메뉴 건너뛰기




Volumn 2, Issue 1, 2004, Pages 53-61

Topoisomerase I and II Inhibitors Control Caspase-2 Pre-Messenger RNA Splicing in Human Cells

Author keywords

[No Author keywords available]

Indexed keywords

7 ETHYL 10 HYDROXYCAMPTOTHECIN; ALKYLATING AGENT; AMSACRINE; BN 80765; BN 80927; CAMPTOTHECIN; CARBAZOLE DERIVATIVE; CASPASE 2; CASPASE 2L; CASPASE 2S; CIS ACTING ELEMENT; CISPLATIN; CYTOTOXIC AGENT; DIFLOMOTECAN; DNA TOPOISOMERASE; DNA TOPOISOMERASE (ATP HYDROLYSING); DNA TOPOISOMERASE INHIBITOR; DOXORUBICIN; ETOPOSIDE; FLUOROURACIL; GLYCOSYLINDOLOCARBAZOLE DERIVATIVE; HOMOCAMPTOTHECIN DERIVATIVE; INTERCALATING AGENT; MELPHALAN; MESSENGER RNA PRECURSOR; MITOXANTRONE; TOPOISOMERASE I INHIBITOR; TOPOISOMERASE II INHIBITOR; UNCLASSIFIED DRUG; UNINDEXED DRUG; VINBLASTINE;

EID: 0842304139     PISSN: 15417786     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (59)

References (51)
  • 1
    • 0036337915 scopus 로고    scopus 로고
    • A genomic view of alternative splicing
    • Modrek, B. and Lee, C. A genomic view of alternative splicing. Nat. Genet., 30: 13-19, 2002.
    • (2002) Nat. Genet. , vol.30 , pp. 13-19
    • Modrek, B.1    Lee, C.2
  • 2
    • 0036534129 scopus 로고    scopus 로고
    • Alternative splicing: Multiple control mechanisms and involvement in human disease
    • Caceres, J. F. and Komblihtt, A. R. Alternative splicing: multiple control mechanisms and involvement in human disease. Trends Genet., 18: 186-193, 2002.
    • (2002) Trends Genet. , vol.18 , pp. 186-193
    • Caceres, J.F.1    Komblihtt, A.R.2
  • 3
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • Zhou, Z., Licklider, L. J., Gygi, S. P., and Reed, R. Comprehensive proteomic analysis of the human spliceosome. Nature, 419: 182-185, 2002.
    • (2002) Nature , vol.419 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4
  • 4
    • 0029767662 scopus 로고    scopus 로고
    • SR proteins and splicing control
    • Manley, J. L. and Tacke, R. SR proteins and splicing control. Genes Dev., 10: 1569-1579, 1996.
    • (1996) Genes Dev. , vol.10 , pp. 1569-1579
    • Manley, J.L.1    Tacke, R.2
  • 5
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley, B. R. Sorting out the complexity of SR protein functions. RNA, 6: 1197-1211, 2000.
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 6
    • 0033152209 scopus 로고    scopus 로고
    • Determinants of SR protein specificity
    • Tacke, R. and Manley J. L. Determinants of SR protein specificity. Curr. Opin. Cell Biol., 11: 358-362, 1999.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 358-362
    • Tacke, R.1    Manley, J.L.2
  • 7
    • 0036207384 scopus 로고    scopus 로고
    • Listening to silence and understanding nonsense: Exonic mutations that affect splicing
    • Cartegni, L., Chew, S. L., and Krainer, A. R. Listening to silence and understanding nonsense: exonic mutations that affect splicing. Nat. Rev. Genet., 3: 285-298, 2002.
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 285-298
    • Cartegni, L.1    Chew, S.L.2    Krainer, A.R.3
  • 8
    • 0027137934 scopus 로고
    • Specific interactions between proteins implicated in splice site selection and regulated alternative splicing
    • Wu, J. Y. and Maniatis, T. Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell, 75: 1061-1070, 1993.
    • (1993) Cell , vol.75 , pp. 1061-1070
    • Wu, J.Y.1    Maniatis, T.2
  • 9
    • 0028324929 scopus 로고
    • The role of specific protein-RNA and protein-protein interactions in positive and negative control of pre-mRNA splicing by Transformer 2
    • Amrein, H., Hedley, M. L., and Maniatis, T. The role of specific protein-RNA and protein-protein interactions in positive and negative control of pre-mRNA splicing by Transformer 2. Cell, 76: 735-746, 1994.
    • (1994) Cell , vol.76 , pp. 735-746
    • Amrein, H.1    Hedley, M.L.2    Maniatis, T.3
  • 10
    • 0037062982 scopus 로고    scopus 로고
    • Alternative pre-mRNA splicing and proteome expansion in metazoans
    • Maniatis, T. and Tasic, B. Alternative pre-mRNA splicing and proteome expansion in metazoans. Nature, 418: 236-243, 2002.
    • (2002) Nature , vol.418 , pp. 236-243
    • Maniatis, T.1    Tasic, B.2
  • 11
    • 0030828196 scopus 로고    scopus 로고
    • DNA topoisomemse I: Customs officer at the border between DNA and RNA worlds?
    • Tazi, J., Rossi, F., Labourier, E., Gallouzi, I., Brunel, C., and Antoine, E. DNA topoisomemse I: customs officer at the border between DNA and RNA worlds? J. Mol. Med., 75: 786-800, 1997.
    • (1997) J. Mol. Med. , vol.75 , pp. 786-800
    • Tazi, J.1    Rossi, F.2    Labourier, E.3    Gallouzi, I.4    Brunel, C.5    Antoine, E.6
  • 12
    • 0035884180 scopus 로고    scopus 로고
    • Specific inhibition of serine- and arginine-rich splicing factors phosphorylation, spliceosome assembly, and splicing by the antitumor drug NB-506
    • Pilch, B., Allemand, E., Facompre, M., Bailly, C., Riou, J., F., Soret, J., and Tazi, J. Specific inhibition of serine- and arginine-rich splicing factors phosphorylation, spliceosome assembly, and splicing by the antitumor drug NB-506. Cancer Res., 61: 6876-6884, 2001.
    • (2001) Cancer Res. , vol.61 , pp. 6876-6884
    • Pilch, B.1    Allemand, E.2    Facompre, M.3    Bailly, C.4    Riou, J.F.5    Soret, J.6    Tazi, J.7
  • 13
    • 0032914182 scopus 로고    scopus 로고
    • Alternative splicing and programmed cell death
    • Jiang, Z. H. and Wu, J. Y. Alternative splicing and programmed cell death. Proc. Soc. Exp. Biol. Med., 220: 64-72, 1999.
    • (1999) Proc. Soc. Exp. Biol. Med. , vol.220 , pp. 64-72
    • Jiang, Z.H.1    Wu, J.Y.2
  • 14
    • 0035877605 scopus 로고    scopus 로고
    • Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3
    • Paroni, G., Henderson, C., Schneider, C., and Brancolini, C. Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3. J. Biol. Chem., 276: 21907-21915, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21907-21915
    • Paroni, G.1    Henderson, C.2    Schneider, C.3    Brancolini, C.4
  • 15
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization
    • Lassus, P., Opitz-Araya, X., and Lazebnik, Y. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science, 297: 1352-1354, 2002.
    • (2002) Science , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 16
    • 0028168593 scopus 로고
    • Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death
    • Wang, L., Miura, M., Bergeron, L., Zhu, H., and Yuan, J. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell, 78: 739-750, 1994.
    • (1994) Cell , vol.78 , pp. 739-750
    • Wang, L.1    Miura, M.2    Bergeron, L.3    Zhu, H.4    Yuan, J.5
  • 17
    • 0035843138 scopus 로고    scopus 로고
    • Modulation of apoptosis by procaspase-2 short isoform: Selective inhibition of chromatin condensation, apoptotic body formation and phosphatidylserine externalization
    • Droin, N., Rebe, C., Bichat, F., Hammann, A., Bertrand, R., and Solary E. Modulation of apoptosis by procaspase-2 short isoform: selective inhibition of chromatin condensation, apoptotic body formation and phosphatidylserine externalization. Oncogene, 20: 260-269, 2001.
    • (2001) Oncogene , vol.20 , pp. 260-269
    • Droin, N.1    Rebe, C.2    Bichat, F.3    Hammann, A.4    Bertrand, R.5    Solary, E.6
  • 18
    • 0035970031 scopus 로고    scopus 로고
    • Caspase-2 pre-mRNA alternative splicing: Identification of an intronic element containing a decoy 3′ acceptor site
    • Cote, J., Dupuis, S., Jiang, Z., and Wu, J. Y. Caspase-2 pre-mRNA alternative splicing: identification of an intronic element containing a decoy 3′ acceptor site. Proc. Natl. Acad. Sci. USA, 98: 938-943, 2001.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 938-943
    • Cote, J.1    Dupuis, S.2    Jiang, Z.3    Wu, J.Y.4
  • 19
    • 0032482968 scopus 로고    scopus 로고
    • Regulation of Ich-1 pre-mRNA alternative splicing and apoptosis by mammalian splicing factors
    • Jiang, Z. H., Zhang, W. J., Rao, Y., and Wu, J. Y. Regulation of Ich-1 pre-mRNA alternative splicing and apoptosis by mammalian splicing factors. Proc. Natl. Acad. Sci. USA, 95: 9155-9160, 1998.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9155-9160
    • Jiang, Z.H.1    Zhang, W.J.2    Rao, Y.3    Wu, J.Y.4
  • 20
    • 0035896511 scopus 로고    scopus 로고
    • Polypyrimidine track-binding protein binding downstream of caspase-2 alternative exon 9 represses its inclusion
    • Cote, J., Dupuis, S., and Wu, J. Y. Polypyrimidine track-binding protein binding downstream of caspase-2 alternative exon 9 represses its inclusion. J. Biol. Chem., 276: 8535-8543, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8535-8543
    • Cote, J.1    Dupuis, S.2    Wu, J.Y.3
  • 21
    • 0037191508 scopus 로고    scopus 로고
    • Differential influence of etoposide on two caspase-2 mRNA isoforms in leukemic cells
    • Wotawa, A., Solier, S., Logette, E., Solary, E., and Corcos, L. Differential influence of etoposide on two caspase-2 mRNA isoforms in leukemic cells. Cancer Lett., 185: 181-189, 2002.
    • (2002) Cancer Lett. , vol.185 , pp. 181-189
    • Wotawa, A.1    Solier, S.2    Logette, E.3    Solary, E.4    Corcos, L.5
  • 22
    • 0035863393 scopus 로고    scopus 로고
    • Use of camptothecin-resistant mammalian cell lines to evaluate the role of topoisomerase I in the antiproliferative activity of the indolocarbazole, NB-506, and its topoisomerase I binding site
    • Urasaki, Y., Laco, G., Takebayashi, Y., Bailly, C., Kohlhagen, G., and Pommier, Y. Use of camptothecin-resistant mammalian cell lines to evaluate the role of topoisomerase I in the antiproliferative activity of the indolocarbazole, NB-506, and its topoisomerase I binding site. Cancer Res., 61: 504-508, 2001.
    • (2001) Cancer Res. , vol.61 , pp. 504-508
    • Urasaki, Y.1    Laco, G.2    Takebayashi, Y.3    Bailly, C.4    Kohlhagen, G.5    Pommier, Y.6
  • 23
    • 0033057286 scopus 로고    scopus 로고
    • The staurosporine-like compound L-753,000 (NB-506) potentiates the neurotrophic effects of neurotrophin-3 by acting selectively at the TrkA receptor
    • Pollack, S., Young, L., Bilsland, J., Wilkie, N., Ellis, S., Hefti, F., Broughton, H., and Harper, S. The staurosporine-like compound L-753,000 (NB-506) potentiates the neurotrophic effects of neurotrophin-3 by acting selectively at the TrkA receptor. Mol. Pharmacol., 56: 185-195, 1999.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 185-195
    • Pollack, S.1    Young, L.2    Bilsland, J.3    Wilkie, N.4    Ellis, S.5    Hefti, F.6    Broughton, H.7    Harper, S.8
  • 24
    • 0028957974 scopus 로고
    • Mutation at the catalytic site of topoisomerase I in CEM/C2, a human leukemia cell line resistant to camptothecin
    • Fujimori, A., Harker, W. G., Kohlhagen, G., Hoki, Y., and Pommier, Y. Mutation at the catalytic site of topoisomerase I in CEM/C2, a human leukemia cell line resistant to camptothecin. Cancer Res., 55: 1339-1346, 1995.
    • (1995) Cancer Res. , vol.55 , pp. 1339-1346
    • Fujimori, A.1    Harker, W.G.2    Kohlhagen, G.3    Hoki, Y.4    Pommier, Y.5
  • 26
    • 0037632570 scopus 로고    scopus 로고
    • Targeting DNA topoisomerase I with indolocarbazole antitumor agents
    • M. Demeunynck, C. Bailly, and W. D. Wilson. Weinheim, Germany: Wiley-VCH
    • Bailly, C. Targeting DNA and topoisomerase I with indolocarbazole antitumor agents. In: M. Demeunynck, C. Bailly, and W. D. Wilson, Small Molecule DNA and RNA Binders, Vol. 2, pp. 538-575. Weinheim, Germany: Wiley-VCH, 2003.
    • (2003) Small Molecule DNA and RNA Binders , vol.2 , pp. 538-575
    • Bailly, C.1
  • 27
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: A molecular perspective
    • Wang, J. C. Cellular roles of DNA topoisomerases: a molecular perspective. Nat. Rev. Mol. Cell Biol., 3: 430-440, 2002.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 28
    • 0037022269 scopus 로고    scopus 로고
    • Subnuclear distribution of topoisomerase I is linked to ongoing transcription and p53 status
    • Mao, Y., Mehl, I. R., and Muller, M. T. Subnuclear distribution of topoisomerase I is linked to ongoing transcription and p53 status. Proc. Natl. Acad. Sci. USA, 99: 1235-1240, 2002.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1235-1240
    • Mao, Y.1    Mehl, I.R.2    Muller, M.T.3
  • 29
    • 0031806623 scopus 로고    scopus 로고
    • Targeting to transcriptionally active loci by the hydrophilic N-terminal domain of Drosophila DNA topoisomerase I
    • Shaiu, W. L. and Hsieh, T. S. Targeting to transcriptionally active loci by the hydrophilic N-terminal domain of Drosophila DNA topoisomerase I. Mol. Cell. Biol., 18: 4358-4367, 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4358-4367
    • Shaiu, W.L.1    Hsieh, T.S.2
  • 32
    • 0037200032 scopus 로고    scopus 로고
    • Overexpression of the atypical protein kinase C ζ reduces topoisomerase II catalytic activity, cleavable complexes formation, and drug-induced cytotoxicity in monocytic U937 leukemia cells
    • Plo, I., Hernandez, H., Kohlhagen, G., Lautier, D., Pommier, Y., and Laurent, G. Overexpression of the atypical protein kinase C ζ reduces topoisomerase II catalytic activity, cleavable complexes formation, and drug-induced cytotoxicity in monocytic U937 leukemia cells. J. Biol. Chem., 277: 31407-31415, 2002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31407-31415
    • Plo, I.1    Hernandez, H.2    Kohlhagen, G.3    Lautier, D.4    Pommier, Y.5    Laurent, G.6
  • 33
    • 0033820092 scopus 로고    scopus 로고
    • Positive and negative regulation of apoptotic pathways by cytotoxic agents in hematological malignancies
    • Solary, E., Droin, N., Bettaieb, A., Corcos, L., Dimanche-Boitrel, M. T., and Garrido, C. Positive and negative regulation of apoptotic pathways by cytotoxic agents in hematological malignancies. Leukemia, 14: 1833-1849, 2000.
    • (2000) Leukemia , vol.14 , pp. 1833-1849
    • Solary, E.1    Droin, N.2    Bettaieb, A.3    Corcos, L.4    Dimanche-Boitrel, M.T.5    Garrido, C.6
  • 34
    • 0036400817 scopus 로고    scopus 로고
    • Phospholipid synthesis, diacylglycerol compartmentation, and apoptosis
    • Wright, M. M. and McMaster, C. R. Phospholipid synthesis, diacylglycerol compartmentation, and apoptosis. Biol. Res., 35: 223-229, 2002.
    • (2002) Biol. Res. , vol.35 , pp. 223-229
    • Wright, M.M.1    McMaster, C.R.2
  • 35
    • 0035502956 scopus 로고    scopus 로고
    • Activation of nuclear factor κB through the IKK complex by the topoisomerase poisons SN38 and doxorubicin: A brake to apoptosis in HeLa human carcinoma cells
    • Bottero, V., Busuttil, V., Loubat, A., Magne, N., Fischel, J. L., Milano, G., and Peyron, J. F. Activation of nuclear factor κB through the IKK complex by the topoisomerase poisons SN38 and doxorubicin: a brake to apoptosis in HeLa human carcinoma cells. Cancer Res., 61: 7785-7791, 2001.
    • (2001) Cancer Res. , vol.61 , pp. 7785-7791
    • Bottero, V.1    Busuttil, V.2    Loubat, A.3    Magne, N.4    Fischel, J.L.5    Milano, G.6    Peyron, J.F.7
  • 36
    • 0031762425 scopus 로고    scopus 로고
    • In vitro evaluation of synergism or antagonism with combinations of new cytotoxic agents
    • Budman, D. R., Calabro, A., and Kreis, W. In vitro evaluation of synergism or antagonism with combinations of new cytotoxic agents. Anticancer Drugs, 9: 697-702, 1998.
    • (1998) Anticancer Drugs , vol.9 , pp. 697-702
    • Budman, D.R.1    Calabro, A.2    Kreis, W.3
  • 37
    • 0034773290 scopus 로고    scopus 로고
    • Combination of oxaliplatin and irinotecan on human colon cancer cell lines: Activity in vitro and in vivo
    • Guichard, S., Amould, S., Hennebelle, I., Bugat, R., and Canal, P. Combination of oxaliplatin and irinotecan on human colon cancer cell lines: activity in vitro and in vivo. Anticancer Drugs, 12: 741-751, 2001.
    • (2001) Anticancer Drugs , vol.12 , pp. 741-751
    • Guichard, S.1    Amould, S.2    Hennebelle, I.3    Bugat, R.4    Canal, P.5
  • 38
    • 0346365373 scopus 로고    scopus 로고
    • Altered serine/arginine-rich protein phosphorylation and exonic enhancer-dependent splicing in mammalian cells lacking topoisomerase I
    • Soret, J. A., Gabut, M., Dupon, C., Kohlhagen, G., Stévenin, J., Pommier, Y. and Tazi, L.J. Altered serine/arginine-rich protein phosphorylation and exonic enhancer-dependent splicing in mammalian cells lacking topoisomerase I. Cancer Res., 63: 8203-8211, 2003.
    • (2003) Cancer Res. , vol.63 , pp. 8203-8211
    • Soret, J.A.1    Gabut, M.2    Dupon, C.3    Kohlhagen, G.4    Stévenin, J.5    Pommier, Y.6    Tazi, L.J.7
  • 40
    • 0029080274 scopus 로고
    • Pharmacokinetics of SN-38 [(+)-(4S)-4,11-diethyl-4,9-dihydroxy-1H-pyrano[3′,4′:6,7] -indolizino[1,2-b]quinoline-3,14(4H,12H)-21 dione], an active metabolite of irinotecan, after a single intravenous dosing of 14C-SN-38 to rats
    • Atsumi, R., Okazaki, O., and Hakusui, H. Pharmacokinetics of SN-38 [(+)-(4S)-4,11-diethyl-4,9-dihydroxy-1H-pyrano[3′,4′:6,7] -indolizino[1,2-b]quinoline-3,14(4H,12H)-21 dione], an active metabolite of irinotecan, after a single intravenous dosing of 14C-SN-38 to rats. Biol. Pharm. Bull., 18: 1114-1119, 1995.
    • (1995) Biol. Pharm. Bull. , vol.18 , pp. 1114-1119
    • Atsumi, R.1    Okazaki, O.2    Hakusui, H.3
  • 41
    • 0037212083 scopus 로고    scopus 로고
    • Homocamptothecins: Potent topoisomerase 1 inhibitors and promising anticancer drugs
    • Bailly, C. Homocamptothecins: potent topoisomerase 1 inhibitors and promising anticancer drugs. Crit. Rev. Oncol. Hematol., 45, 91-108, 2003.
    • (2003) Crit. Rev. Oncol. Hematol. , vol.45 , pp. 91-108
    • Bailly, C.1
  • 42
    • 0036080107 scopus 로고    scopus 로고
    • Discovery of antitumor indolocarbazoles: Rebeccamycin, NSC 655649, and fluoroindolocarbazoles
    • Long, B. H., Rose, W. C., Vyas, D. M., Matson, J. A., and Forenza, S. Discovery of antitumor indolocarbazoles: rebeccamycin, NSC 655649, and fluoroindolocarbazoles. Curr. Med. Chem. Anti-Canc. Agents, 2: 255-266, 2002.
    • (2002) Curr. Med. Chem. Anti-Canc. Agents , vol.2 , pp. 255-266
    • Long, B.H.1    Rose, W.C.2    Vyas, D.M.3    Matson, J.A.4    Forenza, S.5
  • 43
    • 0037130269 scopus 로고    scopus 로고
    • Sequence-specific interactions of drugs interfering with the topoisomerase-DNA cleavage complex
    • Palumbo, M., Gatto, B., Moro, S., Sissi, C., and Zagotto, G. Sequence-specific interactions of drugs interfering with the topoisomerase-DNA cleavage complex. Biochim. Biophys. Acta, 1587: 145-154, 2002.
    • (2002) Biochim. Biophys. Acta , vol.1587 , pp. 145-154
    • Palumbo, M.1    Gatto, B.2    Moro, S.3    Sissi, C.4    Zagotto, G.5
  • 45
    • 0036781733 scopus 로고    scopus 로고
    • DNA topoisomerases in cancer chemotherapy: Using enzymes to generate selective DNA damage
    • Nitiss, J. L. DNA topoisomerases in cancer chemotherapy: using enzymes to generate selective DNA damage. Curr. Opin. Investig. Drugs, 3: 1512-1516, 2002.
    • (2002) Curr. Opin. Investig. Drugs , vol.3 , pp. 1512-1516
    • Nitiss, J.L.1
  • 46
    • 0033598702 scopus 로고    scopus 로고
    • DNA topoisomerases as targets for the anticancer drug TAS-103: DNA interactions and topoisomemse catalytic inhibition
    • Fortune, J. M., Velea, L., Graves, D. E., Utsugi, T., Yamada, Y., and Osheroff, N. DNA topoisomerases as targets for the anticancer drug TAS-103: DNA interactions and topoisomemse catalytic inhibition. Biochemistry, 38: 15580-15586, 1999.
    • (1999) Biochemistry , vol.38 , pp. 15580-15586
    • Fortune, J.M.1    Velea, L.2    Graves, D.E.3    Utsugi, T.4    Yamada, Y.5    Osheroff, N.6
  • 47
    • 0032168167 scopus 로고    scopus 로고
    • Etoposide: Four decades of development of a topoisomerase II inhibiton
    • Hande, K. R. Etoposide: four decades of development of a topoisomerase II inhibiton. Eur. J. Cancer, 34: 1514-1521, 1998.
    • (1998) Eur. J. Cancer , vol.34 , pp. 1514-1521
    • Hande, K.R.1
  • 48
    • 0038387494 scopus 로고    scopus 로고
    • 5-Fluorouracil: Mechanisms of action and clinical strategies
    • Longley, D. B., Harkin, D. P., and Johnston, P. G. 5-Fluorouracil: mechanisms of action and clinical strategies. Nat. Rev. Cancer, 3: 330-338, 2003.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 330-338
    • Longley, D.B.1    Harkin, D.P.2    Johnston, P.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.