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Volumn 451, Issue 1-2, 2000, Pages 39-51

Base excision repair in yeast and mammals

Author keywords

Base excision repair; Mammals; Yeast

Indexed keywords

DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA GLYCOSYLTRANSFERASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE;

EID: 0034733694     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0027-5107(00)00039-7     Document Type: Review
Times cited : (242)

References (104)
  • 2
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature. 362(6422):1993;709-715.
    • (1993) Nature , vol.362 , Issue.6422 , pp. 709-715
    • Lindahl, T.1
  • 6
    • 0029892791 scopus 로고    scopus 로고
    • DNA repair in eukaryotes
    • Wood R.D. DNA repair in eukaryotes. Annu. Rev. Biochem. 65:1996;135-167.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 135-167
    • Wood, R.D.1
  • 7
    • 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. 10:1997;713-732.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 713-732
    • Singer, B.1    Hang, B.2
  • 8
    • 0030727940 scopus 로고    scopus 로고
    • The yeast 8-Oxoguanine DNA glycosylase (Ogg1) contains a DNA deoxyribophosphodiesterase (dRPase) activity
    • Sandigursky M., Yacoub A., Kelley M.R., Xu Y., Franklin W.A., Deutsch W.A. The yeast 8-Oxoguanine DNA glycosylase (Ogg1) contains a DNA deoxyribophosphodiesterase (dRPase) activity. Nucleic Acids Res. 25(22):1997;4557-4561.
    • (1997) Nucleic Acids Res. , vol.25 , Issue.22 , pp. 4557-4561
    • Sandigursky, M.1    Yacoub, A.2    Kelley, M.R.3    Xu, Y.4    Franklin, W.A.5    Deutsch, W.A.6
  • 10
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision repair with purified human proteins-interaction between DNA polymerase β and the Xrcc1 protein
    • Kubota Y., Nash R.A., Klungland A., Schar P., Barnes D.E., Lindahl T. Reconstitution of DNA base excision repair with purified human proteins-interaction between DNA polymerase β and the Xrcc1 protein. EMBO J. 15(23):1996;6662-6670.
    • (1996) EMBO J. , vol.15 , Issue.23 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 12
    • 0031104841 scopus 로고    scopus 로고
    • The FEN-1 family of structure-specific nucleases in eukaryotic DNA replication, recombination and repair
    • Lieber M.R. The FEN-1 family of structure-specific nucleases in eukaryotic DNA replication, recombination and repair. Bioessays. 19(3):1997;233-240.
    • (1997) Bioessays , vol.19 , Issue.3 , pp. 233-240
    • Lieber, M.R.1
  • 13
    • 0025073229 scopus 로고
    • Molecular cloning, structure and expression of the yeast proliferating cell nuclear antigen gene
    • Bauer G.A., Burgers P.M. Molecular cloning, structure and expression of the yeast proliferating cell nuclear antigen gene. Nucl. Acids Res. 18(2):1990;261-265.
    • (1990) Nucl. Acids Res. , vol.18 , Issue.2 , pp. 261-265
    • Bauer, G.A.1    Burgers, P.M.2
  • 14
    • 0025748842 scopus 로고
    • Saccharomyces cerevisiae replication factor C: I. Purification and characterization of its ATPase activity
    • Yoder B.L., Burgers P.M. Saccharomyces cerevisiae replication factor C: I. Purification and characterization of its ATPase activity. J. Biol. Chem. 266(33):1991;22689-22697.
    • (1991) J. Biol. Chem. , vol.266 , Issue.33 , pp. 22689-22697
    • Yoder, B.L.1    Burgers, P.M.2
  • 15
    • 0027050566 scopus 로고
    • Isolation and analysis of the fission yeast gene encoding polymerase δ accessory protein PCNA
    • Waseem N.H., Labib K., Nurse P., Lane D.P. Isolation and analysis of the fission yeast gene encoding polymerase δ accessory protein PCNA. EMBO J. 11(13):1992;5111-5120.
    • (1992) EMBO J. , vol.11 , Issue.13 , pp. 5111-5120
    • Waseem, N.H.1    Labib, K.2    Nurse, P.3    Lane, D.P.4
  • 16
    • 0033180391 scopus 로고    scopus 로고
    • 3-methyladenine DNA glycosylases: Structure, function, and biological importance
    • Wyatt M.D., Allan J.M., Lau A.Y., Ellenberger T.E., Samson L.D. 3-methyladenine DNA glycosylases: structure, function, and biological importance. Bioessays. 21:1999;668-676.
    • (1999) Bioessays , vol.21 , pp. 668-676
    • Wyatt, M.D.1    Allan, J.M.2    Lau, A.Y.3    Ellenberger, T.E.4    Samson, L.D.5
  • 17
    • 0024110769 scopus 로고
    • MutM, a second mutator locus in Escherichia coli that generates GC to TA transversions
    • Cabrera M., Nghiem Y., Miller J. mutM, a second mutator locus in Escherichia coli that generates GC to TA transversions. J. Bacteriol. 170:1988;5405-5407.
    • (1988) J. Bacteriol. , vol.170 , pp. 5405-5407
    • Cabrera, M.1    Nghiem, Y.2    Miller, J.3
  • 18
    • 0023433565 scopus 로고
    • Formamidopyrimidine-DNA glycosylase of Escherichia coli: Cloning and sequencing of the fpg structural gene and overproduction of the protein
    • Boiteux S., O'Connor T.R., Laval J. Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein. EMBO J. 6:1987;3177-3183.
    • (1987) EMBO J. , vol.6 , pp. 3177-3183
    • Boiteux, S.1    O'Connor, T.R.2    Laval, J.3
  • 19
    • 0025871264 scopus 로고
    • MutM, a protein that prevents G:C to T:A transversions, is formamidopyrimidine-DNA glycosylase
    • Michaels M.L., Pham L., Cruz C., Miller J.H. MutM, a protein that prevents G:C to T:A transversions, is formamidopyrimidine-DNA glycosylase. Nucl. Acids Res. 19:1991;3629-3632.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 3629-3632
    • Michaels, M.L.1    Pham, L.2    Cruz, C.3    Miller, J.H.4
  • 20
    • 0026701365 scopus 로고
    • The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)
    • Michaels M.L., Miller J.H. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 174:1992;6321-6325.
    • (1992) J. Bacteriol. , vol.174 , pp. 6321-6325
    • Michaels, M.L.1    Miller, J.H.2
  • 21
    • 0029896229 scopus 로고    scopus 로고
    • Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine
    • van der Kemp P., Thomas D., Barbey R., de Olviera R., Boiteux S. Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine. Proc. Natl. Acad. Sci. U. S. A. 93:1996;5197-5202.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 5197-5202
    • Van Der Kemp, P.1    Thomas, D.2    Barbey, R.3    De Olviera, R.4    Boiteux, S.5
  • 22
    • 0030760240 scopus 로고    scopus 로고
    • Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage
    • Arai K., Morishita K., Shinmura K., Kohno T., Kim S.R., Nohmi T.et al. Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage. Oncogene. 14:1997;2857-2861.
    • (1997) Oncogene , vol.14 , pp. 2857-2861
    • Arai, K.1    Morishita, K.2    Shinmura, K.3    Kohno, T.4    Kim, S.R.5    Nohmi, T.6
  • 23
    • 0030912695 scopus 로고    scopus 로고
    • Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue
    • Auburtani H., Hippo Y., Ishida T., Takashima R., Matsuba C., Kodama T.et al. Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue. Cancer Res. 57:1997;2151-2156.
    • (1997) Cancer Res. , vol.57 , pp. 2151-2156
    • Auburtani, H.1    Hippo, Y.2    Ishida, T.3    Takashima, R.4    Matsuba, C.5    Kodama, T.6
  • 24
    • 0029814011 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of a Schizosaccharomyces pombe homologue of Escherichia coli endonuclease III
    • Roldan-Arjona T., Anselmino C., Lindahl T. Molecular cloning and functional analysis of a Schizosaccharomyces pombe homologue of Escherichia coli endonuclease III. Nucl. Acids Res. 24(17):1996;3307-3312.
    • (1996) Nucl. Acids Res. , vol.24 , Issue.17 , pp. 3307-3312
    • Roldan-Arjona, T.1    Anselmino, C.2    Lindahl, T.3
  • 25
    • 0030738194 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian 8-Oxoguanine DNA glycosylase
    • Rosenquist T.A., Zharkov D.O., Grollman A.P. Cloning and characterization of a mammalian 8-Oxoguanine DNA glycosylase. Proc. Natl. Acad. Sci. U. S. A. 94(14):1997;7429-7434.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , Issue.14 , pp. 7429-7434
    • Rosenquist, T.A.1    Zharkov, D.O.2    Grollman, A.P.3
  • 26
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOgg1, a human homolog of the Ogg1 gene of Saccharomyces cerevisiae
    • Radicella J.P., Dherin C., Desmaze C., Fox M.S., Boiteux S. Cloning and characterization of hOgg1, a human homolog of the Ogg1 gene of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 94(15):1997;8010-8015.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , Issue.15 , pp. 8010-8015
    • Radicella, J.P.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.4    Boiteux, S.5
  • 28
    • 0027171266 scopus 로고
    • Oxidants, antioxidants, and the degenerative diseases of aging
    • Ames B.N., Shigenaga M.K., Hagen T.M. Oxidants, antioxidants, and the degenerative diseases of aging. Proc. Natl. Acad. Sci. U. S. A. 90(17):1993;7915-7922.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , Issue.17 , pp. 7915-7922
    • Ames, B.N.1    Shigenaga, M.K.2    Hagen, T.M.3
  • 29
    • 0344759851 scopus 로고
    • Spontaneous cancer and its possible relationship to oxygen metabolism
    • Totter J.R. Spontaneous cancer and its possible relationship to oxygen metabolism. Proc. Natl. Acad. Sci. U. S. A. 77(4):1980;1763-1767.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , Issue.4 , pp. 1763-1767
    • Totter, J.R.1
  • 30
    • 1842371454 scopus 로고    scopus 로고
    • No evidence of microsatellite instability but frequent loss of heterozygosity in primary resected lung cancer
    • Pylkkanen L., Karjalainen A., Anttila S., Vainio H., Husgafvel-Pursiainen K. No evidence of microsatellite instability but frequent loss of heterozygosity in primary resected lung cancer. Environ. Mol. Mutagen. 30(2):1997;217-223.
    • (1997) Environ. Mol. Mutagen. , vol.30 , Issue.2 , pp. 217-223
    • Pylkkanen, L.1    Karjalainen, A.2    Anttila, S.3    Vainio, H.4    Husgafvel-Pursiainen, K.5
  • 31
    • 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. 63:1994;915-948.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 32
    • 0031296962 scopus 로고    scopus 로고
    • The apurinic-apyrimidinic endonuclease IV family of DNA repair enzymes
    • Ramotar D. The apurinic-apyrimidinic endonuclease IV family of DNA repair enzymes. Biochem. Cell Biol. 75:1997;327-336.
    • (1997) Biochem. Cell Biol. , vol.75 , pp. 327-336
    • Ramotar, D.1
  • 33
    • 0032980426 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae ETH1 gene, an inducible homolog of exonuclease III that provides resistance to DNA-damaging agents and limits spontaneous mutagenesis
    • Bennett R.A.O. The Saccharomyces cerevisiae ETH1 gene, an inducible homolog of exonuclease III that provides resistance to DNA-damaging agents and limits spontaneous mutagenesis. Mol. Cell. Biol. 19(3):1999;1800-1809.
    • (1999) Mol. Cell. Biol. , vol.19 , Issue.3 , pp. 1800-1809
    • Bennett, R.A.O.1
  • 34
    • 0031846463 scopus 로고    scopus 로고
    • Role of yeast Rth1 nuclease and its homologs in mutation avoidance, DNA repair, and DNA replication
    • Johnson R.E., Kovvali G.K., Prakash L., Prakash S. Role of yeast Rth1 nuclease and its homologs in mutation avoidance, DNA repair, and DNA replication. Curr. Genet. 34(1):1998;21-29.
    • (1998) Curr. Genet. , vol.34 , Issue.1 , pp. 21-29
    • Johnson, R.E.1    Kovvali, G.K.2    Prakash, L.3    Prakash, S.4
  • 35
    • 0025120572 scopus 로고
    • The enzymology of apurinic/apyrimidinic endonucleases
    • Doetsch P.W., Cunningham R.P. The enzymology of apurinic/apyrimidinic endonucleases. Mutat. Res. 236(2-3):1990;173-201.
    • (1990) Mutat. Res. , vol.236 , Issue.23 , pp. 173-201
    • Doetsch, P.W.1    Cunningham, R.P.2
  • 36
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer M.M., Ahern H., Xing D.X., Cunningham R.P., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 14(16):1995;4108-4120.
    • (1995) EMBO J. , vol.14 , Issue.16 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.X.3    Cunningham, R.P.4    Tainer, J.A.5
  • 38
    • 16044372779 scopus 로고    scopus 로고
    • Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli
    • Yamagata Y., Kato M., Odawara K., Tokuno Y., Nakashima Y., Matsushima N.et al. Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli. Cell. 86:1996;311-319.
    • (1996) Cell , vol.86 , pp. 311-319
    • Yamagata, Y.1    Kato, M.2    Odawara, K.3    Tokuno, Y.4    Nakashima, Y.5    Matsushima, N.6
  • 39
    • 0030220956 scopus 로고    scopus 로고
    • Cloning of a yeast 8-Oxoguanine DNA glycosylase reveals the existence of a base excision DNA repair protein superfamily
    • Nash H.M., Bruner S.D., Scharer O.D., Kawate T., Addona T.A., Sponner E.et al. Cloning of a yeast 8-Oxoguanine DNA glycosylase reveals the existence of a base excision DNA repair protein superfamily. Curr. Biol. 6(8):1996;968-980.
    • (1996) Curr. Biol. , vol.6 , Issue.8 , pp. 968-980
    • Nash, H.M.1    Bruner, S.D.2    Scharer, O.D.3    Kawate, T.4    Addona, T.A.5    Sponner, E.6
  • 40
    • 0030600463 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA encoding a 3-methyladenine DNA glycosylase from the fission yeast Schizosaccharomyces pombe
    • Memisoglu A., Samson L. Cloning and characterization of a cDNA encoding a 3-methyladenine DNA glycosylase from the fission yeast Schizosaccharomyces pombe. Gene. 177(1-2):1996;229-235.
    • (1996) Gene , vol.177 , Issue.12 , pp. 229-235
    • Memisoglu, A.1    Samson, L.2
  • 41
    • 0025864553 scopus 로고
    • Cellular role of yeast Apn1 apurinic endonuclease/3′-diesterase: Repair of oxidative and alkylation DNA damage and control of spontaneous mutation
    • Ramotar D., Popoff S.C., Gralla E.B., Demple B. Cellular role of yeast Apn1 apurinic endonuclease/3′-diesterase: repair of oxidative and alkylation DNA damage and control of spontaneous mutation. Mol. Cell Biol. 11:1991;4537-4544.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 4537-4544
    • Ramotar, D.1    Popoff, S.C.2    Gralla, E.B.3    Demple, B.4
  • 42
    • 0027477075 scopus 로고
    • In vivo evidence for endogenous DNA alkylation damage as a source of spontaneous mutation in eukaryotic cells
    • Xiao W., Samson L. In vivo evidence for endogenous DNA alkylation damage as a source of spontaneous mutation in eukaryotic cells. Proc. Natl. Acad. Sci. U. S. A. 90:1993;2117-2121.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2117-2121
    • Xiao, W.1    Samson, L.2
  • 44
    • 0032747178 scopus 로고    scopus 로고
    • Imbalanced base excision repair increases spontaneous mutation and alkylation sensitivity in Escherichia coli
    • Posnick L., Samson L. Imbalanced base excision repair increases spontaneous mutation and alkylation sensitivity in Escherichia coli. J. Bacteriol. 181:1999;6763-6771.
    • (1999) J. Bacteriol. , vol.181 , pp. 6763-6771
    • Posnick, L.1    Samson, L.2
  • 46
    • 0032518911 scopus 로고    scopus 로고
    • Release of normal bases from intact DNA by a native DNA repair enzyme
    • Berdal K.G., Johansen R.F., Seeberg E. Release of normal bases from intact DNA by a native DNA repair enzyme. EMBO J. 17(2):1998;363-367.
    • (1998) EMBO J. , vol.17 , Issue.2 , pp. 363-367
    • Berdal, K.G.1    Johansen, R.F.2    Seeberg, E.3
  • 47
    • 0027398114 scopus 로고
    • Increased resistance of the Chinese hamster mutant irs1 cells to monofunctional alkylating agents by transfection of the E. coli or mammalian N3-methyladenine-DNA glycosylase genes
    • Habraken Y., Laval F. Increased resistance of the Chinese hamster mutant irs1 cells to monofunctional alkylating agents by transfection of the E. coli or mammalian N3-methyladenine-DNA glycosylase genes. Mutat. Res., DNA Repair. 293:1993;187-195.
    • (1993) Mutat. Res., DNA Repair , vol.293 , pp. 187-195
    • Habraken, Y.1    Laval, F.2
  • 48
    • 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
    • Klungland A., Fairbairn L., Watson A.J., Margison G.P., Seeberg E. 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
  • 49
    • 0029012012 scopus 로고
    • Effect of alkyl-N-purine DNA glycosylase overexpression on cellular resistance to bifunctional alkylating agents
    • Bramson J., O'Connor T., Panasci L. Effect of alkyl-N-purine DNA glycosylase overexpression on cellular resistance to bifunctional alkylating agents. Biochem. Pharmacol. 50:1995;39-44.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 39-44
    • Bramson, J.1    O'Connor, T.2    Panasci, L.3
  • 50
    • 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
    • Ibeanu G., Hartenstein B., Dunn W.C., Chang L.Y., Hofmann E., Coquerelle T.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 alkylating agents in Chinese hamster ovary cells. Carcinogenesis. 13(11):1992;1989-1995.
    • (1992) Carcinogenesis , vol.13 , Issue.11 , pp. 1989-1995
    • Ibeanu, G.1    Hartenstein, B.2    Dunn, W.C.3    Chang, L.Y.4    Hofmann, E.5    Coquerelle, T.6
  • 51
    • 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 imbalanced DNA repair
    • Coquerelle T., Dosch J., Kaina B. 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 imbalanced 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
  • 52
    • 0004732033 scopus 로고
    • Cloning a eukaryotic DNA glycosylase repair gene by the suppression of a DNA repair defect in Escherichia coli
    • Chen J., Derfler B., Maskati A., Samson L. Cloning a eukaryotic DNA glycosylase repair gene by the suppression of a DNA repair defect in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 86(20):1989;7961-7965.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , Issue.20 , pp. 7961-7965
    • Chen, J.1    Derfler, B.2    Maskati, A.3    Samson, L.4
  • 53
    • 0020057737 scopus 로고
    • Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents
    • Karran P., Hjelmgren T., Lindahl T. Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents. Nature. 296(5859):1982;770-773.
    • (1982) Nature , vol.296 , Issue.5859 , pp. 770-773
    • Karran, P.1    Hjelmgren, T.2    Lindahl, T.3
  • 54
    • 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
    • Engelward B.P., Dreslin A., Christensen J., Huszar D., Kurahara C., Samson L. Repair-deficient 3-methyladenine DNA glycosylase homozygous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing. EMBO J. 15(4):1996;945-952.
    • (1996) EMBO J. , vol.15 , Issue.4 , pp. 945-952
    • Engelward, B.P.1    Dreslin, A.2    Christensen, J.3    Huszar, D.4    Kurahara, C.5    Samson, L.6
  • 55
    • 0034031405 scopus 로고    scopus 로고
    • Contribution of base excision repair, nucleotide excision repair and DNA recombination to alkylation resistance of the fission yeast Schizosaccharomyces pombe
    • Memisoglu A., Samson L. Contribution of base excision repair, nucleotide excision repair and DNA recombination to alkylation resistance of the fission yeast Schizosaccharomyces pombe. J. Bacteriol. 182:2000;2104-2112.
    • (2000) J. Bacteriol. , vol.182 , pp. 2104-2112
    • Memisoglu, A.1    Samson, L.2
  • 56
    • 0028954628 scopus 로고
    • Recombinational rescue of the stalled DNA replication fork: A model based on analysis of an Escherichia coli strain with a chromosome region difficult to replicate
    • Horiuchi T., Fujimura Y. Recombinational rescue of the stalled DNA replication fork: a model based on analysis of an Escherichia coli strain with a chromosome region difficult to replicate. J. Bacteriol. 177:1995;783-791.
    • (1995) J. Bacteriol. , vol.177 , pp. 783-791
    • Horiuchi, T.1    Fujimura, Y.2
  • 58
    • 0030004207 scopus 로고    scopus 로고
    • Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxididative DNA damage
    • Slupska M.M., Baikalov C., Luther W.M., Chiang J., Wei Y., Miller J. Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxididative DNA damage. J. Bacteriol. 178:1996;3885-3892.
    • (1996) J. Bacteriol. , vol.178 , pp. 3885-3892
    • Slupska, M.M.1    Baikalov, C.2    Luther, W.M.3    Chiang, J.4    Wei, Y.5    Miller, J.6
  • 59
    • 0027368923 scopus 로고
    • Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis
    • Sakumi K., Furichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H.et al. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 268(31):1993;23524-23530.
    • (1993) J. Biol. Chem. , vol.268 , Issue.31 , pp. 23524-23530
    • Sakumi, K.1    Furichi, M.2    Tsuzuki, T.3    Kakuma, T.4    Kawabata, S.5    Maki, H.6
  • 60
    • 0032568337 scopus 로고    scopus 로고
    • Repair of oxidatively damaged guanine in Saccharomyces cerevisiae by an alternative pathway
    • Bruner S.D., Nash H.M., Lane W.S., Verdine G.L. Repair of oxidatively damaged guanine in Saccharomyces cerevisiae by an alternative pathway. Curr. Biol. 8(7):1998;393-403.
    • (1998) Curr. Biol. , vol.8 , Issue.7 , pp. 393-403
    • Bruner, S.D.1    Nash, H.M.2    Lane, W.S.3    Verdine, G.L.4
  • 61
    • 0017236583 scopus 로고
    • An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA
    • Radman M. An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA. J. Biol. Chem. 251(5):1976;1438-1445.
    • (1976) J. Biol. Chem. , vol.251 , Issue.5 , pp. 1438-1445
    • Radman, M.1
  • 62
    • 0024328839 scopus 로고
    • UV-induced pyrimidine hydrates in DNA are repaired by bacterial and mammalian DNA glycosylase activities
    • Boorstein R.J., Hilbert T.P., Cadet J., Cunningham R.P., Teebor G.W. UV-induced pyrimidine hydrates in DNA are repaired by bacterial and mammalian DNA glycosylase activities. Biochemistry. 28(15):1989;6164-6170.
    • (1989) Biochemistry , vol.28 , Issue.15 , pp. 6164-6170
    • Boorstein, R.J.1    Hilbert, T.P.2    Cadet, J.3    Cunningham, R.P.4    Teebor, G.W.5
  • 63
    • 0021331957 scopus 로고
    • DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli
    • Breimer L.H., Lindahl T. DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli. J. Biol. Chem. 259(9):1984;5543-5548.
    • (1984) J. Biol. Chem. , vol.259 , Issue.9 , pp. 5543-5548
    • Breimer, L.H.1    Lindahl, T.2
  • 64
    • 0028305721 scopus 로고
    • New substrates for old enzymes. 5-Hydroxy-2′-deoxycytidine and 5-hydroxy-2′-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNA N-glycosylase
    • Hatahet Z., Kow Y.W., Purmal A.A., Cunningham R.P., Wallace S.S. New substrates for old enzymes. 5-Hydroxy-2′-deoxycytidine and 5-hydroxy-2′-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNA N-glycosylase. J. Biol. Chem. 269(29):1994;18814-18820.
    • (1994) J. Biol. Chem. , vol.269 , Issue.29 , pp. 18814-18820
    • Hatahet, Z.1    Kow, Y.W.2    Purmal, A.A.3    Cunningham, R.P.4    Wallace, S.S.5
  • 65
    • 0343879974 scopus 로고
    • Endonuclease III (nth) mutants of Escherichia coli
    • Cunningham R.P., Weiss B. Endonuclease III (nth) mutants of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 82(2):1985;474-478.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , Issue.2 , pp. 474-478
    • Cunningham, R.P.1    Weiss, B.2
  • 66
    • 0344734089 scopus 로고    scopus 로고
    • Substrate specificity of Schizosaccharomyces pombe Nth protein for products of oxidative DNA damage
    • Karahalil B., Teresa R.A., Dizdaroglu M. Substrate specificity of Schizosaccharomyces pombe Nth protein for products of oxidative DNA damage. Biochemistry. 37:1998;590-595.
    • (1998) Biochemistry , vol.37 , pp. 590-595
    • Karahalil, B.1    Teresa, R.A.2    Dizdaroglu, M.3
  • 67
    • 0029743301 scopus 로고    scopus 로고
    • Base excision of oxidative purine and pyrimidine DNA damage in Saccharomyces cerevisiae by a DNA glycosylase with sequence similarity to endonuclease III from Escherichia coli
    • Eide L., Bjoras M., Pirovano M., Alseth I., Berdal K.G., Seeberg E. Base excision of oxidative purine and pyrimidine DNA damage in Saccharomyces cerevisiae by a DNA glycosylase with sequence similarity to endonuclease III from Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 93(20):1996;10735-10740.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , Issue.20 , pp. 10735-10740
    • Eide, L.1    Bjoras, M.2    Pirovano, M.3    Alseth, I.4    Berdal, K.G.5    Seeberg, E.6
  • 68
    • 0031046689 scopus 로고    scopus 로고
    • Purification, characterization, gene cloning, and expression of Saccharomyces cerevisiae redoxyendonuclease, a homolog of Escherichia coli endonuclease III
    • Augeri L., Lee Y.M., Barton A.B., Doetsch P.W. Purification, characterization, gene cloning, and expression of Saccharomyces cerevisiae redoxyendonuclease, a homolog of Escherichia coli endonuclease III. Biochemistry. 36(4):1997;721-729.
    • (1997) Biochemistry , vol.36 , Issue.4 , pp. 721-729
    • Augeri, L.1    Lee, Y.M.2    Barton, A.B.3    Doetsch, P.W.4
  • 69
    • 0001409610 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae possesses two functional homologues of Escherichia coli endonuclease III
    • You H.J., Swanson R.L., Doetsch P.W. Saccharomyces cerevisiae possesses two functional homologues of Escherichia coli endonuclease III. Biochemistry. 37(17):1998;6033-6040.
    • (1998) Biochemistry , vol.37 , Issue.17 , pp. 6033-6040
    • You, H.J.1    Swanson, R.L.2    Doetsch, P.W.3
  • 70
    • 0032960862 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae homologues of endonuclease III from Escherichia coli, Ntg1 and Ntg2, are both required for efficient repair of spontaneous and induced oxidative DNA damage in yeast
    • Alseth I., Eide L., Pirovano M., Rognes T., Seeberg E., Bjoras M. The Saccharomyces cerevisiae homologues of endonuclease III from Escherichia coli, Ntg1 and Ntg2, are both required for efficient repair of spontaneous and induced oxidative DNA damage in yeast. Mol. Cell. Biol. 19(5):1999;3779-3787.
    • (1999) Mol. Cell. Biol. , vol.19 , Issue.5 , pp. 3779-3787
    • Alseth, I.1    Eide, L.2    Pirovano, M.3    Rognes, T.4    Seeberg, E.5    Bjoras, M.6
  • 72
    • 0032401931 scopus 로고    scopus 로고
    • Substrate specificities of the Ntg1 and Ntg2 proteins of Saccharomyces cerevisiae for oxidized DNA bases are not identical
    • Senturker S., Auffret van der Kemp P., You H.J., Doetsch P.W., Dizdaroglu M., Boiteux S. Substrate specificities of the Ntg1 and Ntg2 proteins of Saccharomyces cerevisiae for oxidized DNA bases are not identical. Nucl. Acids Res. 26:1998;5270-5276.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 5270-5276
    • Senturker, S.1    Auffret Van Der Kemp, P.2    You, H.J.3    Doetsch, P.W.4    Dizdaroglu, M.5    Boiteux, S.6
  • 73
    • 0032913570 scopus 로고    scopus 로고
    • Overlapping specificities of base excision repair, nucleotide excision repair, recombination, and translesion synthesis pathways for DNA base damage in Saccharomyces cerevisiae
    • Swanson R.L., Morey N.J., Doetsch P.W., Jinks-Robertson S. Overlapping specificities of base excision repair, nucleotide excision repair, recombination, and translesion synthesis pathways for DNA base damage in Saccharomyces cerevisiae. Mol. Cell. Biol. 19(4):1999;2929-2935.
    • (1999) Mol. Cell. Biol. , vol.19 , Issue.4 , pp. 2929-2935
    • Swanson, R.L.1    Morey, N.J.2    Doetsch, P.W.3    Jinks-Robertson, S.4
  • 75
    • 0028059099 scopus 로고
    • Deletion of a DNA polymerase β gene segment in T cells using cell type-specific gene targeting
    • Gu H., Marth J.D., Orban P.C., Mossmann H., Rajewsky K. Deletion of a DNA polymerase β gene segment in T cells using cell type-specific gene targeting. Science. 265(5168):1994;103-106.
    • (1994) Science , vol.265 , Issue.5168 , pp. 103-106
    • Gu, H.1    Marth, J.D.2    Orban, P.C.3    Mossmann, H.4    Rajewsky, K.5
  • 77
    • 0026541430 scopus 로고
    • Mammalian DNA polymerase β can substitute for DNA polymerase I during DNA replication in Escherichia coli
    • Sweasy J.B., Loeb L.A. Mammalian DNA polymerase β can substitute for DNA polymerase I during DNA replication in Escherichia coli. J. Biol. Chem. 267(3):1992;1407-1410.
    • (1992) J. Biol. Chem. , vol.267 , Issue.3 , pp. 1407-1410
    • Sweasy, J.B.1    Loeb, L.A.2
  • 78
    • 0029064878 scopus 로고
    • Characterization of DNA polymerase β mutants with amino acid substitutions located in the C-terminal portion of the enzyme
    • Sweasy J.B., Yoon M.S. Characterization of DNA polymerase β mutants with amino acid substitutions located in the C-terminal portion of the enzyme. Mol. Gen. Genet. 248(2):1995;217-224.
    • (1995) Mol. Gen. Genet. , vol.248 , Issue.2 , pp. 217-224
    • Sweasy, J.B.1    Yoon, M.S.2
  • 79
    • 0027158355 scopus 로고
    • Detection and characterization of mammalian DNA polymerase β mutants by functional complementation in Escherichia coli
    • Sweasy J.B., Loeb L.A. Detection and characterization of mammalian DNA polymerase β mutants by functional complementation in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 90(10):1993;4626-4630.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , Issue.10 , pp. 4626-4630
    • Sweasy, J.B.1    Loeb, L.A.2
  • 80
    • 0030067386 scopus 로고    scopus 로고
    • Dominant negative rat DNA polymerase β mutants interfere with base excision repair in Saccharomyces cerevisiae
    • Clairmont C.A., Sweasy J.B. Dominant negative rat DNA polymerase β mutants interfere with base excision repair in Saccharomyces cerevisiae. J. Bacteriol. 178(3):1996;656-661.
    • (1996) J. Bacteriol. , vol.178 , Issue.3 , pp. 656-661
    • Clairmont, C.A.1    Sweasy, J.B.2
  • 81
    • 0031979307 scopus 로고    scopus 로고
    • The Pol β-14 dominant negative rat DNA polymerase β mutator mutant commits errors during the gap-filling step of base excision repair in Saccharomyces cerevisiae
    • Clairmont C.A., Sweasy J.B. The Pol β-14 dominant negative rat DNA polymerase β mutator mutant commits errors during the gap-filling step of base excision repair in Saccharomyces cerevisiae. J. Bacteriol. 180(9):1998;2292-2297.
    • (1998) J. Bacteriol. , vol.180 , Issue.9 , pp. 2292-2297
    • Clairmont, C.A.1    Sweasy, J.B.2
  • 84
    • 0026671855 scopus 로고
    • DNA polymerase β mutations in human colorectal cancer
    • Wang L., Patel U., Ghosh L., Banerjee S. DNA polymerase β mutations in human colorectal cancer. Cancer Res. 52(17):1992;4824-4827.
    • (1992) Cancer Res. , vol.52 , Issue.17 , pp. 4824-4827
    • Wang, L.1    Patel, U.2    Ghosh, L.3    Banerjee, S.4
  • 85
    • 0030885254 scopus 로고    scopus 로고
    • A variant of DNA polymerase β acts as a dominant negative mutant
    • Bhattacharyya N., Banerjee S. A variant of DNA polymerase β acts as a dominant negative mutant. Proc. Natl. Acad. Sci. 94(19):1997;10324-10329.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , Issue.19 , pp. 10324-10329
    • Bhattacharyya, N.1    Banerjee, S.2
  • 86
    • 0024969622 scopus 로고
    • Molecular cloning and primary structure of the uracil-DNA-glycosylase gene from Saccharomyces cerevisiae
    • Percival K.J., Klein M.B., Burgers P.M. Molecular cloning and primary structure of the uracil-DNA-glycosylase gene from Saccharomyces cerevisiae. J. Biol. Chem. 264(5):1989;2593-2598.
    • (1989) J. Biol. Chem. , vol.264 , Issue.5 , pp. 2593-2598
    • Percival, K.J.1    Klein, M.B.2    Burgers, P.M.3
  • 87
    • 0024414264 scopus 로고
    • Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme
    • Olsen L.C., Aasland R., Wittwer C.U., Krokan H.E., Helland D.E. Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme. EMBO J. 8(10):1989;3121-3125.
    • (1989) EMBO J. , vol.8 , Issue.10 , pp. 3121-3125
    • Olsen, L.C.1    Aasland, R.2    Wittwer, C.U.3    Krokan, H.E.4    Helland, D.E.5
  • 88
    • 0025108951 scopus 로고
    • Isolation and structure of a cDNA expressing a mammalian 3-methyladenine-DNA glycosylase
    • O'Connor T.R., Laval F. Isolation and structure of a cDNA expressing a mammalian 3-methyladenine-DNA glycosylase. EMBO J. 9(10):1990;3337-3342.
    • (1990) EMBO J. , vol.9 , Issue.10 , pp. 3337-3342
    • O'Connor, T.R.1    Laval, F.2
  • 89
    • 0025990209 scopus 로고
    • Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16
    • Samson L., Derfler B., Boosalis M., Call K. Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16. Proc. Natl. Acad. Sci. U. S. A. 88(20):1991;9127-9131.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , Issue.20 , pp. 9127-9131
    • Samson, L.1    Derfler, B.2    Boosalis, M.3    Call, K.4
  • 90
    • 0025949662 scopus 로고
    • Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase
    • Chakravarti D., Ibeanu G.C., Tano K., Mitra S. Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase. J. Biol. Chem. 266(24):1991;15710-15715.
    • (1991) J. Biol. Chem. , vol.266 , Issue.24 , pp. 15710-15715
    • Chakravarti, D.1    Ibeanu, G.C.2    Tano, K.3    Mitra, S.4
  • 91
    • 15844419144 scopus 로고    scopus 로고
    • Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase
    • Neddermann P., Gallinari P., Lettieri T., Schmid D., Truong O., Hsuan J.J.et al. Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase. J. Biol. Chem. 271(22):1996;12767-12774.
    • (1996) J. Biol. Chem. , vol.271 , Issue.22 , pp. 12767-12774
    • Neddermann, P.1    Gallinari, P.2    Lettieri, T.3    Schmid, D.4    Truong, O.5    Hsuan, J.J.6
  • 92
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: Definition of a family of DNA repair enzymes
    • Demple B., Herman T., Chen D.S. Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. Proc. Natl. Acad. Sci. U. S. A. 88(24):1991;11450-11454.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , Issue.24 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 93
    • 0025936119 scopus 로고
    • Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants
    • Robson C.N., Hickson I.D. Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants. Nucleic Acids Res. 19(20):1991;5519-5523.
    • (1991) Nucleic Acids Res. , vol.19 , Issue.20 , pp. 5519-5523
    • Robson, C.N.1    Hickson, I.D.2
  • 94
    • 0026683715 scopus 로고
    • CDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III
    • Seki S., Hatsushika M., Watanabe S., Akiyama K., Nagao K., Tsutsui K. cDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III. Biochim. Biophys. Acta. 1131(3):1992;287-299.
    • (1992) Biochim. Biophys. Acta , vol.1131 , Issue.3 , pp. 287-299
    • Seki, S.1    Hatsushika, M.2    Watanabe, S.3    Akiyama, K.4    Nagao, K.5    Tsutsui, K.6
  • 95
    • 0032190633 scopus 로고    scopus 로고
    • Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites
    • Johnson R.E., Torres-Ramos C.A., Izumi T., Mitra S., Prakash S., Prakash L. Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites. Genes Dev. 12:1998;3137-3143.
    • (1998) Genes Dev. , vol.12 , pp. 3137-3143
    • Johnson, R.E.1    Torres-Ramos, C.A.2    Izumi, T.3    Mitra, S.4    Prakash, S.5    Prakash, L.6
  • 96
    • 0025324303 scopus 로고
    • Yeast structural gene (APN1) for the major apurinic endonuclease: Homology to Escherichia coli endonuclease IV
    • Popoff S.C., Spira A.I., Johnson A.W., Demple B. Yeast structural gene (APN1) for the major apurinic endonuclease: homology to Escherichia coli endonuclease IV. Proc. Natl. Acad. Sci. U. S. A. 87(11):1990;4193-4197.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , Issue.11 , pp. 4193-4197
    • Popoff, S.C.1    Spira, A.I.2    Johnson, A.W.3    Demple, B.4
  • 97
    • 0025202114 scopus 로고
    • Molecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange
    • Thompson L.H., Brookman K.W., Jones N.J., Allen S.A., Carrano A.V. Molecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange. Mol. Cell. Biol. 10(12):1990;6160-6171.
    • (1990) Mol. Cell. Biol. , vol.10 , Issue.12 , pp. 6160-6171
    • Thompson, L.H.1    Brookman, K.W.2    Jones, N.J.3    Allen, S.A.4    Carrano, A.V.5
  • 98
    • 0032100860 scopus 로고    scopus 로고
    • Mammalian base excision repair and DNA polymerase β
    • Wilson S.H. Mammalian base excision repair and DNA polymerase β Mutat. Res. 407(3):1998;203-215.
    • (1998) Mutat. Res. , vol.407 , Issue.3 , pp. 203-215
    • Wilson, S.H.1
  • 99
    • 0030825134 scopus 로고    scopus 로고
    • The roles of the eukaryotic DNA polymerases in DNA repair synthesis
    • Budd M.E., Campbell J.L. The roles of the eukaryotic DNA polymerases in DNA repair synthesis. Mutat. Res. 384(3):1997;157-167.
    • (1997) Mutat. Res. , vol.384 , Issue.3 , pp. 157-167
    • Budd, M.E.1    Campbell, J.L.2
  • 101
    • 0025900035 scopus 로고
    • The 3′ to 5′ exonuclease activity located in the DNA polymerase δ subunit of Saccharomyces cerevisiae is required for accurate replication
    • Simon M., Giot L., Faye G. The 3′ to 5′ exonuclease activity located in the DNA polymerase δ subunit of Saccharomyces cerevisiae is required for accurate replication. EMBO J. 10(8):1991;2165-2170.
    • (1991) EMBO J. , vol.10 , Issue.8 , pp. 2165-2170
    • Simon, M.1    Giot, L.2    Faye, G.3
  • 102
    • 0031596849 scopus 로고    scopus 로고
    • DNA polymerase ε encoded by cdc20+ is required for chromosomal DNA replication in the fission yeast Schizosaccharomyces pombe
    • Sugino A., Ohara T., Sebastian J., Nakashima N., Araki H. DNA polymerase ε encoded by cdc20+ is required for chromosomal DNA replication in the fission yeast Schizosaccharomyces pombe. Genes Cells. 3(2):1998;99-110.
    • (1998) Genes Cells , vol.3 , Issue.2 , pp. 99-110
    • Sugino, A.1    Ohara, T.2    Sebastian, J.3    Nakashima, N.4    Araki, H.5
  • 104
    • 0031972353 scopus 로고    scopus 로고
    • Structure and function of mammalian DNA ligases
    • Tomkinson A.E., Mackey Z.B. Structure and function of mammalian DNA ligases. Mutat. Res., DNA Repair. 407(1):1998;1-9.
    • (1998) Mutat. Res., DNA Repair , vol.407 , Issue.1 , pp. 1-9
    • Tomkinson, A.E.1    MacKey, Z.B.2


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