메뉴 건너뛰기




Volumn 9, Issue 12, 2003, Pages 4494-4504

Anti-leukemia effect of perillyl alcohol in Bcr/Abl-transformed cells indirectly inhibits signaling through Mek in a Ras- and Raf-independent fashion

Author keywords

[No Author keywords available]

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; BCR ABL PROTEIN; MEVINOLIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE KINASE; PERILLYL ALCOHOL;

EID: 0141925956     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (28)

References (80)
  • 1
    • 0031900740 scopus 로고    scopus 로고
    • Signal transduction through MAP kinase cascades
    • Lewis, T. S., Shapiro, P. S., and Ahn, N. G. Signal transduction through MAP kinase cascades. Adv. Cancer Res., 74: 49-139, 1998.
    • (1998) Adv. Cancer Res. , vol.74 , pp. 49-139
    • Lewis, T.S.1    Shapiro, P.S.2    Ahn, N.G.3
  • 2
    • 0024376173 scopus 로고
    • ras oncogenes in human cancer: A review
    • Bos, J. L. ras oncogenes in human cancer: a review. Cancer Res., 49: 4682-4689, 1989.
    • (1989) Cancer Res. , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 3
    • 0025240615 scopus 로고
    • The pattern of mutational involvement of RAS genes in human hematologic malignancies determined by DNA amplification and direct sequencing
    • Ahuja, H. G., Foti, A., Bar-Eli, M., and Cline, M. J. The pattern of mutational involvement of RAS genes in human hematologic malignancies determined by DNA amplification and direct sequencing. Blood, 75: 1684-1690, 1990.
    • (1990) Blood , vol.75 , pp. 1684-1690
    • Ahuja, H.G.1    Foti, A.2    Bar-Eli, M.3    Cline, M.J.4
  • 4
    • 0028351698 scopus 로고
    • Chronic myelomonocytic leukemia: Tel-a-kinase what Ets all about
    • Sawyers, C. L., and Denny, C. T. Chronic myelomonocytic leukemia: Tel-a-kinase what Ets all about. Cell, 77: 171-173, 1994.
    • (1994) Cell , vol.77 , pp. 171-173
    • Sawyers, C.L.1    Denny, C.T.2
  • 5
    • 0024990090 scopus 로고
    • N-ras mutations in adult de novo acute myelogenous leukemia: Prevalence and clinical significance
    • Radich, J. P., Kopecky, K. J., Willman, C. L., Weick, J., Head, D., Appelbaum, F., and Collins, S. J. N-ras mutations in adult de novo acute myelogenous leukemia: prevalence and clinical significance. Blood, 76: 801-807, 1990.
    • (1990) Blood , vol.76 , pp. 801-807
    • Radich, J.P.1    Kopecky, K.J.2    Willman, C.L.3    Weick, J.4    Head, D.5    Appelbaum, F.6    Collins, S.J.7
  • 8
    • 0024316910 scopus 로고
    • Mutations of the ras protooncogenes in chronic myelogenous leukemia: A high frequency of ras mutations in bcr/abl rearrangement-negative chronic myelogenous leukemia
    • Cogswell, P. C., Morgan, R., Dunn, M., Neubauer, A., Nelson, P., Poland-Johnston, N. K., Sandberg, A. A., and Liu, E. Mutations of the ras protooncogenes in chronic myelogenous leukemia: a high frequency of ras mutations in bcr/abl rearrangement-negative chronic myelogenous leukemia. Blood, 74: 2629-2633, 1989.
    • (1989) Blood , vol.74 , pp. 2629-2633
    • Cogswell, P.C.1    Morgan, R.2    Dunn, M.3    Neubauer, A.4    Nelson, P.5    Poland-Johnston, N.K.6    Sandberg, A.A.7    Liu, E.8
  • 9
    • 0024998851 scopus 로고
    • RAS mutations are rare events in Philadelphia chromosome-negative/bcr gene rearrangement-negative chronic myelogenous leukemia, but are prevalent in chronic myelomonocytic leukemia
    • Hirsch-Ginsberg, C., LeMaistre, A. C., Kantarjian, H., Talpaz, M., Cork, A., Freireich, E. J., Trujillo, J. M., Lee, M. S., and Stass, S. A. RAS mutations are rare events in Philadelphia chromosome-negative/bcr gene rearrangement-negative chronic myelogenous leukemia, but are prevalent in chronic myelomonocytic leukemia. Blood, 76: 1214-1219, 1990.
    • (1990) Blood , vol.76 , pp. 1214-1219
    • Hirsch-Ginsberg, C.1    LeMaistre, A.C.2    Kantarjian, H.3    Talpaz, M.4    Cork, A.5    Freireich, E.J.6    Trujillo, J.M.7    Lee, M.S.8    Stass, S.A.9
  • 10
    • 0031937682 scopus 로고    scopus 로고
    • The molecular pathophysiology of myeloid leukaemias: Ras revisited
    • Byrne, J. L., and Marshall, C. J. The molecular pathophysiology of myeloid leukaemias: Ras revisited. Br. J. Haematol., 100: 256-264, 1998.
    • (1998) Br. J. Haematol. , vol.100 , pp. 256-264
    • Byrne, J.L.1    Marshall, C.J.2
  • 11
    • 0033014304 scopus 로고    scopus 로고
    • RAS leukemia: From basic mechanisms to gene-directed therapy
    • Beaupre, D. M., and Kurzrock, R. RAS and leukemia: from basic mechanisms to gene-directed therapy. J. Clin. Oncol., 17: 1071-1079, 1999.
    • (1999) J. Clin. Oncol. , vol.17 , pp. 1071-1079
    • Beaupre, D.M.1    Kurzrock, R.2
  • 12
    • 0034284027 scopus 로고    scopus 로고
    • Targeting the Ras signaling pathway: A rational, mechanism-based treatment for hematologic malignancies?
    • Reuter, C. W., Morgan, M. A., and Bergmann, L. Targeting the Ras signaling pathway: a rational, mechanism-based treatment for hematologic malignancies?. Blood, 96: 1655-1669, 2000.
    • (2000) Blood , vol.96 , pp. 1655-1669
    • Reuter, C.W.1    Morgan, M.A.2    Bergmann, L.3
  • 13
    • 0026528368 scopus 로고
    • Abnormal regulation of mammalian p21ras contributes to malignant tumor growth in von Recklinghausen (type 1) neurofibromatosis
    • DeClue, J. E., Papageorge, A. G., Fletcher, J. A., Diehl, S. R., Ratner, N., Vass, W. C., and Lowy, D. R. Abnormal regulation of mammalian p21ras contributes to malignant tumor growth in von Recklinghausen (type 1) neurofibromatosis. Cell, 69: 265-273, 1992.
    • (1992) Cell , vol.69 , pp. 265-273
    • DeClue, J.E.1    Papageorge, A.G.2    Fletcher, J.A.3    Diehl, S.R.4    Ratner, N.5    Vass, W.C.6    Lowy, D.R.7
  • 14
    • 0026521070 scopus 로고
    • Aberrant regulation of ras proteins in malignant tumour cells from type 1 neurofibromatosis patients
    • Basu, T. N., Gutmann, D. H., Fletcher, J. A., Glover, T. W., Collins, F. S., and Downward, J. Aberrant regulation of ras proteins in malignant tumour cells from type 1 neurofibromatosis patients. Nature (Lond.), 356: 713-715, 1992.
    • (1992) Nature (Lond.) , vol.356 , pp. 713-715
    • Basu, T.N.1    Gutmann, D.H.2    Fletcher, J.A.3    Glover, T.W.4    Collins, F.S.5    Downward, J.6
  • 16
    • 0028263606 scopus 로고
    • Negative regulation of p120GAP GTPase promoting activity by p210bcr/abl: Implication for RAS-dependent Philadelphia chromosome positive cell growth
    • Skorski, T., Kanakaraj, P., Ku, D. H., Nieborowska-Skorska, M., Canaani, E., Zon, G., Perussia, B., and Calabretta, B. Negative regulation of p120GAP GTPase promoting activity by p210bcr/abl: implication for RAS-dependent Philadelphia chromosome positive cell growth. J. Exp. Med., 179: 1855-1865, 1994.
    • (1994) J. Exp. Med. , vol.179 , pp. 1855-1865
    • Skorski, T.1    Kanakaraj, P.2    Ku, D.H.3    Nieborowska-Skorska, M.4    Canaani, E.5    Zon, G.6    Perussia, B.7    Calabretta, B.8
  • 19
    • 0028950123 scopus 로고
    • Genetic requirement for Ras in the transformation of fibroblasts and hematopoietic cells by the Bcr-Abl oncogene
    • Sawyers, C. L., McLaughlin, J., and Witte, O. N. Genetic requirement for Ras in the transformation of fibroblasts and hematopoietic cells by the Bcr-Abl oncogene. J. Exp. Med., 181: 307-313, 1995.
    • (1995) J. Exp. Med. , vol.181 , pp. 307-313
    • Sawyers, C.L.1    McLaughlin, J.2    Witte, O.N.3
  • 20
    • 0024335553 scopus 로고
    • Molecular pathogenesis of Ph-positive leukemias
    • Clark, S. S., Crist, W. M., and Witte, O. N. Molecular pathogenesis of Ph-positive leukemias. Ann. Rev. Med., 40: 113-122, 1989.
    • (1989) Ann. Rev. Med. , vol.40 , pp. 113-122
    • Clark, S.S.1    Crist, W.M.2    Witte, O.N.3
  • 21
    • 0029589929 scopus 로고
    • The Bcr-Abl leukemia oncogene activates Jun kinase and requires Jun for transformation
    • Raitano, A. B., Halpern, J. R., Hambuch, T. M., and Sawyers, C. L. The Bcr-Abl leukemia oncogene activates Jun kinase and requires Jun for transformation. Proc. Natl. Acad. Sci. USA, 92: 11746-11750, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11746-11750
    • Raitano, A.B.1    Halpern, J.R.2    Hambuch, T.M.3    Sawyers, C.L.4
  • 22
    • 0028559163 scopus 로고
    • A temperature sensitive p210 BCR-ABL mutant defines the primary consequences of BCR-ABL tyrosine kinase expression in growth factor dependent cells
    • Kabarowski, J. H., Allen, P. B., and Wiedemann, L. M. A temperature sensitive p210 BCR-ABL mutant defines the primary consequences of BCR-ABL tyrosine kinase expression in growth factor dependent cells. EMBO J., 13: 5887-5895, 1994.
    • (1994) EMBO J. , vol.13 , pp. 5887-5895
    • Kabarowski, J.H.1    Allen, P.B.2    Wiedemann, L.M.3
  • 24
    • 0035298060 scopus 로고    scopus 로고
    • Role of ERK activation in growth and erythroid differentiation of K562 cells
    • Woessmann, W., and Mivechi, N. F. Role of ERK activation in growth and erythroid differentiation of K562 cells. Exp. Cell Res., 264: 193-200, 2001.
    • (2001) Exp. Cell Res. , vol.264 , pp. 193-200
    • Woessmann, W.1    Mivechi, N.F.2
  • 25
    • 0034001970 scopus 로고    scopus 로고
    • The inhibition of ERK/MAPK not the activation of JNK/SAPK is primarily required to induce apoptosis in chronic myelogenous leukemic K562 cells
    • Kang, C. D., Yoo, S. D., Hwang, B. W., Kim, K. W., Kim, D. W., Kim, C. M., Kim, S. H., and Chung, B. S. The inhibition of ERK/MAPK not the activation of JNK/SAPK is primarily required to induce apoptosis in chronic myelogenous leukemic K562 cells. Leuk. Res., 24: 527-534, 2000.
    • (2000) Leuk. Res. , vol.24 , pp. 527-534
    • Kang, C.D.1    Yoo, S.D.2    Hwang, B.W.3    Kim, K.W.4    Kim, D.W.5    Kim, C.M.6    Kim, S.H.7    Chung, B.S.8
  • 26
    • 0035313251 scopus 로고    scopus 로고
    • In vitro cytotoxic effects of a tyrosine kinase inhibitor STI571 in combination with commonly used antileukemic agents
    • Kano, Y., Akutsu, M., Tsunoda, S., Mano, H., Sato, Y., Honma, Y., and Furukawa, Y. In vitro cytotoxic effects of a tyrosine kinase inhibitor STI571 in combination with commonly used antileukemic agents. Blood, 97: 1999-2007, 2001,
    • (2001) Blood , vol.97 , pp. 1999-2007
    • Kano, Y.1    Akutsu, M.2    Tsunoda, S.3    Mano, H.4    Sato, Y.5    Honma, Y.6    Furukawa, Y.7
  • 27
    • 0034665903 scopus 로고    scopus 로고
    • CGP57148B (STI-571) induces differentiation and apoptosis and sensitizes Bcr-Abl-positive human leukemia cells to apoptosis due to antileukemic drugs
    • Fang, G., Kim, C. N., Perkins, C. L., Ramadevi, N., Winton, E., Wittmann, S., and Bhalla, K. N. CGP57148B (STI-571) induces differentiation and apoptosis and sensitizes Bcr-Abl-positive human leukemia cells to apoptosis due to antileukemic drugs. Blood, 96: 2246-2253, 2000.
    • (2000) Blood , vol.96 , pp. 2246-2253
    • Fang, G.1    Kim, C.N.2    Perkins, C.L.3    Ramadevi, N.4    Winton, E.5    Wittmann, S.6    Bhalla, K.N.7
  • 29
    • 0035810142 scopus 로고    scopus 로고
    • Activity of a specific inhibitor of the BCR-ABL tyrosine kinase in the blast crisis of chronic myeloid leukemia and acute lymphoblastic leukemia with the Philadelphia chromosome
    • Druker, B. J., Sawyers, C. L., Kantarjian, H., Resta, D. J., Reese, S. F., Ford, J. M., Capdeville, R., and Talpaz, M. Activity of a specific inhibitor of the BCR-ABL tyrosine kinase in the blast crisis of chronic myeloid leukemia and acute lymphoblastic leukemia with the Philadelphia chromosome. N. Engl. J. Med., 344: 1038-1042, 2001.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1038-1042
    • Druker, B.J.1    Sawyers, C.L.2    Kantarjian, H.3    Resta, D.J.4    Reese, S.F.5    Ford, J.M.6    Capdeville, R.7    Talpaz, M.8
  • 31
    • 0034868659 scopus 로고    scopus 로고
    • Signal transduction inhibition: Results from phase I clinical trials in chronic myeloid leukemia
    • Druker, B. Signal transduction inhibition: results from phase I clinical trials in chronic myeloid leukemia. Semin. Hematol., 38: 9-14, 2001.
    • (2001) Semin. Hematol. , vol.38 , pp. 9-14
    • Druker, B.1
  • 32
    • 0035800507 scopus 로고    scopus 로고
    • Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification
    • Gorre, M. E., Mohammed, M., Ellwood, K., Hsu, N., Paquette, R., Rao, P. N., and Sawyers, C. L. Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification, Science (Wash. DC), 293: 876-880, 2001.
    • (2001) Science (Wash. DC) , vol.293 , pp. 876-880
    • Gorre, M.E.1    Mohammed, M.2    Ellwood, K.3    Hsu, N.4    Paquette, R.5    Rao, P.N.6    Sawyers, C.L.7
  • 33
    • 0028928294 scopus 로고
    • Induction of apoptosis in liver tumors by the monoterpene perillyl alcohol
    • Mills, J. J., Chari, R. S., Boyer, I. J., Gould, M. N., and Jirtle, R. L. Induction of apoptosis in liver tumors by the monoterpene perillyl alcohol. Cancer Res., 55: 979-983, 1995.
    • (1995) Cancer Res. , vol.55 , pp. 979-983
    • Mills, J.J.1    Chari, R.S.2    Boyer, I.J.3    Gould, M.N.4    Jirtle, R.L.5
  • 34
    • 0026636635 scopus 로고
    • Limonene-induced regression of mammary carcinomas
    • Haag, J. D., Lindstrom, M. J., and Gould, M. N. Limonene-induced regression of mammary carcinomas. Cancer Res., 52: 4021-4026, 1992,
    • (1992) Cancer Res. , vol.52 , pp. 4021-4026
    • Haag, J.D.1    Lindstrom, M.J.2    Gould, M.N.3
  • 35
    • 0029132661 scopus 로고
    • Chemotherapy of pancreatic cancer with the monoterpene perillyl alcohol
    • Stark, M. J., Burke, Y. D., McKinzie, J. H., Ayoubi, A. S., and Crowell, P. L. Chemotherapy of pancreatic cancer with the monoterpene perillyl alcohol. Cancer Lett., 96: 15-21, 1995.
    • (1995) Cancer Lett. , vol.96 , pp. 15-21
    • Stark, M.J.1    Burke, Y.D.2    McKinzie, J.H.3    Ayoubi, A.S.4    Crowell, P.L.5
  • 37
    • 0031427722 scopus 로고    scopus 로고
    • Induction of the apoptosis-promoting protein Bak by perillyl alcohol in pancreatic ductal adenocarcinoma relative to untransformed ductal epithelial cells
    • Stayrook, K. R., McKinzie, J. H., Burke, Y. D., Burke, Y. A., and Crowell, P. L. Induction of the apoptosis-promoting protein Bak by perillyl alcohol in pancreatic ductal adenocarcinoma relative to untransformed ductal epithelial cells. Carcinogenesis (Lond.), 18: 1655-1658, 1997.
    • (1997) Carcinogenesis (Lond.) , vol.18 , pp. 1655-1658
    • Stayrook, K.R.1    McKinzie, J.H.2    Burke, Y.D.3    Burke, Y.A.4    Crowell, P.L.5
  • 38
    • 0032519560 scopus 로고    scopus 로고
    • Inhibitory effects of perillyl alcohol on UVB-induced murine skin cancer and AP-1 transactivation
    • Barthelman, M., Chen, W., Gensler, H. L., Huang, C., Dong, Z., and Bowden, G. T. Inhibitory effects of perillyl alcohol on UVB-induced murine skin cancer and AP-1 transactivation. Cancer Res., 58: 711-716, 1998.
    • (1998) Cancer Res. , vol.58 , pp. 711-716
    • Barthelman, M.1    Chen, W.2    Gensler, H.L.3    Huang, C.4    Dong, Z.5    Bowden, G.T.6
  • 39
    • 0026497014 scopus 로고
    • Identification of metabolites of the antitumor agent d-limonene capable of inhibiting protein isoprenylation and cell growth
    • Crowell, P. L., Lin, S., Vedejs, E., and Gould, M. N. Identification of metabolites of the antitumor agent d-limonene capable of inhibiting protein isoprenylation and cell growth. Cancer Chemother. Pharmacol., 31: 205-212, 1992.
    • (1992) Cancer Chemother. Pharmacol. , vol.31 , pp. 205-212
    • Crowell, P.L.1    Lin, S.2    Vedejs, E.3    Gould, M.N.4
  • 40
    • 0028158306 scopus 로고
    • Inhibition of ubiquinone and cholesterol synthesis by the monoterpene perillyl alcohol
    • Ren, Z., and Gould, M. N. Inhibition of ubiquinone and cholesterol synthesis by the monoterpene perillyl alcohol. Cancer Lett., 76: 185-190, 1994.
    • (1994) Cancer Lett. , vol.76 , pp. 185-190
    • Ren, Z.1    Gould, M.N.2
  • 41
    • 0028343655 scopus 로고
    • Structure-activity relationships among monoterpene inhibitors of protein isoprenylation and cell proliferation
    • Crowell, P. L., Ren, Z., Lin, S., Vedejs, E., and Gould, M. N. Structure-activity relationships among monoterpene inhibitors of protein isoprenylation and cell proliferation. Biochem. Pharmacol., 47: 1405-1415, 1994.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 1405-1415
    • Crowell, P.L.1    Ren, Z.2    Lin, S.3    Vedejs, E.4    Gould, M.N.5
  • 42
    • 0029055687 scopus 로고
    • The inhibition of protein prenyltransferases by oxygenated metabolites of limonene and perillyl alcohol
    • Gelb, M. H., Tamanoi, F., Yokoyama, K., Ghomashchi, F., Esson, K., and Gould, M. N. The inhibition of protein prenyltransferases by oxygenated metabolites of limonene and perillyl alcohol. Cancer Lett., 91: 169-175, 1995.
    • (1995) Cancer Lett. , vol.91 , pp. 169-175
    • Gelb, M.H.1    Tamanoi, F.2    Yokoyama, K.3    Ghomashchi, F.4    Esson, K.5    Gould, M.N.6
  • 43
    • 0025952954 scopus 로고
    • Selective inhibition of isoprenylation of 21-26-kDa proteins by the anticarcinogen D-limonene and its metabolites
    • Crowell, P. L., Chang, R. R., Ren, Z. B., Elson, C. E., and Gould, M. N. Selective inhibition of isoprenylation of 21-26-kDa proteins by the anticarcinogen D-limonene and its metabolites. J. Biol. Chem., 266: 17679-17685, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17679-17685
    • Crowell, P.L.1    Chang, R.R.2    Ren, Z.B.3    Elson, C.E.4    Gould, M.N.5
  • 44
    • 0027952748 scopus 로고
    • Prenylated proteins and lymphocyte proliferation: Inhibition by d-limonene related monoterpenes
    • Schulz, S., Buhling, F., and Ansorge, S. Prenylated proteins and lymphocyte proliferation: inhibition by d-limonene related monoterpenes. Eur. J. Immunol., 24: 301-307, 1994.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 301-307
    • Schulz, S.1    Buhling, F.2    Ansorge, S.3
  • 45
    • 0031841099 scopus 로고    scopus 로고
    • Effects of the antitumor agent perillyl alcohol on H-Ras vs. K-Ras farnesylation and signal transduction in pancreatic cells
    • Stayrook, K. R., McKinzie, J. H., Barbhaiya, L. H., and Crowell, P. L. Effects of the antitumor agent perillyl alcohol on H-Ras vs. K-Ras farnesylation and signal transduction in pancreatic cells. Anticancer Res., 18: 823-828, 1998.
    • (1998) Anticancer Res. , vol.18 , pp. 823-828
    • Stayrook, K.R.1    McKinzie, J.H.2    Barbhaiya, L.H.3    Crowell, P.L.4
  • 46
  • 47
    • 0029455962 scopus 로고
    • Prevention and therapy of mammary cancer by monoterpenes
    • Gould, M. N. Prevention and therapy of mammary cancer by monoterpenes. J. Cell. Biochem., (Suppl. 22): 139-144, 1995.
    • (1995) J. Cell. Biochem. , Issue.SUPPL. 22 , pp. 139-144
    • Gould, M.N.1
  • 49
    • 0032827382 scopus 로고    scopus 로고
    • Perillyl alcohol selectively induces G0/G1 arrest and apoptosis in Bcr/Abl-transformed myeloid cell lines
    • Sahin, M. B., Perman, S. M., Jenkins, G., and Clark, S. S. Perillyl alcohol selectively induces G0/G1 arrest and apoptosis in Bcr/Abl-transformed myeloid cell lines. Leukemia (Baltimore), 13: 1581-1591, 1999.
    • (1999) Leukemia (Baltimore) , vol.13 , pp. 1581-1591
    • Sahin, M.B.1    Perman, S.M.2    Jenkins, G.3    Clark, S.S.4
  • 50
    • 0029131231 scopus 로고
    • BCR-ABL-mediated inhibition of apoptosis with delay of G2/M transition after DNA damage: A mechanism of resistance to multiple anticancer agents
    • Bedi, A., Barber, J. P., Bedi, G. C., el-Deiry, W. S., Sidransky, D., Vala, M. S., Akhtar, A. J., Hilton, J., and Jones, R. J. BCR-ABL-mediated inhibition of apoptosis with delay of G2/M transition after DNA damage: a mechanism of resistance to multiple anticancer agents. Blood, 86: 1148-1158, 1995.
    • (1995) Blood , vol.86 , pp. 1148-1158
    • Bedi, A.1    Barber, J.P.2    Bedi, G.C.3    El-Deiry, W.S.4    Sidransky, D.5    Vala, M.S.6    Akhtar, A.J.7    Hilton, J.8    Jones, R.J.9
  • 52
    • 0023133732 scopus 로고
    • Unique forms of the abl tyrosine kinase distinguish Ph1-positive CML from Ph1-positive ALL
    • Clark, S. S., McLaughlin, J., Crist, W. M., Champlin, R., and Witte, O. N. Unique forms of the abl tyrosine kinase distinguish Ph1-positive CML from Ph1-positive ALL. Science (Wash. DC), 235: 85-88, 1987.
    • (1987) Science (Wash. DC) , vol.235 , pp. 85-88
    • Clark, S.S.1    McLaughlin, J.2    Crist, W.M.3    Champlin, R.4    Witte, O.N.5
  • 54
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., Reddy, H., Caivano, M., and Cohen, P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J., 351: 95-105, 2000.
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 55
    • 0036172970 scopus 로고    scopus 로고
    • Antileukemia activity ofperillyl alcohol (POH): Uncoupling apoptosis from G0/G1 arrest suggests that the primary effect of POH on Bcr/Abl transformed cells is to induce growth arrest
    • Clark, S. S., Perman, S. M., Sahin, M. B., Jenkins, G., and Elegbede, J. A. Antileukemia activity ofperillyl alcohol (POH): Uncoupling apoptosis from G0/G1 arrest suggests that the primary effect of POH on Bcr/Abl transformed cells is to induce growth arrest. Leukemia (Baltimore), 16: 213-222, 2002.
    • (2002) Leukemia (Baltimore) , vol.16 , pp. 213-222
    • Clark, S.S.1    Perman, S.M.2    Sahin, M.B.3    Jenkins, G.4    Elegbede, J.A.5
  • 56
    • 0030757145 scopus 로고    scopus 로고
    • Inhibition of type I and type II geranylgeranyl-protein transferases by the monoterpene perillyl alcohol in NIH3T3 cells
    • Ren, Z., Elson, C. E., and Gould, M. N. Inhibition of type I and type II geranylgeranyl-protein transferases by the monoterpene perillyl alcohol in NIH3T3 cells. Biochem. Pharmacol., 54: 113-120, 1997.
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 113-120
    • Ren, Z.1    Elson, C.E.2    Gould, M.N.3
  • 57
    • 0028152845 scopus 로고
    • In vivo antitumor activity of herbimycin A. a tyrosine kinase inhibitor, targeted against BCR/ABL oncoprotein in mice bearing BCR/ABL-transfected cells
    • Okabe, M., Uehara, Y., Noshima, T., Itaya, T., Kunieda, Y., and Kurosawa, M. In vivo antitumor activity of herbimycin A. a tyrosine kinase inhibitor, targeted against BCR/ABL oncoprotein in mice bearing BCR/ABL-transfected cells. Leuk. Res., 18: 867-873, 1994.
    • (1994) Leuk. Res. , vol.18 , pp. 867-873
    • Okabe, M.1    Uehara, Y.2    Noshima, T.3    Itaya, T.4    Kunieda, Y.5    Kurosawa, M.6
  • 58
    • 0031819425 scopus 로고    scopus 로고
    • Modulation of small G protein isoprenylation by anticancer monoterpenes in in situ mammary gland epithelial cells
    • Ren, Z., and Gould, M. N. Modulation of small G protein isoprenylation by anticancer monoterpenes in in situ mammary gland epithelial cells. Carcinogenesis (Lond.), 19: 827-832, 1998.
    • (1998) Carcinogenesis (Lond.) , vol.19 , pp. 827-832
    • Ren, Z.1    Gould, M.N.2
  • 59
    • 0021711754 scopus 로고
    • Metabolic turnover of human c-rasH p21 protein of EJ bladder carcinoma and its normal cellular and viral homologs
    • Ulsh, L. S., and Shih, T. Y. Metabolic turnover of human c-rasH p21 protein of EJ bladder carcinoma and its normal cellular and viral homologs. Mol. Cell. Biol., 4: 1647-1652, 1984.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1647-1652
    • Ulsh, L.S.1    Shih, T.Y.2
  • 60
    • 0027965512 scopus 로고
    • Mammary carcinoma regression induced by perillyl alcohol, a hydroxylated analog of limonene
    • Haag, J. D., and Gould, M. N. Mammary carcinoma regression induced by perillyl alcohol, a hydroxylated analog of limonene. Cancer Chemother. Pharmacol., 34: 477-483, 1994.
    • (1994) Cancer Chemother. Pharmacol. , vol.34 , pp. 477-483
    • Haag, J.D.1    Gould, M.N.2
  • 63
    • 0030725775 scopus 로고    scopus 로고
    • The Bcr-Abl tyrosine kinase activates mitogenic signaling pathways and stimulates G1-to-S phase transition in hematopoietic cells
    • Cortez, D., Reuther, G., and Pendergast, A. M. The Bcr-Abl tyrosine kinase activates mitogenic signaling pathways and stimulates G1-to-S phase transition in hematopoietic cells. Oncogene, 15: 2333-2342, 1997.
    • (1997) Oncogene , vol.15 , pp. 2333-2342
    • Cortez, D.1    Reuther, G.2    Pendergast, A.M.3
  • 64
    • 0036142963 scopus 로고    scopus 로고
    • Pharmacologic mitogen-activated protein/extracellular signal-regulated kinase kinase/mitogen-activated protein kinase inhibitors interact synergistically with STI571 to induce apoptosis in Bcr/Abl-expressing human leukemia cells
    • Yu, C., Krystal, G., Varticovksi, L., McKinstry, R., Rahmani, M., Dent, P., and Grant, S. Pharmacologic mitogen-activated protein/extracellular signal-regulated kinase kinase/mitogen-activated protein kinase inhibitors interact synergistically with STI571 to induce apoptosis in Bcr/Abl-expressing human leukemia cells. Cancer Res., 62: 188-199, 2002.
    • (2002) Cancer Res. , vol.62 , pp. 188-199
    • Yu, C.1    Krystal, G.2    Varticovksi, L.3    McKinstry, R.4    Rahmani, M.5    Dent, P.6    Grant, S.7
  • 65
    • 0032526544 scopus 로고    scopus 로고
    • Expression of constitutively active Raf-1 in the mitochondria restores antiapoptotic and leukemogenic potential of a transformation-deficient BCR/ABL mutant
    • Salomoni, P., Wasik, M. A., Riedel, R. F., Reiss, K., Choi, J. K., Skorski, T., and Calabretta, B. Expression of constitutively active Raf-1 in the mitochondria restores antiapoptotic and leukemogenic potential of a transformation-deficient BCR/ABL mutant. J. Exp. Med., 187: 1995-2007, 1998.
    • (1998) J. Exp. Med. , vol.187 , pp. 1995-2007
    • Salomoni, P.1    Wasik, M.A.2    Riedel, R.F.3    Reiss, K.4    Choi, J.K.5    Skorski, T.6    Calabretta, B.7
  • 66
    • 0033959620 scopus 로고    scopus 로고
    • The survival function of the Bcr-Abl oncogene is mediated by Bad-dependent and -independent pathways: Roles for phosphatidylinositol 3-kinase and Raf
    • Neshat, M. S., Raitano, A. B., Wang, H. G., Reed, J. C., and Sawyers, C. L. The survival function of the Bcr-Abl oncogene is mediated by Bad-dependent and -independent pathways: roles for phosphatidylinositol 3-kinase and Raf. Mol. Cell. Biol., 20: 1179-1186, 2000.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1179-1186
    • Neshat, M.S.1    Raitano, A.B.2    Wang, H.G.3    Reed, J.C.4    Sawyers, C.L.5
  • 67
    • 0029955970 scopus 로고    scopus 로고
    • Interdependent domains controlling the enzymatic activity of mitogen-activated protein kinase kinase 1
    • Mansour, S. J., Candia, J. M., Matsuura, J. E., Manning, M. C., and Ahn, N. G. Interdependent domains controlling the enzymatic activity of mitogen-activated protein kinase kinase 1. Biochemistry, 35: 15529-15536, 1996.
    • (1996) Biochemistry , vol.35 , pp. 15529-15536
    • Mansour, S.J.1    Candia, J.M.2    Matsuura, J.E.3    Manning, M.C.4    Ahn, N.G.5
  • 68
    • 0031939937 scopus 로고    scopus 로고
    • Feedback regulation of Raf-1 and mitogen-activated protein kinase (MAP) kinase kinases 1 and 2 by MAP kinase phosphatase-1 (MKP-1)
    • Shapiro, P. S., and Ahn, N. G. Feedback regulation of Raf-1 and mitogen-activated protein kinase (MAP) kinase kinases 1 and 2 by MAP kinase phosphatase-1 (MKP-1). J. Biol. Chem., 273: 1788-1793, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1788-1793
    • Shapiro, P.S.1    Ahn, N.G.2
  • 70
    • 0027936410 scopus 로고
    • Simian virus 40 small t antigen cooperates with mitogen-activated kinases to stimulate AP-1 activity
    • Frost, J. A., Alberts, A. S., Sontag, E., Guan, K., Mumby, M. C., and Feramisco, J. R. Simian virus 40 small t antigen cooperates with mitogen-activated kinases to stimulate AP-1 activity. Mol. Cell. Biol., 14: 6244-6252, 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6244-6252
    • Frost, J.A.1    Alberts, A.S.2    Sontag, E.3    Guan, K.4    Mumby, M.C.5    Feramisco, J.R.6
  • 71
    • 0027772552 scopus 로고
    • The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation
    • Sontag, E., Fedorov, S., Kamibayashi, C., Robbins, D., Cobb, M., and Mumby, M. The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation. Cell, 75: 887-897, 1993.
    • (1993) Cell , vol.75 , pp. 887-897
    • Sontag, E.1    Fedorov, S.2    Kamibayashi, C.3    Robbins, D.4    Cobb, M.5    Mumby, M.6
  • 72
    • 0035058697 scopus 로고    scopus 로고
    • Inhibition of protein phosphatase PP1 in GH3B6, but not in GH3 cells, activates the MEK/ ERK/c-fos pathway and the human prolactin promoter, involving the coactivator CPB/p300
    • Manfroid, I., Martial, J. A., and Muller, M. Inhibition of protein phosphatase PP1 in GH3B6, but not in GH3 cells, activates the MEK/ ERK/c-fos pathway and the human prolactin promoter, involving the coactivator CPB/p300. Mol. Endocrinol., 15: 625-637, 2001.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 625-637
    • Manfroid, I.1    Martial, J.A.2    Muller, M.3
  • 73
    • 0025181418 scopus 로고
    • Okadaic acid: A new probe for the study of cellular regulation
    • Cohen, P., Holmes, C. F., and Tsukitani, Y. Okadaic acid: a new probe for the study of cellular regulation. Trends Biochem. Sci., 15: 98-102, 1990.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 98-102
    • Cohen, P.1    Holmes, C.F.2    Tsukitani, Y.3
  • 74
    • 0023691731 scopus 로고
    • Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics
    • Bialojan, C., and Takai, A. Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics. Biochem. J., 256: 283-290, 1988.
    • (1988) Biochem. J. , vol.256 , pp. 283-290
    • Bialojan, C.1    Takai, A.2
  • 75
    • 0035056221 scopus 로고    scopus 로고
    • Scaffold protein regulation of mitogen-activated protein kinase cascade
    • W. Balch, C. J. Der, and A. Hall (eds.). New York: Academic Press
    • Catling, A. D., Eblen, S. T., Schaeffer, H. J., and Weber, M. J. Scaffold protein regulation of mitogen-activated protein kinase cascade. In: W. Balch, C. J. Der, and A. Hall (eds.), Regulators and Effectors of Small GTPases, Part F: Ras Family I, Vol. 332, pp. 368-387. New York: Academic Press, 2001.
    • (2001) Regulators and Effectors of Small GTPases, Part F: Ras Family I , vol.332 , pp. 368-387
    • Catling, A.D.1    Eblen, S.T.2    Schaeffer, H.J.3    Weber, M.J.4
  • 76
    • 0031974812 scopus 로고    scopus 로고
    • Regulation of the MAP kinase pathway by mammalian Ksr through direct interaction with MEK and ERK
    • Yu, W., Fantl, W. J., Harrowe, G., and Williams, L. T. Regulation of the MAP kinase pathway by mammalian Ksr through direct interaction with MEK and ERK. Curr. Biol., 8: 56-64, 1998.
    • (1998) Curr. Biol. , vol.8 , pp. 56-64
    • Yu, W.1    Fantl, W.J.2    Harrowe, G.3    Williams, L.T.4
  • 79
    • 0030946366 scopus 로고    scopus 로고
    • Hyperexpression of mitogen-activated protein kinase in human breast cancer
    • Sivaraman, V. S., Wang, H., Nuovo, G. J., and Malbon, C. C. Hyperexpression of mitogen-activated protein kinase in human breast cancer. J. Clin. Invest., 99: 1478-1483, 1997.
    • (1997) J. Clin. Invest. , vol.99 , pp. 1478-1483
    • Sivaraman, V.S.1    Wang, H.2    Nuovo, G.J.3    Malbon, C.C.4
  • 80
    • 0031769940 scopus 로고    scopus 로고
    • In situ visualization of intratumor growth factor signaling: Immunohistochemical localization of activated ERK/MAP kinase in glial neoplasms
    • Mandell, J. W., Hussaini, I. M., Zecevic, M., Weber, M. J., and VandenBerg, S. R. In situ visualization of intratumor growth factor signaling: immunohistochemical localization of activated ERK/MAP kinase in glial neoplasms. Am. J. Pathol., 153: 1411-1423, 1998.
    • (1998) Am. J. Pathol. , vol.153 , pp. 1411-1423
    • Mandell, J.W.1    Hussaini, I.M.2    Zecevic, M.3    Weber, M.J.4    VandenBerg, S.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.