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Volumn 9, Issue 6, 1996, Pages 1143-1168

Flavopiridol (L86 8275; NSC 649890), a new kinase inhibitor for tumor therapy

Author keywords

cyclin dependent kinase; Flavopiridol; inhibitor; pharmacokinetic; preclinical activity; toxicity; tumor therapy

Indexed keywords

CYCLIN DEPENDENT KINASE; ENZYME INHIBITOR; FLAVONE DERIVATIVE; FLAVOPIRIDOL; UNCLASSIFIED DRUG;

EID: 0029807115     PISSN: 10196439     EISSN: None     Source Type: Journal    
DOI: 10.3892/ijo.9.6.1143     Document Type: Article
Times cited : (301)

References (133)
  • 2
    • 0023924162 scopus 로고
    • An antiinflammatory piperidinylbenzopyranone from dysoxylum binectariferum: Isolation, structure and total synthesis
    • Naik RG, Kattige Sl, Bhat SV, Alrejy B, de Souza NJ and Rupp RH: An antiinflammatory piperidinylbenzopyranone from dysoxylum binectariferum: isolation, structure and total synthesis. Tetrahedron 44: 2081-2086, 1988.
    • (1988) Tetrahedron , vol.44 , pp. 2081-2086
    • Naik, R.G.1    Kattige, Sl.2    Bhat, S.V.3    Alrejy, B.4    De Souza, N.J.5    Rupp, R.H.6
  • 3
    • 34347275375 scopus 로고    scopus 로고
    • New 4H-1-Benzopyran-4-on derivatives and pharmaceutical use. DE 383 6676; EP 036 6061; USP 528 4856, 1988
    • Naik RG, Lal B, Rupp RH, Sedlacek HH, Dickneite G and Czech J: New 4H-1-Benzopyran-4-on derivatives and pharmaceutical use. DE 383 6676; EP 036 6061; USP 528 4856, 1988.
    • Naik, R.G.1    Lal, B.2    Rupp, R.H.3    Sedlacek, H.H.4    Dickneite, G.5    Czech, J.6
  • 4
    • 0020635362 scopus 로고
    • The effect of quercetin on the phosphorylation activity of the Rous sarcoma virus transforming gene product in vitro and in vivo
    • Graziani Y, Erikson E and Erikson RL: The effect of quercetin on the phosphorylation activity of the Rous sarcoma virus transforming gene product in vitro and in vivo. Eur J Biochem 135: 583-589, 1983.
    • (1983) Eur J Biochem , vol.135 , pp. 583-589
    • Graziani, Y.1    Erikson, E.2    Erikson, R.L.3
  • 5
    • 0028172837 scopus 로고
    • Tyrosine protein kinase inhibition and cancer
    • Boutin JA: Tyrosine protein kinase inhibition and cancer. Int J Biochem 26: 1203-1226, 1994.
    • (1994) Int J Biochem , vol.26 , pp. 1203-1226
    • Boutin, J.A.1
  • 6
    • 0028918028 scopus 로고
    • Transcriptional regulation during the mammalian cell cycle
    • Müller R: Transcriptional regulation during the mammalian cell cycle. Trends Genet 11: 173-178, 1995.
    • (1995) Trends Genet , vol.11 , pp. 173-178
    • Müller, R.1
  • 7
    • 0021958679 scopus 로고
    • Autocrine growth factors and cancer
    • Sporn MB and Roberts AB: Autocrine growth factors and cancer. Nature 313: 745-747, 1985.
    • (1985) Nature , vol.313 , pp. 745-747
    • Sporn, M.B.1    Roberts, A.B.2
  • 8
    • 0023100052 scopus 로고
    • Synthesis of messenger RNAs for transforming growth factors α and β and the epidermal growth factor receptor by human tumors
    • Derynck R, Goeddel DV, Ullrich A, Gutterman JU, William RD, Bringman TS and Berger WH: Synthesis of messenger RNAs for transforming growth factors α and β and the epidermal growth factor receptor by human tumors. Cancer Res 47: 707-712, 1987.
    • (1987) Cancer Res , vol.47 , pp. 707-712
    • Derynck, R.1    Goeddel, D.V.2    Ullrich, A.3    Gutterman, J.U.4    William, R.D.5    Bringman, T.S.6    Berger, W.H.7
  • 9
    • 0024355092 scopus 로고
    • Autocrine interaction between TGFα and the EGF receptor: Quantitative requirements for induction of the malignant phenotype
    • Marco Di E, Pierce JH, Fleming TP, Kraus MH, Molloy CJ, Aaronson ST and Fiore Di PP: Autocrine interaction between TGFα and the EGF receptor: quantitative requirements for induction of the malignant phenotype. Oncogene 4: 831-838, 1989.
    • (1989) Oncogene , vol.4 , pp. 831-838
    • Marco Di, E.1    Pierce, J.H.2    Fleming, T.P.3    Kraus, M.H.4    Molloy, C.J.5    Aaronson, S.T.6    Fiore Di, P.P.7
  • 10
    • 0024375271 scopus 로고
    • Purification and complementary DNA cloning of a receptor for basic fibroblast growth factor
    • Lee PL, Johnson DE, Cousens LS, Fried VA and Williams LT: Purification and complementary DNA cloning of a receptor for basic fibroblast growth factor. Science 245: 57-60, 1989.
    • (1989) Science , vol.245 , pp. 57-60
    • Lee, P.L.1    Johnson, D.E.2    Cousens, L.S.3    Fried, V.A.4    Williams, L.T.5
  • 11
    • 0024276837 scopus 로고
    • Molecular analysis of signal transduction by growth factors
    • Yarden Y and Ullrich A: Molecular analysis of signal transduction by growth factors. Biochemistry 27: 3113-3119, 1988.
    • (1988) Biochemistry , vol.27 , pp. 3113-3119
    • Yarden, Y.1    Ullrich, A.2
  • 12
    • 0029417882 scopus 로고
    • Chemical inhibitors of cyclin-dependent kinases
    • Meijer L: Chemical inhibitors of cyclin-dependent kinases. Progress in Cell Cycle Res 1: 351-363, 1995.
    • (1995) Progress in Cell Cycle Res , vol.1 , pp. 351-363
    • Meijer, L.1
  • 17
    • 0029665778 scopus 로고    scopus 로고
    • Flavopiridol induces G1 arrest with inhibition of cyclin-dependent kinase (cdk) 2 and ckd4 in human breast carcinoma cells
    • Carlson BA, Dubay MM, Sausville EA, Brizuela L and Worland PJ: Flavopiridol induces G1 arrest with inhibition of cyclin-dependent kinase (cdk) 2 and ckd4 in human breast carcinoma cells. Cancer Res 56: 2973-2978, 1996.
    • (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
  • 19
    • 0023897154 scopus 로고
    • Differential effects of flavonoids as inhibitors of tyrosine protein kinases and serine/threonine protein kinases
    • Hagiwara M, Inoue S, Tanaka T, Nunoki K, Ito M and Hidaka H: Differential effects of flavonoids as inhibitors of tyrosine protein kinases and serine/threonine protein kinases. Biochem Pharmacol 37: 2987-2992, 1988.
    • (1988) Biochem Pharmacol , vol.37 , pp. 2987-2992
    • Hagiwara, M.1    Inoue, S.2    Tanaka, T.3    Nunoki, K.4    Ito, M.5    Hidaka, H.6
  • 20
    • 0026285357 scopus 로고
    • Protein kinase inhibitors: Probes for the functions of protein phosphorylation
    • Casnellie JE: Protein kinase inhibitors: probes for the functions of protein phosphorylation. Adv Pharmacol 22: 167-205, 1991.
    • (1991) Adv Pharmacol , vol.22 , pp. 167-205
    • Casnellie, J.E.1
  • 23
    • 0024238244 scopus 로고
    • Effect of genistein on topoisomerase activity and the growth of Val 12 H-ras-transformed NIH3T3 cells
    • Okura A, Arakawa H, Oka H, Yoshainari T and Monden Y: Effect of genistein on topoisomerase activity and the growth of Val 12 H-ras-transformed NIH3T3 cells. Biochem Biophys Res Commun 157: 183-189, 1988.
    • (1988) Biochem Biophys Res Commun , vol.157 , pp. 183-189
    • Okura, A.1    Arakawa, H.2    Oka, H.3    Yoshainari, T.4    Monden, Y.5
  • 24
    • 0025181752 scopus 로고
    • Mechanisms of action in HIH-3T3 cells of genistein, an inhibitor of EGF-receptor tyrosine kinase activity
    • Linassier C, Pierre M, Le Pecq JB and Pierre J: Mechanisms of action in HIH-3T3 cells of genistein, an inhibitor of EGF-receptor tyrosine kinase activity. Biochem Pharmacol 39: 187-193, 1990.
    • (1990) Biochem Pharmacol , vol.39 , pp. 187-193
    • Linassier, C.1    Pierre, M.2    Le Pecq, J.B.3    Pierre, J.4
  • 25
    • 0027164776 scopus 로고
    • Inhibitory effects of semisynthetic flavonoid derivatives on the biochemical markers of tumor promotion in mouse epidermis in vivo
    • Gali HU, Perchellet EM, Gao XM, Laks PE and Perchellet JP: Inhibitory effects of semisynthetic flavonoid derivatives on the biochemical markers of tumor promotion in mouse epidermis in vivo. Cancer Lett 72: 149-156, 1993.
    • (1993) Cancer Lett , vol.72 , pp. 149-156
    • Gali, H.U.1    Perchellet, E.M.2    Gao, X.M.3    Laks, P.E.4    Perchellet, J.P.5
  • 26
    • 0028968949 scopus 로고
    • Tyrosine kinase inhibition: An approach to drug development
    • Levitzki A and Gazit A: Tyrosine kinase inhibition: an approach to drug development. Science 267: 1782-1788, 1995.
    • (1995) Science , vol.267 , pp. 1782-1788
    • Levitzki, A.1    Gazit, A.2
  • 28
    • 0022589148 scopus 로고
    • Flavone acetic acid: Novel agent with preclinical anti-tumour activity against colon adenocarcinoma 38 in mice
    • Plowman J, Narayanan VL, Dykes D, Szarvasi E, Briet P, Yoder OC and Paull KD: Flavone acetic acid: novel agent with preclinical anti-tumour activity against colon adenocarcinoma 38 in mice. Cancer Treat Rep 70: 631-635, 1986.
    • (1986) Cancer Treat Rep , vol.70 , pp. 631-635
    • Plowman, J.1    Narayanan, V.L.2    Dykes, D.3    Szarvasi, E.4    Briet, P.5    Yoder, O.C.6    Paull, K.D.7
  • 30
    • 0023889926 scopus 로고
    • Effect of flavone acetic acid in Lewis lung carcinoma: Evidence for an indirect effect
    • Finlay GJ, Smith GP, Fray LM and Baguley BC: Effect of flavone acetic acid in Lewis lung carcinoma: evidence for an indirect effect. J Natl Cancer Int 80: 241-245, 1988.
    • (1988) J Natl Cancer Int , vol.80 , pp. 241-245
    • Finlay, G.J.1    Smith, G.P.2    Fray, L.M.3    Baguley, B.C.4
  • 31
    • 0023129401 scopus 로고
    • Factors involved in the anti-cancer activity of the investigational agents LM985 (flavone acetic acid ester) and LM975 (flavone acetic acid)
    • Bibby MC, Double JA, Philips RM and Loadman PM: Factors involved in the anti-cancer activity of the investigational agents LM985 (flavone acetic acid ester) and LM975 (flavone acetic acid). Br J Cancer 55: 159-163, 1987.
    • (1987) Br J Cancer , vol.55 , pp. 159-163
    • Bibby, M.C.1    Double, J.A.2    Philips, R.M.3    Loadman, P.M.4
  • 34
    • 0023215827 scopus 로고
    • Flavone acetic acid (NSC 347512) induces hemorrhagic necrosis of mouse colon 26 and 38 tumours
    • Smith GP, Calverley SB, Smith MJ and Baguley BC: Flavone acetic acid (NSC 347512) induces hemorrhagic necrosis of mouse colon 26 and 38 tumours. Eur J Cancer Clin Oncol 23: 1209-1211, 1987.
    • (1987) Eur J Cancer Clin Oncol , vol.23 , pp. 1209-1211
    • Smith, G.P.1    Calverley, S.B.2    Smith, M.J.3    Baguley, B.C.4
  • 36
    • 9044239197 scopus 로고
    • Flavone acetic acid (FAA (LM975), NSC 347512) induces a rapid massive necrosis in a murine transplantable adenocarcinoma (MAC26)
    • Duke CV, Double JA and Bibby MC: Flavone acetic acid (FAA (LM975), NSC 347512) induces a rapid massive necrosis in a murine transplantable adenocarcinoma (MAC26) Br J Cancer 58: 532, 1988.
    • (1988) Br J Cancer , vol.58 , pp. 532
    • Duke, C.V.1    Double, J.A.2    Bibby, M.C.3
  • 37
    • 0023809013 scopus 로고
    • Flavone acetic acid (NSC347512) induced modulation of tumour physiology monitored by in vivo nuclear magnetic resonance spectroscopy
    • Evelhoch JL, Bissery MC, Chabot GG, Simpson NE, McCoy CL, Heilbrun LK and Corbett TH: Flavone acetic acid (NSC347512) induced modulation of tumour physiology monitored by in vivo nuclear magnetic resonance spectroscopy Cancer Res 48: 4749-4755, 1988.
    • (1988) Cancer Res , vol.48 , pp. 4749-4755
    • Evelhoch, J.L.1    Bissery, M.C.2    Chabot, G.G.3    Simpson, N.E.4    McCoy, C.L.5    Heilbrun, L.K.6    Corbett, T.H.7
  • 38
    • 0024465844 scopus 로고
    • Vascular collapse after flavone acetic acid: A possible mechanism of its anti-tumor action
    • Hill S, Williams KB and Denekamp J: Vascular collapse after flavone acetic acid: a possible mechanism of its anti-tumor action. Eur J Cancer Clin Oncol 25: 1419-1424, 1989.
    • (1989) Eur J Cancer Clin Oncol , vol.25 , pp. 1419-1424
    • Hill, S.1    Williams, K.B.2    Denekamp, J.3
  • 39
    • 0025298797 scopus 로고
    • The use of vascularised spheroids to investigate the action of flavone acetic acid on tumour blood vessels
    • Zwi LJ, Baguley BC, Gavin JB and Wilson WR: The use of vascularised spheroids to investigate the action of flavone acetic acid on tumour blood vessels. Br J Cancer 62: 231-237, 1990.
    • (1990) Br J Cancer , vol.62 , pp. 231-237
    • Zwi, L.J.1    Baguley, B.C.2    Gavin, J.B.3    Wilson, W.R.4
  • 40
    • 0025818177 scopus 로고
    • Early spatial and temporal changes in tumour perfusion after administration of flavone acetic acid
    • Peters CE, Trotter MJ and Chaplin DJ: Early spatial and temporal changes in tumour perfusion after administration of flavone acetic acid. Int J Radiat Biol 60: 341-348, 1991.
    • (1991) Int J Radiat Biol , vol.60 , pp. 341-348
    • Peters, C.E.1    Trotter, M.J.2    Chaplin, D.J.3
  • 41
    • 0024407747 scopus 로고
    • Flavone acetic acid induces a coagulopathy in mice
    • Murray JC, Smith KA and Thurston G: Flavone acetic acid induces a coagulopathy in mice. Br J Cancer 60: 729-733, 1989.
    • (1989) Br J Cancer , vol.60 , pp. 729-733
    • Murray, J.C.1    Smith, K.A.2    Thurston, G.3
  • 42
    • 0025763448 scopus 로고
    • Flavone acetic acid potentiates the induction of endothelial procoagulant activity by tumor necrosis factor
    • Murray CJ, Smith KA and Stern DM: Flavone acetic acid potentiates the induction of endothelial procoagulant activity by tumor necrosis factor. Eur J Cancer 27: 765-770, 1991.
    • (1991) Eur J Cancer , vol.27 , pp. 765-770
    • Murray, C.J.1    Smith, K.A.2    Stern, D.M.3
  • 43
    • 0026089375 scopus 로고
    • Tumour-dependent increased plasma nitrate concentrations as an indication of the antitumor effect of flavone-8-acetic acid and analogues in mice
    • Thomsen LL, Ching LM, Zhuang L, Gavin JB and Baguley BC: Tumour-dependent increased plasma nitrate concentrations as an indication of the antitumor effect of flavone-8-acetic acid and analogues in mice. Cancer Res 51: 77-81, 1991.
    • (1991) Cancer Res , vol.51 , pp. 77-81
    • Thomsen, L.L.1    Ching, L.M.2    Zhuang, L.3    Gavin, J.B.4    Baguley, B.C.5
  • 44
    • 0023177550 scopus 로고
    • Induction of natural killer cell activity by the antitumour compound flavone acetic acid (NSC 347512)
    • Ching LM and Baguley BC: Induction of natural killer cell activity by the antitumour compound flavone acetic acid (NSC 347512). Eur J Cancer Clin Oncol 23: 1047-1050, 1987.
    • (1987) Eur J Cancer Clin Oncol , vol.23 , pp. 1047-1050
    • Ching, L.M.1    Baguley, B.C.2
  • 45
    • 0023934095 scopus 로고
    • Flavone-8-acetic acid augments systemic natural killer cell activity and synergizes with IL-2 for treatment of murine renal cancer
    • Wiltrout RH, Boyd MR, Back TC, Salup RR, Arthur JA and Hornung RL: Flavone-8-acetic acid augments systemic natural killer cell activity and synergizes with IL-2 for treatment of murine renal cancer. J Immunol 140: 3261-3265, 1988.
    • (1988) J Immunol , vol.140 , pp. 3261-3265
    • Wiltrout, R.H.1    Boyd, M.R.2    Back, T.C.3    Salup, R.R.4    Arthur, J.A.5    Hornung, R.L.6
  • 46
    • 0025320055 scopus 로고
    • Correlation between in vivo induction of cytokine gene expression by flavone acetic acid and strict dose dependency and therapeutic efficacy against murine renal cancer
    • Mace KF, Hornung RL, Wiltrout RH and Young HA: Correlation between in vivo induction of cytokine gene expression by flavone acetic acid and strict dose dependency and therapeutic efficacy against murine renal cancer. Cancer Res 50: 1742-3 747, 1990.
    • (1990) Cancer Res , vol.50 , pp. 1742-3747
    • Mace, K.F.1    Hornung, R.L.2    Wiltrout, R.H.3    Young, H.A.4
  • 47
    • 34347277881 scopus 로고
    • Immunocompetence: A necessary component for the anti-tumour activity of flavone acetic acid (FAA)
    • Bibby MC and Double JA: Immunocompetence: a necessary component for the anti-tumour activity of flavone acetic acid (FAA). Br J Cancer 62: 516, 1990.
    • (1990) Br J Cancer , vol.62 , pp. 516
    • Bibby, M.C.1    Double, J.A.2
  • 48
    • 0026011266 scopus 로고
    • Antitumour activity of flavone acetic acid (NSC 347512) in mice - Influence of immune status
    • Bibby MC, Phillips RM, Double JA and Pratesi G: Antitumour activity of flavone acetic acid (NSC 347512) in mice - influence of immune status. Br J Cancer 63: 57-62, 1991.
    • (1991) Br J Cancer , vol.63 , pp. 57-62
    • Bibby, M.C.1    Phillips, R.M.2    Double, J.A.3    Pratesi, G.4
  • 49
    • 0025602742 scopus 로고
    • Role of T cells and tumour necrosis factor in antitumour activity and toxicity of flavone acetic acid
    • Pratesi G, Rodolfo M, Rovetta G and Parmiani G: Role of T cells and tumour necrosis factor in antitumour activity and toxicity of flavone acetic acid. Eur J Cancer 26: 1079-1083, 1990.
    • (1990) Eur J Cancer , vol.26 , pp. 1079-1083
    • Pratesi, G.1    Rodolfo, M.2    Rovetta, G.3    Parmiani, G.4
  • 50
    • 0027459147 scopus 로고
    • Flavone acetic acid - From laboratory to clinic and back
    • Bibby MC and Double JA: Flavone acetic acid - from laboratory to clinic and back. Anti-Cancer Drugs 4: 3-17, 1993.
    • (1993) Anti-Cancer Drugs , vol.4 , pp. 3-17
    • Bibby, M.C.1    Double, J.A.2
  • 51
    • 0018396088 scopus 로고
    • Structure of Rohitukine, the main alkaloid of amoora-rohituka (Syn. Aphanamixispolystachya) (meliaceae)
    • Harmon A, Weiss U and Silverton JV: Structure of Rohitukine, the main alkaloid of amoora-rohituka (Syn. Aphanamixispolystachya) (meliaceae). Tetrahedron Lett 721-724, 1979.
    • (1979) Tetrahedron Lett , pp. 721-724
    • Harmon, A.1    Weiss, U.2    Silverton, J.V.3
  • 52
    • 0023259073 scopus 로고
    • Further chromone alkaloids from Schumanniophyton-magnificum
    • Houghton PJ and Hairon Y: Further chromone alkaloids from Schumanniophyton-magnificum. Planta Med 53: 262-264, 1987.
    • (1987) Planta Med , vol.53 , pp. 262-264
    • Houghton, P.J.1    Hairon, Y.2
  • 54
    • 34347275865 scopus 로고
    • bFGF-stimulation of human tumor cell proliferation in vitro
    • Czech J and Sedlacek HH: bFGF-stimulation of human tumor cell proliferation in vitro. Cancer Chemother Pharmacol 24: 72, 1989.
    • (1989) Cancer Chemother Pharmacol , vol.24 , pp. 72
    • Czech, J.1    Sedlacek, H.H.2
  • 55
    • 0038239906 scopus 로고
    • Transforming and nontransforming growth factors are present in medium conditioned by fetal rat calvariae
    • Centrella M and Canalis E: Transforming and nontransforming growth factors are present in medium conditioned by fetal rat calvariae. Proc Natl Acad Sci USA 88: 7335-7339, 1985.
    • (1985) Proc Natl Acad Sci USA , vol.88 , pp. 7335-7339
    • Centrella, M.1    Canalis, E.2
  • 56
    • 0023245094 scopus 로고
    • Suramin inhibition of growth factor receptor binding and mitogenicity in AKR-2B cells
    • Coffey RJ Jr, Leof EB, Shipley GD and Moses HL: Suramin inhibition of growth factor receptor binding and mitogenicity in AKR-2B cells. J Cell Physiol 1232: 143-148, 1987.
    • (1987) J Cell Physiol , vol.1232 , pp. 143-148
    • Coffey Jr., R.J.1    Leof, E.B.2    Shipley, G.D.3    Moses, H.L.4
  • 57
    • 0024312538 scopus 로고
    • Display and analysis of patterns of differential activity of drugs against human tumor cell lines: Development of mean graph and COMPARE algorithm
    • Paull KD, Shoemaker RH, Hodes L, Monks A, Scudiero DA, Rubinstein L, Plowman J and Boyd MR: Display and analysis of patterns of differential activity of drugs against human tumor cell lines: development of mean graph and COMPARE algorithm. J Natl Cancer Inst 81: 1088-1092, 1989.
    • (1989) J Natl Cancer Inst , vol.81 , pp. 1088-1092
    • Paull, K.D.1    Shoemaker, R.H.2    Hodes, L.3    Monks, A.4    Scudiero, D.A.5    Rubinstein, L.6    Plowman, J.7    Boyd, M.R.8
  • 58
    • 0026574138 scopus 로고
    • Site-specific DNA cleavage by mammalian DNA topoisomerase II induced by novel flavone and catechin derivatives
    • Austin CA, Patel S, Ono K, Nakane H and Fischer LM: Site-specific DNA cleavage by mammalian DNA topoisomerase II induced by novel flavone and catechin derivatives. Biochem J 282: 883-889, 1992.
    • (1992) Biochem J , vol.282 , pp. 883-889
    • Austin, C.A.1    Patel, S.2    Ono, K.3    Nakane, H.4    Fischer, L.M.5
  • 59
    • 0026471968 scopus 로고
    • Effects of genistein on the growth and cell cycle progression of normal human lymphocytes and human leukemic MOLT-4 and HL-60 cells
    • Traganos F, Ardelt B, Halko N, Bruno S and Darzynkiewicz Z: Effects of genistein on the growth and cell cycle progression of normal human lymphocytes and human leukemic MOLT-4 and HL-60 cells. Cancer Res 52: 6200-6208, 1992.
    • (1992) Cancer Res , vol.52 , pp. 6200-6208
    • Traganos, F.1    Ardelt, B.2    Halko, N.3    Bruno, S.4    Darzynkiewicz, Z.5
  • 60
    • 0025189757 scopus 로고
    • Induction of mammalian topoisomerase II dependent DNA cleavage by nonintercalative flavonoids, genistein and orobol
    • Yamashita Y, Kawada S and Nakano H: Induction of mammalian topoisomerase II dependent DNA cleavage by nonintercalative flavonoids, genistein and orobol. Biochem Pharmacol 39: 737-744, 1990.
    • (1990) Biochem Pharmacol , vol.39 , pp. 737-744
    • Yamashita, Y.1    Kawada, S.2    Nakano, H.3
  • 61
    • 0019991171 scopus 로고
    • A fluorescence enhancement assay for cellular DNA damage
    • Kanter PM and Schwartz HS: A fluorescence enhancement assay for cellular DNA damage. Mol Pharmacol 22: 145-151, 1982.
    • (1982) Mol Pharmacol , vol.22 , pp. 145-151
    • Kanter, P.M.1    Schwartz, H.S.2
  • 62
    • 0014225275 scopus 로고
    • The interaction of amino-acridines with nucleic acids
    • Blake A and Peacock AR: The interaction of amino-acridines with nucleic acids. Biopolymers 6: 1225-1228, 1968.
    • (1968) Biopolymers , vol.6 , pp. 1225-1228
    • Blake, A.1    Peacock, A.R.2
  • 63
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation an cytotoxicity assays
    • Mossman T: Rapid colorimetric assay for cellular growth and survival: Application to proliferation an cytotoxicity assays. J Immunol Methods 65: 55-63, 1983.
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mossman, T.1
  • 65
    • 0018966230 scopus 로고
    • Production of large numbers of mitotic mammalian cells by use of the reversible microtubule inhibitor nocodazole. Nocodazole accumulated mitotic cells
    • Zieve GW, Turnbull D, Mullins JM and McIntosh JR: Production of large numbers of mitotic mammalian cells by use of the reversible microtubule inhibitor nocodazole. Nocodazole accumulated mitotic cells. Exp Cell Res 126: 397-405, 1980.
    • (1980) Exp Cell Res , vol.126 , pp. 397-405
    • Zieve, G.W.1    Turnbull, D.2    Mullins, J.M.3    McIntosh, J.R.4
  • 66
    • 0016821736 scopus 로고
    • The effect of flavonoids on aerobic glycolysis and growth of tumor cells
    • Suolinna EM, Buchsbaum RN and Racker E: The effect of flavonoids on aerobic glycolysis and growth of tumor cells. Cancer Res 35: 1865-1872, 1975.
    • (1975) Cancer Res , vol.35 , pp. 1865-1872
    • Suolinna, E.M.1    Buchsbaum, R.N.2    Racker, E.3
  • 68
    • 0025365850 scopus 로고
    • Inhibitory effect of quercetin on the synthesis of a possibly cell-cycle-related 17-kDa protein, in human colon cancer cells
    • Hosokawa N, Hosokawa Y, Sakai T, Yoshida M, Marui N, Nishino H, Kawai K and Aoike A: Inhibitory effect of quercetin on the synthesis of a possibly cell-cycle-related 17-kDa protein, in human colon cancer cells. Int J Cancer 45: 1119-1124, 1990.
    • (1990) Int J Cancer , vol.45 , pp. 1119-1124
    • Hosokawa, N.1    Hosokawa, Y.2    Sakai, T.3    Yoshida, M.4    Marui, N.5    Nishino, H.6    Kawai, K.7    Aoike, A.8
  • 69
    • 0028931265 scopus 로고
    • Principles of cdk regulation
    • Morgan DO: Principles of cdk regulation. Nature 374: 131-134, 1995.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 70
    • 0029948789 scopus 로고    scopus 로고
    • Cyclin C/cdk8 is a novel CTD kinase associated with RNA polymerase II
    • Rickert P, Seghezzi W, Shanahan F, Cho H and Lees E: Cyclin C/cdk8 is a novel CTD kinase associated with RNA polymerase II. Oncogene 12: 2631-2640, 1996.
    • (1996) Oncogene , vol.12 , pp. 2631-2640
    • Rickert, P.1    Seghezzi, W.2    Shanahan, F.3    Cho, H.4    Lees, E.5
  • 71
    • 0027219918 scopus 로고
    • Signals and genes in the control of cell-cycle progression
    • Müller R, Mumberg D and Lucibello FC: Signals and genes in the control of cell-cycle progression. Biochim Biophys Acta 1155: 151-179, 1993.
    • (1993) Biochim Biophys Acta , vol.1155 , pp. 151-179
    • Müller, R.1    Mumberg, D.2    Lucibello, F.C.3
  • 72
    • 0028290362 scopus 로고
    • Lineage-specific regulation of cell cycle gene expression in differentiating myeloid cells
    • Bürger C, Wick M and Müller R: Lineage-specific regulation of cell cycle gene expression in differentiating myeloid cells. J Cell Sci 107: 2047-2054, 1994.
    • (1994) J Cell Sci , vol.107 , pp. 2047-2054
    • Bürger, C.1    Wick, M.2    Müller, R.3
  • 73
    • 0028880855 scopus 로고
    • Cyclins, cyclin-dependent kinases and cdk inhibitors: Implications in cell cycle control and cancer
    • MacLachlan TK, Sang N and Giordano A: Cyclins, cyclin-dependent kinases and cdk inhibitors: implications in cell cycle control and cancer. Crit Rev Eukar Gene Expr 5: 127-156, 1995.
    • (1995) Crit Rev Eukar Gene Expr , vol.5 , pp. 127-156
    • MacLachlan, T.K.1    Sang, N.2    Giordano, A.3
  • 74
    • 0028292621 scopus 로고
    • DP and E2F proteins: Components of a heterodimeric transcription factor implicated in cell cycle control
    • La Thangue NB: DP and E2F proteins: components of a heterodimeric transcription factor implicated in cell cycle control. Curr Opinion Cell Biol 6: 443-450, 1994.
    • (1994) Curr Opinion Cell Biol , vol.6 , pp. 443-450
    • La Thangue, N.B.1
  • 75
    • 0028568315 scopus 로고
    • Cell cycle control and cancer
    • Hartwell LH and Kastan MB: Cell cycle control and cancer. Science 266: 1821-1828, 1994.
    • (1994) Science , vol.266 , pp. 1821-1828
    • Hartwell, L.H.1    Kastan, M.B.2
  • 76
    • 0028053581 scopus 로고
    • Cell cycle checkpoints
    • Murray A: Cell cycle checkpoints. Curr Opinion Cell Biol 6: 872-876, 1994.
    • (1994) Curr Opinion Cell Biol , vol.6 , pp. 872-876
    • Murray, A.1
  • 77
    • 0027938209 scopus 로고
    • Cyclins and cancer. II: Cyclin D and cdk inhibitors come of age
    • Hunter T and Pines J: Cyclins and cancer. II: Cyclin D and cdk inhibitors come of age. Cell 79: 573-582, 1994.
    • (1994) Cell , vol.79 , pp. 573-582
    • Hunter, T.1    Pines, J.2
  • 79
    • 0025983818 scopus 로고
    • Mutations at sites involved in Suc1 binding inactivate cdc2
    • Ducommun B, Brambilla P and Draetta G: Mutations at sites involved in Suc1 binding inactivate cdc2. Mol Cell Biol 11: 6177-6184, 1991.
    • (1991) Mol Cell Biol , vol.11 , pp. 6177-6184
    • Ducommun, B.1    Brambilla, P.2    Draetta, G.3
  • 80
    • 0026070261 scopus 로고
    • Phosphorylation at Thr167 is required for Schizosaccharomyces pombe p34cdc2 function
    • Gould KL, Moreno S, Owen DJ, Sazer S and Nurse P: Phosphorylation at Thr167 is required for Schizosaccharomyces pombe p34cdc2 function. EMBO J 10: 3297-3309, 1991.
    • (1991) EMBO J , vol.10 , pp. 3297-3309
    • Gould, K.L.1    Moreno, S.2    Owen, D.J.3    Sazer, S.4    Nurse, P.5
  • 81
    • 0027097609 scopus 로고
    • Identification of the domains in cyclin A required for binding to, and activation of, p34cdc2 and p32cdk2 protein kinase subunits
    • Kobayashi H, Stewart E, Poon R, Adamczewski JP, Gannon J and Hunt T: Identification of the domains in cyclin A required for binding to, and activation of, p34cdc2 and p32cdk2 protein kinase subunits. Mol Biol Cell 3: 1279-1294, 1992.
    • (1992) Mol Biol Cell , vol.3 , pp. 1279-1294
    • Kobayashi, H.1    Stewart, E.2    Poon, R.3    Adamczewski, J.P.4    Gannon, J.5    Hunt, T.6
  • 82
    • 0027465945 scopus 로고
    • Sequences within the conserved cyclin box of human cyclin A are sufficient for binding to and activation of cdc2 kinase
    • Lees EM and Harlow E: Sequences within the conserved cyclin box of human cyclin A are sufficient for binding to and activation of cdc2 kinase. Mol Cell Biol 13: 1194-1201, 1993.
    • (1993) Mol Cell Biol , vol.13 , pp. 1194-1201
    • Lees, E.M.1    Harlow, E.2
  • 83
    • 0028174131 scopus 로고
    • Mutational analysis supports a sructural model for the cell cycle protein kinase p34
    • Endicott JA, Nurse P and Johnson LN: Mutational analysis supports a sructural model for the cell cycle protein kinase p34. Protein Engineering 7: 243-253, 1994.
    • (1994) Protein Engineering , vol.7 , pp. 243-253
    • Endicott, J.A.1    Nurse, P.2    Johnson, L.N.3
  • 84
    • 0028021003 scopus 로고
    • Substrate specificity of cdc2 kinase from human HeLa cells as determined with synthetic peptides and molecular modeling
    • Zhang J, Sanchez RJ, Wang S, Guarnaccia C, Tossi A, Zahariev S and Pongor S: Substrate specificity of cdc2 kinase from human HeLa cells as determined with synthetic peptides and molecular modeling. Arch Biochem Biophys 315: 415-424, 1994.
    • (1994) Arch Biochem Biophys , vol.315 , pp. 415-424
    • Zhang, J.1    Sanchez, R.J.2    Wang, S.3    Guarnaccia, C.4    Tossi, A.5    Zahariev, S.6    Pongor, S.7
  • 85
    • 0028138670 scopus 로고
    • The function(s) of CAK, the p34cdc2-activating kinase
    • Solomon MJ: The function(s) of CAK, the p34cdc2-activating kinase. Trends Biochem Sci 19: 496-500, 1994.
    • (1994) Trends Biochem Sci , vol.19 , pp. 496-500
    • Solomon, M.J.1
  • 87
    • 0028950016 scopus 로고
    • Effects of phosphorylation by CAK on cyclin binding by cdc2 and cdk2
    • Desai D, Wessling HC, Fisher RP and Morgan DO: Effects of phosphorylation by CAK on cyclin binding by cdc2 and cdk2. Mol Cell Biol 15: 345-350, 1995.
    • (1995) Mol Cell Biol , vol.15 , pp. 345-350
    • Desai, D.1    Wessling, H.C.2    Fisher, R.P.3    Morgan, D.O.4
  • 88
    • 0026573437 scopus 로고
    • Interaction between the cell-cycle-control proteins p34cdc2 and p3CKShs2. Evidence for two cooperative binding domains in p3CKShs2
    • Azzi L, Meijer L, Reed SI, Pidikiti R and Tung HYL: Interaction between the cell-cycle-control proteins p34cdc2 and p3CKShs2. Evidence for two cooperative binding domains in p3CKShs2. Eur J Biochem 203: 353-360, 1992.
    • (1992) Eur J Biochem , vol.203 , pp. 353-360
    • Azzi, L.1    Meijer, L.2    Reed, S.I.3    Pidikiti, R.4    Tung, H.Y.L.5
  • 89
    • 0027482006 scopus 로고
    • Human CksHs2 atomic structure: A role for its hexameric assembly in cell cycle control
    • Parge HE, Arvai AS, Murtadi DJ, Reed SI and Tainer JA: Human CksHs2 atomic structure: a role for its hexameric assembly in cell cycle control. Science 262: 387-395, 1993.
    • (1993) Science , vol.262 , pp. 387-395
    • Parge, H.E.1    Arvai, A.S.2    Murtadi, D.J.3    Reed, S.I.4    Tainer, J.A.5
  • 90
    • 0028365109 scopus 로고
    • Purification of a 15-kDa cdk4- and cdk5-binding protein
    • Azzi L, Meijer L, Ostvold AC, Lew J and Wang JH: Purification of a 15-kDa cdk4- and cdk5-binding protein. J Biol Chem 269: 13279-13288, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 13279-13288
    • Azzi, L.1    Meijer, L.2    Ostvold, A.C.3    Lew, J.4    Wang, J.H.5
  • 91
    • 0026319225 scopus 로고
    • Specific activation of cdc25 tyrosine phosphatases by B-type cyclin: Evidence for multiple roles of mitotic cyclins
    • Galaktionov K and Beach D: Specific activation of cdc25 tyrosine phosphatases by B-type cyclin: evidence for multiple roles of mitotic cyclins. Cell 67: 1181-1194, 1991.
    • (1991) Cell , vol.67 , pp. 1181-1194
    • Galaktionov, K.1    Beach, D.2
  • 92
    • 0027482633 scopus 로고
    • Functional analysis of the P box, a domain in cyclin B required for the acitvatio of cdc25
    • Zheng XF and Ruderman JV: Functional analysis of the P box, a domain in cyclin B required for the acitvatio of cdc25. Cell 75: 155-164, 1993.
    • (1993) Cell , vol.75 , pp. 155-164
    • Zheng, X.F.1    Ruderman, J.V.2
  • 93
    • 0028072520 scopus 로고
    • Joining the complex: Cyclin-dependent kinase inhibitory proteins and the cell cycle
    • Peter M and Herskowitz I: Joining the complex: cyclin-dependent kinase inhibitory proteins and the cell cycle. Cell 79: 181-184, 1994.
    • (1994) Cell , vol.79 , pp. 181-184
    • Peter, M.1    Herskowitz, I.2
  • 94
    • 0028168242 scopus 로고
    • p15INK4B is a potential effector of TGFfl-induced cell cycle arrest
    • Hannon GJ and Beach D: p15INK4B is a potential effector of TGFfl-induced cell cycle arrest. Nature 371: 257-261, 1994.
    • (1994) Nature , vol.371 , pp. 257-261
    • Hannon, G.J.1    Beach, D.2
  • 95
    • 0028582034 scopus 로고
    • Growth suppression by p18, a P16INK4/MTS1- and p14INK4B/MTS2-related cdk6 inhibitor, correlates with wild-type pRb function
    • Guan KL, Jenkins CW, Li Y, Nichols MA, Wu X, O'Keefe CL, Matera AG and Xiong Y: Growth suppression by p18, a P16INK4/MTS1- and p14INK4B/MTS2-related cdk6 inhibitor, correlates with wild-type pRb function. Genes Dev 8: 2939-2952, 1994.
    • (1994) Genes Dev , vol.8 , pp. 2939-2952
    • Guan, K.L.1    Jenkins, C.W.2    Li, Y.3    Nichols, M.A.4    Wu, X.5    O'Keefe, C.L.6    Matera, A.G.7    Xiong, Y.8
  • 96
    • 0028342664 scopus 로고
    • Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen
    • Noda A, Ning Y, Venable SF, Pereira-Smith OM and Smith JR: Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen. Exp Cell Res 211: 90-98, 1994.
    • (1994) Exp Cell Res , vol.211 , pp. 90-98
    • Noda, A.1    Ning, Y.2    Venable, S.F.3    Pereira-Smith, O.M.4    Smith, J.R.5
  • 100
    • 0027319328 scopus 로고
    • Anaphase is initiated by proteolysis rather than by the inactivatio of maturation-promoting factor
    • Holloway SL, Glotzer M, King RW and Murray AW: Anaphase is initiated by proteolysis rather than by the inactivatio of maturation-promoting factor. Cell 73: 1393-1402, 1993.
    • (1993) Cell , vol.73 , pp. 1393-1402
    • Holloway, S.L.1    Glotzer, M.2    King, R.W.3    Murray, A.W.4
  • 101
    • 0026568213 scopus 로고
    • Relocation and distinct subcellular localization of p34cdc2-cyclin B complex at meiosis reinitiation in starfish oocytes
    • Ookata K, Hisanaga SI, Okano T, Tachibana K and Kishimoto T: Relocation and distinct subcellular localization of p34cdc2-cyclin B complex at meiosis reinitiation in starfish oocytes. EMBO J 11: 1763-1772, 1992.
    • (1992) EMBO J , vol.11 , pp. 1763-1772
    • Ookata, K.1    Hisanaga, S.I.2    Okano, T.3    Tachibana, K.4    Kishimoto, T.5
  • 102
    • 0027933911 scopus 로고
    • The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B
    • Pines J and Hunter T: The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B. EMBO J 13: 3772-3781, 1994.
    • (1994) EMBO J , vol.13 , pp. 3772-3781
    • Pines, J.1    Hunter, T.2
  • 107
    • 0025196215 scopus 로고
    • 2 arrest in Chinese hamster ovary cells
    • 2 arrest in Chinese hamster ovary cells. Cancer Res 50: 3761-3766, 1990.
    • (1990) Cancer Res , vol.50 , pp. 3761-3766
    • Lock, R.B.1    Ross, W.E.2
  • 108
    • 0025196216 scopus 로고
    • Possible role for p34cdc2 kinase in Etoposide-induced cell death of Chinese hamster ovary cells
    • Lock RB and Ross WE: Possible role for p34cdc2 kinase in Etoposide-induced cell death of Chinese hamster ovary cells. Cancer Res 50: 3767-2771, 1990.
    • (1990) Cancer Res , vol.50 , pp. 3767-12771
    • Lock, R.B.1    Ross, W.E.2
  • 109
    • 0026611089 scopus 로고
    • cdc2 tyrosine dephosphorylation, and mitotic progression in Chinese hamster ovary cells exposed to etoposide
    • cdc2 tyrosine dephosphorylation, and mitotic progression in Chinese hamster ovary cells exposed to etoposide. Cancer Res 52: 1817-1822, 1992.
    • (1992) Cancer Res , vol.52 , pp. 1817-1822
    • Lock, R.B.1
  • 114
    • 0027989510 scopus 로고
    • Chromatin condensation during apoptosis is accompanied by degradation of lamin A+B, without enhanced activatio of cdc2 kinase
    • Oberhammer FA, Hochegger K, Fröschl G, Tiefenbacher R and Pavelka MJ: Chromatin condensation during apoptosis is accompanied by degradation of lamin A+B, without enhanced activatio of cdc2 kinase. Cell Biol 126: 827-837, 1994.
    • (1994) Cell Biol , vol.126 , pp. 827-837
    • Oberhammer, F.A.1    Hochegger, K.2    Fröschl, G.3    Tiefenbacher, R.4    Pavelka, M.J.5
  • 116
    • 0028094424 scopus 로고
    • The role of cell cycle progression in cisplatin induced apoptosis in Chinese hamster ovary cells
    • Demarcq C, Bunch RT, Creswell D and Easterman A: The role of cell cycle progression in cisplatin induced apoptosis in Chinese hamster ovary cells. Cell Growth Different 5: 983-993, 1994.
    • (1994) Cell Growth Different , vol.5 , pp. 983-993
    • Demarcq, C.1    Bunch, R.T.2    Creswell, D.3    Easterman, A.4
  • 117
    • 0016633504 scopus 로고
    • 2
    • 2. Nature 254: 245-247, 1975.
    • (1975) Nature , vol.254 , pp. 245-247
    • Tobey, R.A.1
  • 118
    • 0018138138 scopus 로고
    • Induction of concentration-dependent blockade in the G2 phase of the cell cycle by cancer chemotherapeutic agents
    • Kimler BF, Schneiderman MH and Leeper DB: Induction of concentration-dependent blockade in the G2 phase of the cell cycle by cancer chemotherapeutic agents. Cancer Res 38: 809-814, 1978.
    • (1978) Cancer Res , vol.38 , pp. 809-814
    • Kimler, B.F.1    Schneiderman, M.H.2    Leeper, D.B.3
  • 120
    • 0024341613 scopus 로고
    • 2 and mitotic Chinese hamster ovary cell progression
    • 2 and mitotic Chinese hamster ovary cell progression. Cancer Res 49: 4752-4747, 1989.
    • (1989) Cancer Res , vol.49 , pp. 4752-14747
    • Rowley, R.1    Kort, L.2
  • 121
    • 0028025563 scopus 로고
    • Apoptosis in cancer therapy: Crossing the threshold
    • Fisher DE: Apoptosis in cancer therapy: crossing the threshold. Cell 78: 539-542, 1994.
    • (1994) Cell , vol.78 , pp. 539-542
    • Fisher, D.E.1
  • 125
    • 0026501878 scopus 로고
    • Different effects of Staurosporine, an inhibitor of protein kinases, on the cell cycle and chromatin structure of normal and leukemic lymphocytes
    • Bruno S, Ardelt B, Skierski JS, Traganos F and Darzynkiewicz Z: Different effects of Staurosporine, an inhibitor of protein kinases, on the cell cycle and chromatin structure of normal and leukemic lymphocytes. Cancer Res 52: 470-473, 1992.
    • (1992) Cancer Res , vol.52 , pp. 470-473
    • Bruno, S.1    Ardelt, B.2    Skierski, J.S.3    Traganos, F.4    Darzynkiewicz, Z.5
  • 126
    • 0027990255 scopus 로고
    • A cyclin-dependent kinase inhibitor, butyrolactone I, inhibits phosphorylation of RB protein and cell cycle progression
    • Kitagawa M, Higashi H, Suzuki-Takahashi I, Okabe T, Ogino H, Taya Y, Nishimura S and Okuyama A: A cyclin-dependent kinase inhibitor, butyrolactone I, inhibits phosphorylation of RB protein and cell cycle progression. Oncogene 9: 2549-2557, 1994.
    • (1994) Oncogene , vol.9 , pp. 2549-2557
    • Kitagawa, M.1    Higashi, H.2    Suzuki-Takahashi, I.3    Okabe, T.4    Ogino, H.5    Taya, Y.6    Nishimura, S.7    Okuyama, A.8
  • 128
    • 0025250131 scopus 로고
    • Effects of Suramin, an anti-human immunodeficiency virus reverse transcriptase agent, on protein kinase C. Differential activation and inhibition of protein kinase C isozymes
    • Mahoney CW, Azzi A and Huang KP: Effects of Suramin, an anti-human immunodeficiency virus reverse transcriptase agent, on protein kinase C. Differential activation and inhibition of protein kinase C isozymes. J Biol Chem 265: 5424-5428, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 5424-5428
    • Mahoney, C.W.1    Azzi, A.2    Huang, K.P.3
  • 132
    • 0024365171 scopus 로고
    • Influence of site on the chemosensitivity of transplantable murine colon tumours to flavone acetic acid (LM975, NSC 347512)
    • Bibby MC, Philips RM and Double JA: Influence of site on the chemosensitivity of transplantable murine colon tumours to flavone acetic acid (LM975, NSC 347512) Cancer Chemother Pharmacol 24: 87-94, 1989.
    • (1989) Cancer Chemother Pharmacol , vol.24 , pp. 87-94
    • Bibby, M.C.1    Philips, R.M.2    Double, J.A.3
  • 133
    • 0005953097 scopus 로고
    • Protein kinase activity associated with the avian sarcoma virus src gene product
    • Collett MS and Erikson RL: Protein kinase activity associated with the avian sarcoma virus src gene product. Proc Natl Acad Sci USA 75: 2021-2024, 1978.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 2021-2024
    • Collett, M.S.1    Erikson, R.L.2


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