메뉴 건너뛰기




Volumn 1, Issue 3, 2006, Pages 311-332

Cyclin dependent kinases as targets for cancer therapy

Author keywords

Bryostatin; Cell cycle; Cyclin; Cyclin dependent kinases; Flavopiridol; Programmed cell death; Restriction point; UCN 01

Indexed keywords

7 HYDROXYSTAUROSPORINE; ANTIDIARRHEAL AGENT; BRYOSTATIN; CAMPTOTHECIN; CAMPTOTHECIN DERIVATIVE; CISPLATIN; COLCHICINE; CREATININE; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 4; CYCLIN DEPENDENT KINASE INHIBITOR; CYCLINE; CYTOTOXIC AGENT; FLAVOPIRIDOL; FLUOROURACIL; GEMCITABINE; IMIDAZOPYRIDINE DERIVATIVE; INDISULAM; IRINOTECAN; N [5 (5 TERT BUTYL 2 OXAZOLYLMETHYLTHIO) 2 THIAZOLYL]ISONIPECOTAMIDE; OLOMOUCINE; PACLITAXEL; PD 0332991; PODOPHYLLOTOXIN; ROSCOVITINE; TAXANE DERIVATIVE; TOPOTECAN; UNCLASSIFIED DRUG; VINCA ALKALOID;

EID: 33748577701     PISSN: 1872115X     EISSN: 1872115X     Source Type: Journal    
DOI: 10.1016/j.uct.2006.08.001     Document Type: Review
Times cited : (11)

References (261)
  • 1
    • 4444340989 scopus 로고    scopus 로고
    • Cyclin-dependent kinases as targets for cancer therapy
    • [Annual 21]
    • Shah M.A., and Schwartz G.K. Cyclin-dependent kinases as targets for cancer therapy. Cancer Chemother Biol Response Modif 21 (2003) 145-170 [Annual 21]
    • (2003) Cancer Chemother Biol Response Modif , vol.21 , pp. 145-170
    • Shah, M.A.1    Schwartz, G.K.2
  • 3
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: positive and negative regulators of G1-phase progression
    • Sherr C.J., and Roberts J.M. CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev 13 12 (1999) 1501-1512
    • (1999) Genes Dev , vol.13 , Issue.12 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 4
    • 0029119740 scopus 로고
    • Cell cycle control in mammalian cells: role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs)
    • Grana X., and Reddy E.P. Cell cycle control in mammalian cells: role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs). Oncogene 11 (1995) 211-219
    • (1995) Oncogene , vol.11 , pp. 211-219
    • Grana, X.1    Reddy, E.P.2
  • 6
    • 0031686960 scopus 로고    scopus 로고
    • Human and yeast cdk-activating kinases (CAKs) display distinct substrate specificities
    • Kaldis P., Russo A.A., Chou H.S., Pavletich N.P., and Solomon M.J. Human and yeast cdk-activating kinases (CAKs) display distinct substrate specificities. Mol Biol Cell 9 9 (1998) 2545-2560
    • (1998) Mol Biol Cell , vol.9 , Issue.9 , pp. 2545-2560
    • Kaldis, P.1    Russo, A.A.2    Chou, H.S.3    Pavletich, N.P.4    Solomon, M.J.5
  • 7
    • 0003418645 scopus 로고
    • A restriction point control for normal animal cell proliferation
    • Pardee A.B. A restriction point control for normal animal cell proliferation. Proc Natl Acad Sci 71 (1974) 1286-1290
    • (1974) Proc Natl Acad Sci , vol.71 , pp. 1286-1290
    • Pardee, A.B.1
  • 8
    • 0035754080 scopus 로고    scopus 로고
    • To cycle or not to cycle: a critical decision in cancer
    • Malumbres M., and Barbacid M. To cycle or not to cycle: a critical decision in cancer. Nat Cancer Rev 1 3 (2001) 222-231
    • (2001) Nat Cancer Rev , vol.1 , Issue.3 , pp. 222-231
    • Malumbres, M.1    Barbacid, M.2
  • 9
    • 0034660892 scopus 로고    scopus 로고
    • The Pezcoller Lecture: cancer cell cycles revisited
    • Sherr C.J. The Pezcoller Lecture: cancer cell cycles revisited. Cancer Res 60 (2000) 3689-3695
    • (2000) Cancer Res , vol.60 , pp. 3689-3695
    • Sherr, C.J.1
  • 10
    • 0032540498 scopus 로고    scopus 로고
    • The role of protein stability in the cell cycle and cancer
    • Elledge S.J., and Harper J.W. The role of protein stability in the cell cycle and cancer. Biochim Biophys Acta 1377 (1998) M61-M70
    • (1998) Biochim Biophys Acta , vol.1377
    • Elledge, S.J.1    Harper, J.W.2
  • 11
    • 0032433141 scopus 로고    scopus 로고
    • The S-phase: beginning, middle, and end: a perspective
    • Ford H.L., and Pardee A.B. The S-phase: beginning, middle, and end: a perspective. J Cell Biochem 30/31 Suppl. (1998) 1-7
    • (1998) J Cell Biochem , vol.30-31 , Issue.SUPPL , pp. 1-7
    • Ford, H.L.1    Pardee, A.B.2
  • 12
    • 0035032649 scopus 로고    scopus 로고
    • Involvement of BRCA1 in S-phase and G2-phase checkpoints after ionizing radiation
    • Xu B., Kim S.-T., and Kastan M.B. Involvement of BRCA1 in S-phase and G2-phase checkpoints after ionizing radiation. Mol Cell Biol 21 (2001) 3445-3450
    • (2001) Mol Cell Biol , vol.21 , pp. 3445-3450
    • Xu, B.1    Kim, S.-T.2    Kastan, M.B.3
  • 13
    • 0037085932 scopus 로고    scopus 로고
    • An ATM-independent S phase checkpoint response involves Chk1 pathway
    • Zhou X., Wang X., Hu B., et al. An ATM-independent S phase checkpoint response involves Chk1 pathway. Cancer Res 62 (2002) 1598-1603
    • (2002) Cancer Res , vol.62 , pp. 1598-1603
    • Zhou, X.1    Wang, X.2    Hu, B.3
  • 14
    • 0033256231 scopus 로고    scopus 로고
    • Cancer and the cell cycle
    • Ford H.L., and Pardee A.B. Cancer and the cell cycle. J Cell Biochem 32/33 Suppl. (1999) 166-172
    • (1999) J Cell Biochem , vol.32-33 , Issue.SUPPL , pp. 166-172
    • Ford, H.L.1    Pardee, A.B.2
  • 16
    • 0034237676 scopus 로고    scopus 로고
    • Spindle assembly and the art of regulating microtubule dynamics by MAPs and stathmin/Op18
    • Anderson S.S.L. Spindle assembly and the art of regulating microtubule dynamics by MAPs and stathmin/Op18. Trends Cell Biol 10 (2000) 261-267
    • (2000) Trends Cell Biol , vol.10 , pp. 261-267
    • Anderson, S.S.L.1
  • 18
    • 14444267778 scopus 로고    scopus 로고
    • How cells get the right chromosome
    • Nicklas R.B. How cells get the right chromosome. Science 275 (1997) 632-637
    • (1997) Science , vol.275 , pp. 632-637
    • Nicklas, R.B.1
  • 20
    • 0038142215 scopus 로고    scopus 로고
    • Polar expeditions - provisioning the centrosome for mitosis
    • Blagden S.P., and Glover D.M. Polar expeditions - provisioning the centrosome for mitosis. Nat Cell Biol 5 6 (2003) 505-511
    • (2003) Nat Cell Biol , vol.5 , Issue.6 , pp. 505-511
    • Blagden, S.P.1    Glover, D.M.2
  • 21
    • 0028938482 scopus 로고
    • Mutations in aurora prevent centrosome separation leading to the formation of monopolar spindles
    • Glover D.M., Leibowitz M.H., McLean D.A., and Perry H. Mutations in aurora prevent centrosome separation leading to the formation of monopolar spindles. Cell 81 (1995) 95-105
    • (1995) Cell , vol.81 , pp. 95-105
    • Glover, D.M.1    Leibowitz, M.H.2    McLean, D.A.3    Perry, H.4
  • 22
    • 0037017398 scopus 로고    scopus 로고
    • Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules
    • Geit R., McLean D., Descamps S., Lee M.J., Raff J.W., Pringent C., et al. Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules. J Biol Chem 156 3 (2002) 437-451
    • (2002) J Biol Chem , vol.156 , Issue.3 , pp. 437-451
    • Geit, R.1    McLean, D.2    Descamps, S.3    Lee, M.J.4    Raff, J.W.5    Pringent, C.6
  • 23
    • 0034266807 scopus 로고    scopus 로고
    • Ringing chromosomes through cell division-and survivin' the experience
    • Reed J.C., and Bischoff J.R. Ringing chromosomes through cell division-and survivin' the experience. Cell 102 (2000) 545-548
    • (2000) Cell , vol.102 , pp. 545-548
    • Reed, J.C.1    Bischoff, J.R.2
  • 24
    • 0035204883 scopus 로고    scopus 로고
    • The molecular basis and potential role of survivin in cancer diagnosis and therapy
    • Altieri D.C. The molecular basis and potential role of survivin in cancer diagnosis and therapy. Trends Mol Med 7 (2001) 542-547
    • (2001) Trends Mol Med , vol.7 , pp. 542-547
    • Altieri, D.C.1
  • 26
    • 0347093300 scopus 로고    scopus 로고
    • NF-kappa B promotes survival during mitotic cell cycle arrest
    • Mistry P., Deacon K., Mistry S., et al. NF-kappa B promotes survival during mitotic cell cycle arrest. J Biol Chem (2003)
    • (2003) J Biol Chem
    • Mistry, P.1    Deacon, K.2    Mistry, S.3
  • 27
    • 0036009115 scopus 로고    scopus 로고
    • NF-kB at the crossroad of Life and Death
    • Karin M., and Lin A. NF-kB at the crossroad of Life and Death. Nat Immunol 3 (2002) 221-227
    • (2002) Nat Immunol , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 28
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella V.J., Rando O.J., Goldberg A.L., and Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 78 5 (1994) 773-785
    • (1994) Cell , vol.78 , Issue.5 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 29
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-kappaB
    • Wang C.Y., Mayo M.W., and Baldwin A.S.J. TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-kappaB. Science 274 5288 (1996) 784-787
    • (1996) Science , vol.274 , Issue.5288 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin, A.S.J.3
  • 30
    • 0034719680 scopus 로고    scopus 로고
    • The transcription factor NF-kappaB: control of oncogenesis and cancer therapy resistance
    • Mayo M., and Balwin A.S. The transcription factor NF-kappaB: control of oncogenesis and cancer therapy resistance. Biochim Biophys Acta 1472 2 (2000) M55-M62
    • (2000) Biochim Biophys Acta , vol.1472 , Issue.2
    • Mayo, M.1    Balwin, A.S.2
  • 31
    • 0015383455 scopus 로고
    • Apoptosis: a basic biological phenomenon with wide ranging implications in tissue kinetics
    • Kerr J.F.R., Wyllie A.H., and Currie A.R. Apoptosis: a basic biological phenomenon with wide ranging implications in tissue kinetics. Br J Cancer 26 (1972) 239-257
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 32
    • 0032877668 scopus 로고    scopus 로고
    • Dysregulation of apoptosis in cancer
    • Reed J.C. Dysregulation of apoptosis in cancer. J Clin Oncol 117 9 (1999) 2941-2953
    • (1999) J Clin Oncol , vol.117 , Issue.9 , pp. 2941-2953
    • Reed, J.C.1
  • 33
    • 0029125701 scopus 로고
    • Protease activation during apoptosis. Death by a thousand cuts?
    • Martin S.J., and Green D.R. Protease activation during apoptosis. Death by a thousand cuts?. Cell 82 (1995) 349-352
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.J.1    Green, D.R.2
  • 35
    • 0027255417 scopus 로고
    • Specific proteolytic cleavage of poly (ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis
    • Kaufmann S.H., Desnoyers S., Ottaviano Y., Davidson N.E., and Poirier G.G. Specific proteolytic cleavage of poly (ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis. Cancer Res 53 (1993) 3976-3985
    • (1993) Cancer Res , vol.53 , pp. 3976-3985
    • Kaufmann, S.H.1    Desnoyers, S.2    Ottaviano, Y.3    Davidson, N.E.4    Poirier, G.G.5
  • 36
    • 0027451668 scopus 로고
    • p53-Dependent apoptosis modulates the cytotoxicity of anticancer agents
    • Lowe S.W., Ruley H.E., Jact T., and Housman D.E. p53-Dependent apoptosis modulates the cytotoxicity of anticancer agents. Cell 74 (1993) 957-967
    • (1993) Cell , vol.74 , pp. 957-967
    • Lowe, S.W.1    Ruley, H.E.2    Jact, T.3    Housman, D.E.4
  • 37
    • 0028880293 scopus 로고
    • The control of apoptosis and drug resistance in ovarian cancer: influence of p53 and Bcl-2
    • Eliopoulos A.G., Kerr D.J., Herod J., Hodgkins L., Krajewski S., Reed J.C., et al. The control of apoptosis and drug resistance in ovarian cancer: influence of p53 and Bcl-2. Oncogene 11 (1995) 1217-1228
    • (1995) Oncogene , vol.11 , pp. 1217-1228
    • Eliopoulos, A.G.1    Kerr, D.J.2    Herod, J.3    Hodgkins, L.4    Krajewski, S.5    Reed, J.C.6
  • 38
    • 0029658187 scopus 로고    scopus 로고
    • Bcl-xl overexpression inhibits taxol-induced yama protease activity and apoptosis
    • Ibardo A.M., Huang Y., Fang G., and Bhalla K. Bcl-xl overexpression inhibits taxol-induced yama protease activity and apoptosis. Cell Growth Differ 7 (1996) 1087-1094
    • (1996) Cell Growth Differ , vol.7 , pp. 1087-1094
    • Ibardo, A.M.1    Huang, Y.2    Fang, G.3    Bhalla, K.4
  • 39
    • 0028987830 scopus 로고
    • Overexpression of Bcl-xl by cytotoxic drug exposure confers resistance to ionizing radiation-induced internucleosomal DNA fragmentation
    • Datta R., Manome Y., Taneja N., Boise L.H., Weichselbaum R., Thompson C.B., et al. Overexpression of Bcl-xl by cytotoxic drug exposure confers resistance to ionizing radiation-induced internucleosomal DNA fragmentation. Cell Growth Differ 6 (1995) 363-370
    • (1995) Cell Growth Differ , vol.6 , pp. 363-370
    • Datta, R.1    Manome, Y.2    Taneja, N.3    Boise, L.H.4    Weichselbaum, R.5    Thompson, C.B.6
  • 40
    • 0030584079 scopus 로고    scopus 로고
    • Apoptosis meets signal transduction: elimination of a BAD influence
    • Gajewski T.F., and Thompson C.B. Apoptosis meets signal transduction: elimination of a BAD influence. Cell 87 4 (1996) 589-592
    • (1996) Cell , vol.87 , Issue.4 , pp. 589-592
    • Gajewski, T.F.1    Thompson, C.B.2
  • 41
    • 0033386539 scopus 로고    scopus 로고
    • Protein kinase C targeting in antineoplastic treatment strategies
    • Jarvis W.D., and Grant S. Protein kinase C targeting in antineoplastic treatment strategies. Invest New Drugs 17 3 (1999) 227-240
    • (1999) Invest New Drugs , vol.17 , Issue.3 , pp. 227-240
    • Jarvis, W.D.1    Grant, S.2
  • 42
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine A.J. p53, the cellular gatekeeper for growth and division. Cell 88 (1997) 323-331
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 43
    • 0028294605 scopus 로고
    • Waf1/Cip1 is induced in p53-mediated G1 arrest and apoptosis
    • El-Diery W.S., Harper J.W., O'Connor P.M., et al. Waf1/Cip1 is induced in p53-mediated G1 arrest and apoptosis. Cancer Res 54 (1994) 1169-1174
    • (1994) Cancer Res , vol.54 , pp. 1169-1174
    • El-Diery, W.S.1    Harper, J.W.2    O'Connor, P.M.3
  • 45
    • 0032701521 scopus 로고    scopus 로고
    • Disruption of p53 in human cancer cells alters the responses to therapeutic agents
    • Bunz F., Hwang P.M., Torrance C., Waldman T., Zhang Y., Dillehay L., et al. Disruption of p53 in human cancer cells alters the responses to therapeutic agents. J Clin Invest 104 3 (1999) 263-269
    • (1999) J Clin Invest , vol.104 , Issue.3 , pp. 263-269
    • Bunz, F.1    Hwang, P.M.2    Torrance, C.3    Waldman, T.4    Zhang, Y.5    Dillehay, L.6
  • 46
    • 0033453226 scopus 로고    scopus 로고
    • Identification and classification of p53-regulated genes
    • Yu J., Zhang L., Hwan P.M., et al. Identification and classification of p53-regulated genes. Proc Natl Acad Sci 96 (1999) 14517-14522
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 14517-14522
    • Yu, J.1    Zhang, L.2    Hwan, P.M.3
  • 47
    • 0028301094 scopus 로고
    • p53 Dependence of early apoptotic and proliferative responses within the mouse intestinal epithelium following gamma-irradiation
    • Clarke A.R., Gledhill S., Hooper M.L., et al. p53 Dependence of early apoptotic and proliferative responses within the mouse intestinal epithelium following gamma-irradiation. Oncogene 9 (1994) 1767-1773
    • (1994) Oncogene , vol.9 , pp. 1767-1773
    • Clarke, A.R.1    Gledhill, S.2    Hooper, M.L.3
  • 49
    • 0028568315 scopus 로고
    • Cell cycle control and cancer
    • Hartwell L.H., and Kastan M.B. Cell cycle control and cancer. Science 266 (1994) 1821-1828
    • (1994) Science , vol.266 , pp. 1821-1828
    • Hartwell, L.H.1    Kastan, M.B.2
  • 50
    • 0030044817 scopus 로고    scopus 로고
    • Cdk inhibitors in develpment and cancer
    • Harper J., and Elledge S.J. Cdk inhibitors in develpment and cancer. Curr Opin Genet Dev 6 (1996) 56-64
    • (1996) Curr Opin Genet Dev , vol.6 , pp. 56-64
    • Harper, J.1    Elledge, S.J.2
  • 51
    • 0034929515 scopus 로고    scopus 로고
    • DNA methylation: an alternative pathway to cancer
    • Shahjehan W.A., Laird P., and DeMeester T. DNA methylation: an alternative pathway to cancer. Ann Surg 234 (2001) 10-20
    • (2001) Ann Surg , vol.234 , pp. 10-20
    • Shahjehan, W.A.1    Laird, P.2    DeMeester, T.3
  • 52
    • 0036146815 scopus 로고    scopus 로고
    • Cyclin D1 and mammary carcinoma: new insights from transgenic mouse models
    • Sutherland R., and Musgrove E. Cyclin D1 and mammary carcinoma: new insights from transgenic mouse models. Breast Cancer Res 4 (2002) 14-17
    • (2002) Breast Cancer Res , vol.4 , pp. 14-17
    • Sutherland, R.1    Musgrove, E.2
  • 53
    • 0027280084 scopus 로고
    • Expression and amplification of cyclin genes in human breast cancer
    • Buckley M., Sweeney K.J., Hamilton J.A., et al. Expression and amplification of cyclin genes in human breast cancer. Oncogene 8 (1993) 2127-2133
    • (1993) Oncogene , vol.8 , pp. 2127-2133
    • Buckley, M.1    Sweeney, K.J.2    Hamilton, J.A.3
  • 54
    • 0033551066 scopus 로고    scopus 로고
    • Selective killing of transformed cells by cyclin/cyclin-dependent kinase 2 antagonists
    • Chen Y.-N., Sharma S.K., Ramsey T.M., Jiang L., Martin M.S., Baker K., et al. Selective killing of transformed cells by cyclin/cyclin-dependent kinase 2 antagonists. Proc Natl Acad Sci 96 8 (1999) 4325-4329
    • (1999) Proc Natl Acad Sci , vol.96 , Issue.8 , pp. 4325-4329
    • Chen, Y.-N.1    Sharma, S.K.2    Ramsey, T.M.3    Jiang, L.4    Martin, M.S.5    Baker, K.6
  • 55
    • 0037073061 scopus 로고    scopus 로고
    • Regulation of transcription elongation by phosphorylation
    • Kobor M., and Greenblatt J. Regulation of transcription elongation by phosphorylation. Biochim Biophys Acta 13 (2002) 261-275
    • (2002) Biochim Biophys Acta , vol.13 , pp. 261-275
    • Kobor, M.1    Greenblatt, J.2
  • 56
    • 0036136668 scopus 로고    scopus 로고
    • Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control
    • Oelgeschlager T. Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control. J Cell Physiol 190 (2002) 160-169
    • (2002) J Cell Physiol , vol.190 , pp. 160-169
    • Oelgeschlager, T.1
  • 57
    • 0037072781 scopus 로고    scopus 로고
    • HIV-1 Tat interaction with RNA polymerase II C-terminal domain (CTD) and a dynamic association with CDK2 induce CTD phosphorylation and transcription from HIV-1 promoter
    • Deng L., Ammosova T., Pumfery A., et al. HIV-1 Tat interaction with RNA polymerase II C-terminal domain (CTD) and a dynamic association with CDK2 induce CTD phosphorylation and transcription from HIV-1 promoter. J Biol Cell 277 (2002) 33922-33929
    • (2002) J Biol Cell , vol.277 , pp. 33922-33929
    • Deng, L.1    Ammosova, T.2    Pumfery, A.3
  • 58
    • 0030666852 scopus 로고    scopus 로고
    • Transformed cell require continuous activity of RNA polymerase II to resist oncogene-induced apoptosis
    • Koumenis C., and Giaccia A. Transformed cell require continuous activity of RNA polymerase II to resist oncogene-induced apoptosis. Mol Cell Biol 17 (1997) 7306-7316
    • (1997) Mol Cell Biol , vol.17 , pp. 7306-7316
    • Koumenis, C.1    Giaccia, A.2
  • 59
    • 0033554609 scopus 로고    scopus 로고
    • RNA synthesis block by 5,6-dichloro-1-β-d-ribofuranosylbenzimidazole (DRB) triggers p53-dependent apoptosis in human colon carcinoma cells
    • Te Poele R., Okorokov A., and Joel S. RNA synthesis block by 5,6-dichloro-1-β-d-ribofuranosylbenzimidazole (DRB) triggers p53-dependent apoptosis in human colon carcinoma cells. Oncogene 18 (1999) 5765-5772
    • (1999) Oncogene , vol.18 , pp. 5765-5772
    • Te Poele, R.1    Okorokov, A.2    Joel, S.3
  • 60
    • 0038654123 scopus 로고    scopus 로고
    • Cyclin-dependent kinases as targets for cancer therapy
    • Giaccone G., Schilsky R., and Sondel P. (Eds), Elsevier Science
    • Senderowicz A.M. Cyclin-dependent kinases as targets for cancer therapy. In: Giaccone G., Schilsky R., and Sondel P. (Eds). Cancer chemotherapy and biological response modifiers, annual 20 (2002), Elsevier Science 169-188
    • (2002) Cancer chemotherapy and biological response modifiers, annual 20 , pp. 169-188
    • Senderowicz, A.M.1
  • 62
    • 0029665778 scopus 로고    scopus 로고
    • Flavopiridol induces G1 arrest with inhibition of cyclin-dependent kinase CDC2 and CDK4 in human breast carcinoma cells
    • Carlson B.A., Dubay M.M., Sausville E.A., Brizuela L., and Worland P.J. Flavopiridol induces G1 arrest with inhibition of cyclin-dependent kinase CDC2 and CDK4 in human breast carcinoma cells. Cancer Res 56 (1996) 2973-2978
    • (1996) Cancer Res , vol.56 , pp. 2973-2978
    • Carlson, B.A.1    Dubay, M.M.2    Sausville, E.A.3    Brizuela, L.4    Worland, P.J.5
  • 64
    • 33748526108 scopus 로고    scopus 로고
    • Dumant, JA, HMR Report No. B/98/0189/R, B/98/0188/R, 8/98/0187/R. HMR Oncology, 1996.
  • 65
    • 0035866782 scopus 로고    scopus 로고
    • The Cyclin-dependent kinase inhibitor (CDKI) flavopiridol disrupts phorbol 12-myristate 13-acetate-induced differentiation and CDKI Expression while enhancing apoptosis in human myeloid leukemia cells
    • Cartee L., Wang Z., Decker R.H., Chellappan S.P., Fusaro G., Hirsch K.G., et al. The Cyclin-dependent kinase inhibitor (CDKI) flavopiridol disrupts phorbol 12-myristate 13-acetate-induced differentiation and CDKI Expression while enhancing apoptosis in human myeloid leukemia cells. Cancer Res 61 6 (2001) 2583-2591
    • (2001) Cancer Res , vol.61 , Issue.6 , pp. 2583-2591
    • Cartee, L.1    Wang, Z.2    Decker, R.H.3    Chellappan, S.P.4    Fusaro, G.5    Hirsch, K.G.6
  • 66
    • 0040932434 scopus 로고    scopus 로고
    • The novel cyclin-dependent kinase inhibitor flavopiridol downregulates Bcl-2 and induces growth arrest and apoptosis in chronic B-cell leukemia cell lines
    • Konig A., Schwartz G.K., Mohammad R.M., et al. The novel cyclin-dependent kinase inhibitor flavopiridol downregulates Bcl-2 and induces growth arrest and apoptosis in chronic B-cell leukemia cell lines. Blood 90 (1997) 4307-4312
    • (1997) Blood , vol.90 , pp. 4307-4312
    • Konig, A.1    Schwartz, G.K.2    Mohammad, R.M.3
  • 67
    • 0035679234 scopus 로고    scopus 로고
    • Augmentation of apoptosis and tumor regressions by flavopiridol in the presence of CPT-11 in HCT116 colon cancer monolayers and xenografts
    • Motwani M., Jung C., Sirotnak F.M., She Y., Shah M.A., Gonen M., et al. Augmentation of apoptosis and tumor regressions by flavopiridol in the presence of CPT-11 in HCT116 colon cancer monolayers and xenografts. Clin Cancer Res 7 (2001) 4209-4219
    • (2001) Clin Cancer Res , vol.7 , pp. 4209-4219
    • Motwani, M.1    Jung, C.2    Sirotnak, F.M.3    She, Y.4    Shah, M.A.5    Gonen, M.6
  • 68
    • 0034661538 scopus 로고    scopus 로고
    • Protein kinase inhibitors flavopiridol and 7-hydroxy-staurosporine down-regulate antiapoptosis proteins in B-cell chronic lymphocytic leukemia
    • Kitada S., Zapata J., Andreeff M., and Reed J.C. Protein kinase inhibitors flavopiridol and 7-hydroxy-staurosporine down-regulate antiapoptosis proteins in B-cell chronic lymphocytic leukemia. Blood 96 (2000) 393-397
    • (2000) Blood , vol.96 , pp. 393-397
    • Kitada, S.1    Zapata, J.2    Andreeff, M.3    Reed, J.C.4
  • 69
    • 4844224868 scopus 로고    scopus 로고
    • Contribution of disruption of the nuclear factor-kappaB pathway to induction of apoptosis in human leukemia cells by histone deacetylase inhibitors and flavopiridol
    • Gao N., Dai Y., Rahmani M., Dent P., and Grant S. Contribution of disruption of the nuclear factor-kappaB pathway to induction of apoptosis in human leukemia cells by histone deacetylase inhibitors and flavopiridol. Mol Pharmacol 66 (2004) 956-963
    • (2004) Mol Pharmacol , vol.66 , pp. 956-963
    • Gao, N.1    Dai, Y.2    Rahmani, M.3    Dent, P.4    Grant, S.5
  • 70
    • 0033568521 scopus 로고    scopus 로고
    • Down-regulation of cyclin D1 by transcriptional repression in MCF-7 human breast carcinoma cells induced by flavopiridol
    • Carlson B., Lahusen T., Singh S., Loaiza-Perez A., Worland P.J., Pestell R., et al. Down-regulation of cyclin D1 by transcriptional repression in MCF-7 human breast carcinoma cells induced by flavopiridol. Cancer Res 59 18 (1999) 4634-4641
    • (1999) Cancer Res , vol.59 , Issue.18 , pp. 4634-4641
    • Carlson, B.1    Lahusen, T.2    Singh, S.3    Loaiza-Perez, A.4    Worland, P.J.5    Pestell, R.6
  • 71
    • 0037228959 scopus 로고    scopus 로고
    • Suppression of survivin phosphorylation on Thr34 by flavopiridol enhances tumor cell apoptosis
    • Wall N.R., O'Connor D.S., Plescia J., Pommier Y., and Altieri D.C. Suppression of survivin phosphorylation on Thr34 by flavopiridol enhances tumor cell apoptosis. Cancer Res 63 (2003) 230-235
    • (2003) Cancer Res , vol.63 , pp. 230-235
    • Wall, N.R.1    O'Connor, D.S.2    Plescia, J.3    Pommier, Y.4    Altieri, D.C.5
  • 73
    • 0035233239 scopus 로고    scopus 로고
    • Genomic-scale measurement of mRNA turnover and the mechanisms of action of the anti-cancer drug flavopiridol
    • Lam L., Pickeral O., Peng A., et al. Genomic-scale measurement of mRNA turnover and the mechanisms of action of the anti-cancer drug flavopiridol. Genome Bio 2 (2001) 1465-6914
    • (2001) Genome Bio , vol.2 , pp. 1465-6914
    • Lam, L.1    Pickeral, O.2    Peng, A.3
  • 74
    • 0037099517 scopus 로고    scopus 로고
    • A novel target for modulating sensitivity to CPT-11 in colon cancer cells
    • Motwani M.V., Sirotnak F., She Y., Commes T., and Schwartz G.K. A novel target for modulating sensitivity to CPT-11 in colon cancer cells. Cancer Res 62 (2002) 3950-3955
    • (2002) Cancer Res , vol.62 , pp. 3950-3955
    • Motwani, M.V.1    Sirotnak, F.2    She, Y.3    Commes, T.4    Schwartz, G.K.5
  • 75
    • 21044432331 scopus 로고    scopus 로고
    • A phase I clinical trial of the sequential combination of irinotecan followed by flavopiridol
    • Shah M.A., Kortmansky J., Motwani M., Drobjnak M., Gonen M., Yi S., et al. A phase I clinical trial of the sequential combination of irinotecan followed by flavopiridol. Clin Cancer Res 11 10 (2005) 3836-3845
    • (2005) Clin Cancer Res , vol.11 , Issue.10 , pp. 3836-3845
    • Shah, M.A.1    Kortmansky, J.2    Motwani, M.3    Drobjnak, M.4    Gonen, M.5    Yi, S.6
  • 76
    • 0029904810 scopus 로고    scopus 로고
    • Flavopiridol: a cytotoxic flavone that induces cell death in noncycling A549 human lung carcinoma cells
    • Bible K.C., and Kaufmann S.H. Flavopiridol: a cytotoxic flavone that induces cell death in noncycling A549 human lung carcinoma cells. Cancer Res 56 21 (1996) 4856-4861
    • (1996) Cancer Res , vol.56 , Issue.21 , pp. 4856-4861
    • Bible, K.C.1    Kaufmann, S.H.2
  • 77
    • 0031725137 scopus 로고    scopus 로고
    • Flavopiridol mediates cell cycle arrest and apoptosis in esophageal cancer cell lines
    • Schrump D.S., Mathews W., Chen G.A., et al. Flavopiridol mediates cell cycle arrest and apoptosis in esophageal cancer cell lines. Clin Cancer Res 4 (1998) 2885-2890
    • (1998) Clin Cancer Res , vol.4 , pp. 2885-2890
    • Schrump, D.S.1    Mathews, W.2    Chen, G.A.3
  • 78
    • 0031019034 scopus 로고    scopus 로고
    • Flavopiridol (L86-8275): selective antitumor activity in vitro and activity in vivo for prostate carcinoma cells
    • Drees M., Dengler W.A., Roth T., et al. Flavopiridol (L86-8275): selective antitumor activity in vitro and activity in vivo for prostate carcinoma cells. Clin Cancer Res 3 2 (1997) 271-279
    • (1997) Clin Cancer Res , vol.3 , Issue.2 , pp. 271-279
    • Drees, M.1    Dengler, W.A.2    Roth, T.3
  • 79
    • 0032212885 scopus 로고    scopus 로고
    • Flavopiridol, a novel cyclin-dependent kinase inhibitor, suppresses the growth of head and neck squamous cell carcinomas by inducing apoptosis
    • Patel V., Senderowicz A.M., Pinto Jr. D., Igishi T., Raffeld M., Quintanilla-Martinez L., et al. Flavopiridol, a novel cyclin-dependent kinase inhibitor, suppresses the growth of head and neck squamous cell carcinomas by inducing apoptosis. J Clin Invest 102 9 (1998) 1674-1681
    • (1998) J Clin Invest , vol.102 , Issue.9 , pp. 1674-1681
    • Patel, V.1    Senderowicz, A.M.2    Pinto Jr., D.3    Igishi, T.4    Raffeld, M.5    Quintanilla-Martinez, L.6
  • 80
    • 0036450831 scopus 로고    scopus 로고
    • Phase I clinical and pharmacokinetic trial of cyclin-dependent kinase inhibitor flavopiridol
    • Thomas J.P., Tutsch K.D., Cleary J.F., et al. Phase I clinical and pharmacokinetic trial of cyclin-dependent kinase inhibitor flavopiridol. Cancer Chemother Pharmacol 50 (2002) 465-472
    • (2002) Cancer Chemother Pharmacol , vol.50 , pp. 465-472
    • Thomas, J.P.1    Tutsch, K.D.2    Cleary, J.F.3
  • 81
    • 0031670668 scopus 로고    scopus 로고
    • Phase I trial of continuous infusion flavopiridol, a novel cyclin-dependent kinase inhibitor, in patients with refractory neoplasms
    • Senderowicz A.M., Headlee D., Stinson S.F., et al. Phase I trial of continuous infusion flavopiridol, a novel cyclin-dependent kinase inhibitor, in patients with refractory neoplasms. J Clin Oncol 16 9 (1998) 2986-2999
    • (1998) J Clin Oncol , vol.16 , Issue.9 , pp. 2986-2999
    • Senderowicz, A.M.1    Headlee, D.2    Stinson, S.F.3
  • 82
    • 0034900178 scopus 로고    scopus 로고
    • A phase II trial of the cyclin-dependent kinase inhibitor flavopiridol in patients with previously untreated stage IV non-small cell lung cancer
    • Shapiro G.I., Patterson A., Lynch C., et al. A phase II trial of the cyclin-dependent kinase inhibitor flavopiridol in patients with previously untreated stage IV non-small cell lung cancer. Clin Cancer Res 7 6 (2001) 1590-1599
    • (2001) Clin Cancer Res , vol.7 , Issue.6 , pp. 1590-1599
    • Shapiro, G.I.1    Patterson, A.2    Lynch, C.3
  • 83
    • 0035300684 scopus 로고    scopus 로고
    • Phase II study of the cyclin-dependent kinase inhibitor flavopiridol administered to patients with advanced gastric carcinoma
    • Schwartz G.K., Ilson D., Saltz L., O'Reilly E., Tong W., Maslak P., et al. Phase II study of the cyclin-dependent kinase inhibitor flavopiridol administered to patients with advanced gastric carcinoma. J Clin Oncol 19 7 (2001) 1985-1992
    • (2001) J Clin Oncol , vol.19 , Issue.7 , pp. 1985-1992
    • Schwartz, G.K.1    Ilson, D.2    Saltz, L.3    O'Reilly, E.4    Tong, W.5    Maslak, P.6
  • 84
    • 0033955395 scopus 로고    scopus 로고
    • Flavopiridol, a novel cyclin-dependent kinase inhibitor, in metastatic renal cancer: a University of Chicago Phase II Consortium Study
    • Stadler W.M., Vogelzang N.J., Amato R., Sosman J., Taber D., Liebowitz D., et al. Flavopiridol, a novel cyclin-dependent kinase inhibitor, in metastatic renal cancer: a University of Chicago Phase II Consortium Study. J Clin Oncol 18 2 (2000) 371-375
    • (2000) J Clin Oncol , vol.18 , Issue.2 , pp. 371-375
    • Stadler, W.M.1    Vogelzang, N.J.2    Amato, R.3    Sosman, J.4    Taber, D.5    Liebowitz, D.6
  • 85
    • 12444280811 scopus 로고    scopus 로고
    • NCIC CTG phase II study of flavopiridol in patients with previously untreated metastatic malignant melanoma
    • Burdette-Radoux S., Tozer R.G., Lohmann R., et al. NCIC CTG phase II study of flavopiridol in patients with previously untreated metastatic malignant melanoma. Proc Am Soc Clin Oncol (2002)
    • (2002) Proc Am Soc Clin Oncol
    • Burdette-Radoux, S.1    Tozer, R.G.2    Lohmann, R.3
  • 86
    • 0043011497 scopus 로고    scopus 로고
    • Phase II study of flavopiridol in patients with advanced colorectal cancer
    • Aklilu M., Kindler H.L., Donehower R.C., Mani S., and Vokes E.E. Phase II study of flavopiridol in patients with advanced colorectal cancer. Ann Oncol 14 8 (2003) 1270-1273
    • (2003) Ann Oncol , vol.14 , Issue.8 , pp. 1270-1273
    • Aklilu, M.1    Kindler, H.L.2    Donehower, R.C.3    Mani, S.4    Vokes, E.E.5
  • 87
    • 0038473927 scopus 로고    scopus 로고
    • Flavopiridol in untreated or relapsed mantle-cell lymphoma: results of a phase II study of the National Cancer Institute of Canada Clinical Trials Group
    • Kouroukis C.T., Belch A., Crump M., et al. Flavopiridol in untreated or relapsed mantle-cell lymphoma: results of a phase II study of the National Cancer Institute of Canada Clinical Trials Group. J Clin Oncol 21 9 (2003) 1740-1745
    • (2003) J Clin Oncol , vol.21 , Issue.9 , pp. 1740-1745
    • Kouroukis, C.T.1    Belch, A.2    Crump, M.3
  • 88
    • 0036240601 scopus 로고    scopus 로고
    • Seventy-two hour continuous infusion flavopiridol in relapsed and refractory mantle cell lymphoma
    • Lin T.S., Howard O.M., Neuberg D.S., et al. Seventy-two hour continuous infusion flavopiridol in relapsed and refractory mantle cell lymphoma. Leuk Lymphoma 43 4 (2002) 793-797
    • (2002) Leuk Lymphoma , vol.43 , Issue.4 , pp. 793-797
    • Lin, T.S.1    Howard, O.M.2    Neuberg, D.S.3
  • 89
    • 20344382459 scopus 로고    scopus 로고
    • Flavopiridol administered as a 24-hour continuous infusion in chronic lymphocytic leukemia lacks clinical activity
    • Flinn I.W., Byrd J.C., Bartlett N., Kipps T., Gribben J., et al. Flavopiridol administered as a 24-hour continuous infusion in chronic lymphocytic leukemia lacks clinical activity. Leuk Res 29 11 (2005) 1253-1257
    • (2005) Leuk Res , vol.29 , Issue.11 , pp. 1253-1257
    • Flinn, I.W.1    Byrd, J.C.2    Bartlett, N.3    Kipps, T.4    Gribben, J.5
  • 90
    • 0036789539 scopus 로고    scopus 로고
    • A phase I clinical and pharmacokinetic study of flavopiridol administered as a daily 1-hour infusion in patients with advanced neoplasms
    • Tan A.R., Headlee D., Messmann R., Sausville E.A., Arbuck S., et al. A phase I clinical and pharmacokinetic study of flavopiridol administered as a daily 1-hour infusion in patients with advanced neoplasms. J Clin Oncol 20 19 (2002) 4074-4082
    • (2002) J Clin Oncol , vol.20 , Issue.19 , pp. 4074-4082
    • Tan, A.R.1    Headlee, D.2    Messmann, R.3    Sausville, E.A.4    Arbuck, S.5
  • 91
    • 33748532096 scopus 로고    scopus 로고
    • Flavopiridol given as a 30 minute intravenous (IV) bolus followed by 4-hr continous IV infusion results in clinical activity and tumor lysis in refractory chronic lymphocytic leukemia
    • [abstract #6564]
    • Lin T., Dalton J.T., Wu B., et al. Flavopiridol given as a 30 minute intravenous (IV) bolus followed by 4-hr continous IV infusion results in clinical activity and tumor lysis in refractory chronic lymphocytic leukemia. Proc ASCO 23 (2004) 571 [abstract #6564]
    • (2004) Proc ASCO , vol.23 , pp. 571
    • Lin, T.1    Dalton, J.T.2    Wu, B.3
  • 92
    • 0027157590 scopus 로고
    • Cell cycle arrest and growth inhibition by the protein kinase antagonist UCN-01 in human breast carcinoma cells
    • Seynaeve C.M., Stetler-Stevenson M., Sebers S., Kaur G., Sausville E.A., and Worland P.J. Cell cycle arrest and growth inhibition by the protein kinase antagonist UCN-01 in human breast carcinoma cells. Cancer Res 53 9 (1993) 2081-2086
    • (1993) Cancer Res , vol.53 , Issue.9 , pp. 2081-2086
    • Seynaeve, C.M.1    Stetler-Stevenson, M.2    Sebers, S.3    Kaur, G.4    Sausville, E.A.5    Worland, P.J.6
  • 93
    • 0028057513 scopus 로고
    • Effect of UCN-01, a selective inhibitor of protein kinase C, on the cell-cycle distribution of human epidermoind carcinoma, A431 cells
    • Akinaga S., Nomura K., Gomi K., and Okabe M. Effect of UCN-01, a selective inhibitor of protein kinase C, on the cell-cycle distribution of human epidermoind carcinoma, A431 cells. Cancer Chemother Pharmacol 33 4 (1994) 273-280
    • (1994) Cancer Chemother Pharmacol , vol.33 , Issue.4 , pp. 273-280
    • Akinaga, S.1    Nomura, K.2    Gomi, K.3    Okabe, M.4
  • 94
    • 0029871688 scopus 로고    scopus 로고
    • UCN-01, 7-hydroxylstaurosporine, inhibits kinase activity of cyclin-dependent kinases and reduces the phosphorylation of the retinoblastoma susceptibility gene product in A549 human lung cancer cell line
    • Kawakami K., Futami H., Takahara J., and Yamaguchi K. UCN-01, 7-hydroxylstaurosporine, inhibits kinase activity of cyclin-dependent kinases and reduces the phosphorylation of the retinoblastoma susceptibility gene product in A549 human lung cancer cell line. Biochem Biophys Res Commun 219 3 (1996) 778-783
    • (1996) Biochem Biophys Res Commun , vol.219 , Issue.3 , pp. 778-783
    • Kawakami, K.1    Futami, H.2    Takahara, J.3    Yamaguchi, K.4
  • 95
    • 0030615323 scopus 로고    scopus 로고
    • G1 phase accumulation induced by UCN-01 is associated with dephosphorylation of Rb and CDK2 proteins as well as the induction of CDK inhibitor p21/CIP/WAF1/Sdi1 in p53-mutated human epidermoid carcinoma A431 cells
    • Akiyama T., Yoshida T., Tsujita T., Shimizu M., Mizukami T., Okabe M., et al. G1 phase accumulation induced by UCN-01 is associated with dephosphorylation of Rb and CDK2 proteins as well as the induction of CDK inhibitor p21/CIP/WAF1/Sdi1 in p53-mutated human epidermoid carcinoma A431 cells. Cancer Res 57 8 (1997) 1495-1501
    • (1997) Cancer Res , vol.57 , Issue.8 , pp. 1495-1501
    • Akiyama, T.1    Yoshida, T.2    Tsujita, T.3    Shimizu, M.4    Mizukami, T.5    Okabe, M.6
  • 96
    • 0030445460 scopus 로고    scopus 로고
    • The retinoblastoma gene product is a negative modulator of the apoptotic pathway
    • Fan G., and Steer C.J. The retinoblastoma gene product is a negative modulator of the apoptotic pathway. Adv Enzyme Regul 36 (1996) 283-303
    • (1996) Adv Enzyme Regul , vol.36 , pp. 283-303
    • Fan, G.1    Steer, C.J.2
  • 97
    • 0031670310 scopus 로고    scopus 로고
    • UCN-01 suppresses thymidylate synthase gene expression and enhances 5-fluorouracil-induced apoptosis in a sequence-dependent manner
    • Hsueh C.T., Kelsen D., and Schwartz G.K. UCN-01 suppresses thymidylate synthase gene expression and enhances 5-fluorouracil-induced apoptosis in a sequence-dependent manner. Clin Cancer Res 4 9 (1998) 2201-2206
    • (1998) Clin Cancer Res , vol.4 , Issue.9 , pp. 2201-2206
    • Hsueh, C.T.1    Kelsen, D.2    Schwartz, G.K.3
  • 98
    • 0034053130 scopus 로고    scopus 로고
    • The Chk1 protein kinase and the Cdc25C regulatory pathways are targets of the anticancer agent UCN-01
    • Graves P.R., Yu L., Schwarz J.K., Gales J., Sausville E.A., O'Connor P.M., et al. The Chk1 protein kinase and the Cdc25C regulatory pathways are targets of the anticancer agent UCN-01. J Biol Chem 275 8 (2000) 5600-5605
    • (2000) J Biol Chem , vol.275 , Issue.8 , pp. 5600-5605
    • Graves, P.R.1    Yu, L.2    Schwarz, J.K.3    Gales, J.4    Sausville, E.A.5    O'Connor, P.M.6
  • 99
    • 0034655281 scopus 로고    scopus 로고
    • The radiosensitizing agent 7-hydroxystaurosporine (UCN-01) inhibits the DNA damage checkpoint kinase hChk1
    • Busby E.C., Leistritz D.F., Abraham R.T., Karnitz L.M., and Sarkaria J.N. The radiosensitizing agent 7-hydroxystaurosporine (UCN-01) inhibits the DNA damage checkpoint kinase hChk1. Cancer Res 60 8 (2000) 2108-2112
    • (2000) Cancer Res , vol.60 , Issue.8 , pp. 2108-2112
    • Busby, E.C.1    Leistritz, D.F.2    Abraham, R.T.3    Karnitz, L.M.4    Sarkaria, J.N.5
  • 100
    • 0037108873 scopus 로고    scopus 로고
    • UCN-01 inhibits p53 up-regulation and abrogates gamma-radiation-induced G2-M Checkpoint independently of p53 by targeting both of the checkpoint kinases, Chk2 and Chk1
    • Yu Q., Rose J.H., Zhang H., et al. UCN-01 inhibits p53 up-regulation and abrogates gamma-radiation-induced G2-M Checkpoint independently of p53 by targeting both of the checkpoint kinases, Chk2 and Chk1. Cancer Res 62 (2002) 5743-5748
    • (2002) Cancer Res , vol.62 , pp. 5743-5748
    • Yu, Q.1    Rose, J.H.2    Zhang, H.3
  • 101
    • 0035871444 scopus 로고    scopus 로고
    • Phase I trial of 72-hour continuous infusion of UCN-01 in patients with refractory neoplasms
    • Sausville E.A., Arbuck S.G., Messmann R., Headlee D., Bauer K.S., Lush R.M., et al. Phase I trial of 72-hour continuous infusion of UCN-01 in patients with refractory neoplasms. J Clin Oncol 19 8 (2001) 2319-2333
    • (2001) J Clin Oncol , vol.19 , Issue.8 , pp. 2319-2333
    • Sausville, E.A.1    Arbuck, S.G.2    Messmann, R.3    Headlee, D.4    Bauer, K.S.5    Lush, R.M.6
  • 102
    • 0032145499 scopus 로고    scopus 로고
    • Unpredicted clinical pharmacology of UCN-01 caused by specific binding to human alpha1-acid glycoprotein
    • Fuse E., Tanii H., Kurata N., et al. Unpredicted clinical pharmacology of UCN-01 caused by specific binding to human alpha1-acid glycoprotein. Cancer Res 58 (1998) 3248-3253
    • (1998) Cancer Res , vol.58 , pp. 3248-3253
    • Fuse, E.1    Tanii, H.2    Kurata, N.3
  • 105
    • 0003316495 scopus 로고    scopus 로고
    • A phase I and pharmacologic study of UCN-01, a protein kinase C inhibitor
    • Dees E.C., O'Reilly S., Figg W.D., et al. A phase I and pharmacologic study of UCN-01, a protein kinase C inhibitor. Proc Am Soc Clin Oncol 19 (2000) 205a
    • (2000) Proc Am Soc Clin Oncol , vol.19
    • Dees, E.C.1    O'Reilly, S.2    Figg, W.D.3
  • 106
    • 20144373035 scopus 로고    scopus 로고
    • Phase I trial of the cyclin-dependent kinase inhibitor/protein kinase C inhibitor UCN-01 in combination with 5-FU in patients with advanced solid tumors
    • Kortmansky J., Shah M.A., Kaubisch A., Weyerbacher A., Yi S., et al. Phase I trial of the cyclin-dependent kinase inhibitor/protein kinase C inhibitor UCN-01 in combination with 5-FU in patients with advanced solid tumors. JCO 23 9 (2005) 1875-1884
    • (2005) JCO , vol.23 , Issue.9 , pp. 1875-1884
    • Kortmansky, J.1    Shah, M.A.2    Kaubisch, A.3    Weyerbacher, A.4    Yi, S.5
  • 107
    • 8444244787 scopus 로고    scopus 로고
    • 7-Hydroxystaurosporine (UCN-01) inhibition of Akt Thr308 but not Ser473 phosphorylation: a basis for decreased insulin-stimulated glucose transport
    • Kondapaka S.B., Zarnowski M., Yver D.R., Sausville E.A., and Cushman S.W. 7-Hydroxystaurosporine (UCN-01) inhibition of Akt Thr308 but not Ser473 phosphorylation: a basis for decreased insulin-stimulated glucose transport. Clin Cancer Res 10 (2004) 7192-7198
    • (2004) Clin Cancer Res , vol.10 , pp. 7192-7198
    • Kondapaka, S.B.1    Zarnowski, M.2    Yver, D.R.3    Sausville, E.A.4    Cushman, S.W.5
  • 108
    • 0010543768 scopus 로고
    • Bryostatin, an activator of the calcium phospholipid-dependent protein kinase, blocks phorbol ester-induced differentiation of human promyelocytic leukemia cells HL-60
    • Kraft A.S., Smith J.B., and Berkow R.L. Bryostatin, an activator of the calcium phospholipid-dependent protein kinase, blocks phorbol ester-induced differentiation of human promyelocytic leukemia cells HL-60. Proc Natl Acad Sci 83 (1986) 1334-1338
    • (1986) Proc Natl Acad Sci , vol.83 , pp. 1334-1338
    • Kraft, A.S.1    Smith, J.B.2    Berkow, R.L.3
  • 109
    • 0027322773 scopus 로고
    • Inhibition of phorbol ester-induced T cell proliferation by bryostatin is associated with rapid degradation of protein kinase C
    • Isakov N., Galron D., Mustelin T., Pettit G.R., and Altman A. Inhibition of phorbol ester-induced T cell proliferation by bryostatin is associated with rapid degradation of protein kinase C. J Immunol 150 4 (1993) 1195-1204
    • (1993) J Immunol , vol.150 , Issue.4 , pp. 1195-1204
    • Isakov, N.1    Galron, D.2    Mustelin, T.3    Pettit, G.R.4    Altman, A.5
  • 110
    • 0029812896 scopus 로고    scopus 로고
    • Ubiquitination of protein kinase C-alpha and degradation by the proteasome
    • Lee H.W., Smith L., Pettit G.R., Vinitsky A., and Smith J.B. Ubiquitination of protein kinase C-alpha and degradation by the proteasome. J Biol Chem 271 (1996) 20973-20976
    • (1996) J Biol Chem , vol.271 , pp. 20973-20976
    • Lee, H.W.1    Smith, L.2    Pettit, G.R.3    Vinitsky, A.4    Smith, J.B.5
  • 111
    • 0029150243 scopus 로고
    • Inhibition of leukemic cell growth by the protein kinase C activator bryostatin-1 correlates with the dephosphorylation of cyclin-dependent kinase 2
    • Asiedu C., Biggs J., Lilly M., and Kraft M. Inhibition of leukemic cell growth by the protein kinase C activator bryostatin-1 correlates with the dephosphorylation of cyclin-dependent kinase 2. Cancer Res 55 (1995) 3716-3720
    • (1995) Cancer Res , vol.55 , pp. 3716-3720
    • Asiedu, C.1    Biggs, J.2    Lilly, M.3    Kraft, M.4
  • 112
    • 0031954011 scopus 로고    scopus 로고
    • Divergent effects of bryostatin 1 and phorbol myristate acetate on cell cycle arrest and maturation in human myelomonocytic leukemia cells (U937)
    • Vrana J.A., Saunders A.M., Chellappan S.P., and Grant S. Divergent effects of bryostatin 1 and phorbol myristate acetate on cell cycle arrest and maturation in human myelomonocytic leukemia cells (U937). Differentiation 63 (1998) 33-42
    • (1998) Differentiation , vol.63 , pp. 33-42
    • Vrana, J.A.1    Saunders, A.M.2    Chellappan, S.P.3    Grant, S.4
  • 113
    • 0033168213 scopus 로고    scopus 로고
    • Inhibition of protein kinase C activator-mediated induction of p21cip1 and p27kip1 by deoxycytidine analogs in human leukemia cells: relationship to apoptosis and differentiation
    • Vrana J.A., Kramer L.B., Saunders A.M., Zhang X.F., Dent P., Povirk L.F., et al. Inhibition of protein kinase C activator-mediated induction of p21cip1 and p27kip1 by deoxycytidine analogs in human leukemia cells: relationship to apoptosis and differentiation. Biochem Pharmacol 58 (1999) 121-131
    • (1999) Biochem Pharmacol , vol.58 , pp. 121-131
    • Vrana, J.A.1    Kramer, L.B.2    Saunders, A.M.3    Zhang, X.F.4    Dent, P.5    Povirk, L.F.6
  • 114
    • 0034006706 scopus 로고    scopus 로고
    • The in vitro effect of bryostatin-1 on paclitaxel-induced tumor growth, mitotic entry, and blood flow
    • Koutcher J.A., Motwani M., Zakian K.L., Li X.L., Matei C., et al. The in vitro effect of bryostatin-1 on paclitaxel-induced tumor growth, mitotic entry, and blood flow. Clin Cancer Res 6 (2000) 1498-1507
    • (2000) Clin Cancer Res , vol.6 , pp. 1498-1507
    • Koutcher, J.A.1    Motwani, M.2    Zakian, K.L.3    Li, X.L.4    Matei, C.5
  • 115
    • 0028787625 scopus 로고
    • Bryostatin 1, a novel antineoplastic agent and protein kinase C activator, induces human myalgia and muscle metabolic defects: a 31P magnetic resonance spectroscopic study
    • Hickman P.F., Kemp G.J., Thompson C.H., Salisbury A.J., Wade K., Harris A.L., et al. Bryostatin 1, a novel antineoplastic agent and protein kinase C activator, induces human myalgia and muscle metabolic defects: a 31P magnetic resonance spectroscopic study. Br J Cancer 72 (1995) 998-1003
    • (1995) Br J Cancer , vol.72 , pp. 998-1003
    • Hickman, P.F.1    Kemp, G.J.2    Thompson, C.H.3    Salisbury, A.J.4    Wade, K.5    Harris, A.L.6
  • 117
    • 0027489606 scopus 로고
    • Phase I study of bryostatin 1: assessment of interleukin 6 and tumor necrosis factor alpha induction in vivo. The Cancer Research Campaign Phase I Committee
    • Philip P.A., Rea D., Thavasu P., Carmichael J., Stuart N.S., et al. Phase I study of bryostatin 1: assessment of interleukin 6 and tumor necrosis factor alpha induction in vivo. The Cancer Research Campaign Phase I Committee. J Natl Cancer Inst 85 (1993) 1812-1818
    • (1993) J Natl Cancer Inst , vol.85 , pp. 1812-1818
    • Philip, P.A.1    Rea, D.2    Thavasu, P.3    Carmichael, J.4    Stuart, N.S.5
  • 118
    • 0029084804 scopus 로고
    • A phase I trial of bryostatin 1 in patients with advanced malignancy using a 24-hour intravenous infusion
    • Jayson G.C., Crowther D., Prendiville J., McGown A., Scheid C., et al. A phase I trial of bryostatin 1 in patients with advanced malignancy using a 24-hour intravenous infusion. Br J Cancer 72 (1995) 461-468
    • (1995) Br J Cancer , vol.72 , pp. 461-468
    • Jayson, G.C.1    Crowther, D.2    Prendiville, J.3    McGown, A.4    Scheid, C.5
  • 119
    • 0031982782 scopus 로고    scopus 로고
    • Phase I study of bryostatin 1 in patients with relapsed non-Hodgkin's lymphoma and chronic lymphocytic leukemia
    • Varterasian M.L., Mohammad R.M., Eilender D.S., Hulburd K., Rodriguez D.H., Pemberton P.A., et al. Phase I study of bryostatin 1 in patients with relapsed non-Hodgkin's lymphoma and chronic lymphocytic leukemia. J Clin Oncol 16 (1998) 56-62
    • (1998) J Clin Oncol , vol.16 , pp. 56-62
    • Varterasian, M.L.1    Mohammad, R.M.2    Eilender, D.S.3    Hulburd, K.4    Rodriguez, D.H.5    Pemberton, P.A.6
  • 121
    • 0033407483 scopus 로고    scopus 로고
    • Treatment of patients with metastatic melanoma with bryostatin-1 - a phase II study
    • Gonzalez R., Ebbinghaus S., Henthorn T.K., Miller D., and Kraft A.S. Treatment of patients with metastatic melanoma with bryostatin-1 - a phase II study. Melanoma Res 9 (1999) 599-606
    • (1999) Melanoma Res , vol.9 , pp. 599-606
    • Gonzalez, R.1    Ebbinghaus, S.2    Henthorn, T.K.3    Miller, D.4    Kraft, A.S.5
  • 123
    • 0036210351 scopus 로고    scopus 로고
    • A phase II trial of bryostatin-1 in patients with metastatic or recurrent squamous cell carcinoma of the head and neck
    • Pfister D.G., McCaffrey J., Zahalsky A.J., et al. A phase II trial of bryostatin-1 in patients with metastatic or recurrent squamous cell carcinoma of the head and neck. Invest New Drugs 20 1 (2002) 123-127
    • (2002) Invest New Drugs , vol.20 , Issue.1 , pp. 123-127
    • Pfister, D.G.1    McCaffrey, J.2    Zahalsky, A.J.3
  • 125
    • 0037312095 scopus 로고    scopus 로고
    • A phase II study of bryostatin-1 and paclitaxel in patients with advanced non-small cell lung cancer
    • Winegarden J.D., Mauer A.M., Gajewsky T.F., et al. A phase II study of bryostatin-1 and paclitaxel in patients with advanced non-small cell lung cancer. Lung Cancer 39 2 (2003) 191-196
    • (2003) Lung Cancer , vol.39 , Issue.2 , pp. 191-196
    • Winegarden, J.D.1    Mauer, A.M.2    Gajewsky, T.F.3
  • 127
    • 0034851020 scopus 로고    scopus 로고
    • Phase II studies of bryostatin-1 in patients with advanced sarcoma and advanced head and neck cancer
    • Brockstein B., Samuels B., Humerickhouse R., Arietta R., Fishkin P., Wade J., et al. Phase II studies of bryostatin-1 in patients with advanced sarcoma and advanced head and neck cancer. Invest New Drugs 19 (2001) 249-254
    • (2001) Invest New Drugs , vol.19 , pp. 249-254
    • Brockstein, B.1    Samuels, B.2    Humerickhouse, R.3    Arietta, R.4    Fishkin, P.5    Wade, J.6
  • 128
    • 0345283114 scopus 로고    scopus 로고
    • A randomized phase II evaluation of bryostatin-1 (NSC #339555) in recurrent or persistent platinum-sensitive ovarian cancer: a Gynecologic Oncology Group Study
    • Armstrong D.K., Blessing J.A., Look K.Y., Schilder R., and Nunez E.R. A randomized phase II evaluation of bryostatin-1 (NSC #339555) in recurrent or persistent platinum-sensitive ovarian cancer: a Gynecologic Oncology Group Study. Invest New Drugs 21 3 (2003) 373-377
    • (2003) Invest New Drugs , vol.21 , Issue.3 , pp. 373-377
    • Armstrong, D.K.1    Blessing, J.A.2    Look, K.Y.3    Schilder, R.4    Nunez, E.R.5
  • 129
    • 1642452915 scopus 로고    scopus 로고
    • A randomized phase II evaluation of bryostatin-1 (NSC #339555) in persistent or recurrent squamous cell carcinoma of the cervix: a Gynecologic Oncology Group Study
    • Armstrong D.K., Blessing J.A., Rader J., and Sorosky J.I. A randomized phase II evaluation of bryostatin-1 (NSC #339555) in persistent or recurrent squamous cell carcinoma of the cervix: a Gynecologic Oncology Group Study. Invest New Drugs 21 4 (2003) 453-457
    • (2003) Invest New Drugs , vol.21 , Issue.4 , pp. 453-457
    • Armstrong, D.K.1    Blessing, J.A.2    Rader, J.3    Sorosky, J.I.4
  • 130
    • 0242298228 scopus 로고    scopus 로고
    • A phase II trial of bryostatin-1 administered by weekly 24-hour infusion in recurrent epithelial ovarian carcinoma
    • Clamp A.R., Blackhall F.H., Vasey P., et al. A phase II trial of bryostatin-1 administered by weekly 24-hour infusion in recurrent epithelial ovarian carcinoma. Br J Cancer 89 7 (2003) 52-54
    • (2003) Br J Cancer , vol.89 , Issue.7 , pp. 52-54
    • Clamp, A.R.1    Blackhall, F.H.2    Vasey, P.3
  • 131
    • 12244275670 scopus 로고    scopus 로고
    • Weekly bryostatin-1 in metastatic renal cell carcinoma: a phase II study
    • Haas N.B., Smith M., Lewis N., et al. Weekly bryostatin-1 in metastatic renal cell carcinoma: a phase II study. Clin Cancer Res 9 1 (2003) 109-114
    • (2003) Clin Cancer Res , vol.9 , Issue.1 , pp. 109-114
    • Haas, N.B.1    Smith, M.2    Lewis, N.3
  • 132
    • 0242491493 scopus 로고    scopus 로고
    • A multicenter phase II trial of bryostatin-1 in patients with advanced renal cancer
    • Madhusudan S., Protheroe A., Propper D., et al. A multicenter phase II trial of bryostatin-1 in patients with advanced renal cancer. Br J Cancer 89 8 (2003) 1418-1422
    • (2003) Br J Cancer , vol.89 , Issue.8 , pp. 1418-1422
    • Madhusudan, S.1    Protheroe, A.2    Propper, D.3
  • 133
    • 0034254971 scopus 로고    scopus 로고
    • A phase II trial of bryostatin-1 for patients with metastatic renal cell carcinoma
    • Pagliaro L., Daliani D., Amato R., Tu S.M., Jones D., et al. A phase II trial of bryostatin-1 for patients with metastatic renal cell carcinoma. Cancer 89 (2000) 615-618
    • (2000) Cancer , vol.89 , pp. 615-618
    • Pagliaro, L.1    Daliani, D.2    Amato, R.3    Tu, S.M.4    Jones, D.5
  • 134
    • 0037058678 scopus 로고    scopus 로고
    • In vitro and in vivo antitumor properties of the cyclin dependent kinase inhibitor CYC202 (R-roscovitine)
    • McClue S.J., Blake D., Clarke A.R., Cowan A., Cummings L., Fischer P.M., et al. In vitro and in vivo antitumor properties of the cyclin dependent kinase inhibitor CYC202 (R-roscovitine). Int J Cancer 102 5 (2002) 463-468
    • (2002) Int J Cancer , vol.102 , Issue.5 , pp. 463-468
    • McClue, S.J.1    Blake, D.2    Clarke, A.R.3    Cowan, A.4    Cummings, L.5    Fischer, P.M.6
  • 135
    • 33748535994 scopus 로고    scopus 로고
    • Studies on the mechanism of action of CYC202 (R-roscovitine)
    • McClue S.J., Fischer P., Blake D., et al. Studies on the mechanism of action of CYC202 (R-roscovitine). Am Assoc Cancer Res (2002)
    • (2002) Am Assoc Cancer Res
    • McClue, S.J.1    Fischer, P.2    Blake, D.3
  • 137
    • 0031037714 scopus 로고    scopus 로고
    • Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2, and cdk5
    • Meijer L., Borgne A., Mulner O., Chong J.P., Blow J.J., Inagaki N., et al. Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2, and cdk5. Eur J Biochem 243 (1997) 527-536
    • (1997) Eur J Biochem , vol.243 , pp. 527-536
    • Meijer, L.1    Borgne, A.2    Mulner, O.3    Chong, J.P.4    Blow, J.J.5    Inagaki, N.6
  • 138
    • 13244294925 scopus 로고    scopus 로고
    • A novel CDK inhibitor, CYC202 (R-roscovitine), overcomes the defect in p53-independent apoptosis in B-cell chronic lymphocytic leukemia by down-regulation of genes involved in transcription regulation and repair
    • [abstract]
    • Alvi A., Gianella-Borradori A., Lane D., et al. A novel CDK inhibitor, CYC202 (R-roscovitine), overcomes the defect in p53-independent apoptosis in B-cell chronic lymphocytic leukemia by down-regulation of genes involved in transcription regulation and repair. Blood 102 11 (2003) 1587 [abstract]
    • (2003) Blood , vol.102 , Issue.11 , pp. 1587
    • Alvi, A.1    Gianella-Borradori, A.2    Lane, D.3
  • 139
    • 11144316653 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitor Roscovitine induces apoptosis in chronic lymphocytic leukemia cells
    • Hahntow I., Schneller F., Oelsner M., et al. Cyclin-dependent kinase inhibitor Roscovitine induces apoptosis in chronic lymphocytic leukemia cells. Leukemia 18 (2004) 747-755
    • (2004) Leukemia , vol.18 , pp. 747-755
    • Hahntow, I.1    Schneller, F.2    Oelsner, M.3
  • 140
    • 0842329845 scopus 로고    scopus 로고
    • Roscovitine sensitizes glioma cells to TRAIL-mediated apoptosis by downregulation of survivin and XIAP
    • Kim E., Kim S., Shin D., et al. Roscovitine sensitizes glioma cells to TRAIL-mediated apoptosis by downregulation of survivin and XIAP. Oncogene 23 (2004) 446-456
    • (2004) Oncogene , vol.23 , pp. 446-456
    • Kim, E.1    Kim, S.2    Shin, D.3
  • 141
    • 19044365679 scopus 로고    scopus 로고
    • CYC202 (R-Roscovitine) induces apoptosis in multiple myeloma cells by down regulation of Mcl-1
    • [abstract]
    • Maccallum D., Melville J., Watt K., et al. CYC202 (R-Roscovitine) induces apoptosis in multiple myeloma cells by down regulation of Mcl-1. Proc Am Assoc Cancer Res 45 (2004) 823 [abstract]
    • (2004) Proc Am Assoc Cancer Res , vol.45 , pp. 823
    • Maccallum, D.1    Melville, J.2    Watt, K.3
  • 142
    • 78649629584 scopus 로고    scopus 로고
    • Antitumor activity of CYC202, a cyclin-dependent kinase inhibitor, in human tumor xenografts in vitro
    • [abstract]
    • Maier A., Kelter G., Gianella-Borradori A., et al. Antitumor activity of CYC202, a cyclin-dependent kinase inhibitor, in human tumor xenografts in vitro. Am Assoc Cancer Res 44 (2003) 713 [abstract]
    • (2003) Am Assoc Cancer Res , vol.44 , pp. 713
    • Maier, A.1    Kelter, G.2    Gianella-Borradori, A.3
  • 143
    • 1642494839 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor CYC202 (R-Roscovitine) inhibits retinoblastoma protein phosphorylation, causes loss of cyclin D1, and activates the mitogen-activated protein kinase pathway
    • Whittaker S.R., Walton M.I., Garrett M.D., and Workman P. The cyclin-dependent kinase inhibitor CYC202 (R-Roscovitine) inhibits retinoblastoma protein phosphorylation, causes loss of cyclin D1, and activates the mitogen-activated protein kinase pathway. Cancer Res 64 (2004) 262-272
    • (2004) Cancer Res , vol.64 , pp. 262-272
    • Whittaker, S.R.1    Walton, M.I.2    Garrett, M.D.3    Workman, P.4
  • 144
    • 0013271756 scopus 로고    scopus 로고
    • Pharmacokinetics (PK) of the oral cyclin dependent kinase inhibitor CYC202 (R-roscovitine) in patients with cancer
    • [abstract]
    • Benson C., Raynaud F., O'Donnell A., et al. Pharmacokinetics (PK) of the oral cyclin dependent kinase inhibitor CYC202 (R-roscovitine) in patients with cancer. Am Assoc Cancer Res 43 (2002) 273 [abstract]
    • (2002) Am Assoc Cancer Res , vol.43 , pp. 273
    • Benson, C.1    Raynaud, F.2    O'Donnell, A.3
  • 145
    • 13244292822 scopus 로고    scopus 로고
    • A phase I trial of oral cyclin dependent kinase inhibitor CYC202 in patients with advanced malignancy
    • [abstract]
    • White J.D., Cassidy J., Twelves C., et al. A phase I trial of oral cyclin dependent kinase inhibitor CYC202 in patients with advanced malignancy. Proc Am Soc Clin Oncol (2004) 3042 [abstract]
    • (2004) Proc Am Soc Clin Oncol , pp. 3042
    • White, J.D.1    Cassidy, J.2    Twelves, C.3
  • 146
    • 2442541492 scopus 로고    scopus 로고
    • A phase I and pharmacokinetic (PK) trial of CYC202, a novel oral cyclin-dependent kinase (CDK) inhibitor, in patients (pts) with advanced solid tumors
    • [abstract 840]
    • Pierga J.Y., Faivre S., Vera K., et al. A phase I and pharmacokinetic (PK) trial of CYC202, a novel oral cyclin-dependent kinase (CDK) inhibitor, in patients (pts) with advanced solid tumors. Proc Am Soc Clin Oncol 22 (2003) 210 [abstract 840]
    • (2003) Proc Am Soc Clin Oncol , vol.22 , pp. 210
    • Pierga, J.Y.1    Faivre, S.2    Vera, K.3
  • 147
    • 1642405155 scopus 로고    scopus 로고
    • A phase I study to determine the safety and pharmacokinetics (PK) of BMS-387032 given intravenously every three weeks in patients with metastatic refractory solid tumors
    • [abstract]
    • Jones S.F., Burris H.A., Kies M., et al. A phase I study to determine the safety and pharmacokinetics (PK) of BMS-387032 given intravenously every three weeks in patients with metastatic refractory solid tumors. Am Soc Clin Oncol 22 (2003) 199 [abstract]
    • (2003) Am Soc Clin Oncol , vol.22 , pp. 199
    • Jones, S.F.1    Burris, H.A.2    Kies, M.3
  • 148
    • 1642405155 scopus 로고    scopus 로고
    • A phase I study to determine the safety and pharmacokinetics (PK) of BMS-387032 with a 24-hour infusion given every three weeks in patients with metastatic refractory solid tumors
    • [abstract]
    • Shapiro G.I., Lewis N., Bai S., et al. A phase I study to determine the safety and pharmacokinetics (PK) of BMS-387032 with a 24-hour infusion given every three weeks in patients with metastatic refractory solid tumors. Am Soc Clin Oncol 22 (2003) 200 [abstract]
    • (2003) Am Soc Clin Oncol , vol.22 , pp. 200
    • Shapiro, G.I.1    Lewis, N.2    Bai, S.3
  • 149
    • 5344257605 scopus 로고    scopus 로고
    • Novel cell cycle inhibitors: characterization in tumor cell lines and normal cycling cells
    • [abstract]
    • Byth K., Geh C., Forder C., et al. Novel cell cycle inhibitors: characterization in tumor cell lines and normal cycling cells. Am Assoc Cancer Res 44 (2003) 714 [abstract]
    • (2003) Am Assoc Cancer Res , vol.44 , pp. 714
    • Byth, K.1    Geh, C.2    Forder, C.3
  • 150
    • 19044392404 scopus 로고    scopus 로고
    • A novel CDK inhibitor induces cell cycle blockade, E2F-1 dependent apoptosis, and cytotoxic synergy with DNA damaging agents
    • [abstract #828]
    • Cai D., Byth K., Shapiro G., et al. A novel CDK inhibitor induces cell cycle blockade, E2F-1 dependent apoptosis, and cytotoxic synergy with DNA damaging agents. Proc AACR 45 (2004) 190 [abstract #828]
    • (2004) Proc AACR , vol.45 , pp. 190
    • Cai, D.1    Byth, K.2    Shapiro, G.3
  • 151
    • 0034843846 scopus 로고    scopus 로고
    • Mechanisms of action of the novel sulfonamide anticancer agent E7070 on cell cycle progression in human non-small cell lung cancer cells
    • Fukuoka K., Usuda J., Iwamoto Y., Fukumoto H., Nakamura T., Yoneda T., et al. Mechanisms of action of the novel sulfonamide anticancer agent E7070 on cell cycle progression in human non-small cell lung cancer cells. Invest New Drugs 19 (2001) 219-227
    • (2001) Invest New Drugs , vol.19 , pp. 219-227
    • Fukuoka, K.1    Usuda, J.2    Iwamoto, Y.3    Fukumoto, H.4    Nakamura, T.5    Yoneda, T.6
  • 152
    • 0036866878 scopus 로고    scopus 로고
    • E7070: a novel synthetic sulfonamide targeting the cell cycle progression for the treatment of cancer
    • Van Kesteren C., Beijnen J.H., and Schellens J.H. E7070: a novel synthetic sulfonamide targeting the cell cycle progression for the treatment of cancer. Anticancer Drugs 13 10 (2002) 989-997
    • (2002) Anticancer Drugs , vol.13 , Issue.10 , pp. 989-997
    • Van Kesteren, C.1    Beijnen, J.H.2    Schellens, J.H.3
  • 153
    • 0036789730 scopus 로고    scopus 로고
    • Population pharmacokinetics of the novel anticancer agent E7070 during four phase I studies: model building and validation
    • Kesteren V., Mathot R.A.A., Raymond J.P., Armand J.P., Dittrich C., Dumez H., et al. Population pharmacokinetics of the novel anticancer agent E7070 during four phase I studies: model building and validation. J Clin Oncol 20 19 (2002) 4065-4073
    • (2002) J Clin Oncol , vol.20 , Issue.19 , pp. 4065-4073
    • Kesteren, V.1    Mathot, R.A.A.2    Raymond, J.P.3    Armand, J.P.4    Dittrich, C.5    Dumez, H.6
  • 154
    • 0034772246 scopus 로고    scopus 로고
    • Phase I and pharmacokinetic study of E7070, a novel sulfonamide, given at a daily times five schedule in patients with solid tumors. A study by the EORTC-early clinical studies group
    • Punt C.J.A., Fumoleau P., van de Walle B., Faber M.N., Ravic M., and Campone M. Phase I and pharmacokinetic study of E7070, a novel sulfonamide, given at a daily times five schedule in patients with solid tumors. A study by the EORTC-early clinical studies group. Ann Oncol 12 9 (2001) 1289-1293
    • (2001) Ann Oncol , vol.12 , Issue.9 , pp. 1289-1293
    • Punt, C.J.A.1    Fumoleau, P.2    van de Walle, B.3    Faber, M.N.4    Ravic, M.5    Campone, M.6
  • 155
    • 0037102283 scopus 로고    scopus 로고
    • Phase I and pharmacokinetic study of E7070, a novel chloroindolyl sulfonamide cell-cycle inhibitor, administered as a 1-hour infusion every three weeks in patietns with advanced cancer
    • Raymond E., ten Bokkel-Huinink W.W., Taieb J., Beijnen J.H., Faivre S., Wanders J., et al. Phase I and pharmacokinetic study of E7070, a novel chloroindolyl sulfonamide cell-cycle inhibitor, administered as a 1-hour infusion every three weeks in patietns with advanced cancer. J Clin Oncol 20 16 (2002) 3508-3521
    • (2002) J Clin Oncol , vol.20 , Issue.16 , pp. 3508-3521
    • Raymond, E.1    ten Bokkel-Huinink, W.W.2    Taieb, J.3    Beijnen, J.H.4    Faivre, S.5    Wanders, J.6
  • 156
    • 0038402755 scopus 로고    scopus 로고
    • A phase I clinical and pharmacokinetic study of E7070, a novel sulfonamide given as a 5-day continuous infusion repeated every 3 weeks in patients with solid tumors
    • Terret C., Zanetta S., Roche H., Schellens J.H., Faber M.N., Waners J., et al. A phase I clinical and pharmacokinetic study of E7070, a novel sulfonamide given as a 5-day continuous infusion repeated every 3 weeks in patients with solid tumors. Eur J Cancer 39 8 (2003) 1097-1104
    • (2003) Eur J Cancer , vol.39 , Issue.8 , pp. 1097-1104
    • Terret, C.1    Zanetta, S.2    Roche, H.3    Schellens, J.H.4    Faber, M.N.5    Waners, J.6
  • 157
    • 0242525657 scopus 로고    scopus 로고
    • Phase I and pharmacokinetic study of E7070, a chloroindolyl-sulfonamide anticancer agent, administered on a weekly schedule to patients with solid tumors
    • Dittrich C., Dumez H., Calvert H., Hanauske A., Faber M.N., Wanders J., et al. Phase I and pharmacokinetic study of E7070, a chloroindolyl-sulfonamide anticancer agent, administered on a weekly schedule to patients with solid tumors. Clin Cancer Res 9 14 (2003) 5195-5204
    • (2003) Clin Cancer Res , vol.9 , Issue.14 , pp. 5195-5204
    • Dittrich, C.1    Dumez, H.2    Calvert, H.3    Hanauske, A.4    Faber, M.N.5    Wanders, J.6
  • 158
    • 2142792056 scopus 로고    scopus 로고
    • A phase II study of E7070 in patients with metastatic, recurrent, or refractory head and neck squamous cell carcinoma (HNSCC): clinical activity and post-treatment modulation of Rb phosphorylation
    • [abstract]
    • Haddad R.I., Shapiro G., Weinstein L., et al. A phase II study of E7070 in patients with metastatic, recurrent, or refractory head and neck squamous cell carcinoma (HNSCC): clinical activity and post-treatment modulation of Rb phosphorylation. Am Soc Clin Oncol 22 (2003) 201 [abstract]
    • (2003) Am Soc Clin Oncol , vol.22 , pp. 201
    • Haddad, R.I.1    Shapiro, G.2    Weinstein, L.3
  • 160
    • 33748557388 scopus 로고    scopus 로고
    • Highly selective inhibition of CDK4 with pyrido[2,3-d]pyrimidine-7-ones
    • [abstract #828]
    • Vanderwel S., Harvey P.J., Sheehan D.J., et al. Highly selective inhibition of CDK4 with pyrido[2,3-d]pyrimidine-7-ones. Proc AACR 45 (2004) 190 [abstract #828]
    • (2004) Proc AACR , vol.45 , pp. 190
    • Vanderwel, S.1    Harvey, P.J.2    Sheehan, D.J.3
  • 161
    • 13344286390 scopus 로고    scopus 로고
    • Inhibition of Cdk4 causes tumor regression
    • [abstract]
    • Booth J., Elliott W., Fry D.W., et al. Inhibition of Cdk4 causes tumor regression. Proc Am Assoc Cancer Res 45 (2004) 831 [abstract]
    • (2004) Proc Am Assoc Cancer Res , vol.45 , pp. 831
    • Booth, J.1    Elliott, W.2    Fry, D.W.3
  • 162
    • 9444228344 scopus 로고    scopus 로고
    • Specific inhibition of cyclin-dependent kinase 4/6 by PD 0332991 and associated antitumor activity in human tumor xenografts
    • Fry D.W., Harvey P.J., Keller P.R., et al. Specific inhibition of cyclin-dependent kinase 4/6 by PD 0332991 and associated antitumor activity in human tumor xenografts. Mol Cancer Ther 3 (2004) 1427-1438
    • (2004) Mol Cancer Ther , vol.3 , pp. 1427-1438
    • Fry, D.W.1    Harvey, P.J.2    Keller, P.R.3
  • 163
    • 0001641514 scopus 로고
    • Mutations of bacteria from virus sensitivity to virus resistance
    • Luria S.E., and Delbruck M. Mutations of bacteria from virus sensitivity to virus resistance. Genetics 28 (1943) 491
    • (1943) Genetics , vol.28 , pp. 491
    • Luria, S.E.1    Delbruck, M.2
  • 164
    • 33748581564 scopus 로고    scopus 로고
    • DeVita, VT. Principles of cancer management: chemotherapy. In: HS DeVita VT, Rosenberg SA, editors. Cancer: principles and practice of oncology. Lippincott-Raven Publishers: Philadelphia PA; 1997. p. 333-47.
  • 165
    • 0022409386 scopus 로고
    • A model for tumor response to chemotherapy: an integration of the stem cell and somatic mutation hypotheses
    • Goldie J.H., and Coldman A.J. A model for tumor response to chemotherapy: an integration of the stem cell and somatic mutation hypotheses. Cancer Invest 3 6 (1985) 553-564
    • (1985) Cancer Invest , vol.3 , Issue.6 , pp. 553-564
    • Goldie, J.H.1    Coldman, A.J.2
  • 166
    • 0018569942 scopus 로고
    • A mathematic model for relating the drug sensitivity of tumors to their spontaneous mutation rate
    • Goldie J.H., and Coldman A.J. A mathematic model for relating the drug sensitivity of tumors to their spontaneous mutation rate. Cancer Treat Rep 63 11-12 (1979) 1727-1733
    • (1979) Cancer Treat Rep , vol.63 , Issue.11-12 , pp. 1727-1733
    • Goldie, J.H.1    Coldman, A.J.2
  • 167
    • 0034887884 scopus 로고    scopus 로고
    • Cell cycle mediated drug resistance: an emerging concept in cancer therapy
    • Shah M.A., and Schwartz G.K. Cell cycle mediated drug resistance: an emerging concept in cancer therapy. Clin Cancer Res 7 8 (2001) 2168-2181
    • (2001) Clin Cancer Res , vol.7 , Issue.8 , pp. 2168-2181
    • Shah, M.A.1    Schwartz, G.K.2
  • 168
    • 0031040149 scopus 로고    scopus 로고
    • The development and clinical utility of the taxane class of antimicrotubule chemotherapy agents
    • Rowinsky E.K. The development and clinical utility of the taxane class of antimicrotubule chemotherapy agents. Annu Rev Med 48 (1997) 353-374
    • (1997) Annu Rev Med , vol.48 , pp. 353-374
    • Rowinsky, E.K.1
  • 169
    • 0018387446 scopus 로고
    • Promotion of microtubule assembly in vitro by taxol
    • Schiff P.B., Fant J., and Horwitz S.B. Promotion of microtubule assembly in vitro by taxol. Nature 277 5698 (1979) 665-667
    • (1979) Nature , vol.277 , Issue.5698 , pp. 665-667
    • Schiff, P.B.1    Fant, J.2    Horwitz, S.B.3
  • 170
    • 0019889058 scopus 로고
    • Taxol assembles tubulin in the absence of exogenous guanosine 5′-triphosphate or microtubule-associated proteins
    • Schiff P.B., and Horwitz S.B. Taxol assembles tubulin in the absence of exogenous guanosine 5′-triphosphate or microtubule-associated proteins. Biochemistry 20 11 (1981) 3247-3252
    • (1981) Biochemistry , vol.20 , Issue.11 , pp. 3247-3252
    • Schiff, P.B.1    Horwitz, S.B.2
  • 171
    • 0000297058 scopus 로고
    • Taxol stabilizes microtubules in mouse fibroblast cells
    • Schiff P.B., and Horwitz S.B. Taxol stabilizes microtubules in mouse fibroblast cells. Proc Natl Acad Sci USA 77 3 (1980) 1561-1565
    • (1980) Proc Natl Acad Sci USA , vol.77 , Issue.3 , pp. 1561-1565
    • Schiff, P.B.1    Horwitz, S.B.2
  • 172
    • 0040077174 scopus 로고    scopus 로고
    • CDK4 down-regulation induced by paclitaxel is associated with G1 arrest in gastric cancer cells
    • Yoo Y.D., Park J.K., Choi J.Y., Lee K.H., Kang Y.K., Kim C.S., et al. CDK4 down-regulation induced by paclitaxel is associated with G1 arrest in gastric cancer cells. Clin Cancer Res 4 12 (1998) 3063-3068
    • (1998) Clin Cancer Res , vol.4 , Issue.12 , pp. 3063-3068
    • Yoo, Y.D.1    Park, J.K.2    Choi, J.Y.3    Lee, K.H.4    Kang, Y.K.5    Kim, C.S.6
  • 173
    • 0028070358 scopus 로고
    • Paclitaxel inhibits progression of mitotic cells to G1 phase by interference with spindle formation without affecting other microtubule functions during anaphase and telephase
    • Long B.H., and Fairchild C.R. Paclitaxel inhibits progression of mitotic cells to G1 phase by interference with spindle formation without affecting other microtubule functions during anaphase and telephase. Cancer Res 54 16 (1994) 4355-4361
    • (1994) Cancer Res , vol.54 , Issue.16 , pp. 4355-4361
    • Long, B.H.1    Fairchild, C.R.2
  • 174
    • 0025809298 scopus 로고
    • A phase I trial of taxol given by a 6-hour intravenous infusion
    • Brown T., Havlin K., Weiss G., Cagnola J., Koeller J., Kuhn J., et al. A phase I trial of taxol given by a 6-hour intravenous infusion. J Clin Oncol 9 7 (1991) 1261-1267
    • (1991) J Clin Oncol , vol.9 , Issue.7 , pp. 1261-1267
    • Brown, T.1    Havlin, K.2    Weiss, G.3    Cagnola, J.4    Koeller, J.5    Kuhn, J.6
  • 175
    • 0028170877 scopus 로고
    • Activation of p34cdc2 coincident with taxol-induced apoptosis
    • Donaldson K.L., Goolsby G.L., Kiener P.A., and Wahl A.F. Activation of p34cdc2 coincident with taxol-induced apoptosis. Cell Growth Differ 5 10 (1994) 1041-1050
    • (1994) Cell Growth Differ , vol.5 , Issue.10 , pp. 1041-1050
    • Donaldson, K.L.1    Goolsby, G.L.2    Kiener, P.A.3    Wahl, A.F.4
  • 176
    • 0031893985 scopus 로고    scopus 로고
    • Accumulation of cyclin B1, activation of cyclin B1-dependent kinase and induction of programmed cell death in human epidermoid carcinoma KB cells treated with Taxol
    • Ling Y.H., Yank Y., Consoli U., Tornos C., Andreeff M., and Perez-Soler R. Accumulation of cyclin B1, activation of cyclin B1-dependent kinase and induction of programmed cell death in human epidermoid carcinoma KB cells treated with Taxol. Int J Cancer 75 (1998) 925-932
    • (1998) Int J Cancer , vol.75 , pp. 925-932
    • Ling, Y.H.1    Yank, Y.2    Consoli, U.3    Tornos, C.4    Andreeff, M.5    Perez-Soler, R.6
  • 177
    • 0033145508 scopus 로고    scopus 로고
    • Temporal and spatial control of cyclin B1 destruction in metaphase
    • Clute P., and Pines J. Temporal and spatial control of cyclin B1 destruction in metaphase. Nat Cell Biol 1 (1999) 82-86
    • (1999) Nat Cell Biol , vol.1 , pp. 82-86
    • Clute, P.1    Pines, J.2
  • 178
    • 0032214980 scopus 로고    scopus 로고
    • Overexpression of ErbB2 blocks taxol-induced apoptosis by upregulation of p21Cip1 which inhibits p34Cdc2 kinase
    • Yu D., Jing T., Liu B., Yau J., Tan M., McDonnel T.J., et al. Overexpression of ErbB2 blocks taxol-induced apoptosis by upregulation of p21Cip1 which inhibits p34Cdc2 kinase. Mol Cell 2 (1998) 581-591
    • (1998) Mol Cell , vol.2 , pp. 581-591
    • Yu, D.1    Jing, T.2    Liu, B.3    Yau, J.4    Tan, M.5    McDonnel, T.J.6
  • 179
    • 0028241451 scopus 로고
    • Cytotoxicity of the anticancer agents cisplatin and taxol during cell proliferation and the cell cycle
    • Donaldson K.L., Goolsby G.L., and Wahl A.F. Cytotoxicity of the anticancer agents cisplatin and taxol during cell proliferation and the cell cycle. Int J Cancer 57 6 (1994) 847-855
    • (1994) Int J Cancer , vol.57 , Issue.6 , pp. 847-855
    • Donaldson, K.L.1    Goolsby, G.L.2    Wahl, A.F.3
  • 181
    • 0030048476 scopus 로고    scopus 로고
    • Phosphorylation of Bcl-2 protein and association with p21Ras in Ras-induced apoptosis
    • Chen C.Y., and Faller D.V. Phosphorylation of Bcl-2 protein and association with p21Ras in Ras-induced apoptosis. J Biol Chem 271 5 (1996) 2376-2379
    • (1996) J Biol Chem , vol.271 , Issue.5 , pp. 2376-2379
    • Chen, C.Y.1    Faller, D.V.2
  • 182
    • 0032883001 scopus 로고    scopus 로고
    • Molecular effects of paclitaxel: myths and reality (a critical review)
    • Blagosklonny M.V., and Fojo T. Molecular effects of paclitaxel: myths and reality (a critical review). Int J Cancer 83 2 (1999) 151-156
    • (1999) Int J Cancer , vol.83 , Issue.2 , pp. 151-156
    • Blagosklonny, M.V.1    Fojo, T.2
  • 183
    • 0029807822 scopus 로고    scopus 로고
    • Differential Taxol-dependent arrest of transformed and nontransformed cells in the G1 phase of the cell cycle, and specific related mortality of transformed cells
    • Trielli M.O., Andreassen P.R., Lacroix F.B., and Margolis R.L. Differential Taxol-dependent arrest of transformed and nontransformed cells in the G1 phase of the cell cycle, and specific related mortality of transformed cells. J Cell Biol 135 (1996) 689-700
    • (1996) J Cell Biol , vol.135 , pp. 689-700
    • Trielli, M.O.1    Andreassen, P.R.2    Lacroix, F.B.3    Margolis, R.L.4
  • 184
    • 0034212385 scopus 로고    scopus 로고
    • Paclitaxel-Induced cell death
    • Wang T.-H., Wang H.-S., and Soong Y.-K. Paclitaxel-Induced cell death. Cancer 88 (2000) 2619-2628
    • (2000) Cancer , vol.88 , pp. 2619-2628
    • Wang, T.-H.1    Wang, H.-S.2    Soong, Y.-K.3
  • 185
    • 0032804733 scopus 로고    scopus 로고
    • Sequential dependent enhancement of caspase activation and apoptosis by flavopiridol on paclitaxel-treated human gastric and breast cancer cells
    • Motwani M., Delohery T.M., and Schwartz G.K. Sequential dependent enhancement of caspase activation and apoptosis by flavopiridol on paclitaxel-treated human gastric and breast cancer cells. Clin Cancer Res 5 7 (1999) 1876-1883
    • (1999) Clin Cancer Res , vol.5 , Issue.7 , pp. 1876-1883
    • Motwani, M.1    Delohery, T.M.2    Schwartz, G.K.3
  • 186
    • 0000351131 scopus 로고    scopus 로고
    • A phase I trial of weekly sequential bryostatin (Bryo) and paclitaxel in patients with advanced solid tumors
    • [abstract]
    • Kaubisch A., Kelsen D.P., Saltz L., Kemeny N., O'Reilly E., Ilson D., et al. A phase I trial of weekly sequential bryostatin (Bryo) and paclitaxel in patients with advanced solid tumors. Proc Am Soc Clin Oncol 18 (1999) 639 [abstract]
    • (1999) Proc Am Soc Clin Oncol , vol.18 , pp. 639
    • Kaubisch, A.1    Kelsen, D.P.2    Saltz, L.3    Kemeny, N.4    O'Reilly, E.5    Ilson, D.6
  • 187
    • 0030812207 scopus 로고    scopus 로고
    • Cytotoxic synergy between flavopiridol (NSC 649890, L86-8275) and various antineoplastic agents: the importance of sequence of administration
    • Bible K.C., and Kaufmann S.H. Cytotoxic synergy between flavopiridol (NSC 649890, L86-8275) and various antineoplastic agents: the importance of sequence of administration. Cancer Res 57 (1997) 3375-3380
    • (1997) Cancer Res , vol.57 , pp. 3375-3380
    • Bible, K.C.1    Kaufmann, S.H.2
  • 188
    • 0033609299 scopus 로고    scopus 로고
    • Loss of the bcl-2 phosphorylation loop domain increases resistance of human leukemia cells (U937) to paclitaxel-mediated mitochondrial dysfunction and apoptosis
    • Wang S., Wang Z., Boise L., Dent P., and Grant S. Loss of the bcl-2 phosphorylation loop domain increases resistance of human leukemia cells (U937) to paclitaxel-mediated mitochondrial dysfunction and apoptosis. Biochem Biophys Res Commun 259 1 (1999) 67-72
    • (1999) Biochem Biophys Res Commun , vol.259 , Issue.1 , pp. 67-72
    • Wang, S.1    Wang, Z.2    Boise, L.3    Dent, P.4    Grant, S.5
  • 189
    • 0031843863 scopus 로고    scopus 로고
    • Bcl-xL modulates apoptosis induced by anticancer drugs and delays DEVDase and DNA fragmentation-promoting activities
    • Schmitt E., Cimoli G., Steyaert A., and Bertrand R. Bcl-xL modulates apoptosis induced by anticancer drugs and delays DEVDase and DNA fragmentation-promoting activities. Exp Cell Res 240 1 (1998) 107-121
    • (1998) Exp Cell Res , vol.240 , Issue.1 , pp. 107-121
    • Schmitt, E.1    Cimoli, G.2    Steyaert, A.3    Bertrand, R.4
  • 190
    • 0032876984 scopus 로고    scopus 로고
    • Wang, S, Wang, Z, Boise, LH, Dent, P, G.S. Bryostatin-1 enhances paclitaxel induced mitochondrial dysfunction and apoptosis in human leukemia cells (U937) ectopically expressing Bcl-xl. Leukemia 1999;13(10):1564-73.
  • 191
    • 0032169905 scopus 로고    scopus 로고
    • Effect of bryostatin-1 on taxol-induced apoptosis and cytotoxicity in human leukemia cells (U937)
    • Wang S., Guo C., Castillo A., Dent P., and Grant S. Effect of bryostatin-1 on taxol-induced apoptosis and cytotoxicity in human leukemia cells (U937). Biochem Pharmacol 56 5 (1998) 635-644
    • (1998) Biochem Pharmacol , vol.56 , Issue.5 , pp. 635-644
    • Wang, S.1    Guo, C.2    Castillo, A.3    Dent, P.4    Grant, S.5
  • 192
    • 0037089691 scopus 로고    scopus 로고
    • Phase I study of the cyclin-dependent kinase inhibitor flavopiridol in combination with paclitaxel in patients with advanced solid tumors
    • Schwartz G.K., O'Reilly E., Ilson D., Saltz L., Sharma S.K., Tong W., et al. Phase I study of the cyclin-dependent kinase inhibitor flavopiridol in combination with paclitaxel in patients with advanced solid tumors. J Clin Oncol 20 8 (2001) 2157-2170
    • (2001) J Clin Oncol , vol.20 , Issue.8 , pp. 2157-2170
    • Schwartz, G.K.1    O'Reilly, E.2    Ilson, D.3    Saltz, L.4    Sharma, S.K.5    Tong, W.6
  • 193
    • 7144248725 scopus 로고
    • Plant anti-tumor agents 1. The isolation and structure of camptothecin, a novel alkaloidal leukemia and tumor inhibitor from camptotheca acuminata
    • Wall M.E., Wani M.C., Cook C.E., et al. Plant anti-tumor agents 1. The isolation and structure of camptothecin, a novel alkaloidal leukemia and tumor inhibitor from camptotheca acuminata. J Am Chem Soc 88 (1966) 3888-3890
    • (1966) J Am Chem Soc , vol.88 , pp. 3888-3890
    • Wall, M.E.1    Wani, M.C.2    Cook, C.E.3
  • 194
    • 0027447420 scopus 로고
    • The current status of camptothecin analogues as antitumor agents
    • Slichenmeyer W.J., Rowinsky E.K., Donehower R.C., and Kaufmann S.C. The current status of camptothecin analogues as antitumor agents. JNCI 85 (1993) 271-291
    • (1993) JNCI , vol.85 , pp. 271-291
    • Slichenmeyer, W.J.1    Rowinsky, E.K.2    Donehower, R.C.3    Kaufmann, S.C.4
  • 195
    • 0015451631 scopus 로고
    • Action of camptothecin on mammalian cells in culture
    • Li L.H., Fraser T.J., Olin E.J., and Bhuyan B.K. Action of camptothecin on mammalian cells in culture. Cancer Res 32 12 (1972) 2643-2650
    • (1972) Cancer Res , vol.32 , Issue.12 , pp. 2643-2650
    • Li, L.H.1    Fraser, T.J.2    Olin, E.J.3    Bhuyan, B.K.4
  • 196
    • 0027972726 scopus 로고
    • Topoisomerase I inhibitors: topotecan and irinotecan
    • Creemers C.J., Lund B., and Verwij J. Topoisomerase I inhibitors: topotecan and irinotecan. Cancer Treat Rev 20 (1994) 73-96
    • (1994) Cancer Treat Rev , vol.20 , pp. 73-96
    • Creemers, C.J.1    Lund, B.2    Verwij, J.3
  • 197
    • 0022340594 scopus 로고
    • Camptothecin induces protein-linked DNA breaks via mammalian Topoisomerase I
    • Hsiang Y.-H., Hertzberg R., Hecht S., and Liu L.F. Camptothecin induces protein-linked DNA breaks via mammalian Topoisomerase I. J Biol Chem 260 (1985) 14873-14878
    • (1985) J Biol Chem , vol.260 , pp. 14873-14878
    • Hsiang, Y.-H.1    Hertzberg, R.2    Hecht, S.3    Liu, L.F.4
  • 198
    • 0024420685 scopus 로고
    • Arrest of replication forks by drug-stabilized topoisomerase I-DNA cleavable complexes as a mechanism of cell killing by camptotheicin
    • Hsiang Y.-H., Lihou M.G., and Liu F. Arrest of replication forks by drug-stabilized topoisomerase I-DNA cleavable complexes as a mechanism of cell killing by camptotheicin. Cancer Res 49 (1989) 5077-5082
    • (1989) Cancer Res , vol.49 , pp. 5077-5082
    • Hsiang, Y.-H.1    Lihou, M.G.2    Liu, F.3
  • 199
    • 0033178946 scopus 로고    scopus 로고
    • Caspase inhibition in camptothecin-treated U-937 cells is coupled with a shift from apoptosis to transient G1 arrest followed by necrotic cell death
    • Sane A.T., and Bertrand R. Caspase inhibition in camptothecin-treated U-937 cells is coupled with a shift from apoptosis to transient G1 arrest followed by necrotic cell death. Cancer Res 59 15 (1999) 3565-3569
    • (1999) Cancer Res , vol.59 , Issue.15 , pp. 3565-3569
    • Sane, A.T.1    Bertrand, R.2
  • 200
    • 0242333898 scopus 로고    scopus 로고
    • Cell-cycle-dependent three-dimensional redistribution of nuclear proteins, P120, pKi-67, and SC 35 splicing factor, in the presence of topoisomerase I inhibitor camptothecin
    • Elias E., Lalun N., Lorenzato M., et al. Cell-cycle-dependent three-dimensional redistribution of nuclear proteins, P120, pKi-67, and SC 35 splicing factor, in the presence of topoisomerase I inhibitor camptothecin. Exp Cell Res 291 1 (2003) 176-188
    • (2003) Exp Cell Res , vol.291 , Issue.1 , pp. 176-188
    • Elias, E.1    Lalun, N.2    Lorenzato, M.3
  • 201
    • 0026625512 scopus 로고
    • The involvement of active DNA synthesis in camptothecin-induced G2 arrest: altered regulation of p34cdc2/cyclin B
    • Tsao Y.P., D'Apra P., and Liu L.F. The involvement of active DNA synthesis in camptothecin-induced G2 arrest: altered regulation of p34cdc2/cyclin B. Cancer Res 52 7 (1992) 1823-1829
    • (1992) Cancer Res , vol.52 , Issue.7 , pp. 1823-1829
    • Tsao, Y.P.1    D'Apra, P.2    Liu, L.F.3
  • 202
    • 0037135554 scopus 로고    scopus 로고
    • Abrogation of the S phase DNA damage checkpoint results in S phase progression of premature mitosis depending on the concentration of 7-hydroxystaurosporine and the kinetics of Cdc25C activation
    • Kohn E.A., Ruth N.D., Brown M.K., Linvingstone M., and Eastman A. Abrogation of the S phase DNA damage checkpoint results in S phase progression of premature mitosis depending on the concentration of 7-hydroxystaurosporine and the kinetics of Cdc25C activation. J Biol Chem 277 29 (2002) 26553-26564
    • (2002) J Biol Chem , vol.277 , Issue.29 , pp. 26553-26564
    • Kohn, E.A.1    Ruth, N.D.2    Brown, M.K.3    Linvingstone, M.4    Eastman, A.5
  • 203
    • 0035848819 scopus 로고    scopus 로고
    • The ATM-Chk2-Cdc25A checkpoint pathway gaurds against radioresistant DNA synthesis
    • Falck J., Mailand N., Syljuasen R.G., Bartek J., and Lukas J. The ATM-Chk2-Cdc25A checkpoint pathway gaurds against radioresistant DNA synthesis. Nature 410 (2001) 842-847
    • (2001) Nature , vol.410 , pp. 842-847
    • Falck, J.1    Mailand, N.2    Syljuasen, R.G.3    Bartek, J.4    Lukas, J.5
  • 204
    • 0031588345 scopus 로고    scopus 로고
    • Topisomerase-I inhibitors for human malignant glioma: differential modulation of p53, p21, bax, and bcl-2 expression and of CD95-mediated apoptosis by camptothecin and beta-lapachone
    • Weller M., Winter S., Schmidt C., Esser P., Fontana A., Dichgans J., et al. Topisomerase-I inhibitors for human malignant glioma: differential modulation of p53, p21, bax, and bcl-2 expression and of CD95-mediated apoptosis by camptothecin and beta-lapachone. Intl J Cancer 73 5 (1997) 707-714
    • (1997) Intl J Cancer , vol.73 , Issue.5 , pp. 707-714
    • Weller, M.1    Winter, S.2    Schmidt, C.3    Esser, P.4    Fontana, A.5    Dichgans, J.6
  • 205
    • 0028873880 scopus 로고
    • Unscheduled activation of cyclin B1/cdc2 kinase in human promyelocytic leukemia cell line HL60 cells ungroing apoptosis induced by DNA damage
    • Shimizu T., O'Connor P.M., Kohn K.W., and Pommier Y. Unscheduled activation of cyclin B1/cdc2 kinase in human promyelocytic leukemia cell line HL60 cells ungroing apoptosis induced by DNA damage. Cancer Res 55 (1995) 228-231
    • (1995) Cancer Res , vol.55 , pp. 228-231
    • Shimizu, T.1    O'Connor, P.M.2    Kohn, K.W.3    Pommier, Y.4
  • 206
    • 0008461578 scopus 로고    scopus 로고
    • Phase I clinical and pharmacokinetic study of irinotecan, fluorouracil, and leucovorin in patients with advanced solid tumors
    • Saltz L.B., Kanowitz J., Kemeny N.E., Schaaf L., Spriggs D., Staton B.A., et al. Phase I clinical and pharmacokinetic study of irinotecan, fluorouracil, and leucovorin in patients with advanced solid tumors. J Clin Oncol 14 11 (1996) 2959-2967
    • (1996) J Clin Oncol , vol.14 , Issue.11 , pp. 2959-2967
    • Saltz, L.B.1    Kanowitz, J.2    Kemeny, N.E.3    Schaaf, L.4    Spriggs, D.5    Staton, B.A.6
  • 207
    • 0034727063 scopus 로고    scopus 로고
    • Irinotecan plus fluorouracil and leucovorin for metastatic colorectal carcinoma. Irinotecan Study Group
    • Saltz L.B., Cox J.V., Blanke C., Rosen L.S., Fehrenbacher L., Moore M.J., et al. Irinotecan plus fluorouracil and leucovorin for metastatic colorectal carcinoma. Irinotecan Study Group. N Engl J Med 343 13 (2000) 905-912
    • (2000) N Engl J Med , vol.343 , Issue.13 , pp. 905-912
    • Saltz, L.B.1    Cox, J.V.2    Blanke, C.3    Rosen, L.S.4    Fehrenbacher, L.5    Moore, M.J.6
  • 208
    • 0030475717 scopus 로고    scopus 로고
    • Clinical trials of irinotecan hydrochloride (CPT, campto injection, topotecan injection) in Japan
    • Saijo N. Clinical trials of irinotecan hydrochloride (CPT, campto injection, topotecan injection) in Japan. Ann N Y Acad Sci 803 (1996) 292-305
    • (1996) Ann N Y Acad Sci , vol.803 , pp. 292-305
    • Saijo, N.1
  • 209
    • 21344454905 scopus 로고    scopus 로고
    • In vitro and in vivo irinotecan-induced changes in expression profiles of cell cycle and apoptosis-associated genes in acute myeloid leukemia cells
    • Minderman H., Conroy J.M., O'Loughlin K.L., McQuaid D., Quinn P., et al. In vitro and in vivo irinotecan-induced changes in expression profiles of cell cycle and apoptosis-associated genes in acute myeloid leukemia cells. Mol Cancer Ther 4 6 (2005) 885-900
    • (2005) Mol Cancer Ther , vol.4 , Issue.6 , pp. 885-900
    • Minderman, H.1    Conroy, J.M.2    O'Loughlin, K.L.3    McQuaid, D.4    Quinn, P.5
  • 210
    • 0028849274 scopus 로고
    • P21 is necessary for the p53 mediated G1 arrest in human cancer cells
    • Waldman T., Kinzler K.W., and Vogelstein B. P21 is necessary for the p53 mediated G1 arrest in human cancer cells. Cancer Res 55 (1995) 5187-5195
    • (1995) Cancer Res , vol.55 , pp. 5187-5195
    • Waldman, T.1    Kinzler, K.W.2    Vogelstein, B.3
  • 211
    • 33748562062 scopus 로고    scopus 로고
    • Shah, MA, Kortmansky, J, Gonen, M, Tse, A, Lefkowitz, R, Kelsen, D, et al. A phase I study of weekly irinotecan (CPT), cisplatin (CIS), and flavopiridol (F). 2004 Annual Meeting Proceedings (Post-Meeting Edition). J Clin Oncol 2004;22(14S):4027.
  • 212
    • 0029661932 scopus 로고    scopus 로고
    • Correlations between S and G2 arrest and the cytotoxicity of camptothecin in human colon carcinoma cells
    • Goldwasser F., Shimizu T., Jackman J., Hoki Y., O'Connor P.M., Kohn K.W., et al. Correlations between S and G2 arrest and the cytotoxicity of camptothecin in human colon carcinoma cells. Cancer Res 56 19 (1996) 4430-4437
    • (1996) Cancer Res , vol.56 , Issue.19 , pp. 4430-4437
    • Goldwasser, F.1    Shimizu, T.2    Jackman, J.3    Hoki, Y.4    O'Connor, P.M.5    Kohn, K.W.6
  • 213
    • 0030870632 scopus 로고    scopus 로고
    • Abrogation of an S-phase checkpoint and potentiation of camptothecin cytotoxicity by 7-hydroxystaurosporine (UCN-01) in human cancer cell lines, possibly influenced by p53 function
    • Shao R.G., Cao C.X., Shimizu T., O'Connor P.M., Kohn K.W., and Pommier Y. Abrogation of an S-phase checkpoint and potentiation of camptothecin cytotoxicity by 7-hydroxystaurosporine (UCN-01) in human cancer cell lines, possibly influenced by p53 function. Cancer Res 57 18 (1997) 4029-4035
    • (1997) Cancer Res , vol.57 , Issue.18 , pp. 4029-4035
    • Shao, R.G.1    Cao, C.X.2    Shimizu, T.3    O'Connor, P.M.4    Kohn, K.W.5    Pommier, Y.6
  • 214
    • 0000061105 scopus 로고    scopus 로고
    • Enhancement of camptothecin-induced cytotoxicity with UCN-01 in breast cancer cells: abrogation of S/G2 arrest
    • Jones C.B., Clements M.K., Wasi S., and Daoud S.S. Enhancement of camptothecin-induced cytotoxicity with UCN-01 in breast cancer cells: abrogation of S/G2 arrest. Cancer Chemother Pharmacol 45 (2000) 252-258
    • (2000) Cancer Chemother Pharmacol , vol.45 , pp. 252-258
    • Jones, C.B.1    Clements, M.K.2    Wasi, S.3    Daoud, S.S.4
  • 215
    • 0032970814 scopus 로고    scopus 로고
    • Apoptotic response to camptothecin and 7-hydroxystaurosporine (UCN-01) in the 8 human breast cancer cell lines of the NCI anticancer drugs screen: multifactorial relationships with topoisomerase I, protein kinase C, Bcl-2, p53, MDM-2, and caspace pathways
    • Nieves-Neira W., and Pommier Y. Apoptotic response to camptothecin and 7-hydroxystaurosporine (UCN-01) in the 8 human breast cancer cell lines of the NCI anticancer drugs screen: multifactorial relationships with topoisomerase I, protein kinase C, Bcl-2, p53, MDM-2, and caspace pathways. Int J Cancer 82 (1999) 396-404
    • (1999) Int J Cancer , vol.82 , pp. 396-404
    • Nieves-Neira, W.1    Pommier, Y.2
  • 216
    • 85011938579 scopus 로고    scopus 로고
    • Abrogation of the G2/M checkpoint by 7-hydroxystaurosporine (UCN-01) on SN-38 treated cells: a strategy for targeting tumors with defective cell cycle checkpoints
    • Tse A., and Schwartz G.K. Abrogation of the G2/M checkpoint by 7-hydroxystaurosporine (UCN-01) on SN-38 treated cells: a strategy for targeting tumors with defective cell cycle checkpoints. Am Assoc Cancer Res (2002)
    • (2002) Am Assoc Cancer Res
    • Tse, A.1    Schwartz, G.K.2
  • 217
    • 0036044864 scopus 로고    scopus 로고
    • Influence of G2 arrest on the cytotoxicity of DNA topoisomerase inhibitors toward human carcinoma cells with different p53 status
    • Bozko P., Larsen A.K., Raymond E., and Skladanowski A. Influence of G2 arrest on the cytotoxicity of DNA topoisomerase inhibitors toward human carcinoma cells with different p53 status. Acta Biochim Pol 49 1 (2002) 109-119
    • (2002) Acta Biochim Pol , vol.49 , Issue.1 , pp. 109-119
    • Bozko, P.1    Larsen, A.K.2    Raymond, E.3    Skladanowski, A.4
  • 218
    • 0000329023 scopus 로고    scopus 로고
    • Antimetabolites
    • DeVita V.T., Hellman S., and Rosenberg S.A. (Eds), Lippincott-Raven, Philadelphia
    • Allegra C.J., and Grem J.L. Antimetabolites. In: DeVita V.T., Hellman S., and Rosenberg S.A. (Eds). Cancer: principles and practice of oncology (1997), Lippincott-Raven, Philadelphia 432-452
    • (1997) Cancer: principles and practice of oncology , pp. 432-452
    • Allegra, C.J.1    Grem, J.L.2
  • 219
    • 0023667703 scopus 로고
    • Kinetics and thermodynamics of the interaction of 5-fluoro-2′-deoxyuridylate with thymidylate synthase
    • Santi D.V., McHenry C.S., Raines R.T., and Ivanetich K.M. Kinetics and thermodynamics of the interaction of 5-fluoro-2′-deoxyuridylate with thymidylate synthase. Biochemistry 26 26 (1987) 8606-8613
    • (1987) Biochemistry , vol.26 , Issue.26 , pp. 8606-8613
    • Santi, D.V.1    McHenry, C.S.2    Raines, R.T.3    Ivanetich, K.M.4
  • 220
    • 0032994840 scopus 로고    scopus 로고
    • Thymidylate synthase level as the main predictive parameter for sensitivity to 5-fluorouracil, but not for folate-based thymidylate synthase inhibitors, in 13 nonselected colon cancer cell lines
    • van Triest B., Pinedo H.M., van Hensbergen Y., Smid K., Telleman F., Schoenmakers P.S., et al. Thymidylate synthase level as the main predictive parameter for sensitivity to 5-fluorouracil, but not for folate-based thymidylate synthase inhibitors, in 13 nonselected colon cancer cell lines. Clin Cancer Res 5 3 (1999) 643-654
    • (1999) Clin Cancer Res , vol.5 , Issue.3 , pp. 643-654
    • van Triest, B.1    Pinedo, H.M.2    van Hensbergen, Y.3    Smid, K.4    Telleman, F.5    Schoenmakers, P.S.6
  • 221
    • 0032974159 scopus 로고    scopus 로고
    • Sequence-dependent antagonism between fluorouracil and paclitaxel in human breast cancer cells
    • Grem J.L., Nguyen D., Monahan B.P., Kao V., and Geoffroy F.J. Sequence-dependent antagonism between fluorouracil and paclitaxel in human breast cancer cells. Biochem Pharmacol 58 3 (1999) 477-486
    • (1999) Biochem Pharmacol , vol.58 , Issue.3 , pp. 477-486
    • Grem, J.L.1    Nguyen, D.2    Monahan, B.P.3    Kao, V.4    Geoffroy, F.J.5
  • 222
    • 0032810342 scopus 로고    scopus 로고
    • Effect of 5-fluorouracil on cell cycle regulatory proteins in human colon cancer cell line
    • Takeda H., Haisa M., Naomoto Y., Kawashima R., Satomoto K., Yamatuji T., et al. Effect of 5-fluorouracil on cell cycle regulatory proteins in human colon cancer cell line. Jpn J Cancer Res 90 6 (1999) 677-684
    • (1999) Jpn J Cancer Res , vol.90 , Issue.6 , pp. 677-684
    • Takeda, H.1    Haisa, M.2    Naomoto, Y.3    Kawashima, R.4    Satomoto, K.5    Yamatuji, T.6
  • 223
    • 0021812170 scopus 로고
    • Transcriptional regulation of mouse dihydrofolate reductase in the cell cycle
    • Farnham P.J., and Schimke R.T. Transcriptional regulation of mouse dihydrofolate reductase in the cell cycle. J Biol Chem 260 12 (1985) 7675-7680
    • (1985) J Biol Chem , vol.260 , Issue.12 , pp. 7675-7680
    • Farnham, P.J.1    Schimke, R.T.2
  • 224
    • 0022473119 scopus 로고
    • Cell-cycle-directed regulation of thymidylate synthase messenger RNA in human diploid fibroblasts stimulated to proliferate
    • Ayusawa D., Shimizu K., Koyama H., Kaneda S., Takeishi K., and Seno T. Cell-cycle-directed regulation of thymidylate synthase messenger RNA in human diploid fibroblasts stimulated to proliferate. J Mol Biol 190 4 (1986) 559-567
    • (1986) J Mol Biol , vol.190 , Issue.4 , pp. 559-567
    • Ayusawa, D.1    Shimizu, K.2    Koyama, H.3    Kaneda, S.4    Takeishi, K.5    Seno, T.6
  • 225
    • 33748579826 scopus 로고    scopus 로고
    • A phase I/pharmacologic study of UCN-01 in combination with 5-fluorouracil in patients with advanced solid tumors
    • Miami, FL
    • Kortmansky J., Shah M.A., Kemeny N., Kelsen D., Spriggs D., et al. A phase I/pharmacologic study of UCN-01 in combination with 5-fluorouracil in patients with advanced solid tumors. Proceedings of the NCI-EORTC Conference. Miami, FL (2001)
    • (2001) Proceedings of the NCI-EORTC Conference
    • Kortmansky, J.1    Shah, M.A.2    Kemeny, N.3    Kelsen, D.4    Spriggs, D.5
  • 226
    • 0023681189 scopus 로고
    • Mechanism of cis-diamminedichloroplatinum(II)-induced cytotoxicity: role of G2 arrest and DNA double strand breaks
    • Sorenson C.M., and Eastman A. Mechanism of cis-diamminedichloroplatinum(II)-induced cytotoxicity: role of G2 arrest and DNA double strand breaks. Cancer Res 48 (1988) 4484-4488
    • (1988) Cancer Res , vol.48 , pp. 4484-4488
    • Sorenson, C.M.1    Eastman, A.2
  • 227
    • 0025413184 scopus 로고
    • Premature mitosis induced in mammalian cells by the protein kinase inhibitors 2-aminopurine and 6-dimethylaminopurine
    • Schlegel R., Belinsky G.S., and Harris M.O. Premature mitosis induced in mammalian cells by the protein kinase inhibitors 2-aminopurine and 6-dimethylaminopurine. Cell Growth Differ 1 4 (1990) 171-178
    • (1990) Cell Growth Differ , vol.1 , Issue.4 , pp. 171-178
    • Schlegel, R.1    Belinsky, G.S.2    Harris, M.O.3
  • 228
    • 0028094424 scopus 로고
    • The role of cell cycle progression in cisplatin-induced apoptosis in Chinese hamster ovary cells
    • Demarcq C., Bunch R.T., Creswell D., and Eastman A. The role of cell cycle progression in cisplatin-induced apoptosis in Chinese hamster ovary cells. Cell Growth Differ 5 9 (1994) 983-993
    • (1994) Cell Growth Differ , vol.5 , Issue.9 , pp. 983-993
    • Demarcq, C.1    Bunch, R.T.2    Creswell, D.3    Eastman, A.4
  • 229
    • 0028925744 scopus 로고
    • Rapamycin enhances apoptosis and increases sensitivity to cisplatin in vitro
    • Shi Y., Frankel A., Radvanyi L.G., Penn L.Z., Miller R.G., and Mills G.B. Rapamycin enhances apoptosis and increases sensitivity to cisplatin in vitro. Cancer Res 55 9 (1995) 1982-1988
    • (1995) Cancer Res , vol.55 , Issue.9 , pp. 1982-1988
    • Shi, Y.1    Frankel, A.2    Radvanyi, L.G.3    Penn, L.Z.4    Miller, R.G.5    Mills, G.B.6
  • 230
    • 0003138007 scopus 로고    scopus 로고
    • Cisplatin and its analogues
    • DeVita V.T., Hellman S., and Rosenberg S.A. (Eds), Lippincott-Raven, Philadelphia
    • O'Dwyer P.J., Johnson S.W., and Hamilton T.C. Cisplatin and its analogues. In: DeVita V.T., Hellman S., and Rosenberg S.A. (Eds). Cancer: principles and practice of oncology (1997), Lippincott-Raven, Philadelphia 467-483
    • (1997) Cancer: principles and practice of oncology , pp. 467-483
    • O'Dwyer, P.J.1    Johnson, S.W.2    Hamilton, T.C.3
  • 231
    • 0025047803 scopus 로고
    • Activation of programmed cell death (apoptosis) by cisplatin, other anticancer drugs, toxins and hyperthermia
    • Barry M.A., Behnke C.A., and Eastman A. Activation of programmed cell death (apoptosis) by cisplatin, other anticancer drugs, toxins and hyperthermia. Biochem Pharmacol 40 10 (1990) 2353-2362
    • (1990) Biochem Pharmacol , vol.40 , Issue.10 , pp. 2353-2362
    • Barry, M.A.1    Behnke, C.A.2    Eastman, A.3
  • 232
    • 0033562991 scopus 로고    scopus 로고
    • Cisplatin inhibits paclitaxel-induced apoptosis in cisplatin-resistant ovarian cancer cell lines: possible explanation for failure of combination therapy
    • Judson P.L., Watson J.M., Gehrig P.A., Fowler W.C.J., and Haskill J.S. Cisplatin inhibits paclitaxel-induced apoptosis in cisplatin-resistant ovarian cancer cell lines: possible explanation for failure of combination therapy. Cancer Res 59 10 (1999) 2425-2432
    • (1999) Cancer Res , vol.59 , Issue.10 , pp. 2425-2432
    • Judson, P.L.1    Watson, J.M.2    Gehrig, P.A.3    Fowler, W.C.J.4    Haskill, J.S.5
  • 233
    • 0029875247 scopus 로고    scopus 로고
    • DNA damage and cell cycle checkpoints
    • Kaufmann W.K., and Paules R.S. DNA damage and cell cycle checkpoints. FASEB J 10 (1996) 238-247
    • (1996) FASEB J , vol.10 , pp. 238-247
    • Kaufmann, W.K.1    Paules, R.S.2
  • 234
    • 0030021996 scopus 로고    scopus 로고
    • Inactivation of p53 enhances sensitivity to multiple chemotherapeutic agents
    • Hawkins D.S., Demers G.W., and Galloway D.A. Inactivation of p53 enhances sensitivity to multiple chemotherapeutic agents. Cancer Res 56 (1996) 892-898
    • (1996) Cancer Res , vol.56 , pp. 892-898
    • Hawkins, D.S.1    Demers, G.W.2    Galloway, D.A.3
  • 235
    • 0027369120 scopus 로고
    • Increased accumulation of p53 protein in cisplatin-resistant cell lines
    • Brown R., Clugson C., Burns P., Edlin A., Vasey P., Vojtesek B., et al. Increased accumulation of p53 protein in cisplatin-resistant cell lines. Int J Cancer 55 (1993) 678-684
    • (1993) Int J Cancer , vol.55 , pp. 678-684
    • Brown, R.1    Clugson, C.2    Burns, P.3    Edlin, A.4    Vasey, P.5    Vojtesek, B.6
  • 236
    • 8944263468 scopus 로고    scopus 로고
    • Association between cisplatin resistance and mutation of p53 gene and reduced bax expression in ovarian carcinoma cell systems
    • Perego P., Giarola M., Righetti S.C., Supino R., Caserini C., Delia D., et al. Association between cisplatin resistance and mutation of p53 gene and reduced bax expression in ovarian carcinoma cell systems. Cancer Res 56 (1996) 556-562
    • (1996) Cancer Res , vol.56 , pp. 556-562
    • Perego, P.1    Giarola, M.2    Righetti, S.C.3    Supino, R.4    Caserini, C.5    Delia, D.6
  • 237
    • 0031920710 scopus 로고    scopus 로고
    • Induction of apoptosis by taxol and cisplatin and effect on cell cycle-related proteins in cisplatin-sensitive and -resistant human ovarian cancer cells
    • Zaffaroni N., Silvestrini R., Orlandi L., Bearzatto A., Gornati D., and Villa R. Induction of apoptosis by taxol and cisplatin and effect on cell cycle-related proteins in cisplatin-sensitive and -resistant human ovarian cancer cells. Br J Cancer 77 9 (1998) 1378-1385
    • (1998) Br J Cancer , vol.77 , Issue.9 , pp. 1378-1385
    • Zaffaroni, N.1    Silvestrini, R.2    Orlandi, L.3    Bearzatto, A.4    Gornati, D.5    Villa, R.6
  • 239
    • 0030811613 scopus 로고    scopus 로고
    • 7-Hydroxystaurosporine (UCN-01) causes redistribution of proliferating cell nuclear antigen and abrogates cisplatin-induced S-phase arrest in Chinese hamster ovary cells
    • Bunch R.T., and Eastman A. 7-Hydroxystaurosporine (UCN-01) causes redistribution of proliferating cell nuclear antigen and abrogates cisplatin-induced S-phase arrest in Chinese hamster ovary cells. Cell Growth Differ 8 7 (1997) 779-788
    • (1997) Cell Growth Differ , vol.8 , Issue.7 , pp. 779-788
    • Bunch, R.T.1    Eastman, A.2
  • 240
    • 33748554415 scopus 로고    scopus 로고
    • UCN-01 enhances CDDP cytotoxicity in ovarian cancer cells independent of p53 gene status and abrogation of G2 block
    • Husain A., Yan X.-Y., Rosales N., Schwartz G.K., and Spriggs D.R. UCN-01 enhances CDDP cytotoxicity in ovarian cancer cells independent of p53 gene status and abrogation of G2 block. Clin Cancer Res 4 (1997) 2089-2097
    • (1997) Clin Cancer Res , vol.4 , pp. 2089-2097
    • Husain, A.1    Yan, X.-Y.2    Rosales, N.3    Schwartz, G.K.4    Spriggs, D.R.5
  • 241
    • 0033953099 scopus 로고    scopus 로고
    • UCN-01 selectively enhances mitomycin C cytotoxicity in p53 defective cells which is mediated through S and/or G(2) checkpoint abrogation
    • Sugiyama K., Shimizu M., Akiyama T., Tamaoki T., Yamaguchi K., Takahashi R., et al. UCN-01 selectively enhances mitomycin C cytotoxicity in p53 defective cells which is mediated through S and/or G(2) checkpoint abrogation. Int J Cancer 85 5 (2000) 703-709
    • (2000) Int J Cancer , vol.85 , Issue.5 , pp. 703-709
    • Sugiyama, K.1    Shimizu, M.2    Akiyama, T.3    Tamaoki, T.4    Yamaguchi, K.5    Takahashi, R.6
  • 242
    • 0028783440 scopus 로고
    • Induction of apoptosis by gemcitabine
    • Huang P., and Plunkett W. Induction of apoptosis by gemcitabine. Semin Oncol 22 (1995) 19-25
    • (1995) Semin Oncol , vol.22 , pp. 19-25
    • Huang, P.1    Plunkett, W.2
  • 243
    • 0028799108 scopus 로고
    • Gemcitabine: metabolism, mechanisms of action and self-potentiation
    • Plunkett W., Huang P., Xu Y., Heinemann V., Grunewald R., and Gandhi V. Gemcitabine: metabolism, mechanisms of action and self-potentiation. Semin Oncol 22 4 Suppl. 11 (1995) 3-10
    • (1995) Semin Oncol , vol.22 , Issue.4 SUPPL. 11 , pp. 3-10
    • Plunkett, W.1    Huang, P.2    Xu, Y.3    Heinemann, V.4    Grunewald, R.5    Gandhi, V.6
  • 244
  • 246
    • 0029060757 scopus 로고
    • Fludarabine- and gemcitabine-induced apoptosis: incorporation of analogs into DNA is a critical event
    • Huang P., and Plunkett W. Fludarabine- and gemcitabine-induced apoptosis: incorporation of analogs into DNA is a critical event. Cancer Chemother Pharmacol 36 (1995) 181-188
    • (1995) Cancer Chemother Pharmacol , vol.36 , pp. 181-188
    • Huang, P.1    Plunkett, W.2
  • 247
    • 0034100255 scopus 로고    scopus 로고
    • The role of p53 in gemcitabine-mediated cytotoxicity and radiosensitization
    • Chen M., Hough A.M., and Lawrence T.S. The role of p53 in gemcitabine-mediated cytotoxicity and radiosensitization. Cancer Chemother Pharmacol 45 (2000) 369-374
    • (2000) Cancer Chemother Pharmacol , vol.45 , pp. 369-374
    • Chen, M.1    Hough, A.M.2    Lawrence, T.S.3
  • 249
    • 0034887130 scopus 로고    scopus 로고
    • Flavopiridol increases sensitization to gemcitabine in human gastrointestinal cancer cell lines and correlates with down-regulation of ribonucleotide reductase M2 subunit
    • Jung C.P., Motwani M.V., and Schwartz G.K. Flavopiridol increases sensitization to gemcitabine in human gastrointestinal cancer cell lines and correlates with down-regulation of ribonucleotide reductase M2 subunit. Clin Cancer Res 7 (2001) 2527-2536
    • (2001) Clin Cancer Res , vol.7 , pp. 2527-2536
    • Jung, C.P.1    Motwani, M.V.2    Schwartz, G.K.3
  • 250
    • 16844372227 scopus 로고    scopus 로고
    • Sequence dependent potentiation of gemcitabine by flavopiridol in human breast cancer cells
    • Ali S., El-Rayes B.F., Aranha O., Sarkar F.H., and Philip P.A. Sequence dependent potentiation of gemcitabine by flavopiridol in human breast cancer cells. Breast Cancer Res 90 1 (2005) 25-31
    • (2005) Breast Cancer Res , vol.90 , Issue.1 , pp. 25-31
    • Ali, S.1    El-Rayes, B.F.2    Aranha, O.3    Sarkar, F.H.4    Philip, P.A.5
  • 251
    • 0031938457 scopus 로고    scopus 로고
    • Overexpression of transfected human ribonucleotide reductase M2 subunit in human cancer cells enhances their invasive potential
    • Zhou B.S., Tsai P., Ker R., Tsai J., Ho R., Yu J., et al. Overexpression of transfected human ribonucleotide reductase M2 subunit in human cancer cells enhances their invasive potential. Clin Exp Metastasis 16 (1998) 43-49
    • (1998) Clin Exp Metastasis , vol.16 , pp. 43-49
    • Zhou, B.S.1    Tsai, P.2    Ker, R.3    Tsai, J.4    Ho, R.5    Yu, J.6
  • 252
    • 0033198464 scopus 로고    scopus 로고
    • Overexpression of ribonucleotide reductase as a mechanism of resistance to 2,2-difluorodeoxycytidine in human KB cancer cell line
    • Goan Y.G., Zhou B., Hu E., Mi S., and Yen Y. Overexpression of ribonucleotide reductase as a mechanism of resistance to 2,2-difluorodeoxycytidine in human KB cancer cell line. Cancer Res 59 (1999) 4204-4207
    • (1999) Cancer Res , vol.59 , pp. 4204-4207
    • Goan, Y.G.1    Zhou, B.2    Hu, E.3    Mi, S.4    Yen, Y.5
  • 253
    • 0037086282 scopus 로고    scopus 로고
    • Selective sensitization of transformed cells to flavopiridol-induced apoptosis following recruitment to S-phase
    • Matranga C.B., and Shapiro G.I. Selective sensitization of transformed cells to flavopiridol-induced apoptosis following recruitment to S-phase. Cancer Res 62 (2002) 1707-1717
    • (2002) Cancer Res , vol.62 , pp. 1707-1717
    • Matranga, C.B.1    Shapiro, G.I.2
  • 254
    • 0032033021 scopus 로고    scopus 로고
    • Cell cycle perturbations in acute myeloid leukemia samples following in vitro exposures to therapeutic agents
    • Banker D.E., Groudine M., Willman C.L., Norwood T., and Appelbaum F.R. Cell cycle perturbations in acute myeloid leukemia samples following in vitro exposures to therapeutic agents. Leuk Res 22 (1998) 221-239
    • (1998) Leuk Res , vol.22 , pp. 221-239
    • Banker, D.E.1    Groudine, M.2    Willman, C.L.3    Norwood, T.4    Appelbaum, F.R.5
  • 255
    • 0035116697 scopus 로고    scopus 로고
    • S-phase arrest by nucleoside analogues and abrogation of survival without cell cycle progression by 7-hydroxystaurosporine
    • Shi Z., Azuma A., Sampath D., Li Y.-X., Huang P., and Plunkett W. S-phase arrest by nucleoside analogues and abrogation of survival without cell cycle progression by 7-hydroxystaurosporine. Cancer Res 61 (2001) 1065-1072
    • (2001) Cancer Res , vol.61 , pp. 1065-1072
    • Shi, Z.1    Azuma, A.2    Sampath, D.3    Li, Y.-X.4    Huang, P.5    Plunkett, W.6
  • 256
    • 0642303123 scopus 로고    scopus 로고
    • Targeting aurora2 kinase in oncogenesis: a structural bioinformatics approach to target validation and rational drug design
    • Vankayalapati H., Bearss D.J., Saldanha J.W., Munoz R.M., Rojanala S., Von Hoff D.D., et al. Targeting aurora2 kinase in oncogenesis: a structural bioinformatics approach to target validation and rational drug design. Mol Cancer Ther 2 3 (2003) 283-294
    • (2003) Mol Cancer Ther , vol.2 , Issue.3 , pp. 283-294
    • Vankayalapati, H.1    Bearss, D.J.2    Saldanha, J.W.3    Munoz, R.M.4    Rojanala, S.5    Von Hoff, D.D.6
  • 257
    • 0037648703 scopus 로고    scopus 로고
    • Polo-like kinase 1 (PLK1) is overexpressed in primary colorectal cancers
    • Takahashi T., Sano B., Nagata T., Kato H., Sugiyama Y., Kunieda K., et al. Polo-like kinase 1 (PLK1) is overexpressed in primary colorectal cancers. Cancer Sci 94 2 (2003) 148-152
    • (2003) Cancer Sci , vol.94 , Issue.2 , pp. 148-152
    • Takahashi, T.1    Sano, B.2    Nagata, T.3    Kato, H.4    Sugiyama, Y.5    Kunieda, K.6
  • 258
    • 0038015849 scopus 로고    scopus 로고
    • Aurora2/BTAK/STK15 is involved in cell cycle checkpoint and cell survival of aggressive non-Hodgkin's lymphoma
    • Hamada M., Yakushijin Y., Ohtsuka M., Kakimoto M., Yasukawa M., and Fujita S. Aurora2/BTAK/STK15 is involved in cell cycle checkpoint and cell survival of aggressive non-Hodgkin's lymphoma. Br J Haematol 121 (2003) 439-447
    • (2003) Br J Haematol , vol.121 , pp. 439-447
    • Hamada, M.1    Yakushijin, Y.2    Ohtsuka, M.3    Kakimoto, M.4    Yasukawa, M.5    Fujita, S.6
  • 259
    • 14944369449 scopus 로고    scopus 로고
    • A novel aurora B kinase inhibitor with potent anticancer activity either as a single agent or in combination with chemotherapy
    • [abstract 9568]
    • Nair J.S., Tse A., Keen N., and Schwartz G.K. A novel aurora B kinase inhibitor with potent anticancer activity either as a single agent or in combination with chemotherapy. Proc Am Soc Clin Oncol 45 (2004) 848 [abstract 9568]
    • (2004) Proc Am Soc Clin Oncol , vol.45 , pp. 848
    • Nair, J.S.1    Tse, A.2    Keen, N.3    Schwartz, G.K.4
  • 260
    • 2342639645 scopus 로고    scopus 로고
    • VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo
    • Harrington E.A., Bebbington D., Moore J., Rasmussen R.K., Ajose-Adeogun A.O., Nakayama T., et al. VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo. Nat Med (2004) 262-267
    • (2004) Nat Med , pp. 262-267
    • Harrington, E.A.1    Bebbington, D.2    Moore, J.3    Rasmussen, R.K.4    Ajose-Adeogun, A.O.5    Nakayama, T.6
  • 261
    • 12744268951 scopus 로고    scopus 로고
    • Pulsatile administration of the EGF receptor inhibitor Iressa (ZD1839) is significantly more effective than continuous dosing for sensitizing tumors to taxol
    • Solit D.B., She Y., Moasser M.M., et al. Pulsatile administration of the EGF receptor inhibitor Iressa (ZD1839) is significantly more effective than continuous dosing for sensitizing tumors to taxol. Am Assoc Cancer Res 44 2 (2003) LB-5
    • (2003) Am Assoc Cancer Res , vol.44 , Issue.2
    • Solit, D.B.1    She, Y.2    Moasser, M.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.