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Volumn 9, Issue 2, 1998, Pages 105-123

DNA repair mechanisms associated with cellular resistance to antitumor drugs: Potential novel targets

Author keywords

Antitumor drug; Cellular resistance; DNA repair; Novel targets

Indexed keywords

6 O ALKYLGUANINE DNA ALKYLTRANSFERASE; ANTIBODY; ANTINEOPLASTIC AGENT;

EID: 0031913158     PISSN: 09594973     EISSN: None     Source Type: Journal    
DOI: 10.1097/00001813-199802000-00001     Document Type: Review
Times cited : (35)

References (184)
  • 1
    • 0029929867 scopus 로고    scopus 로고
    • Clinical multidrug resistance in cancer: A multifactorial problem
    • Lehnert M. Clinical multidrug resistance in cancer: a multifactorial problem. Eur J Cancer 1996; 32A: 912-20.
    • (1996) Eur J Cancer , vol.32 A , pp. 912-920
    • Lehnert, M.1
  • 2
    • 0030038297 scopus 로고    scopus 로고
    • Drug resistance: An overview of the current state of the art
    • Hill BT. Drug resistance: an overview of the current state of the art. Int J Oncol 1996; 9: 197-203.
    • (1996) Int J Oncol , vol.9 , pp. 197-203
    • Hill, B.T.1
  • 3
    • 0025195404 scopus 로고
    • 6-alkylguanine-DNA alkyltransferase: Regulation and importance in response to alkylating carcinogenic and therapeutic agents
    • 6-alkylguanine-DNA alkyltransferase: regulation and importance in response to alkylating carcinogenic and therapeutic agents. Cancer Res 1990; 50: 6119-29.
    • (1990) Cancer Res , vol.50 , pp. 6119-6129
    • Pegg, A.E.1
  • 4
    • 0027225260 scopus 로고
    • Role of DNA repair in the mechanisms of cell resistance to alkylating agents and cisplatin
    • Calsou P, Salles B. Role of DNA repair in the mechanisms of cell resistance to alkylating agents and cisplatin. Cancer Chemother Pharmacol 1993; 32: 85-9.
    • (1993) Cancer Chemother Pharmacol , vol.32 , pp. 85-89
    • Calsou, P.1    Salles, B.2
  • 5
    • 0029762815 scopus 로고    scopus 로고
    • DNA repair enzymatic mechanisms and relevance to drug response
    • Chaney SG, Sancar A. DNA repair enzymatic mechanisms and relevance to drug response. J Natl Cancer Inst 1996; 88: 1346-60.
    • (1996) J Natl Cancer Inst , vol.88 , pp. 1346-1360
    • Chaney, S.G.1    Sancar, A.2
  • 6
    • 0024995415 scopus 로고
    • Rapid emergence of acquired cis-platinum(II) resistance in an in vivo model of human ovarian carcinoma
    • Andrews PA, Jones JA, Varki NM, Howell SB. Rapid emergence of acquired cis-platinum(II) resistance in an in vivo model of human ovarian carcinoma. Cancer Commun 1990; 2: 93-100.
    • (1990) Cancer Commun , vol.2 , pp. 93-100
    • Andrews, P.A.1    Jones, J.A.2    Varki, N.M.3    Howell, S.B.4
  • 7
    • 0029618266 scopus 로고
    • DNA repair in humans
    • Sancar A. DNA repair in humans. Annu Rev Genet 1995; 29: 69-105.
    • (1995) Annu Rev Genet , vol.29 , pp. 69-105
    • Sancar, A.1
  • 9
    • 0029892791 scopus 로고    scopus 로고
    • DNA repair in eukaryotes
    • Wood RD. DNA repair in eukaryotes. Annu Rev Biochem 1996; 65: 135-67.
    • (1996) Annu Rev Biochem , vol.65 , pp. 135-167
    • Wood, R.D.1
  • 11
    • 0030608633 scopus 로고    scopus 로고
    • 6-benzylguanine and its role in chemotherapy
    • 6-benzylguanine and its role in chemotherapy. Clin Cancer Res 1997; 3: 837-47.
    • (1997) Clin Cancer Res , vol.3 , pp. 837-847
    • Dolan, M.E.1    Pegg, A.E.2
  • 12
    • 0028987003 scopus 로고
    • 6-alkylguanine-DNA-alkyltransferase: A target for the modulation of drug resistance
    • 6-alkylguanine-DNA-alkyltransferase: a target for the modulation of drug resistance. Hematol Oncol Clin N Am 1995; 9: 431-49.
    • (1995) Hematol Oncol Clin N Am , vol.9 , pp. 431-449
    • Gerson, S.L.1    Wilson, J.K.V.2
  • 13
    • 0029664534 scopus 로고    scopus 로고
    • 6-methylguanine-DNA methyltransferase (MGMT) on the cytotoxic and recombinogeenic activity of difference antineoplastic drugs
    • 6-methylguanine-DNA methyltransferase (MGMT) on the cytotoxic and recombinogeenic activity of difference antineoplastic drugs. Int J Cancer 1996; 65: 506-12.
    • (1996) Int J Cancer , vol.65 , pp. 506-512
    • Preus, I.1    Thust, R.2    Kaina, B.3
  • 16
    • 0025925212 scopus 로고
    • 6-methylguanine-DNA methyltransferase in human normal and tumor tissue from brain, lung, and ovary
    • 6-methylguanine-DNA methyltransferase in human normal and tumor tissue from brain, lung, and ovary. Cancer Res 1991; 51: 4131-4.
    • (1991) Cancer Res , vol.51 , pp. 4131-4134
    • Citron, M.1    Decker, R.2    Chen, S.3
  • 18
    • 0021264521 scopus 로고
    • 6-methylguanine in DNA to inactivation by alkylating agent including chloroethylnitrosoureas
    • 6-methylguanine in DNA to inactivation by alkylating agent including chloroethylnitrosoureas. Cancer Res 1984; 44: 2467-74.
    • (1984) Cancer Res , vol.44 , pp. 2467-2474
    • Scudiero, D.1    Meyer, S.2    Clatterbuck, B.3
  • 19
    • 8944258921 scopus 로고    scopus 로고
    • Targeted disruption of the DNA repair methyltransferase gene renders mice hypersensitive to alkylating agent
    • Tsuzuki T, Sakumi K, Shiraishi A, et al. Targeted disruption of the DNA repair methyltransferase gene renders mice hypersensitive to alkylating agent. Carcinogenesis 1996; 17: 1215-20.
    • (1996) Carcinogenesis , vol.17 , pp. 1215-1220
    • Tsuzuki, T.1    Sakumi, K.2    Shiraishi, A.3
  • 20
    • 13344282752 scopus 로고    scopus 로고
    • Retrospective study of correlation between the DNA repair protein alkyltransferase and survival of brain tumor patients treated with carmustine
    • Belanich M, Pastor M, Randall T, et al. Retrospective study of correlation between the DNA repair protein alkyltransferase and survival of brain tumor patients treated with carmustine. Cancer Res 1996; 56: 783-8.
    • (1996) Cancer Res , vol.56 , pp. 783-788
    • Belanich, M.1    Pastor, M.2    Randall, T.3
  • 21
    • 0030962270 scopus 로고    scopus 로고
    • 6-methylguanine-DNA methyl-transferase associated with resistance to alkylating drugs in a mammalian cell line
    • 6-methylguanine-DNA methyl-transferase associated with resistance to alkylating drugs in a mammalian cell line. J Biol Chem 1997; 272: 13250-4.
    • (1997) J Biol Chem , vol.272 , pp. 13250-13254
    • Tano, K.1    Dunn, W.C.2    Darroudi, F.3
  • 22
    • 0025767132 scopus 로고
    • 6-methylguanine-DNA methyl-transferase in mammalian cells by DNA-damaging treatments
    • 6-methylguanine-DNA methyl-transferase in mammalian cells by DNA-damaging treatments. Mol Cell Biol 1991; 11: 4660-8.
    • (1991) Mol Cell Biol , vol.11 , pp. 4660-4668
    • Fritz, G.1    Tano, K.S.M.2    Kaina, B.3
  • 23
    • 0026493772 scopus 로고
    • 6-methylguanine-DNA methyltransferase mRNA in rat hepatoma cells
    • 6-methylguanine-DNA methyltransferase mRNA in rat hepatoma cells. Biochim Biophys Acta 1992; 1171: 35-40.
    • (1992) Biochim Biophys Acta , vol.1171 , pp. 35-40
    • Fritz, G.1    Kaina, B.2
  • 25
    • 0025924488 scopus 로고
    • 6-benzylguanine analogues on sensitivity of human tumor cells to the cytotoxic effects of alkylating agents
    • 6-benzylguanine analogues on sensitivity of human tumor cells to the cytotoxic effects of alkylating agents. Cancer Res 1991; 51: 3367-72.
    • (1991) Cancer Res , vol.51 , pp. 3367-3372
    • Dolan, M.E.1    Mitchell, R.B.2    Mummert, C.3    Moschel, R.C.4    Pegg, A.E.5
  • 27
    • 0026610238 scopus 로고
    • 6-benzylguanine on the sensitivity of human tumor xenografts to 1,3-bis(2-chloroethyl)-1-nitrosourea and on DNA interstrand cross-link formation
    • 6-benzylguanine on the sensitivity of human tumor xenografts to 1,3-bis(2-chloroethyl)-1-nitrosourea and on DNA interstrand cross-link formation. Cancer Res 1992; 52: 1171-5.
    • (1992) Cancer Res , vol.52 , pp. 1171-1175
    • Mitchell, R.B.1    Moschel, R.C.2    Dolan, M.E.3
  • 28
    • 0027079969 scopus 로고
    • Enhancement of nitrosourea activity in medulloblastoma and glioblastoma multiforme
    • Friedman HS, Dolan ME, Moschel RC, et al. Enhancement of nitrosourea activity in medulloblastoma and glioblastoma multiforme. J Natl Cancer Inst 1992; 84: 1926-31.
    • (1992) J Natl Cancer Inst , vol.84 , pp. 1926-1931
    • Friedman, H.S.1    Dolan, M.E.2    Moschel, R.C.3
  • 29
    • 0027339636 scopus 로고
    • 6-benzylguanine and 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) in a human colon cancer xenograft completely resistant to BCNU alone
    • 6-benzylguanine and 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) in a human colon cancer xenograft completely resistant to BCNU alone. Biochem Pharmacol 1993; 45: 483-91.
    • (1993) Biochem Pharmacol , vol.45 , pp. 483-491
    • Gerson, S.L.1    Zborowska, E.2    Norton, K.3    Gordon, N.H.4    Willson, J.K.V.5
  • 30
    • 0030614374 scopus 로고    scopus 로고
    • 6-benzylguanine enables the specific therapy of nitrosourea-resistant intracranial human glioma xenografts in athymic rats with 1,3-bis(2-chloroethyl)-1-nitrosourea
    • 6-benzylguanine enables the specific therapy of nitrosourea-resistant intracranial human glioma xenografts in athymic rats with 1,3-bis(2-chloroethyl)-1-nitrosourea. Cancer Chemother Pharmacol 1997; 39: 307-16.
    • (1997) Cancer Chemother Pharmacol , vol.39 , pp. 307-316
    • Kurpad, S.N.1    Dolan, M.E.2    McLendon, R.E.3
  • 31
    • 0029657595 scopus 로고    scopus 로고
    • 6-methylguanine-DNA transferase in resistance of human brain tumor cell lines to the clinically relevant methylating agents temozolomide and streptozotocin
    • 6-methylguanine-DNA transferase in resistance of human brain tumor cell lines to the clinically relevant methylating agents temozolomide and streptozotocin. Clin Cancer Res 1996; 2: 735-41.
    • (1996) Clin Cancer Res , vol.2 , pp. 735-741
    • Bobola, M.S.1    Tseng, S.H.2    Blank, A.3    Berger, M.S.4    Silber, J.R.5
  • 32
    • 0028991603 scopus 로고
    • 6-alkylguanine alkyltransferase-directed DNA repair in metastatic colon cancers
    • 6-alkylguanine alkyltransferase-directed DNA repair in metastatic colon cancers. J Clin Oncol 1995; 13: 2301-8.
    • (1995) J Clin Oncol , vol.13 , pp. 2301-2308
    • Willson, J.K.V.1    Haaga, J.R.2    Trey, J.E.3
  • 33
    • 0028173143 scopus 로고
    • 6-benzylguanine and its effectiveness against human brain tumor xenografts when given in polyethylene glycol or cremophor-EL
    • 6-benzylguanine and its effectiveness against human brain tumor xenografts when given in polyethylene glycol or cremophor-EL. Cancer Chemother Pharmacol 1994; 35: 121-6.
    • (1994) Cancer Chemother Pharmacol , vol.35 , pp. 121-126
    • Dolan, M.E.1    Pegg, A.E.2    Moschel, R.C.3
  • 36
    • 0041851154 scopus 로고    scopus 로고
    • 6-fluorobenzylguanines on chloroethylnitrosourea cytotoxicity in tumor cells
    • 6-fluorobenzylguanines on chloroethylnitrosourea cytotoxicity in tumor cells. Life Sci 1996; 58: 303-8.
    • (1996) Life Sci , vol.58 , pp. 303-308
    • Mineura, K.1    Fukuchi, M.2    Kowada, M.3
  • 39
    • 0031558241 scopus 로고    scopus 로고
    • Inhibition of DNA repair as a means of increasing the antitumor activity of DNA reactive agents
    • Dolan ME. Inhibition of DNA repair as a means of increasing the antitumor activity of DNA reactive agents. Adv Drug Deliv Rev 1997; 26: 105-18.
    • (1997) Adv Drug Deliv Rev , vol.26 , pp. 105-118
    • Dolan, M.E.1
  • 41
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase β and XRCC1 protein
    • Kubota Y, Nash RA, Klungland A, et al. Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase β and XRCC1 protein. EMBO J 1996; 15: 6662-70.
    • (1996) EMBO J , vol.15 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3
  • 42
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1)
    • Klungland A, Lindahl T. Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). EMBO J 1997; 16: 3341-8.
    • (1997) EMBO J , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 43
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan HE, Standal R, Slupphaug G. DNA glycosylases in the base excision repair of DNA. Biochem J 1997; 325: 1-16.
    • (1997) Biochem J , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 44
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • Demple B, Harrison L. Repair of oxidative damage to DNA: enzymology and biology. Annu Rev Biochem 1994; 63: 915-48.
    • (1994) Annu Rev Biochem , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 45
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair
    • Matsumoto Y, Kim K. Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair. Science 1995; 269: 699-702.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 46
    • 0029810085 scopus 로고    scopus 로고
    • Characterization of the DNA polymerase requirement of human base excision repair
    • Nealon K, Nichol ID, Kenny MK. Characterization of the DNA polymerase requirement of human base excision repair. Nucleic Acids Res 1996; 24: 3763-70.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3763-3770
    • Nealon, K.1    Nichol, I.D.2    Kenny, M.K.3
  • 47
    • 0030030379 scopus 로고    scopus 로고
    • Requirement of mammalian DNA polymerase-β in base-excision repair
    • Sobol RW, Horton JK, Kühn R, et al. Requirement of mammalian DNA polymerase-β in base-excision repair. Nature 1996; 379: 183-6.
    • (1996) Nature , vol.379 , pp. 183-186
    • Sobol, R.W.1    Horton, J.K.2    Kühn, R.3
  • 48
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway
    • Bennett RAO, Wilson III DM, Wong D, Demple B. Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway. Proc Natl Acad Sci USA 1997; 94: 7166-9.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7166-7169
    • Bennett, R.A.O.1    Wilson III, D.M.2    Wong, D.3    Demple, B.4
  • 49
    • 0029957245 scopus 로고    scopus 로고
    • XRCC1 polypeptide interacts with polymerase β and possibly poly(ADP-ribose) polymerase, and DNA ligase III is a novel molecular 'nick-sensor' in vitro
    • Caldecott KW, Aoufouchi S, Johnson P, Shall S. XRCC1 polypeptide interacts with polymerase β and possibly poly(ADP-ribose) polymerase, and DNA ligase III is a novel molecular 'nick-sensor' in vitro. Nucleic Acids Res 1996; 24: 4387-94.
    • (1996) Nucleic Acids Res , vol.24 , pp. 4387-4394
    • Caldecott, K.W.1    Aoufouchi, S.2    Johnson, P.3    Shall, S.4
  • 50
    • 0030018848 scopus 로고    scopus 로고
    • Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base excision repair complex from bovine testis
    • Prasad R, Singhal RK, Srivastava DK, et al. Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base excision repair complex from bovine testis. J Biol Chem 1996; 271: 16000-7.
    • (1996) J Biol Chem , vol.271 , pp. 16000-16007
    • Prasad, R.1    Singhal, R.K.2    Srivastava, D.K.3
  • 51
    • 0031416756 scopus 로고    scopus 로고
    • Which DNA polymerases are used for DNA-repair in eukaryotes?
    • Wood RD, Shivji MKK. Which DNA polymerases are used for DNA-repair in eukaryotes? Carcinogenesis 1997; 18: 605-10.
    • (1997) Carcinogenesis , vol.18 , pp. 605-610
    • Wood, R.D.1    Shivji, M.K.K.2
  • 52
    • 0027136120 scopus 로고
    • Protection against chloroethylnitrosourea cytotoxicity by eukaryotic 3-methyladenine DNA glycosylase
    • Matijasevic Z, Boosalis M, Mackay W, Samson L, Ludlum DB. Protection against chloroethylnitrosourea cytotoxicity by eukaryotic 3-methyladenine DNA glycosylase. Proc Natl Acad Sci USA 1993; 90: 11855-9.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11855-11859
    • Matijasevic, Z.1    Boosalis, M.2    Mackay, W.3    Samson, L.4    Ludlum, D.B.5
  • 53
    • 0027340166 scopus 로고
    • 3-methyladenine-DNA-glycosylase in human cells exposed to DNA damaging agents
    • 3-methyladenine-DNA-glycosylase in human cells exposed to DNA damaging agents. DNA Cell Biol 1993; 12: 233-41.
    • (1993) DNA Cell Biol , vol.12 , pp. 233-241
    • Lefebvre, P.1    Zak, P.2    Laval, F.3
  • 54
    • 0026465075 scopus 로고
    • Overexpression of human DNA repair protein N-methylpurine-DNA glycosylase results in the increased removal of N-methylpurines in DNA without a concomitant increase in resistance to alleviating agents in Chinese hamster ovary cells
    • Ibeanu G, Hartenstein B, Dunn WC, et al. Overexpression of human DNA repair protein N-methylpurine-DNA glycosylase results in the increased removal of N-methylpurines in DNA without a concomitant increase in resistance to alleviating agents in Chinese hamster ovary cells. Carcinogenesis 1992; 13: 1989-95.
    • (1992) Carcinogenesis , vol.13 , pp. 1989-1995
    • Ibeanu, G.1    Hartenstein, B.2    Dunn, W.C.3
  • 55
    • 0030041960 scopus 로고    scopus 로고
    • Repair-deficient 3-methyladenine DNA glycosylase homozigous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing
    • Engelward BP, Dreslin A, Christensen J, et al. Repair-deficient 3-methyladenine DNA glycosylase homozigous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing. EMBO J 1996; 15: 945-52.
    • (1996) EMBO J , vol.15 , pp. 945-952
    • Engelward, B.P.1    Dreslin, A.2    Christensen, J.3
  • 56
    • 0024591908 scopus 로고
    • Induction of β-polymerase mRNA by DNA-damaging agents in Chinese hamster ovary cells
    • Fornace Jr. AJ, Zmudzka B, Hollander C, Wilson SH. Induction of β-polymerase mRNA by DNA-damaging agents in Chinese hamster ovary cells. Mol Cell Biol 1989; 9: 851-3.
    • (1989) Mol Cell Biol , vol.9 , pp. 851-853
    • Fornace Jr., A.J.1    Zmudzka, B.2    Hollander, C.3    Wilson, S.H.4
  • 57
    • 0028228297 scopus 로고
    • Elevated DNA polymerase α, DNA polymerase β, and topoisomerase II in a melphalan-resistant rhabdomyosarcoma xenographt that is cross-resistant to nitrosoureas and topotecan
    • Friedman HS, Dolan ME, Kaufmann SH, et al. Elevated DNA polymerase α, DNA polymerase β, and topoisomerase II in a melphalan-resistant rhabdomyosarcoma xenographt that is cross-resistant to nitrosoureas and topotecan. Cancer Res 1994; 54: 3487-93.
    • (1994) Cancer Res , vol.54 , pp. 3487-3493
    • Friedman, H.S.1    Dolan, M.E.2    Kaufmann, S.H.3
  • 58
    • 0030583583 scopus 로고    scopus 로고
    • Elevated expression of DNA polymerase β gene in glioma cell lines with acquired resistance to 1-(4-amino-2-methyl-5-pyrimidinyl)methyl-3-(2-chloroethy)-3-nitrosourea
    • Gomi A, Shinoda S, Sakai R, et al. Elevated expression of DNA polymerase β gene in glioma cell lines with acquired resistance to 1-(4-amino-2-methyl-5-pyrimidinyl)methyl-3-(2-chloroethy)-3-nitrosourea. Biochem Biophys Res Commun 1996; 227: 558-63.
    • (1996) Biochem Biophys Res Commun , vol.227 , pp. 558-563
    • Gomi, A.1    Shinoda, S.2    Sakai, R.3
  • 59
    • 0029878327 scopus 로고    scopus 로고
    • Enhancement of melphalan activity by inhibition of DNA polymerase-α and DNA polymerase-β
    • Moynihan K, Elion GB, Ali-Osman F, et al. Enhancement of melphalan activity by inhibition of DNA polymerase-α and DNA polymerase-β. Cancer Chemother Pharmacol 1996; 38: 349-54.
    • (1996) Cancer Chemother Pharmacol , vol.38 , pp. 349-354
    • Moynihan, K.1    Elion, G.B.2    Ali-Osman, F.3
  • 60
    • 0025116511 scopus 로고
    • DNA alkylation by haloethylnitrosoureas: Nature of modifications produced and their enzymatic repair of removal
    • Ludlum DB. DNA alkylation by haloethylnitrosoureas: nature of modifications produced and their enzymatic repair of removal. Mutat Res 1990; 233: 117-26.
    • (1990) Mutat Res , vol.233 , pp. 117-126
    • Ludlum, D.B.1
  • 61
    • 0030787013 scopus 로고    scopus 로고
    • What structural features determine repair enzyme specificity and mechanism in chemically modified DNA?
    • Singer B, Hang B. What structural features determine repair enzyme specificity and mechanism in chemically modified DNA? Chem Res Toxicol 1997; 10: 713-32.
    • (1997) Chem Res Toxicol , vol.10 , pp. 713-732
    • Singer, B.1    Hang, B.2
  • 62
    • 0028804386 scopus 로고
    • A designed inhibitor of base-excision DNA repair
    • Schärer OD, Verdine G. A designed inhibitor of base-excision DNA repair. J Am Chem Soc 1995; 117: 10781-2.
    • (1995) J Am Chem Soc , vol.117 , pp. 10781-10782
    • Schärer, O.D.1    Verdine, G.2
  • 63
    • 0031034761 scopus 로고    scopus 로고
    • Overexpression of DNA polymerase β sensitizes mammalian cells to 2′,3′-deoxycytidine and 3′-azido-3′-deoxythymidine
    • Bouayadi K, Hoffman J-S, Fons P, et al. Overexpression of DNA polymerase β sensitizes mammalian cells to 2′,3′-deoxycytidine and 3′-azido-3′-deoxythymidine. Cancer Res 1997; 57: 110-6.
    • (1997) Cancer Res , vol.57 , pp. 110-116
    • Bouayadi, K.1    Hoffman, J.-S.2    Fons, P.3
  • 64
    • 0029817866 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase β complexed with DNA: Implication for catalytic mechanism, processivity, and fidelity
    • Pelletier H, Sawaya MR, Wolfle W, Wilson SH, Kraut J. Crystal structures of human DNA polymerase β complexed with DNA: implication for catalytic mechanism, processivity, and fidelity. Biochemistry 1996; 35: 12742-61.
    • (1996) Biochemistry , vol.35 , pp. 12742-12761
    • Pelletier, H.1    Sawaya, M.R.2    Wolfle, W.3    Wilson, S.H.4    Kraut, J.5
  • 65
    • 0029922601 scopus 로고    scopus 로고
    • Role of the HAP1 protein in repair of oxidativc DNA damage and regulation of transcription factors
    • Barzilay G, Walker LJ, Rothwell DG, Hickson ID. Role of the HAP1 protein in repair of oxidativc DNA damage and regulation of transcription factors. Br J Cancer 1996; 74: S145-50.
    • (1996) Br J Cancer , vol.74
    • Barzilay, G.1    Walker, L.J.2    Rothwell, D.G.3    Hickson, I.D.4
  • 66
    • 0025296127 scopus 로고
    • Design of molecules which specifically cleave abasic sites in DNA
    • Constant J-F, Fkeyrat A, Demeunynck M, et al. Design of molecules which specifically cleave abasic sites in DNA. Anti-Cancer Drugs Des 1990; 5: 59-62.
    • (1990) Anti-Cancer Drugs des , vol.5 , pp. 59-62
    • Constant, J.-F.1    Fkeyrat, A.2    Demeunynck, M.3
  • 67
    • 0003102140 scopus 로고    scopus 로고
    • Efficient and versatile chemical tools for cleavage of abasic sites in DNA
    • Belmont P, Boudali A, Constant J-F, et al. Efficient and versatile chemical tools for cleavage of abasic sites in DNA. New J Chem 1997; 21: 47-54.
    • (1997) New J Chem , vol.21 , pp. 47-54
    • Belmont, P.1    Boudali, A.2    Constant, J.-F.3
  • 68
    • 0001574268 scopus 로고
    • A new class of artificial nucleases that recognize and cleave a purinic site in DNA with great selectivity and efficiency
    • Fkyerat A, Demeunynck M, Constant J-F, Michon P, Lhomme J. A new class of artificial nucleases that recognize and cleave a purinic site in DNA with great selectivity and efficiency. J Am Chem Soc 1993; 115: 9952-9.
    • (1993) J Am Chem Soc , vol.115 , pp. 9952-9959
    • Fkyerat, A.1    Demeunynck, M.2    Constant, J.-F.3    Michon, P.4    Lhomme, J.5
  • 69
    • 0022627085 scopus 로고
    • Efficient breakage of DNA apurinic sites by indole-amine related 9-amino-ellipticine
    • Malvy C, Prévost P, Gansser C, Viel C, Paoletti C. Efficient breakage of DNA apurinic sites by indole-amine related 9-amino-ellipticine. Chem-Biol Interact 1986; 57: 41-53.
    • (1986) Chem-Biol Interact , vol.57 , pp. 41-53
    • Malvy, C.1    Prévost, P.2    Gansser, C.3    Viel, C.4    Paoletti, C.5
  • 70
    • 0023552139 scopus 로고
    • Structure of the adduct formed between 3-amino-carbazole and the apurinic site oligonucleotide model [Tp(Ap)pT]
    • Vasseur JJ, B. R, Imbach JL, et al. Structure of the adduct formed between 3-amino-carbazole and the apurinic site oligonucleotide model [Tp(Ap)pT]. J Org Chem 1987; 52: 4994-8.
    • (1987) J Org Chem , vol.52 , pp. 4994-4998
    • Vasseur, J.J.1    R., B.2    Imbach, J.L.3
  • 71
    • 0019416108 scopus 로고
    • A tryptophan-containing peptide recognizes and cleaves DNA at apurinic sites
    • Behmoaras T, Toulme JJ, Hélène C. A tryptophan-containing peptide recognizes and cleaves DNA at apurinic sites. Nature 1981; 292: 858-9.
    • (1981) Nature , vol.292 , pp. 858-859
    • Behmoaras, T.1    Toulme, J.J.2    Hélène, C.3
  • 72
    • 0013620838 scopus 로고
    • AP endonuclease: A possible target for a novel tumoricidal compound
    • Freiberg E, Lindahl T, Walker G, organizers. Taos, NM
    • Grafström RH, Sun T, Doleniak D. AP endonuclease: a possible target for a novel tumoricidal compound. In: Freiberg E, Lindahl T, Walker G, organizers. Repair and processing of DNA damage. Taos, NM: 1995; 279.
    • (1995) Repair and Processing of DNA Damage , pp. 279
    • Grafström, R.H.1    Sun, T.2    Doleniak, D.3
  • 73
    • 0027587770 scopus 로고
    • The repair of ionising radiation-induced damage to DNA
    • Price A. The repair of ionising radiation-induced damage to DNA. Cancer Biol 1993; 4: 61-71.
    • (1993) Cancer Biol , vol.4 , pp. 61-71
    • Price, A.1
  • 75
    • 0022634961 scopus 로고
    • Metabolic consequences of DNA damage: DNA damage induces alterations in glucose metabolism by activation of poly(ADP-ribose) polymerase
    • Berger S, Sudar DC, Berger NA. Metabolic consequences of DNA damage: DNA damage induces alterations in glucose metabolism by activation of poly(ADP-ribose) polymerase. Biochem Biophys Res Commun 1986; 134: 227-32.
    • (1986) Biochem Biophys Res Commun , vol.134 , pp. 227-232
    • Berger, S.1    Sudar, D.C.2    Berger, N.A.3
  • 76
    • 0027516022 scopus 로고
    • Poly(ADP-ribosyl)ation, DNA strand breaks, chromatin and cancer
    • Boulikas T. Poly(ADP-ribosyl)ation, DNA strand breaks, chromatin and cancer. Toxicol Lett 1993; 67: 129-50.
    • (1993) Toxicol Lett , vol.67 , pp. 129-150
    • Boulikas, T.1
  • 77
    • 0029099358 scopus 로고
    • Involvment of NAD-poly-(ADP-ribose) metabolism in p5.3 regulation and its consequences
    • Whitacre CM, Hashimoto H, Tsai M-L, et al. Involvment of NAD-poly-(ADP-ribose) metabolism in p5.3 regulation and its consequences. Cancer Res 1995; 55: 3697-701.
    • (1995) Cancer Res , vol.55 , pp. 3697-3701
    • Whitacre, C.M.1    Hashimoto, H.2    Tsai, M.-L.3
  • 78
    • 0031007707 scopus 로고    scopus 로고
    • TFIIF, a basal eukaryotic transcription factor, is a substrate for poly(ADP-ribosyl)ation
    • Rawling JM, Alvarez-Gonzalez R. TFIIF, a basal eukaryotic transcription factor, is a substrate for poly(ADP-ribosyl)ation. Biochem J 1997; 324: 249-53.
    • (1997) Biochem J , vol.324 , pp. 249-253
    • Rawling, J.M.1    Alvarez-Gonzalez, R.2
  • 79
    • 0025940008 scopus 로고
    • DNA damage, poly(ADP-rybosyl)ation and apoptotic cell death as a potential common pathway of cytotoxic drug action
    • Marks DI, Fox RM. DNA damage, poly(ADP-rybosyl)ation and apoptotic cell death as a potential common pathway of cytotoxic drug action. Biochem Pharmacol 1991; 42: 1859-67.
    • (1991) Biochem Pharmacol , vol.42 , pp. 1859-1867
    • Marks, D.I.1    Fox, R.M.2
  • 80
    • 0030600536 scopus 로고    scopus 로고
    • Different cleavage pattern for poly(ADP-ribose) polymerase during necrosis and apoptosis in HL-60 cells
    • Shah GM, Shah RG, Poirier GG. Different cleavage pattern for poly(ADP-ribose) polymerase during necrosis and apoptosis in HL-60 cells. Biochem Biophys Res Comm 1996; 229: 838-44.
    • (1996) Biochem Biophys Res Comm , vol.229 , pp. 838-844
    • Shah, G.M.1    Shah, R.G.2    Poirier, G.G.3
  • 82
    • 0025091722 scopus 로고
    • Illegitimate and homologous recombination in mammalian cells: Differential sensitivity to an inhibitor of poly(ADP-ribosylation)
    • Waldman BC, Waldman AS. Illegitimate and homologous recombination in mammalian cells: differential sensitivity to an inhibitor of poly(ADP-ribosylation). Nucleic Acids Res 1990; 18: 5981-8.
    • (1990) Nucleic Acids Res , vol.18 , pp. 5981-5988
    • Waldman, B.C.1    Waldman, A.S.2
  • 83
    • 0025969111 scopus 로고
    • Poly(ADP-ribose)polymerase: A perplexing participant in cellular responses to DNA breakage
    • Cleaver JE, Morgan WF. Poly(ADP-ribose)polymerase: a perplexing participant in cellular responses to DNA breakage Mutat Res 1991; 257: 1-18.
    • (1991) Mutat Res , vol.257 , pp. 1-18
    • Cleaver, J.E.1    Morgan, W.F.2
  • 84
    • 0028922462 scopus 로고
    • Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease
    • Wang Z-Q, Auer B, Stingl L, et al. Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease. Gene Dev 1995; 9: 509-20.
    • (1995) Gene Dev , vol.9 , pp. 509-520
    • Wang, Z.-Q.1    Auer, B.2    Stingl, L.3
  • 85
    • 0040984333 scopus 로고    scopus 로고
    • Requirement of poly(ADP-ribose) polymerase in recovery from DNA damage in mice and in cells
    • Ménissier-de Murcia J, Niedergang C, Trucco C, et al. Requirement of poly(ADP-ribose) polymerase in recovery from DNA damage in mice and in cells. Proc Natl Acad Sci USA 1997; 94: 7303-7.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7303-7307
    • Ménissier-de Murcia, J.1    Niedergang, C.2    Trucco, C.3
  • 86
    • 0030996538 scopus 로고    scopus 로고
    • Interaction of DNA-dependent protein kinase and poly(ADP-ribose) polymerase with radiation-induced DNA strand breaks
    • Weinfeld M, Chaudhry MA, D'Amours D, et al. Interaction of DNA-dependent protein kinase and poly(ADP-ribose) polymerase with radiation-induced DNA strand breaks. Radiat Res 1997; 148: 22-8.
    • (1997) Radiat Res , vol.148 , pp. 22-28
    • Weinfeld, M.1    Chaudhry, M.A.2    D'Amours, D.3
  • 88
    • 0025696390 scopus 로고
    • Hypersensitivity to clinicay useful alkylating agents and radiation in poly(ADP-ribose) polymerase-deficient cell lines
    • Chatterjee S, Cheng MF, Berger NA. Hypersensitivity to clinicay useful alkylating agents and radiation in poly(ADP-ribose) polymerase-deficient cell lines. Cancer Commun 1990; 2: 401-7.
    • (1990) Cancer Commun , vol.2 , pp. 401-407
    • Chatterjee, S.1    Cheng, M.F.2    Berger, N.A.3
  • 89
    • 0025796784 scopus 로고
    • Alkylating agent hypersensitivity in poly(adenosine diphosphate-ribose) polymerase deficient cell lines
    • Chatterjee S, Cheng MF, Berger SJ, Berger NA. Alkylating agent hypersensitivity in poly(adenosine diphosphate-ribose) polymerase deficient cell lines. Cancer Commun 1991; 3: 71-5.
    • (1991) Cancer Commun , vol.3 , pp. 71-75
    • Chatterjee, S.1    Cheng, M.F.2    Berger, S.J.3    Berger, N.A.4
  • 90
    • 0025137179 scopus 로고
    • Expression of poly (ADP-ribose) polymerase gene following natural and induced DNA strand breakage and effect of hyperexpression on DNA repair
    • Bhatia K, Pommier Y, Giri C, et al. Expression of poly (ADP-ribose) polymerase gene following natural and induced DNA strand breakage and effect of hyperexpression on DNA repair. Carcinogenesis 1990; 11: 123-8.
    • (1990) Carcinogenesis , vol.11 , pp. 123-128
    • Bhatia, K.1    Pommier, Y.2    Giri, C.3
  • 91
    • 0024788011 scopus 로고
    • High induction of poly(ADP-ribose) polymerase activity in bleomycin-resistant HeLa cells
    • Urade M, Sugi M, Mima T, Ogura T, Matsuya T. High induction of poly(ADP-ribose) polymerase activity in bleomycin-resistant HeLa cells. Jpn J Cancer Res 1989; 80: 464-8.
    • (1989) Jpn J Cancer Res , vol.80 , pp. 464-468
    • Urade, M.1    Sugi, M.2    Mima, T.3    Ogura, T.4    Matsuya, T.5
  • 92
    • 0028029995 scopus 로고
    • Increased poly(ADP-ribose) formation in cisplatin-resistant rat ovarian tumor cells
    • Chen G, Zeller WJ. Increased poly(ADP-ribose) formation in cisplatin-resistant rat ovarian tumor cells. Anticancer Res 1994; 14: 1462-8.
    • (1994) Anticancer Res , vol.14 , pp. 1462-1468
    • Chen, G.1    Zeller, W.J.2
  • 93
    • 0031417427 scopus 로고    scopus 로고
    • Functional overexpression of human poly(ADP-ribose) polymerase in transfected rat tumor cells
    • Bernges F, Bürkle A, Küpper J-H, Zeller WJ. Functional overexpression of human poly(ADP-ribose) polymerase in transfected rat tumor cells. Carcinogenesis 1997; 18: 663-8.
    • (1997) Carcinogenesis , vol.18 , pp. 663-668
    • Bernges, F.1    Bürkle, A.2    Küpper, J.-H.3    Zeller, W.J.4
  • 94
    • 0344418424 scopus 로고    scopus 로고
    • Overexpression of human poly(ADP-ribose) polymerase in transfected hamster cells to increased poly(ADP-ribosyl)ation and cellular sensitization to γ irradiation
    • van Gool L, Meyer R, Tobiasch E, et al. Overexpression of human poly(ADP-ribose) polymerase in transfected hamster cells to increased poly(ADP-ribosyl)ation and cellular sensitization to γ irradiation. Eur J Biochem 1997; 244: 15-20.
    • (1997) Eur J Biochem , vol.244 , pp. 15-20
    • Van Gool, L.1    Meyer, R.2    Tobiasch, E.3
  • 95
    • 0029929225 scopus 로고    scopus 로고
    • Trans-dominant inhibition of poly(ADP-ribosyl)ation potentiates carcinogen-induced gene amplification in SV40-transformed Chinese hamster cells
    • Küpper J-H, Müller M, Bürkle A. Trans-dominant inhibition of poly(ADP-ribosyl)ation potentiates carcinogen-induced gene amplification in SV40-transformed Chinese hamster cells. Cancer Res 1996; 56: 2715-7.
    • (1996) Cancer Res , vol.56 , pp. 2715-2717
    • Küpper, J.-H.1    Müller, M.2    Bürkle, A.3
  • 96
    • 0025793533 scopus 로고
    • Inhibition of poly(adenosine diphosphate-ribose) polymerase by thymidine and thymidine analogues in L1210 cells and its relationship to the potentiation of the antitumor activity of 1,3-bis(2-chloroethyl)-1-nitrosourea but not of 3′-[3-(2-chloroethyl)-3-nitrosoureido]-3′-deoxythymidine
    • August ME, Cooper DL, Prusoff WH. Inhibition of poly(adenosine diphosphate-ribose) polymerase by thymidine and thymidine analogues in L1210 cells and its relationship to the potentiation of the antitumor activity of 1,3-bis(2-chloroethyl)-1-nitrosourea but not of 3′-[3-(2-chloroethyl)-3-nitrosoureido]-3′-deoxythymidine. Cancer Res 1991; 51: 1586-90.
    • (1991) Cancer Res , vol.51 , pp. 1586-1590
    • August, M.E.1    Cooper, D.L.2    Prusoff, W.H.3
  • 97
    • 0026601666 scopus 로고
    • Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase
    • Banasik M, Komura H, Shimoyama M, Ueda K. Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase. J Biol Chem 1992; 267: 1569-75.
    • (1992) J Biol Chem , vol.267 , pp. 1569-1575
    • Banasik, M.1    Komura, H.2    Shimoyama, M.3    Ueda, K.4
  • 98
    • 0029123236 scopus 로고
    • Nicotinamide and other benzamide analogs as agents for overcoming hypoxic cell radiation resistance in tumors
    • Horsman MR. Nicotinamide and other benzamide analogs as agents for overcoming hypoxic cell radiation resistance in tumors. Acta Oncol 1995; 34: 571-87.
    • (1995) Acta Oncol , vol.34 , pp. 571-587
    • Horsman, M.R.1
  • 99
    • 0028793846 scopus 로고
    • Novel potent inhibitors of the DNA repair enzyme poly(ADP-ribose)-polymerase (PARP)
    • Griffin RJ, Pemberton LC, Rhodes D, et al. Novel potent inhibitors of the DNA repair enzyme poly(ADP-ribose)-polymerase (PARP). Anti-Cancer Drug Des 1995; 10: 507-14.
    • (1995) Anti-Cancer Drug des , vol.10 , pp. 507-514
    • Griffin, R.J.1    Pemberton, L.C.2    Rhodes, D.3
  • 100
    • 0029845902 scopus 로고    scopus 로고
    • The nicotinamide dinucleotide binding motif: A comparison of nucleotide binding proteins
    • Bellamacina CR. The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins. FASEB J 1996; 10: 1257-69.
    • (1996) FASEB J , vol.10 , pp. 1257-1269
    • Bellamacina, C.R.1
  • 101
    • 0029080684 scopus 로고
    • The role of inhibitors of poly(ADP-ribose) polymerase as resistance-modifying agents in cancer therapy
    • Griffin RJ, Curtin NJ, Newell DR, et al. The role of inhibitors of poly(ADP-ribose) polymerase as resistance-modifying agents in cancer therapy. Biochimie 1995; 77: 408-22.
    • (1995) Biochimie , vol.77 , pp. 408-422
    • Griffin, R.J.1    Curtin, N.J.2    Newell, D.R.3
  • 102
    • 0030611436 scopus 로고    scopus 로고
    • 6-alkylguanine DNA-alkyltransferase or poly(ADP-ribose) polymerase increases susceptibility of leukemic cells to apoptosis induced by temozolomide
    • 6-alkylguanine DNA-alkyltransferase or poly(ADP-ribose) polymerase increases susceptibility of leukemic cells to apoptosis induced by temozolomide. Mol Pharmacol 1997; 52: 249-58.
    • (1997) Mol Pharmacol , vol.52 , pp. 249-258
    • Tentori, L.1    Orlando, L.2    Lacal, P.M.3
  • 103
    • 0026642041 scopus 로고
    • Depletion of poly(ADP-ribose) polymerase by antisens RNA expression results in a delay in DNA strand break rejoining
    • Ding R, Pommier Y, Kang VH, Smulson M. Depletion of poly(ADP-ribose) polymerase by antisens RNA expression results in a delay in DNA strand break rejoining. J Biol Chem 1992; 267: 12804-12.
    • (1992) J Biol Chem , vol.267 , pp. 12804-12812
    • Ding, R.1    Pommier, Y.2    Kang, V.H.3    Smulson, M.4
  • 104
    • 0030016534 scopus 로고    scopus 로고
    • DNA damage and repair in tumor and non-tumor tissues of mice induced by nicotinamide
    • Olsson AR, Sheng Y, Pero RW, Chaplin DJ, Horsman MR. DNA damage and repair in tumor and non-tumor tissues of mice induced by nicotinamide. Br J Cancer 1996; 74: 368-73.
    • (1996) Br J Cancer , vol.74 , pp. 368-373
    • Olsson, A.R.1    Sheng, Y.2    Pero, R.W.3    Chaplin, D.J.4    Horsman, M.R.5
  • 105
    • 0029892790 scopus 로고    scopus 로고
    • DNA excision repair
    • Sancar A. DNA excision repair. Annu Rev Biochem 1996; 65: 43-81.
    • (1996) Annu Rev Biochem , vol.65 , pp. 43-81
    • Sancar, A.1
  • 107
    • 0027473181 scopus 로고
    • Mutant rodent cell lines sensitive to ultraviolet light, ionizing radiation and cross-linking agents: A comprehensive survey of genetic and bio chemical characteristics
    • Collins AR. Mutant rodent cell lines sensitive to ultraviolet light, ionizing radiation and cross-linking agents: a comprehensive survey of genetic and bio chemical characteristics. Mutat Res 1993; 293: 99-118.
    • (1993) Mutat Res , vol.293 , pp. 99-118
    • Collins, A.R.1
  • 108
    • 0029654297 scopus 로고
    • Protein that participate in nucleotide excision repair of DNA in mammalian cells
    • Wood RD. Protein that participate in nucleotide excision repair of DNA in mammalian cells. Phil Trans R Soc 1995; 347: 69-74.
    • (1995) Phil Trans R Soc , vol.347 , pp. 69-74
    • Wood, R.D.1
  • 109
    • 0028009789 scopus 로고
    • Cellular responses to cisplatin. The role of DNA-binding proteins and DNA repair
    • Chu G. Cellular responses to cisplatin. The role of DNA-binding proteins and DNA repair. J Biol Chem 1994; 269: 787-90.
    • (1994) J Biol Chem , vol.269 , pp. 787-790
    • Chu, G.1
  • 110
    • 0030013201 scopus 로고    scopus 로고
    • Relationships between DNA repair and transcription
    • Friedberg EC. Relationships between DNA repair and transcription. Annu Rev Biochem 1996; 65: 15-42.
    • (1996) Annu Rev Biochem , vol.65 , pp. 15-42
    • Friedberg, E.C.1
  • 111
    • 0028018885 scopus 로고
    • Role of the human ERCC-1 gene in gene-specific repair of cisplatin-induced DNA damage
    • Larminat F, Bohr VA. Role of the human ERCC-1 gene in gene-specific repair of cisplatin-induced DNA damage. Nucleic Acids Res 1994; 22: 3005-10.
    • (1994) Nucleic Acids Res , vol.22 , pp. 3005-3010
    • Larminat, F.1    Bohr, V.A.2
  • 112
    • 0029843707 scopus 로고    scopus 로고
    • Mutational analysis of the human nucleotide excision repair gene ERCC1
    • Sijbergs AM, van der Spek PJ, Odijk H, et al. Mutational analysis of the human nucleotide excision repair gene ERCC1. Nucleic Acids Res 1996; 24: 3370-80.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3370-3380
    • Sijbergs, A.M.1    Van Der Spek, P.J.2    Odijk, H.3
  • 113
    • 0027457743 scopus 로고
    • DNA excision-repair synthesis is enhanced in a murine leukemia L1210 cell line resistant to cisplatin
    • Calsou P, Barret J-M, Cros S, Salles B. DNA excision-repair synthesis is enhanced in a murine leukemia L1210 cell line resistant to cisplatin. Eur J Biochem 1993; 211: 403-9.
    • (1993) Eur J Biochem , vol.211 , pp. 403-409
    • Calsou, P.1    Barret, J.-M.2    Cros, S.3    Salles, B.4
  • 114
    • 0028818122 scopus 로고
    • Elevated DNA repair capacity is associated with intrinsic resistance of lung cancer chemotherapy
    • Zeng-Rong N, Paterson J, Alpert L, et al. Elevated DNA repair capacity is associated with intrinsic resistance of lung cancer chemotherapy. Cancer Res 1995; 55: 4760-4.
    • (1995) Cancer Res , vol.55 , pp. 4760-4764
    • Zeng-Rong, N.1    Paterson, J.2    Alpert, L.3
  • 115
    • 0028861087 scopus 로고
    • Enhanced host cell reactivation capacity and expression of DNA repair genes in human breast cancer cells resistant to bifunctional alkylating agents
    • Yen L, Woo A, Christopoulopoulos G, et al. Enhanced host cell reactivation capacity and expression of DNA repair genes in human breast cancer cells resistant to bifunctional alkylating agents. Mutat Res 1995; 337: 179-89.
    • (1995) Mutat Res , vol.337 , pp. 179-189
    • Yen, L.1    Woo, A.2    Christopoulopoulos, G.3
  • 116
    • 0029656117 scopus 로고    scopus 로고
    • Repair analysis of 4-hydroperoxycyclophosphamide-induced DNA interstrand crosslinking in the c-myc gene in 4-hydroperoxycyclophosphamide-sensitive and -resistant medullo blastoma cell lines
    • Dong Q, Bullock N, Ali-Osman F, et al. Repair analysis of 4-hydroperoxycyclophosphamide-induced DNA interstrand crosslinking in the c-myc gene in 4-hydroperoxycyclophosphamide-sensitive and -resistant medullo blastoma cell lines. Cancer Chemother Pharmacol 1996; 37: 242-6.
    • (1996) Cancer Chemother Pharmacol , vol.37 , pp. 242-246
    • Dong, Q.1    Bullock, N.2    Ali-Osman, F.3
  • 117
    • 0028141961 scopus 로고
    • Messenger RNA levels of XPAC and ERCC1 in ovarian cancer tissue correlate with response to platinum-based chemotherapy
    • Dabholkar M, Vionnet J, Bostickbruton F, Yu JJ, Reed E. Messenger RNA levels of XPAC and ERCC1 in ovarian cancer tissue correlate with response to platinum-based chemotherapy. J Clin Invest 1994; 94: 703-8.
    • (1994) J Clin Invest , vol.94 , pp. 703-708
    • Dabholkar, M.1    Vionnet, J.2    Bostickbruton, F.3    Yu, J.J.4    Reed, E.5
  • 118
    • 0030606304 scopus 로고    scopus 로고
    • Enhanced XPA mRNA levels in cisplatin-resistant human ovarian cancer are not associated with XPA mutations or gene amplification
    • States JC, Reed E. Enhanced XPA mRNA levels in cisplatin-resistant human ovarian cancer are not associated with XPA mutations or gene amplification. Cancer Lett 1996; 108: 233-7.
    • (1996) Cancer Lett , vol.108 , pp. 233-237
    • States, J.C.1    Reed, E.2
  • 119
    • 0027372625 scopus 로고
    • Cisplatin sensitivity/resistance in UV repair-deficient Chinese hamster ovary cells of complementation groups 1 and 3
    • Lee KB, Parker RJ, Bohr V, Cornelison T, Reed E. Cisplatin sensitivity/resistance in UV repair-deficient Chinese hamster ovary cells of complementation groups 1 and 3. Carcinogenesis 1993; 14: 2177-80.
    • (1993) Carcinogenesis , vol.14 , pp. 2177-2180
    • Lee, K.B.1    Parker, R.J.2    Bohr, V.3    Cornelison, T.4    Reed, E.5
  • 120
    • 0029773392 scopus 로고    scopus 로고
    • Nucleotide excision repair genes as determinants of cellular sensitivity to cyclophosphamide analogs
    • Anderson BS, Sadeghi T, Siciliano MJ, Legerski R, Murray D. Nucleotide excision repair genes as determinants of cellular sensitivity to cyclophosphamide analogs. Cancer Chemother Pharmacol 1996; 38: 406-16.
    • (1996) Cancer Chemother Pharmacol , vol.38 , pp. 406-416
    • Anderson, B.S.1    Sadeghi, T.2    Siciliano, M.J.3    Legerski, R.4    Murray, D.5
  • 121
    • 0029890253 scopus 로고    scopus 로고
    • Sensitivity of CHO mutant cell lines with specific defects in nucleotides excision repair to different anti-cancer agents
    • Damia G, Imperatori L, Stefanini M, D'Incalci M. Sensitivity of CHO mutant cell lines with specific defects in nucleotides excision repair to different anti-cancer agents. Int J Cancer 1996; 66: 779-83.
    • (1996) Int J Cancer , vol.66 , pp. 779-783
    • Damia, G.1    Imperatori, L.2    Stefanini, M.3    D'Incalci, M.4
  • 122
    • 0026648940 scopus 로고
    • ERCC1 and ERCC2 expression in malignant tissues from ovarian cancer patients
    • Dabholkar M, Bostick-Bruton F, Weber C, et al. ERCC1 and ERCC2 expression in malignant tissues from ovarian cancer patients. J Natl Cancer Res 1992; 84: 1512-7.
    • (1992) J Natl Cancer Res , vol.84 , pp. 1512-1517
    • Dabholkar, M.1    Bostick-Bruton, F.2    Weber, C.3
  • 123
    • 0026793818 scopus 로고
    • Effect of topoisomerase poisoning by antitumor drugs VM 26, fostriecin and camptothecin on DNA repair replication by mammalian cell extracts
    • Frosina G, Rossi O. Effect of topoisomerase poisoning by antitumor drugs VM 26, fostriecin and camptothecin on DNA repair replication by mammalian cell extracts. Carcinogenesis 1992; 13: 1371-7.
    • (1992) Carcinogenesis , vol.13 , pp. 1371-1377
    • Frosina, G.1    Rossi, O.2
  • 124
    • 0027333102 scopus 로고
    • Various inhibitors of topoisomerases diminish repair-specific DNA incision in UV-irradiated human fibroblasts
    • Thielmann HW, Popanda O, Gersbach H, Gilberg F. Various inhibitors of topoisomerases diminish repair-specific DNA incision in UV-irradiated human fibroblasts. Carcinogenesis 1993; 14: 2341-51.
    • (1993) Carcinogenesis , vol.14 , pp. 2341-2351
    • Thielmann, H.W.1    Popanda, O.2    Gersbach, H.3    Gilberg, F.4
  • 125
    • 0027993984 scopus 로고
    • A cisplatin-resistant murine leukemia cell line exhibits increased topoisomerase II activity
    • Barret J-M, Calsou P, Kragh Larsen A, Salles B. A cisplatin-resistant murine leukemia cell line exhibits increased topoisomerase II activity. Mol Pharmacol 1994; 46: 431-6.
    • (1994) Mol Pharmacol , vol.46 , pp. 431-436
    • Barret, J.-M.1    Calsou, P.2    Kragh Larsen, A.3    Salles, B.4
  • 126
    • 0031409892 scopus 로고    scopus 로고
    • Evaluation of DNA repair inhibition by antitumor or antibiotic drugs using a chemiluminescence microplate assay
    • in press
    • Barret J-M, Salles B, Provot C, Hill B. Evaluation of DNA repair inhibition by antitumor or antibiotic drugs using a chemiluminescence microplate assay. Carcinogenesis 1997; in press.
    • (1997) Carcinogenesis
    • Barret, J.-M.1    Salles, B.2    Provot, C.3    Hill, B.4
  • 127
    • 0027080829 scopus 로고
    • Helicase inhibition by anthracycline anticancer agents
    • Bachur NR, Yu F, Johnson R, et al. Helicase inhibition by anthracycline anticancer agents. Mol Pharmacol 1992; 41: 993-8.
    • (1992) Mol Pharmacol , vol.41 , pp. 993-998
    • Bachur, N.R.1    Yu, F.2    Johnson, R.3
  • 128
    • 0027490845 scopus 로고
    • Antihelicase action of DNA-binding anticancer agents: Relationship to guanosine-cytidine intercalator binding
    • Bachur NR, Johnson R, Yu F, et al. Antihelicase action of DNA-binding anticancer agents: relationship to guanosine-cytidine intercalator binding. Mol Pharmacol 1993; 44: 1064-9.
    • (1993) Mol Pharmacol , vol.44 , pp. 1064-1069
    • Bachur, N.R.1    Johnson, R.2    Yu, F.3
  • 129
    • 0030970983 scopus 로고    scopus 로고
    • Cytotoxicity synergy between pyrazoloacridine (NSC 366140) and cisplatin in vitro: Inhibition of platinum-DNA adduct removal
    • Adjei AA, Budihardjo II, Rowinsky EK, et al. Cytotoxicity synergy between pyrazoloacridine (NSC 366140) and cisplatin in vitro: inhibition of platinum-DNA adduct removal. Clin Cancer Res 1997; 3: 761-70.
    • (1997) Clin Cancer Res , vol.3 , pp. 761-770
    • Adjei, A.A.1    Budihardjo, I.I.2    Rowinsky, E.K.3
  • 130
    • 0029983352 scopus 로고    scopus 로고
    • DNA repair activity in protein extracts of fresh human malignant lymphoid cells
    • Barret J-M, Calsou P, Laurent G, Salles B. DNA repair activity in protein extracts of fresh human malignant lymphoid cells. Mol Pharmacol 1996; 49: 766-71.
    • (1996) Mol Pharmacol , vol.49 , pp. 766-771
    • Barret, J.-M.1    Calsou, P.2    Laurent, G.3    Salles, B.4
  • 131
    • 0023723764 scopus 로고
    • Anticarcinogenic of DNA-repair modulators
    • Boothman DA, Schlegel R, Pardee AB. Anticarcinogenic of DNA-repair modulators. Mutat Res 1988; 202: 393-411.
    • (1988) Mutat Res , vol.202 , pp. 393-411
    • Boothman, D.A.1    Schlegel, R.2    Pardee, A.B.3
  • 132
    • 0026722362 scopus 로고
    • Activity of aphidicolin glycinate alone and in combination with cisplatin in a murine ovarian tumor resistant to cisplatin
    • Damia G, Tagliabue G, Zucchetti M, et al. Activity of aphidicolin glycinate alone and in combination with cisplatin in a murine ovarian tumor resistant to cisplatin. Cancer Chemother Pharmacol 1992; 30: 459-64.
    • (1992) Cancer Chemother Pharmacol , vol.30 , pp. 459-464
    • Damia, G.1    Tagliabue, G.2    Zucchetti, M.3
  • 133
    • 0027958095 scopus 로고
    • Antitumor activity and biochemical effects of aphidicolin glycinate (NSC 303812) alone and in combination with cisplatin in vivo
    • O'Dwyers PJ, Moyer JD, Suffhess M, et al. Antitumor activity and biochemical effects of aphidicolin glycinate (NSC 303812) alone and in combination with cisplatin in vivo. Cancer Res 1994; 54: 724-9.
    • (1994) Cancer Res , vol.54 , pp. 724-729
    • O'Dwyers, P.J.1    Moyer, J.D.2    Suffhess, M.3
  • 134
    • 0029044763 scopus 로고
    • Potentiation of chlorambucil toxicity in B-CLL lymphocytes using the DNA synthesis inhibitors aphidicolin and 1-β-D-arabinofuranosylcytosine
    • Bramson J, Panasci L. Potentiation of chlorambucil toxicity in B-CLL lymphocytes using the DNA synthesis inhibitors aphidicolin and 1-β-D-arabinofuranosylcytosine. Biochem Pharmacol 1995; 50: 131-5.
    • (1995) Biochem Pharmacol , vol.50 , pp. 131-135
    • Bramson, J.1    Panasci, L.2
  • 135
    • 0029851151 scopus 로고    scopus 로고
    • Aphidicolin markedly increases the platinum sensitivity of cells from primary ovarian tumors
    • Sargent JM, Elgie AW, Williamson CJ, Taylor CG. Aphidicolin markedly increases the platinum sensitivity of cells from primary ovarian tumors. Br J Cancer 1996; 74: 1730-3.
    • (1996) Br J Cancer , vol.74 , pp. 1730-1733
    • Sargent, J.M.1    Elgie, A.W.2    Williamson, C.J.3    Taylor, C.G.4
  • 136
    • 0027244921 scopus 로고
    • Inhibition of DNA repair in cells treated with a combination of alkylating agents
    • Frankfurt OS, Seckinger D, Sugarbaker EV. Inhibition of DNA repair in cells treated with a combination of alkylating agents. Anticancer Res 1993; 13: 947-52.
    • (1993) Anticancer Res , vol.13 , pp. 947-952
    • Frankfurt, O.S.1    Seckinger, D.2    Sugarbaker, E.V.3
  • 137
    • 0029875635 scopus 로고    scopus 로고
    • Synergistic interaction between gemcitabine and cisplatin in vitro
    • Bergman AM, Ruiz van Haperen VWT, Veerman G. Synergistic interaction between gemcitabine and cisplatin in vitro. Clin Cancer Res 1996; 2: 521-30.
    • (1996) Clin Cancer Res , vol.2 , pp. 521-530
    • Bergman, A.M.1    Ruiz Van Haperen, V.W.T.2    Veerman, G.3
  • 138
    • 0029808528 scopus 로고    scopus 로고
    • Preclinical combination therapy with gemcitabine and mechanisms of resistance
    • Peters GJ, Ruiz van Haperen VWT, Bergman AM, et al. Preclinical combination therapy with gemcitabine and mechanisms of resistance. Semin Oncol 1996; 23: 16-24.
    • (1996) Semin Oncol , vol.23 , pp. 16-24
    • Peters, G.J.1    Ruiz Van Haperen, V.W.T.2    Bergman, A.M.3
  • 139
    • 0029859821 scopus 로고    scopus 로고
    • Fludarabine-mediated inhibition of nucleotide excision repair induces apoptosis in quiescent human lyphocytes
    • Sandoval A, Consoli U, Plunkett W. Fludarabine-mediated inhibition of nucleotide excision repair induces apoptosis in quiescent human lyphocytes. Clin Cancer Res 1996; 2: 1731-41.
    • (1996) Clin Cancer Res , vol.2 , pp. 1731-1741
    • Sandoval, A.1    Consoli, U.2    Plunkett, W.3
  • 140
    • 0030921076 scopus 로고    scopus 로고
    • Differential incorporation of ara-C, gemcitabine, and fludarabine into replicating and repairing DNA in proliferating human leukemia cells
    • Iwasaki H, Huang P, Keating MJ, Plunkett W. Differential incorporation of ara-C, gemcitabine, and fludarabine into replicating and repairing DNA in proliferating human leukemia cells. Blood 1997; 90: 270-8.
    • (1997) Blood , vol.90 , pp. 270-278
    • Iwasaki, H.1    Huang, P.2    Keating, M.J.3    Plunkett, W.4
  • 141
    • 17344384670 scopus 로고    scopus 로고
    • Cisplatin-gemcitabine combination in advanced non-small-cell lung cancer: A phase II study
    • Crinò L, Scagliotti G, Marangolo M, et al. Cisplatin-gemcitabine combination in advanced non-small-cell lung cancer: a phase II study. J Clin Oncol 1997; 15: 297-303.
    • (1997) J Clin Oncol , vol.15 , pp. 297-303
    • Crinò, L.1    Scagliotti, G.2    Marangolo, M.3
  • 142
    • 0029563680 scopus 로고
    • In vitro eukaryotic DNA excision repair assays: An overview
    • Salles B, Frit P, Provot C, Jaeg J-P, Calsou P. In vitro eukaryotic DNA excision repair assays: An overview. Biochimie 1995; 77: 796-802.
    • (1995) Biochimie , vol.77 , pp. 796-802
    • Salles, B.1    Frit, P.2    Provot, C.3    Jaeg, J.-P.4    Calsou, P.5
  • 143
    • 0028879965 scopus 로고
    • Homologous recombination and the roles of double-strand breaks
    • Shinohara A, Ogawa T. Homologous recombination and the roles of double-strand breaks. Trends Biochem Sci 1995; 20: 387-91.
    • (1995) Trends Biochem Sci , vol.20 , pp. 387-391
    • Shinohara, A.1    Ogawa, T.2
  • 144
    • 0028960865 scopus 로고
    • Mammalian mutants defective in the response to ionizing radiation-induced DNA damage
    • Zdzienicka MZ. Mammalian mutants defective in the response to ionizing radiation-induced DNA damage. Mutat Res DNA Repair 1995; 336: 203-13
    • (1995) Mutat Res DNA Repair , vol.336 , pp. 203-213
    • Zdzienicka, M.Z.1
  • 145
    • 0030922250 scopus 로고    scopus 로고
    • DNP-PK: At the cross-roads of biochemistry and genetics
    • Jeggo PA. DNP-PK: at the cross-roads of biochemistry and genetics. Mutat Res 1997; 384: 1-14.
    • (1997) Mutat Res , vol.384 , pp. 1-14
    • Jeggo, P.A.1
  • 146
    • 0030339852 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase, DNA-PK: 10 years and no ends in sight
    • Lees-Miller SP. The DNA-dependent protein kinase, DNA-PK: 10 years and no ends in sight. Biochem Cell Biol 1996; 74: 503-12.
    • (1996) Biochem Cell Biol , vol.74 , pp. 503-512
    • Lees-Miller, S.P.1
  • 147
    • 0030907318 scopus 로고    scopus 로고
    • Ku proteins join DNA fragments as shown by atomic force microscopy
    • Pang D, Yoo S, Dynan S, Jung M, Dritschilo A. Ku proteins join DNA fragments as shown by atomic force microscopy. Cancer Res 1997; 57: 1412-5.
    • (1997) Cancer Res , vol.57 , pp. 1412-1415
    • Pang, D.1    Yoo, S.2    Dynan, S.3    Jung, M.4    Dritschilo, A.5
  • 148
    • 0028116725 scopus 로고
    • Human DNA helicase II: Novel DNA unwinding enzyme identified as the Ku autoantigen
    • Tuteja N, Tuteja R, Ochem A, et al. Human DNA helicase II: novel DNA unwinding enzyme identified as the Ku autoantigen. EMBO J 1994; 13: 4991-5001.
    • (1994) EMBO J , vol.13 , pp. 4991-5001
    • Tuteja, N.1    Tuteja, R.2    Ochem, A.3
  • 149
    • 0029395076 scopus 로고
    • Menage a trois: Double strand break repair, V(D)J recombination and DNA-PK
    • Jeggo PA, Taccioli GE, Jackson SP. Menage a trois: double strand break repair, V(D)J recombination and DNA-PK. BioEssays 1995; 17: 949-957.
    • (1995) BioEssays , vol.17 , pp. 949-957
    • Jeggo, P.A.1    Taccioli, G.E.2    Jackson, S.P.3
  • 150
    • 0028791446 scopus 로고
    • DNA double-strand break repair and V(D)J recombination. Involvement of DNA-PK
    • Jackson SP, Jeggo PA. DNA double-strand break repair and V(D)J recombination. Involvement of DNA-PK. Trends Biochem Sci 1995, 20: 412-5.
    • (1995) Trends Biochem Sci , vol.20 , pp. 412-415
    • Jackson, S.P.1    Jeggo, P.A.2
  • 151
    • 0031059531 scopus 로고    scopus 로고
    • Tying loose ends: Roles of Ku and DNA-dependent protein kinase in the repair of double-strand breaks
    • Lieber MR, Grawunder U, Wu X, Yaneva M. Tying loose ends: roles of Ku and DNA-dependent protein kinase in the repair of double-strand breaks. Curr Opin Gen Dev 1997; 7: 99-104.
    • (1997) Curr Opin Gen Dev , vol.7 , pp. 99-104
    • Lieber, M.R.1    Grawunder, U.2    Wu, X.3    Yaneva, M.4
  • 152
    • 0031214080 scopus 로고    scopus 로고
    • Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV
    • Critchlow SE, Bowater RP, Jackson SP. Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV. Curr Biol 1997; 7: 588-98.
    • (1997) Curr Biol , vol.7 , pp. 588-598
    • Critchlow, S.E.1    Bowater, R.P.2    Jackson, S.P.3
  • 153
    • 0030925492 scopus 로고    scopus 로고
    • KARP-1: A novel leucine zipper protein expressed from the Ku86 autoantigen locus is implicated in the control of DNA-dependent protein kinase activity
    • Myung K, He DM, Eun SE, Hendrickson EA. KARP-1: a novel leucine zipper protein expressed from the Ku86 autoantigen locus is implicated in the control of DNA-dependent protein kinase activity. EMBO J 1997; 16: 3172-84.
    • (1997) EMBO J , vol.16 , pp. 3172-3184
    • Myung, K.1    He, D.M.2    Eun, S.E.3    Hendrickson, E.A.4
  • 154
    • 0030605405 scopus 로고    scopus 로고
    • DNA-dependent protein kinase defects are linked to deficiencies in DNA repair and V(D)J recombination
    • Finnie NJ, Gottlieb TM, Blunt T, Jeggo PA, Jackson SP. DNA-dependent protein kinase defects are linked to deficiencies in DNA repair and V(D)J recombination. Phil Trans R Soc 1996; 351: 173-9.
    • (1996) Phil Trans R Soc , vol.351 , pp. 173-179
    • Finnie, N.J.1    Gottlieb, T.M.2    Blunt, T.3    Jeggo, P.A.4    Jackson, S.P.5
  • 157
    • 0028012558 scopus 로고
    • A rapid mechanism-based screen to detect potential anti-cancer agents
    • Swaffar DS, Ireland CM, Barrows LR. A rapid mechanism-based screen to detect potential anti-cancer agents. Anti-Cancer Drugs 1994; 5: 15-23.
    • (1994) Anti-Cancer Drugs , vol.5 , pp. 15-23
    • Swaffar, D.S.1    Ireland, C.M.2    Barrows, L.R.3
  • 158
    • 0025975313 scopus 로고
    • Topoisomerase II activity in a DNA double-strand break repair deficient Chinese hamster ovary cell line
    • Waters RL, Lyons BW, Li TM, Chen DJ. Topoisomerase II activity in a DNA double-strand break repair deficient Chinese hamster ovary cell line. Mutat Res 1991; 254: 167-74.
    • (1991) Mutat Res , vol.254 , pp. 167-174
    • Waters, R.L.1    Lyons, B.W.2    Li, T.M.3    Chen, D.J.4
  • 159
    • 0028938059 scopus 로고
    • Altered metaphase chromosome structure in xrs-5 cells is not related to its radiation sensitivity or defective DNA break rejoining
    • Schwartz JL, Brinkman WJ, Kasten L, et al. Altered metaphase chromosome structure in xrs-5 cells is not related to its radiation sensitivity or defective DNA break rejoining. Mutat Res Fundam Mol Mech Mutagen 1995; 328: 119-26.
    • (1995) Mutat Res Fundam Mol Mech Mutagen , vol.328 , pp. 119-126
    • Schwartz, J.L.1    Brinkman, W.J.2    Kasten, L.3
  • 160
    • 0029935255 scopus 로고    scopus 로고
    • Restoration of X-ray and etoposide resistance, Ku-end binding activity and V(D)J recombination to the Chinese hamster sxi-3 mutant by a hamster Ku86 cDNA
    • He DM, Lee SE, Hendrickson EA. Restoration of X-ray and etoposide resistance, Ku-end binding activity and V(D)J recombination to the Chinese hamster sxi-3 mutant by a hamster Ku86 cDNA. Mutat Res 1996; 363: 43-56.
    • (1996) Mutat Res , vol.363 , pp. 43-56
    • He, D.M.1    Lee, S.E.2    Hendrickson, E.A.3
  • 161
    • 0031591695 scopus 로고    scopus 로고
    • Inhibition of DNA unwinding and ATPase activities of human DNA helicase II by chemotherapeutic agents
    • Tuteja N, Phan TN, Tuteja R, Ochem A, Falaschi A. Inhibition of DNA unwinding and ATPase activities of human DNA helicase II by chemotherapeutic agents. Biochem Biophys Res Comm 1997; 236: 636-40.
    • (1997) Biochem Biophys Res Comm , vol.236 , pp. 636-640
    • Tuteja, N.1    Phan, T.N.2    Tuteja, R.3    Ochem, A.4    Falaschi, A.5
  • 162
    • 0028217223 scopus 로고
    • Wortmannin, a potent and selective inhibitor of phosphatidylinositol-3-kinase
    • Powis G, Bonjouklian R, Berggren MM, et al. Wortmannin, a potent and selective inhibitor of phosphatidylinositol-3-kinase. Cancer Res 1994; 54: 2419-23.
    • (1994) Cancer Res , vol.54 , pp. 2419-2423
    • Powis, G.1    Bonjouklian, R.2    Berggren, M.M.3
  • 163
    • 0029156599 scopus 로고
    • DNA-dependent protein kinase catalytic subunit: A relative of phosphatidylinositol 3-kinase and the ataxia telangiectasia gene product
    • Hartley KO, Gell D, Smith GCM, et al. DNA-dependent protein kinase catalytic subunit: a relative of phosphatidylinositol 3-kinase and the ataxia telangiectasia gene product. Cell 1995; 82: 849-56.
    • (1995) Cell , vol.82 , pp. 849-856
    • Hartley, K.O.1    Gell, D.2    Smith, G.C.M.3
  • 164
    • 0030066023 scopus 로고    scopus 로고
    • The phophatidylinositol 3-kinase inhibitor wortmannin sensitizes murine fibroblasts and human tumor cells to radiation and blocks induction of p53 following DNA damage
    • Price BD, Youmell MB. The phophatidylinositol 3-kinase inhibitor wortmannin sensitizes murine fibroblasts and human tumor cells to radiation and blocks induction of p53 following DNA damage. Cancer Res 1996; 56: 246-50.
    • (1996) Cancer Res , vol.56 , pp. 246-250
    • Price, B.D.1    Youmell, M.B.2
  • 165
    • 0029803485 scopus 로고    scopus 로고
    • Wortmannin is a potent inhibitor of DNA double strand break but not single break repair in Chinese hamster ovary cells
    • Boulton S, Kyle S, Yalçintepe L, Durkacz BW. Wortmannin is a potent inhibitor of DNA double strand break but not single break repair in Chinese hamster ovary cells. Carcinogenesis 1996; 17: 2285-90.
    • (1996) Carcinogenesis , vol.17 , pp. 2285-2290
    • Boulton, S.1    Kyle, S.2    Yalçintepe, L.3    Durkacz, B.W.4
  • 167
    • 0028783512 scopus 로고
    • OK-1035, a selective inhibitor of DNA-dependent protein kinase
    • Take Y, Kumano M, Hamano Y, et al. OK-1035, a selective inhibitor of DNA-dependent protein kinase. Biochem Biophys Res Commun 1995; 215: 41-7.
    • (1995) Biochem Biophys Res Commun , vol.215 , pp. 41-47
    • Take, Y.1    Kumano, M.2    Hamano, Y.3
  • 168
    • 0029979313 scopus 로고    scopus 로고
    • DNA-dependent protein kinase inhibitor (OK-1035) suppresses p21 expression in HCT116 cells containing wild-type p53 induced by adriamycin
    • Take Y, Kumano M, Teraoka H, Nishimura S, Okuyama A. DNA-dependent protein kinase inhibitor (OK-1035) suppresses p21 expression in HCT116 cells containing wild-type p53 induced by adriamycin. Biochem Biophys Res Commun 1996; 221: 207-12.
    • (1996) Biochem Biophys Res Commun , vol.221 , pp. 207-212
    • Take, Y.1    Kumano, M.2    Teraoka, H.3    Nishimura, S.4    Okuyama, A.5
  • 169
    • 0029943449 scopus 로고    scopus 로고
    • Mismatch repair in replication fidelity, genetic recombination and cancer biology
    • Modrich P, Lahue R. Mismatch repair in replication fidelity, genetic recombination and cancer biology. Annu Rev Biochem 1996; 65: 101-33.
    • (1996) Annu Rev Biochem , vol.65 , pp. 101-133
    • Modrich, P.1    Lahue, R.2
  • 170
    • 0029784320 scopus 로고    scopus 로고
    • Biochemistry and genetics of eukaryotic mismatch repair
    • Kolodner R. Biochemistry and genetics of eukaryotic mismatch repair. Genes Dev 1996; 10: 1433-42.
    • (1996) Genes Dev , vol.10 , pp. 1433-1442
    • Kolodner, R.1
  • 171
    • 0030265201 scopus 로고    scopus 로고
    • DNA mismatch repair deficient mice in cancer research
    • Prolla TA, Abuin A, Bradley A. DNA mismatch repair deficient mice in cancer research. Semin Cancer Biol 1996; 7: 241-7.
    • (1996) Semin Cancer Biol , vol.7 , pp. 241-247
    • Prolla, T.A.1    Abuin, A.2    Bradley, A.3
  • 172
    • 0030935386 scopus 로고    scopus 로고
    • DNA polymerase δ is required for human mismatch repair in vitro
    • Longley MJ, Pierce AJ, Modrich P. DNA polymerase δ is required for human mismatch repair in vitro. J Biol Chem 1997; 272: 10917-21.
    • (1997) J Biol Chem , vol.272 , pp. 10917-10921
    • Longley, M.J.1    Pierce, A.J.2    Modrich, P.3
  • 173
    • 0029990917 scopus 로고    scopus 로고
    • Molecular mechanisms underlying hereditary nonpolyposis colorectal carcinoma
    • Rhyu MS. Molecular mechanisms underlying hereditary nonpolyposis colorectal carcinoma. J Natl Cancer Inst 1996; 88: 240-51.
    • (1996) J Natl Cancer Inst , vol.88 , pp. 240-251
    • Rhyu, M.S.1
  • 174
    • 0028867842 scopus 로고    scopus 로고
    • Mismatch repair mechanisms and relationship to cancer susceptibility
    • Kolodner RD. Mismatch repair mechanisms and relationship to cancer susceptibility. Trends Biochem Sci 1996; 20: 397-401.
    • (1996) Trends Biochem Sci , vol.20 , pp. 397-401
    • Kolodner, R.D.1
  • 175
    • 0029812676 scopus 로고    scopus 로고
    • Cisplatin and adryamycin resistance are associated with Mutlα and mismatch repair deficiency in an ovarian tumor cell line
    • Drummond JT, Anthoney A, Brown R, Modrich P. Cisplatin and adryamycin resistance are associated with Mutlα and mismatch repair deficiency in an ovarian tumor cell line. J Biol Chem 1996; 271: 19645-8.
    • (1996) J Biol Chem , vol.271 , pp. 19645-19648
    • Drummond, J.T.1    Anthoney, A.2    Brown, R.3    Modrich, P.4
  • 176
    • 0029822592 scopus 로고    scopus 로고
    • Role of postreplicative DNA mismatch repair in the cytotoxic action of thioguanine
    • Swann PF, Waters TR, Moulton DC, et al. Role of postreplicative DNA mismatch repair in the cytotoxic action of thioguanine. Science 1996; 273: 1109-11.
    • (1996) Science , vol.273 , pp. 1109-1111
    • Swann, P.F.1    Waters, T.R.2    Moulton, D.C.3
  • 177
    • 8944230189 scopus 로고    scopus 로고
    • Loss of DNA mismatch repair in acquired resistance to cisplatin
    • Aebi S, Kurdi-Haidar B, Gordon R, et al. Loss of DNA mismatch repair in acquired resistance to cisplatin. Cancer Res 1996; 56: 3087-90.
    • (1996) Cancer Res , vol.56 , pp. 3087-3090
    • Aebi, S.1    Kurdi-Haidar, B.2    Gordon, R.3
  • 178
    • 0029904811 scopus 로고    scopus 로고
    • The role of DNA mismatch repair in platinum drug resistance
    • Fink D, Nebel S, Aebi S, et al. The role of DNA mismatch repair in platinum drug resistance. Cancer Res 1996; 56: 4881-6.
    • (1996) Cancer Res , vol.56 , pp. 4881-4886
    • Fink, D.1    Nebel, S.2    Aebi, S.3
  • 179
    • 0030741503 scopus 로고    scopus 로고
    • hMLH1 expression and cellular responses of ovarian tumor cells to treatment with cytotoxic anticancer agents
    • Brown R, Hirst GL, Gallagher WM, et al. hMLH1 expression and cellular responses of ovarian tumor cells to treatment with cytotoxic anticancer agents. Oncogene 1997; 15: 45-52.
    • (1997) Oncogene , vol.15 , pp. 45-52
    • Brown, R.1    Hirst, G.L.2    Gallagher, W.M.3
  • 180
    • 0028533694 scopus 로고
    • DNA damage tolerance, mismatch repair and genome instability
    • Karran P, Bignami M. DNA damage tolerance, mismatch repair and genome instability. BioEssays 1994; 16: 833-9.
    • (1994) BioEssays , vol.16 , pp. 833-839
    • Karran, P.1    Bignami, M.2
  • 181
    • 0030479125 scopus 로고    scopus 로고
    • Mismatch repair mutations override alkyltransferase in conferring resistance to temozolomide but not to 1,3-bis(2-chloroethyl)-nitrosourea
    • Liu L, Markowitz S, Gereon SL. Mismatch repair mutations override alkyltransferase in conferring resistance to temozolomide but not to 1,3-bis(2-chloroethyl)-nitrosourea. Cancer Res 1996; 56: 5375-9.
    • (1996) Cancer Res , vol.56 , pp. 5375-5379
    • Liu, L.1    Markowitz, S.2    Gereon, S.L.3
  • 182
    • 0029872790 scopus 로고    scopus 로고
    • Ku protein complex is involved in nucleotide excision repair of DNA
    • Calsou P, Muller C, Frit P, Salles B. Ku protein complex is involved in nucleotide excision repair of DNA. C R Acad Sci 1996; 319: 179-82.
    • (1996) C R Acad Sci , vol.319 , pp. 179-182
    • Calsou, P.1    Muller, C.2    Frit, P.3    Salles, B.4
  • 183
    • 0024507191 scopus 로고
    • Pathways of human cell post-replication repair
    • Kaufmann WK. Pathways of human cell post-replication repair. Carcinogenesis 1989; 10: 1-11.
    • (1989) Carcinogenesis , vol.10 , pp. 1-11
    • Kaufmann, W.K.1
  • 184
    • 0028034467 scopus 로고
    • Cisplatin-induced renal toxicity and toxicity-modulating strategies: A review
    • Pinzani V, Bressolle F, Haug IJ, et al. Cisplatin-induced renal toxicity and toxicity-modulating strategies: a review. Cancer Chemother Pharmacol 1994; 35: 1-9.
    • (1994) Cancer Chemother Pharmacol , vol.35 , pp. 1-9
    • Pinzani, V.1    Bressolle, F.2    Haug, I.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.