메뉴 건너뛰기




Volumn 405, Issue 2, 1998, Pages 179-191

Transgenic systems in studies on genotoxicity of alkylating agents: Critical lesions, thresholds and defense mechanisms

Author keywords

Alkylating agent; Genotoxicity; Transgenic system

Indexed keywords

ALKYLATING AGENT; DIMETHYLBENZ[A]ANTHRACENE; DIMETHYLNITROSAMINE; DNA DIRECTED DNA POLYMERASE BETA; DNA GLYCOSYLTRANSFERASE; ENDONUCLEASE; LIGASE; METHYLATED DNA PROTEIN CYSTEINE METHYLTRANSFERASE; METHYLNITROSOUREA; PHORBOL 13 ACETATE 12 MYRISTATE; POLY(ADENOSINE DIPHOSPHATE RIBOSE);

EID: 0032552632     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0027-5107(98)00135-3     Document Type: Conference Paper
Times cited : (40)

References (77)
  • 1
    • 0025288239 scopus 로고
    • Distribution of methyl and ethyl adducts following alkylation with monofunctional alkylating agents
    • [1] D.T. Beranek, Distribution of methyl and ethyl adducts following alkylation with monofunctional alkylating agents, Mutat. Res. 231 (1990) 11-30.
    • (1990) Mutat. Res. , vol.231 , pp. 11-30
    • Beranek, D.T.1
  • 2
    • 0027340278 scopus 로고
    • 6-alkylguanine and N-alkylpurines to the formation of sister chromatid exchanges, chromosomal aberrations, and gene mutations: New insights gained from studies of genetically engineered mammalian cell lines
    • 6-alkylguanine and N-alkylpurines to the formation of sister chromatid exchanges, chromosomal aberrations, and gene mutations: new insights gained from studies of genetically engineered mammalian cell lines, Environ. Mol. Mutagen. 22 (1993) 283-292.
    • (1993) Environ. Mol. Mutagen. , vol.22 , pp. 283-292
    • Kaina, B.1    Fritz, G.2    Coquerelle, T.3
  • 3
    • 0031589755 scopus 로고    scopus 로고
    • 6-methylguanine in Mex-, Mex+ and methylation-tolerant mismatch repair compromised cells: Facts and models
    • in press
    • 6-methylguanine in Mex-, Mex+ and methylation-tolerant mismatch repair compromised cells: facts and models, Mutat. Res. (1997), in press.
    • (1997) Mutat. Res. (
    • Kaina, B.1    Ziouta, A.2    Ochs, K.3    Coquerelle, T.4
  • 4
    • 0025941670 scopus 로고
    • 6-methylguanine-DNA methyltransferase (MGMT) cDNA in Chinese hamster cells: The role of MGMT in protection against the genotoxic effects of alkylating agents
    • 6-methylguanine-DNA methyltransferase (MGMT) cDNA in Chinese hamster cells: the role of MGMT in protection against the genotoxic effects of alkylating agents, Carcinogenesis 12 (1991) 1857-1867.
    • (1991) Carcinogenesis , vol.12 , pp. 1857-1867
    • Kaina, B.1    Fritz, G.2    Mitra, S.3    Coquerelle, T.4
  • 5
    • 0000017747 scopus 로고
    • Biological consequences of reactions with DNA: Role of specific lesions
    • C.S. Cooper, P.L. Grover (Eds.), Springer, Berlin
    • [5] G.P. Margison, P.J. O'Conner, Biological consequences of reactions with DNA: role of specific lesions, in: C.S. Cooper, P.L. Grover (Eds.), Handbook of Experimental Pharmacology, Springer, Berlin, 1990, p. 547.
    • (1990) Handbook of Experimental Pharmacology , pp. 547
    • Margison, G.P.1    O'Conner, P.J.2
  • 7
    • 0016042235 scopus 로고
    • 6-ethylguanine in rat brain DNA: Correlation with nervous system-specific carcinogenesis by ethylnitrosourea
    • 6-ethylguanine in rat brain DNA: correlation with nervous system-specific carcinogenesis by ethylnitrosourea, Proc. Natl. Acad. Sci. USA 71 (1974) 639-643.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 639-643
    • Goth, R.1    Rajewsky, M.F.2
  • 8
    • 0026613695 scopus 로고
    • 6-alkylguanine-DNA alkyltransferase activity and N-methyl-N′-nitro-N-nitrosoguanidine-induced mutation, transformation, and cytotoxicity in C3H/10T1/2 cells expressing exogenous alkyltransferase genes
    • 6-alkylguanine-DNA alkyltransferase activity and N-methyl-N′-nitro-N-nitrosoguanidine-induced mutation, transformation, and cytotoxicity in C3H/10T1/2 cells expressing exogenous alkyltransferase genes, Proc. Natl. Acad. Sci. USA 89 (1992) 11199-11203.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11199-11203
    • Von Hofe, E.1    Fairbairn, L.2    Margison, G.P.3
  • 11
    • 0029901710 scopus 로고    scopus 로고
    • 6-methylguanine-DNA methyltransferase (MGMT) in transgenic mice protects against tumor initiation in two-stage skin carcinogenesis
    • 6-methylguanine-DNA methyltransferase (MGMT) in transgenic mice protects against tumor initiation in two-stage skin carcinogenesis, Cancer Res. 56 (1996) 3244-3249.
    • (1996) Cancer Res. , vol.56 , pp. 3244-3249
    • Becker, K.1    Dosch, J.2    Gregel, C.M.3    Martin, B.A.4    Kaina, B.5
  • 13
    • 0028169360 scopus 로고
    • 6-methylguanine-DNA adducts protects transgenic mice from N-methylnitrosourea-induced thymic lymphomas
    • 6-methylguanine-DNA adducts protects transgenic mice from N-methylnitrosourea-induced thymic lymphomas, Cancer Res. 54 (1994) 4648-4652.
    • (1994) Cancer Res. , vol.54 , pp. 4648-4652
    • Liu, L.1    Allay, E.2    Dumenco, L.L.3    Gerson, S.L.4
  • 14
    • 0028904619 scopus 로고
    • Transgenic expression of human MGMT protects against azomethane-induced aberrant crypt foci and G to A mutations in the Ka-ras oncogene of mouse colon
    • [14] N.H. Zaidi, T.P. Pretlow, M.A. O'Riordan, L.L. Dumenco, E. Allay, S.L. Gerson, Transgenic expression of human MGMT protects against azomethane-induced aberrant crypt foci and G to A mutations in the Ka-ras oncogene of mouse colon, Carcinogenesis 16 (1995) 451-456.
    • (1995) Carcinogenesis , vol.16 , pp. 451-456
    • Zaidi, N.H.1    Pretlow, T.P.2    O'Riordan, M.A.3    Dumenco, L.L.4    Allay, E.5    Gerson, S.L.6
  • 17
    • 0030749230 scopus 로고    scopus 로고
    • 6-methylguanine-DNA methyltransferase protects against skin tumor formation induced by antineoplastic cloroethylnitrosourea
    • 6-methylguanine-DNA methyltransferase protects against skin tumor formation induced by antineoplastic cloroethylnitrosourea, Cancer Res. 57 (1997) 3335-3338.
    • (1997) Cancer Res. , vol.57 , pp. 3335-3338
    • Becker, K.1    Gregel, C.M.2    Kaina, B.3
  • 18
    • 0022001993 scopus 로고
    • Dependency of the yield of sister chromatid exchanges induced by alkylating agents on fixation time. Possible involvement of secondary lesions in sister chromatid exchange induction
    • [18] B. Kaina, O. Aurich, Dependency of the yield of sister chromatid exchanges induced by alkylating agents on fixation time. Possible involvement of secondary lesions in sister chromatid exchange induction, Mutat. Res. 149 (1985) 451-461.
    • (1985) Mutat. Res. , vol.149 , pp. 451-461
    • Kaina, B.1    Aurich, O.2
  • 20
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair
    • [20] Y. Matsumoto, K. Kim, Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair, Science 269 (1995) 699-702.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 21
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision repair with purified human proteins: Interaction between DNA polymerase β and the XRCC-1 protein
    • [21] Y. Kubota, R.A. Nash, A. Klungland, P. Schär, D.E. Barnes, T. Lindahl, Reconstitution of DNA base excision repair with purified human proteins: interaction between DNA polymerase β and the XRCC-1 protein, EMBO J. 15 (1996) 6662-6670.
    • (1996) EMBO J. , vol.15 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schär, P.4    Barnes, D.E.5    Lindahl, T.6
  • 22
    • 0028966181 scopus 로고
    • DNA polymerase β conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract
    • [22] R.K. Singhal, R. Prasad, S.H. Wilson, DNA polymerase β conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract, J. Biol. Chem. 270 (1995) 949-957.
    • (1995) J. Biol. Chem. , vol.270 , pp. 949-957
    • Singhal, R.K.1    Prasad, R.2    Wilson, S.H.3
  • 23
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • [23] T. Lindahl, Instability and decay of the primary structure of DNA, Nature 362 (1993) 709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 24
    • 0026474380 scopus 로고
    • Expression of the E. Coli 3-methyladenine-DNA glycosylase I gene in mammalian cells reduces the toxic and mutagenic effects of methylating agents
    • [24] A. Klungland, L. Fairbairn, A.J. Watson, G.P. Margison, E. Seeberg, Expression of the E. coli 3-methyladenine-DNA glycosylase I gene in mammalian cells reduces the toxic and mutagenic effects of methylating agents, EMBO J. 11 (1992) 4439-4444.
    • (1992) EMBO J. , vol.11 , pp. 4439-4444
    • Klungland, A.1    Fairbairn, L.2    Watson, A.J.3    Margison, G.P.4    Seeberg, E.5
  • 25
    • 0023273590 scopus 로고
    • Substrate specificity of 3-methyladenine-DNA glycosylase from calf thymus
    • [25] R. Male, B.I. Hankanes, D.E. Helland, K. Kleppe, Substrate specificity of 3-methyladenine-DNA glycosylase from calf thymus, Eur. J. Biochem. 165 (1987) 13-19.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 13-19
    • Male, R.1    Hankanes, B.I.2    Helland, D.E.3    Kleppe, K.4
  • 26
    • 0020057737 scopus 로고
    • Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents
    • [26] P. Karran, T. Hjelmgren, T. Lindahl, Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents, Nature 296 (1982) 770-773.
    • (1982) Nature , vol.296 , pp. 770-773
    • Karran, P.1    Hjelmgren, T.2    Lindahl, T.3
  • 28
    • 0027398114 scopus 로고
    • 3-methyladenine-DNA glycosylase genes
    • 3-methyladenine-DNA glycosylase genes, Mutat. Res. 293 (1993) 187-195.
    • (1993) Mutat. Res. , vol.293 , pp. 187-195
    • Habraken, Y.1    Laval, F.2
  • 29
    • 0022962212 scopus 로고
    • Complementation of sensitivity to alkylating agents in Escherichia coli and Chinese hamster ovary cells by expression of a cloned bacterial DNA repair gene
    • [29] H. Kataoka, J. Hall, P. Karran, Complementation of sensitivity to alkylating agents in Escherichia coli and Chinese hamster ovary cells by expression of a cloned bacterial DNA repair gene, EMBO J. 5 (1986) 3195-3200.
    • (1986) EMBO J. , vol.5 , pp. 3195-3200
    • Kataoka, H.1    Hall, J.2    Karran, P.3
  • 30
    • 0343328947 scopus 로고
    • Suppression of human DNA alkylating repair defects by Escherichia coli DNA repair genes
    • [30] L. Samson, B. Derfler, E.A. Waldstein, Suppression of human DNA alkylating repair defects by Escherichia coli DNA repair genes, Proc. Natl. Acad. Sci. USA 83 (1986) 5607-5610.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5607-5610
    • Samson, L.1    Derfler, B.2    Waldstein, E.A.3
  • 31
    • 0022994130 scopus 로고
    • 6-methylguanine methyltransferase gene into repair-deficient human cells and restoration of cellular resistance to N-methyl-N′-nitro-N-nitrosoguanidine
    • 6-methylguanine methyltransferase gene into repair-deficient human cells and restoration of cellular resistance to N-methyl-N′-nitro-N-nitrosoguanidine, Mutat. Res. 166 (1986) 135-141.
    • (1986) Mutat. Res. , vol.166 , pp. 135-141
    • Ishizaki, K.1    Tsujimura, T.2    Yawata, H.3    Fujio, C.4    Nakabeppu, Y.5    Sekiguchi, M.6    Ikenaga, M.7
  • 32
    • 0022989218 scopus 로고
    • 6-alkylguanine alkyltransferase reduces the toxic effects of alkylating agents
    • 6-alkylguanine alkyltransferase reduces the toxic effects of alkylating agents, Carcinogenesis 7 (1986) 2081-2084.
    • (1986) Carcinogenesis , vol.7 , pp. 2081-2084
    • Brennand, J.1    Margison, G.P.2
  • 33
    • 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 alkylating agents in Chinese hamster ovary cells
    • [33] G. Ibeanu, B. Hartenstein, W.C. Dunn, L.Y. Chang, E. Hofmann, T. Coquerelle, S. Mitra, B. Kaina, 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 alkylating agents in Chinese hamster ovary cells, Carcinogenesis 13 (1992) 1989-1995.
    • (1992) Carcinogenesis , vol.13 , pp. 1989-1995
    • Ibeanu, G.1    Hartenstein, B.2    Dunn, W.C.3    Chang, L.Y.4    Hofmann, E.5    Coquerelle, T.6    Mitra, S.7    Kaina, B.8
  • 34
    • 0028801762 scopus 로고
    • Overexpression of N-methylpurine-DNA glycosylase in Chinese hamster ovary cells renders them more sensitive to the production of chromosomal aberrations by methylating agents - A case of unbalanced DNA repair
    • [34] T. Coquerelle, J. Dosch, B. Kaina, Overexpression of N-methylpurine-DNA glycosylase in Chinese hamster ovary cells renders them more sensitive to the production of chromosomal aberrations by methylating agents - a case of unbalanced DNA repair, Mutat. Res. 336 (1995) 9-17.
    • (1995) Mutat. Res. , vol.336 , pp. 9-17
    • Coquerelle, T.1    Dosch, J.2    Kaina, B.3
  • 35
    • 0027759522 scopus 로고
    • Purification and characterization of human 3-methyladenine-DNA glycosylase
    • [35] T.R. O'Conner, Purification and characterization of human 3-methyladenine-DNA glycosylase, Nucleic Acids Res. 21 (1993) 5561-5569.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5561-5569
    • O'Conner, T.R.1
  • 36
    • 0027217747 scopus 로고
    • Effect of ERCC-1 overexpression on sensitivity of Chinese hamster ovary cells to DNA-damaging agents
    • [36] J. Bramson, L.C. Panasci, Effect of ERCC-1 overexpression on sensitivity of Chinese hamster ovary cells to DNA-damaging agents, Cancer Res. 53 (1993) 3237-3240.
    • (1993) Cancer Res. , vol.53 , pp. 3237-3240
    • Bramson, J.1    Panasci, L.C.2
  • 37
    • 0030041960 scopus 로고    scopus 로고
    • Repair-deficient 3-methyladenine-DNA glycosylase homozygous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing
    • [37] B.P. Engelward, A. Dreslin, J. Christensen, D. Huszar, C. Kurahara, L. Samson, Repair-deficient 3-methyladenine-DNA glycosylase homozygous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing, EMBO J. 15 (1996) 945-952.
    • (1996) EMBO J. , vol.15 , pp. 945-952
    • Engelward, B.P.1    Dreslin, A.2    Christensen, J.3    Huszar, D.4    Kurahara, C.5    Samson, L.6
  • 41
    • 0026004662 scopus 로고
    • Two distinct human DNA diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidized DNA
    • [41] D.S. Chen, V. Herman, B. Demple, Two distinct human DNA diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidized DNA, Nucleic Acids Res. 19 (1991) 5907-5914.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5907-5914
    • Chen, D.S.1    Herman, V.2    Demple, B.3
  • 42
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • [42] S. Xanthoudakis, G. Miao, F. Wang, Y.-C.E. Pan, T. Curran, Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme, EMBO J. 11 (1992) 3323-3335.
    • (1992) EMBO J. , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.-C.E.4    Curran, T.5
  • 43
    • 0029829265 scopus 로고    scopus 로고
    • The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice
    • [43] S. Xanthoudakis, R.J. Smeyne, J.D. Wallace, T. Curran, The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice, Proc. Natl. Acad. Sci. USA 93 (1996) 8919-8923.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8919-8923
    • Xanthoudakis, S.1    Smeyne, R.J.2    Wallace, J.D.3    Curran, T.4
  • 44
    • 0028596574 scopus 로고
    • A role for the human DNA repair enzyme HAP1 in cellular protection against DNA damaging agents and hypoxic stress
    • [44] L.J. Walker, R.B. Craig, A.L. Harris, I.D. Hickson, A role for the human DNA repair enzyme HAP1 in cellular protection against DNA damaging agents and hypoxic stress, Nucleic Acids Res. 22 (1994) 4884-4889.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4884-4889
    • Walker, L.J.1    Craig, R.B.2    Harris, A.L.3    Hickson, I.D.4
  • 45
    • 0028244814 scopus 로고
    • Stable expression in rat glioma cells of sense and antisense nucleic acids to a human multifunctional DNA repair enzyme APEX nuclease
    • [45] Y. Ono, T. Futura, T. Ohmoto, K. Akiyama, S. Seki, Stable expression in rat glioma cells of sense and antisense nucleic acids to a human multifunctional DNA repair enzyme APEX nuclease, Mutat. Res. 315 (1994) 55-63.
    • (1994) Mutat. Res. , vol.315 , pp. 55-63
    • Ono, Y.1    Futura, T.2    Ohmoto, T.3    Akiyama, K.4    Seki, S.5
  • 46
    • 0030933193 scopus 로고    scopus 로고
    • Expression of yeast but not human apurinic/apyrimidinic endonuclease renders Chinese hamster cells more resistant to DNA damaging agents
    • [46] M. Tomicic, E. Eschbach, B. Kaina, Expression of yeast but not human apurinic/apyrimidinic endonuclease renders Chinese hamster cells more resistant to DNA damaging agents, Mutat. Res. 383 (1997) 155-165.
    • (1997) Mutat. Res. , vol.383 , pp. 155-165
    • Tomicic, M.1    Eschbach, E.2    Kaina, B.3
  • 47
    • 0028059099 scopus 로고
    • Deletion of a DNA polymerase β gene segment in T cells using cell type-specific gene targeting
    • [47] H. Gu, J.D. Marth, P.C. Orban, H. Mossmann, K. Rajewsky, Deletion of a DNA polymerase β gene segment in T cells using cell type-specific gene targeting, Science 265 (1994) 103-106.
    • (1994) Science , vol.265 , pp. 103-106
    • Gu, H.1    Marth, J.D.2    Orban, P.C.3    Mossmann, H.4    Rajewsky, K.5
  • 49
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway
    • [49] R.A.O. Bennett, D.M. Wilson III, D. Wong, B. Demple, Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway, Proc. Natl. Acad. Sci USA 94 (1997) 7166-7169.
    • (1997) Proc. Natl. Acad. Sci USA , vol.94 , pp. 7166-7169
    • Bennett, R.A.O.1    Wilson D.M. III2    Wong, D.3    Demple, B.4
  • 50
    • 0029957245 scopus 로고    scopus 로고
    • XRCC-1 polypeptide interacts with DNA polymerase beta and possibly poly (ADP-ribose) polymerase, and DNA ligase III is a novel molecular 'nick-sensor' in vitro
    • [50] K.W. Caldecott, S. Aoufouchi, P. Johnson, S. Shall, XRCC-1 polypeptide interacts with DNA polymerase beta and possibly poly (ADP-ribose) polymerase, and DNA ligase III is a novel molecular 'nick-sensor' in vitro, Nucleic Acids Res. 24 (1996) 4387-4394.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4387-4394
    • Caldecott, K.W.1    Aoufouchi, S.2    Johnson, P.3    Shall, S.4
  • 51
    • 0028819767 scopus 로고
    • Strategic down-regulation of DNA polymerase beta by antisense RNA sensitizes mammalian cells to specific DNA damaging agents
    • [51] J.K. Horton, D.K. Srivastava, B.Z. Zmudzka, S.H. Wilson, Strategic down-regulation of DNA polymerase beta by antisense RNA sensitizes mammalian cells to specific DNA damaging agents, Nucleic Acids Res. 23 (1995) 3810-3815.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3810-3815
    • Horton, J.K.1    Srivastava, D.K.2    Zmudzka, B.Z.3    Wilson, S.H.4
  • 52
    • 0028862933 scopus 로고
    • Characterization of the XRCC-1-DNA ligase III complex in vitro and its absence from mutant hamster cells
    • [52] K.W. Caldecott, J.D. Tucker, L.H. Stanker, L.H. Thompson, Characterization of the XRCC-1-DNA ligase III complex in vitro and its absence from mutant hamster cells, Nucleic Acids Res. 23 (1995) 4836-4843.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4836-4843
    • Caldecott, K.W.1    Tucker, J.D.2    Stanker, L.H.3    Thompson, L.H.4
  • 53
    • 0025202114 scopus 로고
    • Molecular cloning of the human XRCC-1 gene, which corrects defective DNA strand break repair and sister chromatid exchange
    • [53] L.H. Thompson, K.W. Brookman, N.J. Jones, S.A. Allen, A.V. Carrano, Molecular cloning of the human XRCC-1 gene, which corrects defective DNA strand break repair and sister chromatid exchange, Mol. Cell. Biol. (1990) 6160-6171.
    • (1990) Mol. Cell. Biol. ( , pp. 6160-6171
    • Thompson, L.H.1    Brookman, K.W.2    Jones, N.J.3    Allen, S.A.4    Carrano, A.V.5
  • 54
    • 0022971473 scopus 로고
    • Isolation and partial characterization of human cell mutants differing in sensitivity to killing and mutation by methylnitrosourea and N-methyl-N′-nitro-N-nitrosoguanidine
    • [54] V.S. Goldmacher, R.A. Cuzick, W.G. Thilly, Isolation and partial characterization of human cell mutants differing in sensitivity to killing and mutation by methylnitrosourea and N-methyl-N′-nitro-N-nitrosoguanidine, J. Biol. Chem. 261 (1986) 12462-12471.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12462-12471
    • Goldmacher, V.S.1    Cuzick, R.A.2    Thilly, W.G.3
  • 56
    • 0023131169 scopus 로고
    • Cell killing by various monofunctional alkylating agents in Chinese hamster ovary cells
    • [56] R. Goth-Goldstein, M. Hughes, Cell killing by various monofunctional alkylating agents in Chinese hamster ovary cells, Mutat. Res. 177 (1987) 267-276.
    • (1987) Mutat. Res. , vol.177 , pp. 267-276
    • Goth-Goldstein, R.1    Hughes, M.2
  • 57
    • 0023121208 scopus 로고
    • Transfer of human genes conferring resistance to methylating mutagens, but not to UV irradiation and cross-linking agents, into Chinese hamster ovary cells
    • [57] B. Kaina, A.A. van Zeeland, C. Backendorf, H.W. Thielmann, P. van de Putte, Transfer of human genes conferring resistance to methylating mutagens, but not to UV irradiation and cross-linking agents, into Chinese hamster ovary cells, Mol. Cell. Biol. 7 (1987) 2024-2030.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2024-2030
    • Kaina, B.1    Van Zeeland, A.A.2    Backendorf, C.3    Thielmann, H.W.4    Van De Putte, P.5
  • 58
    • 0027494799 scopus 로고
    • Molecular and cellular characterization of Mex - /methylation-resistant phenotype
    • [58] G. Fritz, J. Dosch, H.W. Thielmann, B. Kaina, Molecular and cellular characterization of Mex - /methylation-resistant phenotype, J. Biol. Chem. 268 (1993) 21102-21112.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21102-21112
    • Fritz, G.1    Dosch, J.2    Thielmann, H.W.3    Kaina, B.4
  • 59
    • 0031843622 scopus 로고    scopus 로고
    • Mismatch G-T binding activity and MSH2 expression is quantitatively related to sensitivity of cells to methylating agents
    • [59] J. Dosch, M. Christmann, B. Kaina, Mismatch G-T binding activity and MSH2 expression is quantitatively related to sensitivity of cells to methylating agents, Carcinogenesis 19 (1998) 567-573.
    • (1998) Carcinogenesis , vol.19 , pp. 567-573
    • Dosch, J.1    Christmann, M.2    Kaina, B.3
  • 60
    • 0029101616 scopus 로고
    • Inactivation of the mouse Msh2 gene results in mismatch repair deficiency, methylation tolerance, hyperrecombination, and predisposition to cancer
    • [60] N. De Wind, M. Dekker, A. Berns, M. Radman, H. te Riele, Inactivation of the mouse Msh2 gene results in mismatch repair deficiency, methylation tolerance, hyperrecombination, and predisposition to cancer, Cell 82 (1995) 321-330.
    • (1995) Cell , vol.82 , pp. 321-330
    • De Wind, N.1    Dekker, M.2    Berns, A.3    Radman, M.4    Te Riele, H.5
  • 61
    • 0029784320 scopus 로고    scopus 로고
    • Biochemistry and genetics of eukaryotic mismatch repair
    • [61] R. Kolodner, Biochemistry and genetics of eukaryotic mismatch repair, Genes Dev. 10 (1996) 1433-1442.
    • (1996) Genes Dev. , vol.10 , pp. 1433-1442
    • Kolodner, R.1
  • 62
    • 0028556806 scopus 로고
    • A mismatch recognition defect in colon carcinoma confers DNA microsatellite instability and a mutator phenotype
    • [62] G. Aqiulina, P. Hess, P. Branch, C. MacGeoch, I. Casciano, P. Karran, M. Bigami, A mismatch recognition defect in colon carcinoma confers DNA microsatellite instability and a mutator phenotype, Proc. Natl. Acad. Sci. USA 91 (1994) 8905-8909.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8905-8909
    • Aqiulina, G.1    Hess, P.2    Branch, P.3    MacGeoch, C.4    Casciano, I.5    Karran, P.6    Bigami, M.7
  • 63
    • 0027493111 scopus 로고
    • Endogenous DNA adducts: Potential and paradox
    • [63] L.J. Marnett, P.C. Burcham, Endogenous DNA adducts: potential and paradox, Chem. Res. Toxicol. 6 (1993) 771-785.
    • (1993) Chem. Res. Toxicol. , vol.6 , pp. 771-785
    • Marnett, L.J.1    Burcham, P.C.2
  • 64
    • 0026969362 scopus 로고
    • Poly(ADP-ribosyl)ation: Its role in inducible DNA amplification, and its correlation with the longevity of mammalian species
    • [64] A. Bürkle, K. Grube, J.-H. Küpper, Poly(ADP-ribosyl)ation: its role in inducible DNA amplification, and its correlation with the longevity of mammalian species, Exp. Clin. Immunogenet. 9 (1992) 230-240.
    • (1992) Exp. Clin. Immunogenet. , vol.9 , pp. 230-240
    • Bürkle, A.1    Grube, K.2    Küpper, J.-H.3
  • 65
    • 0028071501 scopus 로고
    • Effect of transfection of human poly(ADP-ribose)polymerase in Chinese hamster cells on mutagen resistance
    • [65] G. Fritz, B. Auer, B. Kaina, Effect of transfection of human poly(ADP-ribose)polymerase in Chinese hamster cells on mutagen resistance, Mutat. Res. 308 (1994) 127-133.
    • (1994) Mutat. Res. , vol.308 , pp. 127-133
    • Fritz, G.1    Auer, B.2    Kaina, B.3
  • 66
    • 0031417427 scopus 로고    scopus 로고
    • Functional overexpression of human poly(ADP-ribose) polymerase in transfected rat tumor cells
    • [66] F. Bernges, A. Bürkle, J.H. Kupper, W.J. Zeller, Functional overexpression of human poly(ADP-ribose) polymerase in transfected rat tumor cells, Carcinogenesis 18 (1997) 663-668.
    • (1997) Carcinogenesis , vol.18 , pp. 663-668
    • Bernges, F.1    Bürkle, A.2    Kupper, J.H.3    Zeller, W.J.4
  • 67
    • 0344418424 scopus 로고    scopus 로고
    • Overexpression of human poly(ADP-ribose) polymerase in transfected hamster cells leads to increased poly(ADP-ribosyl)ation and cellular sensitization to gamma irradiation
    • [67] L. van Gool, R. Meyer, E. Tobiasch, C. Cziepluch, J.C. Jauniaux, A. Mincheva, Licht, Overexpression of human poly(ADP-ribose) polymerase in transfected hamster cells leads to increased poly(ADP-ribosyl)ation and cellular sensitization to gamma irradiation, Eur. J. Biochem. 244 (1997) 15-20.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 15-20
    • Van Gool, L.1    Meyer, R.2    Tobiasch, E.3    Cziepluch, C.4    Jauniaux, J.C.5    Mincheva, A.6    Licht7
  • 68
    • 0028989014 scopus 로고
    • Trans-dominant inhibition of poly(ADP-ribosyl)ation sensitizes cells against gamma irradiation and N-methyl-N′-nitro-nitrosoguanidine but does not limit DNA replication of a polyoma virus replicon
    • [68] J.-H. Küpper, M. Müller, M.K. Jacobson, J. Tatsumi-Miyajima, D. Coyle, E.L. Jacobson, A. Bürkle, Trans-dominant inhibition of poly(ADP-ribosyl)ation sensitizes cells against gamma irradiation and N-methyl-N′-nitro-nitrosoguanidine but does not limit DNA replication of a polyoma virus replicon, Mol. Cell. Biol. 15 (1995) 3154-3163.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3154-3163
    • Küpper, J.-H.1    Müller, M.2    Jacobson, M.K.3    Tatsumi-Miyajima, J.4    Coyle, D.5    Jacobson, E.L.6    Bürkle, A.7
  • 70
    • 0029972260 scopus 로고    scopus 로고
    • 6-methylguanine-DNA methyltransferase (MGMT) and its relationship to cell death, mutation induction and chromosomal instability
    • 6-methylguanine-DNA methyltransferase (MGMT) and its relationship to cell death, mutation induction and chromosomal instability, Oncogene 13 (1996) 1927-1935.
    • (1996) Oncogene , vol.13 , pp. 1927-1935
    • Dosch, J.1    Kaina, B.2
  • 71
    • 0027500246 scopus 로고
    • Induction of nuclear accumulation of the tumor-suppressor protein, p53, by DNA damaging agents
    • [71] M. Fritsche, C. Haessler, G. Brandner, Induction of nuclear accumulation of the tumor-suppressor protein, p53, by DNA damaging agents, Oncogene 8 (1993) 307-318.
    • (1993) Oncogene , vol.8 , pp. 307-318
    • Fritsche, M.1    Haessler, C.2    Brandner, G.3
  • 72
    • 0023782359 scopus 로고
    • The c-Fos protein interacts with c-Jun/AP-1 to stimulate transcription of AP-1 responsive genes
    • [72] R. Chiu, W.J. Boyle, J. Meek, T. Smeal, M. Karin, The c-Fos protein interacts with c-Jun/AP-1 to stimulate transcription of AP-1 responsive genes, Cell 54 (1988) 541-552.
    • (1988) Cell , vol.54 , pp. 541-552
    • Chiu, R.1    Boyle, W.J.2    Meek, J.3    Smeal, T.4    Karin, M.5
  • 74
    • 0030802033 scopus 로고    scopus 로고
    • A general role for c-Fos in cellular protection against DNA damaging carcinogens and cytostatic drugs
    • [74] B. Kaina, S. Haas, H. Kappes, A general role for c-Fos in cellular protection against DNA damaging carcinogens and cytostatic drugs, Cancer Res. 57 (1997) 2721-2731.
    • (1997) Cancer Res. , vol.57 , pp. 2721-2731
    • Kaina, B.1    Haas, S.2    Kappes, H.3
  • 75
    • 0029030428 scopus 로고
    • C-Fos is involved in the cellular defence against the genotoxic effect of UV radiation
    • [75] S. Haas, B. Kaina, c-Fos is involved in the cellular defence against the genotoxic effect of UV radiation, Carcinogenesis 16 (1995) 985-991.
    • (1995) Carcinogenesis , vol.16 , pp. 985-991
    • Haas, S.1    Kaina, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.