulos, and M. Zylicz. 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA. 88: 2874-2878.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 111
    • 0027102871 scopus 로고
    • YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism
    • Caplan, A. J., D. M. Cyr, and M. G. Douglas. 1992. YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell. 71: 1143-1155.
    • (1992) Cell , vol.71 , pp. 1143-1155
    • Caplan, A.J.1    Cyr, D.M.2    Douglas, M.G.3
  • 112
    • 0030830249 scopus 로고    scopus 로고
    • The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding
    • Terada, K., M. Kanazawa, B. Bukau, and M. Mori. 1997. The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding. J. Cell Biol. 139: 1089-1095.
    • (1997) J. Cell Biol. , vol.139 , pp. 1089-1095
    • Terada, K.1    Kanazawa, M.2    Bukau, B.3    Mori, M.4
  • 113
    • 0031008364 scopus 로고    scopus 로고
    • A role for HDJ-2/HSDJ in correcting subnuclear trafficking, transactivation, and transrepression defects of a glucocorticoid receptor zinc finger mutant
    • Tang, Y., C. Ramakrishnan, J. Thomas, and D. B. DeFranco. 1997. A role for HDJ-2/HSDJ in correcting subnuclear trafficking, transactivation, and transrepression defects of a glucocorticoid receptor zinc finger mutant. Mol. Biol. Cell. 8: 795-809.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 795-809
    • Tang, Y.1    Ramakrishnan, C.2    Thomas, J.3    DeFranco, D.B.4
  • 114
    • 0033607770 scopus 로고    scopus 로고
    • Domain requirements of DnaJ-like (Hsp40) molecular chaperones in the activation of a steroid hormone receptor
    • Fliss, A. E., J. Rao, M. W. Melville, M. E. Cheetham, and A. J. Caplan. 1999. Domain requirements of DnaJ-like (Hsp40) molecular chaperones in the activation of a steroid hormone receptor. J. Biol. Chem. 274: 34045-34052.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34045-34052
    • Fliss, A.E.1    Rao, J.2    Melville, M.W.3    Cheetham, M.E.4    Caplan, A.J.5
  • 115
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi, U., J. Cohn, L. Buhle, and L. Gerace. 1986. The nuclear lamina is a meshwork of intermediate-type filaments. Nature. 323: 560-564.
    • (1986) Nature , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 116
    • 0026657886 scopus 로고
    • Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract
    • Ulitzur, N., A. Harel, N. Feinstein, and Y. Gruenbaum. 1992. Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract. J. Cell Biol. 119: 17-25.
    • (1992) J. Cell Biol. , vol.119 , pp. 17-25
    • Ulitzur, N.1    Harel, A.2    Feinstein, N.3    Gruenbaum, Y.4
  • 117
    • 0025362748 scopus 로고
    • Isoprenylation is required for the processing of the lamin A precursor
    • Beck, L. A., T. J. Hosick, and M. Sinensky. 1990. Isoprenylation is required for the processing of the lamin A precursor. J. Cell Biol. 110: 1489-1499.
    • (1990) J. Cell Biol. , vol.110 , pp. 1489-1499
    • Beck, L.A.1    Hosick, T.J.2    Sinensky, M.3
  • 118
    • 0024828257 scopus 로고
    • Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor: Implications for the structure of the nuclear lamina
    • Weber, K., U. Plessmann, and P. Traub. 1989. Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor: implications for the structure of the nuclear lamina. FEBS Lett. 257: 411-414.
    • (1989) FEBS Lett. , vol.257 , pp. 411-414
    • Weber, K.1    Plessmann, U.2    Traub, P.3
  • 120
    • 0028237586 scopus 로고
    • An antibody which specifically recognizes prelamin A but not mature lamin A: Application to detection of blocks in farnesylation-dependent protein processing
    • Sinensky, M., K. Fantle, and M. Dalton. 1994. An antibody which specifically recognizes prelamin A but not mature lamin A: application to detection of blocks in farnesylation-dependent protein processing. Cancer Res. 54: 3229-3232.
    • (1994) Cancer Res. , vol.54 , pp. 3229-3232
    • Sinensky, M.1    Fantle, K.2    Dalton, M.3
  • 123
    • 0026559677 scopus 로고
    • Nucleoplasmic localization of prelamin A: Implications for prenylation-dependent lamin A assembly into the nuclear lamina
    • Lutz, R. J., M. A. Trujillo, K. S. Denham, L. Wenger, and M. Sinensky. 1992. Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina. Proc. Natl. Acad. Sci. USA. 89: 3000-3004.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3000-3004
    • Lutz, R.J.1    Trujillo, M.A.2    Denham, K.S.3    Wenger, L.4    Sinensky, M.5
  • 124
    • 0028831126 scopus 로고
    • Lamin A precursor is localized to intranuclear foci
    • Sasseville, A. M., and Y. Raymond. 1995. Lamin A precursor is localized to intranuclear foci. J. Cell Sci. 108: 273-285.
    • (1995) J. Cell Sci. , vol.108 , pp. 273-285
    • Sasseville, A.M.1    Raymond, Y.2
  • 125
    • 0028274845 scopus 로고
    • The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties
    • Hennekes, H., and E. A. Nigg. 1994. The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties. J. Cell Sci. 107: 1019-1029.
    • (1994) J. Cell Sci. , vol.107 , pp. 1019-1029
    • Hennekes, H.1    Nigg, E.A.2
  • 126
    • 0033569878 scopus 로고    scopus 로고
    • Prenylated prelamin A interacts with Narf, a novel nuclear protein
    • Barton, R. M., and H. J. Worman. 1999. Prenylated prelamin A interacts with Narf, a novel nuclear protein. J. Biol. Chem. 274: 30008-30018.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30008-30018
    • Barton, R.M.1    Worman, H.J.2
  • 132
    • 22544440839 scopus 로고    scopus 로고
    • Blocking protein farnesyltransferase improves nuclear blebbing in mouse fibroblasts with a targeted Hutchinson-Gilford progeria syndrome mutation
    • Yang, S. H., M. O. Bergo, J. I. Toth, X. Qiao, Y. Hu, S. Sandoval, M. Meta, P. Bendale, M. H. Gelb, S. G. Young, et al. 2005. Blocking protein farnesyltransferase improves nuclear blebbing in mouse fibroblasts with a targeted Hutchinson-Gilford progeria syndrome mutation. Proc. Natl. Acad. Sci. USA. 102: 10291-10296.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10291-10296
    • Yang, S.H.1    Bergo, M.O.2    Toth, J.I.3    Qiao, X.4    Hu, Y.5    Sandoval, S.6    Meta, M.7    Bendale, P.8    Gelb, M.H.9    Young, S.G.10
  • 136
    • 4744365244 scopus 로고    scopus 로고
    • Investigation of the effect of the farnesyl protein transferase inhibitor R115777 on isoprenylation and intracellular signalling by the prostacyclin receptor
    • O'Meara, S. J., and B. T. Kinsella. 2004. Investigation of the effect of the farnesyl protein transferase inhibitor R115777 on isoprenylation and intracellular signalling by the prostacyclin receptor. Br. J. Pharmacol. 143: 318-330.
    • (2004) Br. J. Pharmacol. , vol.143 , pp. 318-330
    • O'Meara, S.J.1    Kinsella, B.T.2
  • 137
    • 14344254868 scopus 로고    scopus 로고
    • Antitumor activity of SCH 66336, an orally bioavailable tricyclic inhibitor of farnesyl protein transferase, in human tumor xenograft models and wap-ras transgenic mice
    • Liu, M., M. S. Bryant, J. Chen, S. Lee, B. Yaremko, P. Lipari, M. Malkowski, E. Ferrari, L. Nielsen, N. Prioli, et al. 1998. Antitumor activity of SCH 66336, an orally bioavailable tricyclic inhibitor of farnesyl protein transferase, in human tumor xenograft models and wap-ras transgenic mice. Cancer Res. 58: 4947-4956.
    • (1998) Cancer Res. , vol.58 , pp. 4947-4956
    • Liu, M.1    Bryant, M.S.2    Chen, J.3    Lee, S.4    Yaremko, B.5    Lipari, P.6    Malkowski, M.7    Ferrari, E.8    Nielsen, L.9    Prioli, N.10
  • 139
    • 0032417689 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors induce cytochrome c release and caspase 3 activation preferentially in transformed cells
    • Suzuki, N., J. Urano, and F. Tamanoi. 1998. Farnesyltransferase inhibitors induce cytochrome c release and caspase 3 activation preferentially in transformed cells. Proc. Natl. Acad. Sci. USA. 95: 15356-15361.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15356-15361
    • Suzuki, N.1    Urano, J.2    Tamanoi, F.3
  • 140
    • 0031050738 scopus 로고    scopus 로고
    • Farnesyl transferase inhibitors induce apoptosis of Ras-transformed cells denied substratum attachment
    • Lebowitz, P. F., D. Sakamuro, and G. C. Prendergast. 1997. Farnesyl transferase inhibitors induce apoptosis of Ras-transformed cells denied substratum attachment. Cancer Res. 57: 708-713.
    • (1997) Cancer Res. , vol.57 , pp. 708-713
    • Lebowitz, P.F.1    Sakamuro, D.2    Prendergast, G.C.3
  • 141
    • 0036061374 scopus 로고    scopus 로고
    • Inhibitors of farnesyl protein transferase and MEK1,2 induce apoptosis in fibroblasts transformed with farnesylated but not geranylgeranylated H-Ras
    • Brassard, D. L., J. M. English, M. Malkowski, P. Kirschmeier, T. L. Nagabhushan, and W. R. Bishop. 2002. Inhibitors of farnesyl protein transferase and MEK1,2 induce apoptosis in fibroblasts transformed with farnesylated but not geranylgeranylated H-Ras. Exp. Cell Res. 273: 138-146.
    • (2002) Exp. Cell Res. , vol.273 , pp. 138-146
    • Brassard, D.L.1    English, J.M.2    Malkowski, M.3    Kirschmeier, P.4    Nagabhushan, T.L.5    Bishop, W.R.6
  • 143
    • 0028835253 scopus 로고
    • A peptidomimetic inhibitor of farnesyl:protein transferase blocks the anchorage-dependent and -independent growth of human tumor cell lines
    • Sepp-Lorenzino, L., Z. Ma, E. Rands, N. E. Kohl, J. B. Gibbs, A. Oliff, and N. Rosen. 1995. A peptidomimetic inhibitor of farnesyl:protein transferase blocks the anchorage-dependent and -independent growth of human tumor cell lines. Cancer Res. 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
  • 144
    • 0029154458 scopus 로고
    • Farnesyltransferase inhibitors block the neurofibromatosis type I (NF1) malignant phenotype
    • Yan, N., C. Ricca, J. Fletcher, T. Glover, B. R. Seizinger, and V. Manne. 1995. Farnesyltransferase inhibitors block the neurofibromatosis type I (NF1) malignant phenotype. Cancer Res. 55: 3569-3575.
    • (1995) Cancer Res. , vol.55 , pp. 3569-3575
    • Yan, N.1    Ricca, C.2    Fletcher, J.3    Glover, T.4    Seizinger, B.R.5    Manne, V.6
  • 146
    • 0032763824 scopus 로고    scopus 로고
    • Expression of activated epidermal growth factor receptors, Rasguanosine triphosphate, and mitogen-activated protein kinase in human glioblastoma multiforme specimens
    • Feldkamp, M. M., P. Lala, N. Lau, L. Roncari, and A. Guha. 1999. Expression of activated epidermal growth factor receptors, Rasguanosine triphosphate, and mitogen-activated protein kinase in human glioblastoma multiforme specimens. Neurosurgery. 45: 1442-1453.
    • (1999) Neurosurgery , vol.45 , pp. 1442-1453
    • Feldkamp, M.M.1    Lala, P.2    Lau, N.3    Roncari, L.4    Guha, A.5
  • 147
    • 0035360259 scopus 로고    scopus 로고
    • Isotypespecific Ras.GTP-levels predict the efficacy of farnesyl transferase inhibitors against human astrocytomas regardless of Ras mutational status
    • Feldkamp, M. M., N. Lau, L. Roncari, and A. Guha. 2001. Isotypespecific Ras.GTP-levels predict the efficacy of farnesyl transferase inhibitors against human astrocytomas regardless of Ras mutational status. Cancer Res. 61: 4425-4431.
    • (2001) Cancer Res. , vol.61 , pp. 4425-4431
    • Feldkamp, M.M.1    Lau, N.2    Roncari, L.3    Guha, A.4
  • 148
    • 0032493641 scopus 로고    scopus 로고
    • A farnesyl-protein transferase inhibitor induces p21 expression and G1 block in p53 wild type tumor cells
    • Sepp-Lorenzino, L., and N. Rosen. 1998. A farnesyl-protein transferase inhibitor induces p21 expression and G1 block in p53 wild type tumor cells. J. Biol. Chem. 273: 20243-20251.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20243-20251
    • Sepp-Lorenzino, L.1    Rosen, N.2
  • 149
    • 0029023145 scopus 로고
    • Ras CAAX peptidomimetic FTI 276 selectively blocks tumor growth in nude mice of a human lung carcinoma with K-Ras mutation and p53 deletion
    • Sun, J., Y. Qian, A. D. Hamilton, and S. M. Sebti. 1995. Ras CAAX peptidomimetic FTI 276 selectively blocks tumor growth in nude mice of a human lung carcinoma with K-Ras mutation and p53 deletion. Cancer Res. 55: 4243-4247.
    • (1995) Cancer Res. , vol.55 , pp. 4243-4247
    • Sun, J.1    Qian, Y.2    Hamilton, A.D.3    Sebti, S.M.4
  • 150
    • 0035886842 scopus 로고    scopus 로고
    • Preclinical antitumor activity of BMS-214662, a highly apoptotic and novel farnesyltransferase inhibitor
    • Rose, W. C., F. Y. Lee, C. R. Fairchild, M. Lynch, T. Monticello, R. A. Kramer, and V. Manne. 2001. Preclinical antitumor activity of BMS-214662, a highly apoptotic and novel farnesyltransferase inhibitor. Cancer Res. 61: 7507-7517.
    • (2001) Cancer Res. , vol.61 , pp. 7507-7517
    • Rose, W.C.1    Lee, F.Y.2    Fairchild, C.R.3    Lynch, M.4    Monticello, T.5    Kramer, R.A.6    Manne, V.7
  • 151
    • 0035282901 scopus 로고    scopus 로고
    • Activity of the farnesyl protein transferase inhibitor SCH66336 against BCR/ABL-induced murine leukemia and primary cells from patients with chronic myeloid leukemia
    • Peters, D. G., R. R. Hoover, M. J. Gerlach, E. Y. Koh, H. Zhang, K. Choe, P. Kirschmeier, W. R. Bishop, and G. Q. Daley. 2001. Activity of the farnesyl protein transferase inhibitor SCH66336 against BCR/ABL-induced murine leukemia and primary cells from patients with chronic myeloid leukemia. Blood. 97: 1404-1412.
    • (2001) Blood , vol.97 , pp. 1404-1412
    • Peters, D.G.1    Hoover, R.R.2    Gerlach, M.J.3    Koh, E.Y.4    Zhang, H.5    Choe, K.6    Kirschmeier, P.7    Bishop, W.R.8    Daley, G.Q.9
  • 152
    • 0035282735 scopus 로고    scopus 로고
    • Treatment of Bcr/Abl-positive acute lymphoblastic leukemia in P190 transgenic mice with the farnesyl transferase inhibitor SCH66336
    • Reichert, A., N. Heisterkamp, G. Q. Daley, and J. Groffen. 2001. Treatment of Bcr/Abl-positive acute lymphoblastic leukemia in P190 transgenic mice with the farnesyl transferase inhibitor SCH66336. Blood. 97: 1399-1403.
    • (2001) Blood , vol.97 , pp. 1399-1403
    • Reichert, A.1    Heisterkamp, N.2    Daley, G.Q.3    Groffen, J.4
  • 153
    • 0742306877 scopus 로고    scopus 로고
    • A farnesyltransferase inhibitor increases survival of mice with very advanced stage acute lymphoblastic leukemia/lymphoma caused by P190 Bcr/Abl
    • Mishra, S., B. Zhang, J. Groffen, and N. Heisterkamp. 2004. A farnesyltransferase inhibitor increases survival of mice with very advanced stage acute lymphoblastic leukemia/lymphoma caused by P190 Bcr/Abl. Leukemia. 18: 23-28.
    • (2004) Leukemia , vol.18 , pp. 23-28
    • Mishra, S.1    Zhang, B.2    Groffen, J.3    Heisterkamp, N.4
  • 154
    • 0036683409 scopus 로고    scopus 로고
    • Overcoming STI571 resistance with the farnesyl transferase inhibitor SCH66336
    • Hoover, R. R., F. X. Mahon, J. V. Melo, and G. Q. Daley. 2002. Overcoming STI571 resistance with the farnesyl transferase inhibitor SCH66336. Blood. 100: 1068-1071.
    • (2002) Blood , vol.100 , pp. 1068-1071
    • Hoover, R.R.1    Mahon, F.X.2    Melo, J.V.3    Daley, G.Q.4
  • 155
    • 0344611212 scopus 로고    scopus 로고
    • Efficacy of SCH66336, a farnesyl transferase inhibitor, in conjunction with imatinib against BCR-ABL-positive cells
    • Nakajima, A., T. Tauchi, M. Sumi, W. R. Bishop, and K. Ohyashiki. 2003. Efficacy of SCH66336, a farnesyl transferase inhibitor, in conjunction with imatinib against BCR-ABL-positive cells. Mol. Cancer Ther. 2: 219-224.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 219-224
    • Nakajima, A.1    Tauchi, T.2    Sumi, M.3    Bishop, W.R.4    Ohyashiki, K.5
  • 156
    • 0033986790 scopus 로고    scopus 로고
    • The phosphoinositide 3-OH kinase/AKT2 pathway as a critical target for farnesyltransferase inhibitor-induced apoptosis
    • Jiang, K., D. Coppola, N. C. Crespo, S. V. Nicosia, A. D. Hamilton, S. M. Sebti, and J. Q. Cheng. 2000. The phosphoinositide 3-OH kinase/AKT2 pathway as a critical target for farnesyltransferase inhibitor-induced apoptosis. Mol. Cell. Biol. 20: 139-148.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 139-148
    • Jiang, K.1    Coppola, D.2    Crespo, N.C.3    Nicosia, S.V.4    Hamilton, A.D.5    Sebti, S.M.6    Cheng, J.Q.7
  • 157
    • 0041940129 scopus 로고    scopus 로고
    • Implication of protein kinase B/Akt and Bcl-2/ Bcl-XL suppression by the farnesyl transferase inhibitor SCH66336 in apoptosis induction in squamous carcinoma cells
    • Chun, K. H., H. Y. Lee, K. Hassan, F. Khuri, W. K. Hong, and R. Lotan. 2003. Implication of protein kinase B/Akt and Bcl-2/ Bcl-XL suppression by the farnesyl transferase inhibitor SCH66336 in apoptosis induction in squamous carcinoma cells. Cancer Res. 63: 4796-4800.
    • (2003) Cancer Res. , vol.63 , pp. 4796-4800
    • Chun, K.H.1    Lee, H.Y.2    Hassan, K.3    Khuri, F.4    Hong, W.K.5    Lotan, R.6
  • 158
    • 22144453619 scopus 로고    scopus 로고
    • The farnesyltransferase inhibitor lonafarnib induces growth arrest or apoptosis of human lung cancer cells without downregulation of akt
    • Sun, S. Y., Z. Zhou, R. Wang, H. Fu, and F. R. Khuri. 2004. The farnesyltransferase inhibitor lonafarnib induces growth arrest or apoptosis of human lung cancer cells without downregulation of akt. Cancer Biol. Ther. 3: 1092-1098.
    • (2004) Cancer Biol. Ther. , vol.3 , pp. 1092-1098
    • Sun, S.Y.1    Zhou, Z.2    Wang, R.3    Fu, H.4    Khuri, F.R.5
  • 159
    • 0242489177 scopus 로고    scopus 로고
    • Farnesyl transferase inhibitors enhance death receptor signals and induce apoptosis in multiple myeloma cells
    • Beaupre, D. M., J. McCafferty-Grad, N. J. Bahlis, L. H. Boise, and M. G. Lichtenheld. 2003. Farnesyl transferase inhibitors enhance death receptor signals and induce apoptosis in multiple myeloma cells. Leuk. Lymphoma. 44: 2123-2134.
    • (2003) Leuk. Lymphoma. , vol.44 , pp. 2123-2134
    • Beaupre, D.M.1    McCafferty-Grad, J.2    Bahlis, N.J.3    Boise, L.H.4    Lichtenheld, M.G.5
  • 160
    • 0033539952 scopus 로고    scopus 로고
    • Growth inhibition of astrocytoma cells by farnesyl transferase inhibitors is mediated by a combination of anti-proliferative, pro-apoptotic and antiangiogenic effects
    • Feldkamp, M. M., N. Lau, and A. Guha. 1998. Growth inhibition of astrocytoma cells by farnesyl transferase inhibitors is mediated by a combination of anti-proliferative, pro-apoptotic and antiangiogenic effects. Oncogene. 18: 7514-7526.
    • (1998) Oncogene , vol.18 , pp. 7514-7526
    • Feldkamp, M.M.1    Lau, N.2    Guha, A.3
  • 162
    • 18144363210 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors induce DNA damage via reactive oxygen species in human cancer cells
    • Pan, J., M. She, Z. X. Xu, L. Sun, and S. C. Yeung. 2005. Farnesyltransferase inhibitors induce DNA damage via reactive oxygen species in human cancer cells. Cancer Res. 65: 3671-3681.
    • (2005) Cancer Res. , vol.65 , pp. 3671-3681
    • Pan, J.1    She, M.2    Xu, Z.X.3    Sun, L.4    Yeung, S.C.5
  • 164
    • 0034905234 scopus 로고    scopus 로고
    • Synergy of the protein farnesyltransferase inhibitor SCH66336 and cisplatin in human cancer cell lines
    • Adjei, A. A., J. N. Davis, L. M. Bruzek, C. Erlichman, and S. H. Kaufmann. 2001. Synergy of the protein farnesyltransferase inhibitor SCH66336 and cisplatin in human cancer cell lines. Clin. Cancer Res. 7: 1438-1445.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1438-1445
    • Adjei, A.A.1    Davis, J.N.2    Bruzek, L.M.3    Erlichman, C.4    Kaufmann, S.H.5
  • 165
    • 0037549328 scopus 로고    scopus 로고
    • Additive effects of tamoxifen and the farnesyl transferase inhibitor FTI-277 on inhibition of MCF-7 breast cancer cell-cycle progression
    • Doisneau-Sixou, S. F., P. Cestac, J. C. Faye, G. Favre, and R. L. Sutherland. 2003. Additive effects of tamoxifen and the farnesyl transferase inhibitor FTI-277 on inhibition of MCF-7 breast cancer cell-cycle progression. Int. J. Cancer. 106: 789-798.
    • (2003) Int. J. Cancer. , vol.106 , pp. 789-798
    • Doisneau-Sixou, S.F.1    Cestac, P.2    Faye, J.C.3    Favre, G.4    Sutherland, R.L.5
  • 166
    • 0034702266 scopus 로고    scopus 로고
    • Cdk inhibitors, roscovitine and olomoucine, synergize with farnesyltransferase inhibitor (FTI) to induce efficient apoptosis of human cancer cell lines
    • Edamatsu, H., C. L. Gau, T. Nemoto, L. Guo, and F. Tamanoi. 2000. Cdk inhibitors, roscovitine and olomoucine, synergize with farnesyltransferase inhibitor (FTI) to induce efficient apoptosis of human cancer cell lines. Oncogene. 19: 3059-3068.
    • (2000) Oncogene , vol.19 , pp. 3059-3068
    • Edamatsu, H.1    Gau, C.L.2    Nemoto, T.3    Guo, L.4    Tamanoi, F.5
  • 167
    • 0037143092 scopus 로고    scopus 로고
    • RPR-115135, a farnesyltransferase inhibitor, increases 5-FU cytotoxicity in ten human colon cancer cell lines: Role of p53
    • Russo, P., D. Malacarne, C. Falugi, S. Trombino, and P. M. O'Connor. 2002. RPR-115135, a farnesyltransferase inhibitor, increases 5-FU cytotoxicity in ten human colon cancer cell lines: role of p53. Int. J. Cancer. 100: 266-275.
    • (2002) Int. J. Cancer. , vol.100 , pp. 266-275
    • Russo, P.1    Malacarne, D.2    Falugi, C.3    Trombino, S.4    O'Connor, P.M.5
  • 168
    • 0033729718 scopus 로고    scopus 로고
    • The farnesyl protein transferase inhibitor SCH66336 synergizes with taxanes in vitro and enhances their antitumor activity in vivo
    • Shi, B., B. Yaremko, G. Hajian, G. Terracina, W. R. Bishop, M. Liu, and L. L. Nielsen. 2000. The farnesyl protein transferase inhibitor SCH66336 synergizes with taxanes in vitro and enhances their antitumor activity in vivo. Cancer Chemother. Pharmacol. 46: 387-393.
    • (2000) Cancer Chemother. Pharmacol. , vol.46 , pp. 387-393
    • Shi, B.1    Yaremko, B.2    Hajian, G.3    Terracina, G.4    Bishop, W.R.5    Liu, M.6    Nielsen, L.L.7
  • 169
    • 0036643779 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitor, R115777, reverses the resistance of human glioma cell lines to ionizing radiation
    • Delmas, C., C. Heliez, E. Cohen-Jonathan, D. End, J. Bonnet, G. Favre, and C. Toulas. 2002. Farnesyltransferase inhibitor, R115777, reverses the resistance of human glioma cell lines to ionizing radiation. Int. J. Cancer. 100: 43-48.
    • (2002) Int. J. Cancer. , vol.100 , pp. 43-48
    • Delmas, C.1    Heliez, C.2    Cohen-Jonathan, E.3    End, D.4    Bonnet, J.5    Favre, G.6    Toulas, C.7
  • 172
    • 20444416005 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitor R115777 (Zarnestra, Tipifarnib) synergizes with paclitaxel to induce apoptosis and mitotic arrest and to inhibit tumor growth of multiple myeloma cells
    • Zhu, K., E. Gerbino, D. M. Beaupre, P. A. Mackley, C. Muro-Cacho, C. Beam, A. D. Hamilton, M. G. Lichtenheld, W. G. Kerr, W. Dalton, et al. 2005. Farnesyltransferase inhibitor R115777 (Zarnestra, Tipifarnib) synergizes with paclitaxel to induce apoptosis and mitotic arrest and to inhibit tumor growth of multiple myeloma cells. Blood. 105: 4759-4766.
    • (2005) Blood , vol.105 , pp. 4759-4766
    • Zhu, K.1    Gerbino, E.2    Beaupre, D.M.3    Mackley, P.A.4    Muro-Cacho, C.5    Beam, C.6    Hamilton, A.D.7    Lichtenheld, M.G.8    Kerr, W.G.9    Dalton, W.10
  • 173
    • 20944437248 scopus 로고    scopus 로고
    • The synergistic combination of the farnesyl transferase inhibitor lonafarnib and paclitaxel enhances tubulin acetylation and requires a functional tubulin deacetylase
    • Marcus, A. I., J. Zhou, A. O'Brate, E. Hamel, J. Wong, M. Nivens, A. El-Naggar, T. P. Yao, F. R. Khuri, and P. Giannakakou. 2005. The synergistic combination of the farnesyl transferase inhibitor lonafarnib and paclitaxel enhances tubulin acetylation and requires a functional tubulin deacetylase. Cancer Res. 65: 3883-3893.
    • (2005) Cancer Res. , vol.65 , pp. 3883-3893
    • Marcus, A.I.1    Zhou, J.2    O'Brate, A.3    Hamel, E.4    Wong, J.5    Nivens, M.6    El-Naggar, A.7    Yao, T.P.8    Khuri, F.R.9    Giannakakou, P.10
  • 177
  • 178
  • 179
    • 0035990832 scopus 로고    scopus 로고
    • A phase II trial of farnesyl protein transferase inhibitor SCH 66336, given by twice-daily oral administration, in patients with metastatic colorectal cancer refractory to 5-fluorouracil and irinotecan
    • Sharma, S., N. Kemeny, D. P. Kelsen, D. Ilson, E. O'Reilly, S. Zaknoen, C. Baum, P. Statkevich, E. Hollywood, Y. Zhu, et al. 2002. A phase II trial of farnesyl protein transferase inhibitor SCH 66336, given by twice-daily oral administration, in patients with metastatic colorectal cancer refractory to 5-fluorouracil and irinotecan. Ann. Oncol. 13: 1067-1071.
    • (2002) Ann. Oncol. , vol.13 , pp. 1067-1071
    • Sharma, S.1    Kemeny, N.2    Kelsen, D.P.3    Ilson, D.4    O'Reilly, E.5    Zaknoen, S.6    Baum, C.7    Statkevich, P.8    Hollywood, E.9    Zhu, Y.10
  • 181
    • 30844473579 scopus 로고    scopus 로고
    • Phase I trial of the oral farnesyl protein transferase inhibitor lonafarnib (SCH66336): A Pediatric Brain Tumor Consortium (PBTC) study
    • New Orleans, LA, June 5-8, 2004
    • Kieran, M. W., R. Packer, J. Boyett, M. Sugrue, and L. Kun. 2004. Phase I trial of the oral farnesyl protein transferase inhibitor lonafarnib (SCH66336): a Pediatric Brain Tumor Consortium (PBTC) study (Abstract 1517 in American Society of Clinical Oncology Annual Meeting , New Orleans, LA, June 5-8, 2004).
    • (2004) Abstract 1517 in American Society of Clinical Oncology Annual Meeting
    • Kieran, M.W.1    Packer, R.2    Boyett, J.3    Sugrue, M.4    Kun, L.5
  • 184
    • 13544275900 scopus 로고    scopus 로고
    • Hyperleukocytosis complicating lonafarnib treatment in patients with chronic myelomonocytic leukemia
    • Buresh, A., J. Perentesis, L. Rimsza, S. Kurtin, R. Heaton, M. Sugrue, and A. List. 2005. Hyperleukocytosis complicating lonafarnib treatment in patients with chronic myelomonocytic leukemia. Leukemia. 19: 308-310.
    • (2005) Leukemia , vol.19 , pp. 308-310
    • Buresh, A.1    Perentesis, J.2    Rimsza, L.3    Kurtin, S.4    Heaton, R.5    Sugrue, M.6    List, A.7
  • 186
    • 8644219632 scopus 로고    scopus 로고
    • Clinical activity of farnesyl transferase inhibitors in hematologic malignancies: Possible mechanisms of action
    • Jabbour, E., H. Kantarjian, and J. Cortes. 2004. Clinical activity of farnesyl transferase inhibitors in hematologic malignancies: possible mechanisms of action. Leuk. Lymphoma. 45: 2187-2195.
    • (2004) Leuk. Lymphoma. , vol.45 , pp. 2187-2195
    • Jabbour, E.1    Kantarjian, H.2    Cortes, J.3
  • 188
    • 0035064808 scopus 로고    scopus 로고
    • Phase I and pharmacokinetic study of the orally administered farnesyl transferase inhibitor R115777 in patients with advanced solid tumors
    • Punt, C. J., L. van Maanen, C. J. Bol, W. F. Seifert, and D. J. Wagener. 2001. Phase I and pharmacokinetic study of the orally administered farnesyl transferase inhibitor R115777 in patients with advanced solid tumors. Anticancer Drugs. 12: 193-197.
    • (2001) Anticancer Drugs. , vol.12 , pp. 193-197
    • Punt, C.J.1    Van Maanen, L.2    Bol, C.J.3    Seifert, W.F.4    Wagener, D.J.5
  • 189
    • 0036605562 scopus 로고    scopus 로고
    • Phase I clinical and pharmacologic study of chronic oral administration of the farnesyl protein transferase inhibitor R115777 in advanced cancer
    • Crul, M., G. J. de Klerk, M. Swart, L. J. van't Veer, D. de Jong, L. Boerrigter, P. A. Palmer, C. J. Bol, H. Tan, G. C. de Gast, et al. 2002. Phase I clinical and pharmacologic study of chronic oral administration of the farnesyl protein transferase inhibitor R115777 in advanced cancer. J. Clin. Oncol. 20: 2726-2735.
    • (2002) J. Clin. Oncol. , vol.20 , pp. 2726-2735
    • Crul, M.1    De Klerk, G.J.2    Swart, M.3    Van't Veer, L.J.4    De Jong, D.5    Boerrigter, L.6    Palmer, P.A.7    Bol, C.J.8    Tan, H.9    De Gast, G.C.10
  • 190
    • 0035383789 scopus 로고    scopus 로고
    • Clinical and biologic activity of the farnesyltransferase inhibitor R115777 in adults with refractory and relapsed acute leukemias: A phase 1 clinical-laboratory correlative trial
    • Karp, J. E., J. E. Lancet, S. H. Kaufmann, D. W. End, J. J. Wright, K. Bol, I. Horak, M. L. Tidwell, J. Liesveld, T. J. Kottke, et al. 2001. Clinical and biologic activity of the farnesyltransferase inhibitor R115777 in adults with refractory and relapsed acute leukemias: a phase 1 clinical-laboratory correlative trial. Blood. 97: 3361-3369.
    • (2001) Blood , vol.97 , pp. 3361-3369
    • Karp, J.E.1    Lancet, J.E.2    Kaufmann, S.H.3    End, D.W.4    Wright, J.J.5    Bol, K.6    Horak, I.7    Tidwell, M.L.8    Liesveld, J.9    Kottke, T.J.10
  • 195
    • 11144358447 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitor tipifarnib is well tolerated, induces stabilization of disease, and inhibits farnesylation and oncogenic/tumor survival pathways in patients with advanced multiple myeloma
    • Alsina, M., R. Fonseca, E. F. Wilson, A. N. Belle, E. Gerbino, T. Price-Troska, R. M. Overton, G. Ahmann, L. M. Bruzek, A. A. Adjei, et al. 2004. Farnesyltransferase inhibitor tipifarnib is well tolerated, induces stabilization of disease, and inhibits farnesylation and oncogenic/tumor survival pathways in patients with advanced multiple myeloma. Blood. 103: 3271-3277.
    • (2004) Blood , vol.103 , pp. 3271-3277
    • Alsina, M.1    Fonseca, R.2    Wilson, E.F.3    Belle, A.N.4    Gerbino, E.5    Price-Troska, T.6    Overton, R.M.7    Ahmann, G.8    Bruzek, L.M.9    Adjei, A.A.10
  • 196
    • 20044393284 scopus 로고    scopus 로고
    • Intermittent dosing of the farnesyl transferase inhibitor tipifarnib (R115777) in advanced malignant solid tumors: A phase I California Cancer Consortium trial
    • Lara, P. N., Jr., L. Y. Law, J. J. Wright, P. Frankel, P. Twardowski, H. J. Lenz, D. H. Lau, T. Kawaguchi, P. H. Gumerlock, J. H. Doroshow, et al. 2005. Intermittent dosing of the farnesyl transferase inhibitor tipifarnib (R115777) in advanced malignant solid tumors: a phase I California Cancer Consortium trial. Anticancer Drugs. 16: 317-321.
    • (2005) Anticancer Drugs. , vol.16 , pp. 317-321
    • Lara Jr., P.N.1    Law, L.Y.2    Wright, J.J.3    Frankel, P.4    Twardowski, P.5    Lenz, H.J.6    Lau, D.H.7    Kawaguchi, T.8    Gumerlock, P.H.9    Doroshow, J.H.10
  • 197
    • 17144361932 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitor therapy in acute myelogenous leukemia
    • Gotlib, J. 2005. Farnesyltransferase inhibitor therapy in acute myelogenous leukemia. Curr. Hematol. Rep. 4: 77-84.
    • (2005) Curr. Hematol. Rep. , vol.4 , pp. 77-84
    • Gotlib, J.1
  • 205
    • 10744228789 scopus 로고    scopus 로고
    • A phase I, pharmacokinetic, and biological study of the farnesyltransferase inhibitor tipifarnib in combination with gemcitabine in patients with advanced malignancies
    • Patnaik, A., S. G. Eckhardt, E. Izbicka, A. A. Tolcher, L. A. Hammond, C. H. Takimoto, G. Schwartz, H. McCreery, A. Goetz, M. Mori, et al. 2003. A phase I, pharmacokinetic, and biological study of the farnesyltransferase inhibitor tipifarnib in combination with gemcitabine in patients with advanced malignancies. Clin. Cancer Res. 9: 4761-4771.
    • (2003) Clin. Cancer Res. , vol.9 , pp. 4761-4771
    • Patnaik, A.1    Eckhardt, S.G.2    Izbicka, E.3    Tolcher, A.A.4    Hammond, L.A.5    Takimoto, C.H.6    Schwartz, G.7    McCreery, H.8    Goetz, A.9    Mori, M.10
  • 209
    • 7444232526 scopus 로고    scopus 로고
    • New targets for therapy in breast cancer: Farnesyltransferase inhibitors
    • Head, J., and S. R. Johnston. 2004. New targets for therapy in breast cancer: farnesyltransferase inhibitors. Breast Cancer Res. 6: 262-268.
    • (2004) Breast Cancer Res. , vol.6 , pp. 262-268
    • Head, J.1    Johnston, S.R.2
  • 211
    • 1942502426 scopus 로고    scopus 로고
    • A phase I pharmacokinetic and pharmacodynamic study of the farnesyl transferase inhibitor BMS-214662 in combination with cisplatin in patients with advanced solid tumors
    • Mackay, H. J., R. Hoekstra, F. A. Eskens, W. J. Loos, D. Crawford, M. Voi, A. Van Vreckem, T. R. Evans, and J. Verweij. 2004. A phase I pharmacokinetic and pharmacodynamic study of the farnesyl transferase inhibitor BMS-214662 in combination with cisplatin in patients with advanced solid tumors. Clin. Cancer Res. 10: 2636-2644.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 2636-2644
    • Mackay, H.J.1    Hoekstra, R.2    Eskens, F.A.3    Loos, W.J.4    Crawford, D.5    Voi, M.6    Van Vreckem, A.7    Evans, T.R.8    Verweij, J.9
  • 212
    • 20144386665 scopus 로고    scopus 로고
    • A phase I trial of the novel farnesyl protein transferase inhibitor, BMS-214662, in combination with paclitaxel and carboplatin in patients with advanced cancer
    • Dy, G. K., L. M. Bruzek, G. A. Croghan, S. Mandrekar, C. Erlichman, P. Peethambaram, H. C. Pitot, L. J. Hanson, J. M. Reid, A. Furth, et al. 2005. A phase I trial of the novel farnesyl protein transferase inhibitor, BMS-214662, in combination with paclitaxel and carboplatin in patients with advanced cancer. Clin. Cancer Res. 11: 1877-1883.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 1877-1883
    • Dy, G.K.1    Bruzek, L.M.2    Croghan, G.A.3    Mandrekar, S.4    Erlichman, C.5    Peethambaram, P.6    Pitot, H.C.7    Hanson, L.J.8    Reid, J.M.9    Furth, A.10
  • 215
    • 20244375849 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of weekly 1-hour and 24-hour infusion BMS-214662, a farnesyltransferase inhibitor, in patients with advanced solid tumors
    • Tabernero, J., F. Rojo, I. Marimon, M. Voi, J. Albanell, M. Guix, F. Vazquez, J. Carulla, M. Cooper, J. Andreu, et al. 2005. Phase I pharmacokinetic and pharmacodynamic study of weekly 1-hour and 24-hour infusion BMS-214662, a farnesyltransferase inhibitor, in patients with advanced solid tumors. J. Clin. Oncol. 23: 2521-2533.
    • (2005) J. Clin. Oncol. , vol.23 , pp. 2521-2533
    • Tabernero, J.1    Rojo, F.2    Marimon, I.3    Voi, M.4    Albanell, J.5    Guix, M.6    Vazquez, F.7    Carulla, J.8    Cooper, M.9    Andreu, J.10
  • 219
    • 18844469801 scopus 로고    scopus 로고
    • Preclinical and clinical pharmacodynamic assessment of L-778,123, a dual inhibitor of farnesyl:protein transferase and geranylgeranyl:protein transferase type-I
    • Lobell, R. B., D. Liu, C. A. Buser, J. P. Davide, E. DePuy, K. Hamilton, K. S. Koblan, Y. Lee, S. Mosser, S. L. Motzel, et al. 2002. Preclinical and clinical pharmacodynamic assessment of L-778,123, a dual inhibitor of farnesyl:protein transferase and geranylgeranyl:protein transferase type-I. Mol. Cancer Ther. 1: 747-758.
    • (2002) Mol. Cancer Ther. , vol.1 , pp. 747-758
    • Lobell, R.B.1    Liu, D.2    Buser, C.A.3    Davide, J.P.4    DePuy, E.5    Hamilton, K.6    Koblan, K.S.7    Lee, Y.8    Mosser, S.9    Motzel, S.L.10
  • 220
    • 13144296650 scopus 로고    scopus 로고
    • Microarray analysis reveals genetic pathways modulated by tipifarnib in acute myeloid leukemia
    • Raponi, M., R. T. Belly, J. E. Karp, J. E. Lancet, D. Atkins, and Y. Wang. 2004. Microarray analysis reveals genetic pathways modulated by tipifarnib in acute myeloid leukemia. BMC Cancer. 4: 56-68.
    • (2004) BMC Cancer , vol.4 , pp. 56-68
    • Raponi, M.1    Belly, R.T.2    Karp, J.E.3    Lancet, J.E.4    Atkins, D.5    Wang, Y.6


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