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Volumn 402, Issue 1-2, 1998, Pages 93-102

Antimutagenic role of base-excision repair enzymes upon free radical- induced DNA damage

Author keywords

lyase; C8 oxoguanine; Ethenobase; Fpg protein; OGG1 protein

Indexed keywords

ANTIMUTAGENIC AGENT;

EID: 0032543425     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0027-5107(97)00286-8     Document Type: Conference Paper
Times cited : (87)

References (121)
  • 1
    • 0026589375 scopus 로고
    • Generation of single-nucleotide repair patches following excision of uracil residues from DNA
    • [1] G. Dianov, A. Price, T. Lindahl, Generation of single-nucleotide repair patches following excision of uracil residues from DNA, Mol. Cell. Biol. 12 (1992) 1605-1612.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1605-1612
    • Dianov, G.1    Price, A.2    Lindahl, T.3
  • 3
    • 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)
    • [3] A. Klungland, T. Lindahl, Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1), EMBO J. 16 (1997) 3341-3348.
    • (1997) EMBO J. , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 4
    • 0023277174 scopus 로고
    • Oxygen-derived radicals: A link between reperfusion injury and inflammation
    • [4] J.M. McCord, Oxygen-derived radicals: a link between reperfusion injury and inflammation, Fed. Proc. 46 (1987) 2402-2406.
    • (1987) Fed. Proc. , vol.46 , pp. 2402-2406
    • McCord, J.M.1
  • 5
    • 0026093495 scopus 로고
    • An over review of the relationship between oxidative stress and chemical carcinogenesis
    • [5] M.A. Trus, T.W. Kensler, An over review of the relationship between oxidative stress and chemical carcinogenesis, Free Radic. Biol. Med. 10 (1991) 201-209.
    • (1991) Free Radic. Biol. Med. , vol.10 , pp. 201-209
    • Trus, M.A.1    Kensler, T.W.2
  • 6
    • 0019938797 scopus 로고
    • Production of superoxide, hydrogen peroxide and hydroxyl radicals by phagocytic cells: A cause of chronic inflammatory disease?
    • [6] B. Halliwell, Production of superoxide, hydrogen peroxide and hydroxyl radicals by phagocytic cells: a cause of chronic inflammatory disease?, Cell Biol. Int. Rep. 6 (1982) 529-542.
    • (1982) Cell Biol. Int. Rep. , vol.6 , pp. 529-542
    • Halliwell, B.1
  • 7
    • 0029055175 scopus 로고
    • Oxidative processes and antioxidative defence mechanisms in the aging brain
    • [7] R.J. Reiter, Oxidative processes and antioxidative defence mechanisms in the aging brain, FASEB J. 9 (1995) 526-533.
    • (1995) FASEB J. , vol.9 , pp. 526-533
    • Reiter, R.J.1
  • 8
    • 0030839865 scopus 로고    scopus 로고
    • Oxidative decay of DNA
    • [8] K.B. Beckman, B.N. Ames, Oxidative decay of DNA, J. Biol. Chem. 272 (1997) 19633-19636.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19633-19636
    • Beckman, K.B.1    Ames, B.N.2
  • 9
    • 0002693188 scopus 로고    scopus 로고
    • Repair of oxidized purines in DNA
    • I.D. Hickson (Ed.), Springer-Verlag, Heidelberg, Germany
    • [9] S. Boiteux, J. Laval, Repair of oxidized purines in DNA, in: Base Excision Repair of DNA Damage, I.D. Hickson (Ed.), Springer-Verlag, Heidelberg, Germany, 1997, pp. 31-40.
    • (1997) Base Excision Repair of DNA Damage , pp. 31-40
    • Boiteux, S.1    Laval, J.2
  • 10
    • 0029888579 scopus 로고    scopus 로고
    • Non-linear accumulation of 8-hydroxy-2′-deoxyguanosine, a marker of oxidized DNA damage, during aging
    • [10] T. Kaneko, S. Tahara, M. Matsuo, Non-linear accumulation of 8-hydroxy-2′-deoxyguanosine, a marker of oxidized DNA damage, during aging, Mutat. Res. 316 (1996) 277-285.
    • (1996) Mutat. Res. , vol.316 , pp. 277-285
    • Kaneko, T.1    Tahara, S.2    Matsuo, M.3
  • 11
    • 0022556814 scopus 로고
    • Hydroxylation of guanine in nucleosides and DNA at the C-8 position by heated glucose and oxygen radical-forming agents
    • [11] H. Kasai, S. Nishimura, Hydroxylation of guanine in nucleosides and DNA at the C-8 position by heated glucose and oxygen radical-forming agents, Environ. Health Perspect. 67 (1986) 111-116.
    • (1986) Environ. Health Perspect. , vol.67 , pp. 111-116
    • Kasai, H.1    Nishimura, S.2
  • 12
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • [12] J.M. Imlay, S. Linn, DNA damage and oxygen radical toxicity, Science 240 (1988) 1302-1308.
    • (1988) Science , vol.240 , pp. 1302-1308
    • Imlay, J.M.1    Linn, S.2
  • 13
    • 0028362156 scopus 로고
    • Suppression of hydroxyl radical reactions in biological systems: Considerations based on competition kinetics
    • [13] C. von Sonntag, H.P. Schuchmann, Suppression of hydroxyl radical reactions in biological systems: considerations based on competition kinetics, Meth. Enzymol. 233 (1994) 47-56.
    • (1994) Meth. Enzymol. , vol.233 , pp. 47-56
    • Von Sonntag, C.1    Schuchmann, H.P.2
  • 14
    • 0025835151 scopus 로고
    • Formation of 8-hydroxy(deoxy)guanosine and generation of strand breaks at guanine residues in DNA by singlet oxygen
    • [14] T.P. Devasagayam, S. Steenken, M.S. Obendorf, W.A. Schulz, H. Sies, Formation of 8-hydroxy(deoxy)guanosine and generation of strand breaks at guanine residues in DNA by singlet oxygen, Biochemistry 30 (1991) 6283-6289.
    • (1991) Biochemistry , vol.30 , pp. 6283-6289
    • Devasagayam, T.P.1    Steenken, S.2    Obendorf, M.S.3    Schulz, W.A.4    Sies, H.5
  • 16
    • 0021957619 scopus 로고
    • Radiation-induced decomposition of the purine bases within DNA and related model compounds
    • [16] J. Cadet, M. Berger, Radiation-induced decomposition of the purine bases within DNA and related model compounds, Int. J. Radiat. Biol. 47 (1985) 127-143.
    • (1985) Int. J. Radiat. Biol. , vol.47 , pp. 127-143
    • Cadet, J.1    Berger, M.2
  • 17
    • 0017556605 scopus 로고
    • Isolation of 2-deoxy-D-erythro-pentonic acid from an alkali-labile site in gamma-irradiated DNA
    • [17] M. Dizdaroglu, D. Schulte-Frohlinde, C. von Sonntag, Isolation of 2-deoxy-D-erythro-pentonic acid from an alkali-labile site in gamma-irradiated DNA, Int. J. Radiat. Biol. 32 (1977) 481-483.
    • (1977) Int. J. Radiat. Biol. , vol.32 , pp. 481-483
    • Dizdaroglu, M.1    Schulte-Frohlinde, D.2    Von Sonntag, C.3
  • 18
    • 0019848907 scopus 로고
    • Bleomycin-induced strand-scission of DNA. Mechanism of deoxyribose cleavage
    • [18] L. Giloni, M. Takeshita, F. Johnson, C. Iden, A.P. Grollman, Bleomycin-induced strand-scission of DNA. Mechanism of deoxyribose cleavage, J. Biol. Chem. 256 (1981) 8606-8615.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8606-8615
    • Giloni, L.1    Takeshita, M.2    Johnson, F.3    Iden, C.4    Grollman, A.P.5
  • 19
    • 0021111515 scopus 로고
    • Gamma ray induced deoxyribonucleic acid strand breaks. 3′ glycolate termini
    • [19] W.D. Henner, L.O. Rodriguez, S.M. Hecht, W.A. Haseltine, Gamma ray induced deoxyribonucleic acid strand breaks. 3′ glycolate termini, J. Biol. Chem. 258 (1983) 711-713.
    • (1983) J. Biol. Chem. , vol.258 , pp. 711-713
    • Henner, W.D.1    Rodriguez, L.O.2    Hecht, S.M.3    Haseltine, W.A.4
  • 20
    • 0028690470 scopus 로고
    • DNA adducts of α,β-unsaturated aldehydes and dicarbonyl compounds
    • K. Hemminki, A. Dipple, D.E.G. Shuker, F.F. Kadlubar, D. SegerbŠck, H. Bartsch (Eds.), LARC Scientific Publications, No. 125, Lyon, France
    • [20] L.J. Marnett, DNA adducts of α,β-unsaturated aldehydes and dicarbonyl compounds, in: K. Hemminki, A. Dipple, D.E.G. Shuker, F.F. Kadlubar, D. SegerbŠck, H. Bartsch (Eds.), DNA Adducts: Identification and Biological Significance, LARC Scientific Publications, No. 125, Lyon, France, 1994, pp. 151-163.
    • (1994) DNA Adducts: Identification and Biological Significance , pp. 151-163
    • Marnett, L.J.1
  • 21
    • 0028986148 scopus 로고
    • Formation of 1,N6-ethenoadenine and 3,N4-ethenocytosine by lipid peroxidation products and nucleic acid bases
    • [21] F.E. El-Ghissassi, A. Barbin, J. Nair, H. Bartsch, Formation of 1,N6-ethenoadenine and 3,N4-ethenocytosine by lipid peroxidation products and nucleic acid bases, Chem. Res. Toxicol. 8 (1995) 278-283.
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 278-283
    • El-Ghissassi, F.E.1    Barbin, A.2    Nair, J.3    Bartsch, H.4
  • 22
    • 0023433565 scopus 로고
    • Formamidopyrimidine-DNA glycosylase of Escherichia coli: Cloning and sequencing of the fpg structural gene and overproduction of the protein
    • [22] S. Boiteux, T. O'Connor, J. Laval, 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.2    Laval, J.3
  • 23
    • 0025013468 scopus 로고
    • Physiological properties and repair of apurinic/apyrimidinic sites and imidazole ring-opened guanines in DNA
    • [23] J. Laval, S. Boiteux, T.R. O'Connor, Physiological properties and repair of apurinic/apyrimidinic sites and imidazole ring-opened guanines in DNA, Mutat. Res. 233 (1990) 73-79.
    • (1990) Mutat. Res. , vol.233 , pp. 73-79
    • Laval, J.1    Boiteux, S.2    O'Connor, T.R.3
  • 24
    • 0027250070 scopus 로고
    • Properties and biological functions of the NTH and FPG proteins of Escherichia coli: Two DNA glycosylases that repair oxidative damage in DNA
    • [24] S. Boiteux, Properties and biological functions of the NTH and FPG proteins of Escherichia coli: two DNA glycosylases that repair oxidative damage in DNA, J. Photochem. Photobiol. B: Biol. 19 (1993) 87-96.
    • (1993) J. Photochem. Photobiol. B: Biol. , vol.19 , pp. 87-96
    • Boiteux, S.1
  • 25
    • 0025240665 scopus 로고
    • Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites
    • [25] S. Boiteux, T.R. O'Connor, F. Lederer, A. Gouyette, J. Laval, Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites, J. Biol. Chem. 265 (1990) 3916-3922.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3916-3922
    • Boiteux, S.1    O'Connor, T.R.2    Lederer, F.3    Gouyette, A.4    Laval, J.5
  • 26
    • 0030005132 scopus 로고    scopus 로고
    • Role of DNA repair enzymes in the cellular resistance to oxidative stress
    • [26] J. Laval, Role of DNA repair enzymes in the cellular resistance to oxidative stress, Pathol. Biol. 44 (1996) 14-24.
    • (1996) Pathol. Biol. , vol.44 , pp. 14-24
    • Laval, J.1
  • 27
    • 0004370304 scopus 로고
    • Physical association of the 2,6-diamino-4-hydroxy-5 N-formamidopyrimidine-DNA glycosylase of Escherichia coli and an activity nicking DNA at apurinic/apyrimidinic sites
    • [27] T.R. O'Connor, J. Laval, Physical association of the 2,6-diamino-4-hydroxy-5 N-formamidopyrimidine-DNA glycosylase of Escherichia coli and an activity nicking DNA at apurinic/apyrimidinic sites, Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 5222-5226.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5222-5226
    • O'Connor, T.R.1    Laval, J.2
  • 28
    • 0024462459 scopus 로고
    • Mechanism of DNA strand nicking at apurinic/apyrimidinic sites by Escherichia coli [formamidopyrimidine DNA glycosylase]
    • [28] V. Bailly, W.G. Verly, T. O'Connor, J. Laval, Mechanism of DNA strand nicking at apurinic/apyrimidinic sites by Escherichia coli [formamidopyrimidine DNA glycosylase], Biochemistry 262 (1989) 581-589.
    • (1989) Biochemistry , vol.262 , pp. 581-589
    • Bailly, V.1    Verly, W.G.2    O'Connor, T.3    Laval, J.4
  • 29
    • 0026751221 scopus 로고
    • Excision of 5′-terminal deoxyribose phosphate from damaged DNA is catalysed by the Fpg protein of Escherichia coli
    • [29] R.J. Graves, J. Felzenszwabb, J. Laval, T. O'Connor, Excision of 5′-terminal deoxyribose phosphate from damaged DNA is catalysed by the Fpg protein of Escherichia coli, J. Biol. Chem. 267 (1992) 14429-14435.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14429-14435
    • Graves, R.J.1    Felzenszwabb, J.2    Laval, J.3    O'Connor, T.4
  • 30
    • 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
    • [30] Z. Hatahet, Y.W. Kow, A.A. Purmal, R.P. Cunningham, S. Wallace, 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 (1994) 18814-18820.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18814-18820
    • Hatahet, Z.1    Kow, Y.W.2    Purmal, A.A.3    Cunningham, R.P.4    Wallace, S.5
  • 31
    • 0026101901 scopus 로고
    • Stereochemical studies of the beta-elimination reactions at aldehydic abasic sites in DNA: Endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys
    • [31] A. Mazumder, J.A. Gerlt, M.J. Absalon, J. Stubbe, R.P. Cunningham, J.M. Withka, P.M. Bolton, Stereochemical studies of the beta-elimination reactions at aldehydic abasic sites in DNA: endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys, Biochemistry 30 (1991) 1116-1126.
    • (1991) Biochemistry , vol.30 , pp. 1116-1126
    • Mazumder, A.1    Gerlt, J.A.2    Absalon, M.J.3    Stubbe, J.4    Cunningham, R.P.5    Withka, J.M.6    Bolton, P.M.7
  • 32
    • 0032568654 scopus 로고    scopus 로고
    • The Ring Fragmentation product of Thymidine C5-hydrate when present in DNA is repaired by the Escherichia coli Fpg and Nth proteins
    • in press
    • [32] J. Jurado, M. Saparbaev, M.J. Matray, M.M. Greenberg, J. Laval, The Ring Fragmentation product of Thymidine C5-hydrate when present in DNA is repaired by the Escherichia coli Fpg and Nth proteins (1998 Biochemistry in press).
    • (1998) Biochemistry
    • Jurado, J.1    Saparbaev, M.2    Matray, M.J.3    Greenberg, M.M.4    Laval, J.5
  • 33
    • 0028933674 scopus 로고
    • Functional cooperation of MutT, MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotides in Escherichia coli
    • [33] T. Tajiri, H. Maki, M. Sekiguchi, Functional cooperation of MutT, MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotides in Escherichia coli, Mutat. Res. 336 (1995) 257-267.
    • (1995) Mutat. Res. , vol.336 , pp. 257-267
    • Tajiri, T.1    Maki, H.2    Sekiguchi, M.3
  • 34
    • 0030005059 scopus 로고    scopus 로고
    • Reduction of the toxicity and mutagenicity of aziridine in mammalian cells harboring the E. Coli fpg gene
    • [34] C. Cussac, F. Laval, Reduction of the toxicity and mutagenicity of aziridine in mammalian cells harboring the E. coli fpg gene, Nucleic Acid Res. 24 (1996) 1742-1746.
    • (1996) Nucleic Acid Res. , vol.24 , pp. 1742-1746
    • Cussac, C.1    Laval, F.2
  • 35
    • 0029761401 scopus 로고    scopus 로고
    • Increased resistance to N,N′,N″-triethylenethiophosphoramide (Thiotepa) in cells expressing the Escherichia coli formamidopyrimidine-DNA glycosylase
    • [35] R.D. Gill, C. Cussac, R.L. Souhami, F. Laval, Increased resistance to N,N′,N″-triethylenethiophosphoramide (Thiotepa) in cells expressing the Escherichia coli formamidopyrimidine-DNA glycosylase, Cancer Res. 56 (1996) 3721-3724.
    • (1996) Cancer Res. , vol.56 , pp. 3721-3724
    • Gill, R.D.1    Cussac, C.2    Souhami, R.L.3    Laval, F.4
  • 36
    • 0028556986 scopus 로고
    • Expression of the E. Coli fpg gene in mammalian cells reduces the mutagenicity of γ-rays
    • [36] F. Laval, Expression of the E. coli fpg gene in mammalian cells reduces the mutagenicity of γ-rays, Nucleic Acid Res. 22 (1994) 4943-4946.
    • (1994) Nucleic Acid Res. , vol.22 , pp. 4943-4946
    • Laval, F.1
  • 37
    • 0027462131 scopus 로고
    • Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role
    • [37] T.R. O'Connor, R.J. Graves, G. de Murcia, B. Castaing, J. Laval, Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role, J. Biol. Chem. 268 (1993) 9063-9070.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9063-9070
    • O'Connor, T.R.1    Graves, R.J.2    De Murcia, G.3    Castaing, B.4    Laval, J.5
  • 38
    • 0029013243 scopus 로고
    • The catalytic mechanism of Fpg protein. Evidence for a Schiff base intermediate and amino terminus localization of the catalytic site
    • [38] J. Tchou, A.P. Grollman, The catalytic mechanism of Fpg protein. Evidence for a Schiff base intermediate and amino terminus localization of the catalytic site, J. Biol. Chem. 270 (1995) 11671-11677.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11671-11677
    • Tchou, J.1    Grollman, A.P.2
  • 39
    • 0028604549 scopus 로고
    • Unified catalytic mechanism for DNA glycosylases
    • [39] M.L. Dodson, M.L. Michaels, R.S. Lloyd, Unified catalytic mechanism for DNA glycosylases, J. Biol. Chem. 269 (1994) 32709-32712.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32709-32712
    • Dodson, M.L.1    Michaels, M.L.2    Lloyd, R.S.3
  • 41
    • 0030991774 scopus 로고    scopus 로고
    • Mechanism of action of base release by Escherichia coli Fpg protein: Role of lysine 155 in catalysis
    • [41] L.E. Rabow, Y.W. Kow, Mechanism of action of base release by Escherichia coli Fpg protein: role of lysine 155 in catalysis, Biochemistry 36 (1997) 5084-5096.
    • (1997) Biochemistry , vol.36 , pp. 5084-5096
    • Rabow, L.E.1    Kow, Y.W.2
  • 42
    • 0030614471 scopus 로고    scopus 로고
    • 2-terminal proline acts as a nucleophile in the glycosylase/AP lyase reaction catalyzed by Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg) protein
    • 2-terminal proline acts as a nucleophile in the glycosylase/AP lyase reaction catalyzed by Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg) protein, J. Biol. Chem. 272 (1997) 5335-5341.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5335-5341
    • Zharkov, D.O.1    Rieger, R.A.2    Iden, C.R.3    Grollman, A.P.4
  • 43
    • 0032522428 scopus 로고    scopus 로고
    • Effect of single mutations on the three-dimensional structure dynamics of a DNA repair enzyme, the Escherichia coli protein: A fluorescence study using tryptophane residues as reporter groups
    • in press
    • [43] S.V. Kouznetsov, O.M. Sidorkina, J. Jurado, M. Bazin, Taue J.C. Brochon, J. Laval, R. Santus, Effect of single mutations on the three-dimensional structure dynamics of a DNA repair enzyme, the Escherichia coli protein: a fluorescence study using tryptophane residues as reporter groups. Eur. J. Biochem. (1998) in press.
    • (1998) Eur. J. Biochem.
    • Kouznetsov, S.V.1    Sidorkina, O.M.2    Jurado, J.3    Bazin, M.4    Brochon, T.J.C.5    Laval, J.6    Santus, R.7
  • 44
    • 0028295382 scopus 로고
    • Isolation and characterization of endonuclease VIII from Escherichia coli
    • [44] R.J. Melamede, Z. Hatahet, Y.W. Kow, H. Ide, S.S. Wallace, Isolation and characterization of endonuclease VIII from Escherichia coli, Biochemistry 33 (1994) 1255-1264.
    • (1994) Biochemistry , vol.33 , pp. 1255-1264
    • Melamede, R.J.1    Hatahet, Z.2    Kow, Y.W.3    Ide, H.4    Wallace, S.S.5
  • 45
    • 0030974369 scopus 로고    scopus 로고
    • Escherichia coli endonuclease VIII. Cloning, sequencing, and overexpression of the nei structural gene and characterization of nei and nei nth mutants
    • [45] D. Jiang, Z. Hatahet, J.O. Blaisdell, R.J. Melamede, S.S. Wallace, Escherichia coli endonuclease VIII. Cloning, sequencing, and overexpression of the nei structural gene and characterization of nei and nei nth mutants, J. Bacteriol. 179 (1997) 3773-3782.
    • (1997) J. Bacteriol. , vol.179 , pp. 3773-3782
    • Jiang, D.1    Hatahet, Z.2    Blaisdell, J.O.3    Melamede, R.J.4    Wallace, S.S.5
  • 46
    • 0017236583 scopus 로고
    • An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA
    • [46] M. Radman, An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA, J. Biol. Chem. 251 (1976) 1438-1445.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1438-1445
    • Radman, M.1
  • 47
    • 0017381612 scopus 로고
    • Endonuclease from Escherichia coli that acts specifically upon duplex DNA damaged by ultraviolet light, osmium tetroxide, acid, or X-rays
    • [47] F.T. Gates III, S. Linn, Endonuclease from Escherichia coli that acts specifically upon duplex DNA damaged by ultraviolet light, osmium tetroxide, acid, or X-rays, J. Biol. Chem. 252 (1977) 2802-2807.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2802-2807
    • Gates F.T. III1    Linn, S.2
  • 48
    • 0027366974 scopus 로고
    • Substrate specificity of the Escherichia coli endonuclease: III. Excision of thymine-and cytosine-derived lesions in DNA produced by radiation-generated free radicals
    • [48] M. Dizdaroglu, J. Laval, S. Boiteux, Substrate specificity of the Escherichia coli endonuclease: III. Excision of thymine-and cytosine-derived lesions in DNA produced by radiation-generated free radicals, Biochemistry 32 (1993) 12105-12111.
    • (1993) Biochemistry , vol.32 , pp. 12105-12111
    • Dizdaroglu, M.1    Laval, J.2    Boiteux, S.3
  • 49
    • 0023127167 scopus 로고
    • Escherichia coli endonuclease III is not an endonuclease but a β-elimination catalyst
    • [49] V. Bailly, W.G. Verly, Escherichia coli endonuclease III is not an endonuclease but a β-elimination catalyst, Biochem. J. 242 (1987) 565-572.
    • (1987) Biochem. J. , vol.242 , pp. 565-572
    • Bailly, V.1    Verly, W.G.2
  • 50
    • 0024283985 scopus 로고
    • The mechanism of action of E. Coli endonuclease III and T4UV endonuclease (endonuclease V) at AP sites
    • [50] J. Kim, S. Linn, The mechanism of action of E. coli endonuclease III and T4UV endonuclease (endonuclease V) at AP sites, Nucleic Acids Res. 16 (1988) 1135-1141.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 1135-1141
    • Kim, J.1    Linn, S.2
  • 51
    • 0343879974 scopus 로고
    • Endonuclease III (nth) mutants of Escherichia coli
    • [51] R.P. Cunningham, B. Weiss, Endonuclease III (nth) mutants of Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 82 (1985) 474-478.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 474-478
    • Cunningham, R.P.1    Weiss, B.2
  • 52
    • 0024393445 scopus 로고
    • Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene
    • [52] H. Asahara, P.M. Wistort, J.F. Bank, R.H. Bakerian, R.P. Cunningham, Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene, Biochemistry 28 (1989) 4444-4449.
    • (1989) Biochemistry , vol.28 , pp. 4444-4449
    • Asahara, H.1    Wistort, P.M.2    Bank, J.F.3    Bakerian, R.H.4    Cunningham, R.P.5
  • 54
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA Repair enzyme endonuclease III crystal structure
    • [54] M.M. Thayer, H. Ahern, D. Xing, R.P. Cunningham, J.A. Tainer, Novel DNA binding motifs in the DNA Repair enzyme endonuclease III crystal structure, EMBO J. 14 (1995) 4108-4120.
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 55
    • 0025301064 scopus 로고
    • MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III
    • [55] M.L. Michaels, L. Pham, Y. Ngheim, C. Cruz, J.H. Miller, MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III, Nucleic Acids Res. 18 (1990) 3841-3845.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3841-3845
    • Michaels, M.L.1    Pham, L.2    Ngheim, Y.3    Cruz, C.4    Miller, J.H.5
  • 56
    • 0018072314 scopus 로고
    • Enzymatic excision of free hypoxanthine from polydeoxynucleotides and DNA containing deoxyinosine monophosphate residues
    • [56] P. Karran, T. Lindahl, Enzymatic excision of free hypoxanthine from polydeoxynucleotides and DNA containing deoxyinosine monophosphate residues, J. Biol. Chem. 253 (1978) 5877-5879.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5877-5879
    • Karran, P.1    Lindahl, T.2
  • 58
    • 0019331557 scopus 로고
    • Hypoxanthine in deoxyribonucleic acid: Generation by heat-induced hydrolysis of adenine residues and release in free form by a deoxyribonucleic acid glycosylase from calf thymus
    • [58] P. Karran, T. Lindahl, Hypoxanthine in deoxyribonucleic acid: generation by heat-induced hydrolysis of adenine residues and release in free form by a deoxyribonucleic acid glycosylase from calf thymus, Biochemistry 19 (26) (1980) 6005-6011.
    • (1980) Biochemistry , vol.19 , Issue.26 , pp. 6005-6011
    • Karran, P.1    Lindahl, T.2
  • 59
    • 0022993948 scopus 로고
    • Site-specific mutagenesis in vivo by single methylated or deaminated purine bases
    • [59] M. Hill-Perkins, M.D. Jones, P. Karran, Site-specific mutagenesis in vivo by single methylated or deaminated purine bases, Mutat. Res. 162 (1986) 153-163.
    • (1986) Mutat. Res. , vol.162 , pp. 153-163
    • Hill-Perkins, M.1    Jones, M.D.2    Karran, P.3
  • 60
    • 0028239225 scopus 로고
    • Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases
    • [60] M. Saparbaev, J. Laval, Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases, Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 5873-5877.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5873-5877
    • Saparbaev, M.1    Laval, J.2
  • 61
    • 0021717558 scopus 로고
    • Cloning and characterization of the alkA gene of Escherichia coli that encodes 3-methyladenine DNA glycosylase II
    • [61] Y. Nakabeppu, H. Kondo, M. Sekiguchi, Cloning and characterization of the alkA gene of Escherichia coli that encodes 3-methyladenine DNA glycosylase II, J. Biol. Chem. 259 (1984) 13723-13729.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13723-13729
    • Nakabeppu, Y.1    Kondo, H.2    Sekiguchi, M.3
  • 62
    • 0026507888 scopus 로고
    • Roles of the vinyl chloride oxidation products 1-chlorooxirane and 2-chloroacetaldehyde in the in vitro formation of etheno adducts of nucleic acid bases
    • [62] F.P. Guengerich, Roles of the vinyl chloride oxidation products 1-chlorooxirane and 2-chloroacetaldehyde in the in vitro formation of etheno adducts of nucleic acid bases, Chem. Res. Toxicol. 5 (1992) 2-5.
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 2-5
    • Guengerich, F.P.1
  • 63
    • 0025925384 scopus 로고
    • Release of N2,3-ethanoguanine from haloethylnitrosourea-treated DNA by Escherichia coli 3-methyladenine DNA glycosylase II
    • [63] Y. Habraken, C.A. Carter, M. Sekiguchi, D.B. Ludlum, Release of N2,3-ethanoguanine from haloethylnitrosourea-treated DNA by Escherichia coli 3-methyladenine DNA glycosylase II, Carcinogenesis 12 (1991) 1971-1973.
    • (1991) Carcinogenesis , vol.12 , pp. 1971-1973
    • Habraken, Y.1    Carter, C.A.2    Sekiguchi, M.3    Ludlum, D.B.4
  • 64
    • 0029133553 scopus 로고
    • Escherichia coli, Saccharomyces cerevisiae, rat and human 3-methyladenine DNA glycosylases repair 1,N6-ethenoadenine when present in DNA
    • [64] M. Saparbaev, K. Kleibl, J. Laval, Escherichia coli, Saccharomyces cerevisiae, rat and human 3-methyladenine DNA glycosylases repair 1,N6-ethenoadenine when present in DNA, Nucleic Acids Res. 23 (1995) 3750-3755.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3750-3755
    • Saparbaev, M.1    Kleibl, K.2    Laval, J.3
  • 65
    • 0025220483 scopus 로고
    • 5-Formyldeoxyuridine: A new type of DNA damage induced by ionizing radiation and its mutagenicity to salmonella strain TA102
    • [65] H. Kasai, A. Iida, Z. Yamaizumi, S. Nishimura, H. Tanooka, 5-Formyldeoxyuridine: a new type of DNA damage induced by ionizing radiation and its mutagenicity to salmonella strain TA102, Mutat. Res. 243 (1990) 249-253.
    • (1990) Mutat. Res. , vol.243 , pp. 249-253
    • Kasai, H.1    Iida, A.2    Yamaizumi, Z.3    Nishimura, S.4    Tanooka, H.5
  • 66
    • 0028045942 scopus 로고
    • DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the AlkA enzyme in Escherichia coli
    • [66] S. Bjelland, N.K. Birkeland, T. Benneche, G. Volden, E. Seeberg, DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the AlkA enzyme in Escherichia coli, J. Biol. Chem. 269 (1994) 30489-30495.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30489-30495
    • Bjelland, S.1    Birkeland, N.K.2    Benneche, T.3    Volden, G.4    Seeberg, E.5
  • 70
    • 0017161630 scopus 로고
    • Methyl methane sulfonate-sensitive mutant of Escherichia coli deficient in an endonuclease specific for apurinic sites in deoxyribonucleic acid
    • [70] S. Ljungquist, T. Lindahl, P. Howard-Flanders, Methyl methane sulfonate-sensitive mutant of Escherichia coli deficient in an endonuclease specific for apurinic sites in deoxyribonucleic acid, J. Bacteriol. 126 (1976) 646-653.
    • (1976) J. Bacteriol. , vol.126 , pp. 646-653
    • Ljungquist, S.1    Lindahl, T.2    Howard-Flanders, P.3
  • 71
    • 0006639728 scopus 로고
    • Endonuclease IV of Escherichia coli is induced by paraquat
    • [71] E. Chan, B. Weiss, Endonuclease IV of Escherichia coli is induced by paraquat, Proc. Natl. Acad. Sci. U.S.A. 84 (1987) 3189-3193.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 3189-3193
    • Chan, E.1    Weiss, B.2
  • 72
    • 0027432048 scopus 로고
    • Negative autoregulation by the Escherichia coli SoxS protein: A dampening mechanism for the soxRS redox stress response
    • [72] T. Nunoshiba, E. Hidalgo, Z. Li, B. Demple, Negative autoregulation by the Escherichia coli SoxS protein: a dampening mechanism for the soxRS redox stress response, J. Bacteriol. 175 (1993) 7492-7494.
    • (1993) J. Bacteriol. , vol.175 , pp. 7492-7494
    • Nunoshiba, T.1    Hidalgo, E.2    Li, Z.3    Demple, B.4
  • 73
    • 0025369726 scopus 로고
    • soxR, a locus governing a superoxide response regulon in Escherichia coli K-12
    • [73] I.R. Tsaneva, B. Weiss, soxR, a locus governing a superoxide response regulon in Escherichia coli K-12, J. Bacteriol. 172 (1990) 4197-4205.
    • (1990) J. Bacteriol. , vol.172 , pp. 4197-4205
    • Tsaneva, I.R.1    Weiss, B.2
  • 74
    • 0026335852 scopus 로고
    • Regulation of bacterial oxidative stress genes
    • [74] B. Demple, Regulation of bacterial oxidative stress genes, Annu. Rev. Genet. 25 (1991) 315-337.
    • (1991) Annu. Rev. Genet. , vol.25 , pp. 315-337
    • Demple, B.1
  • 76
    • 0023917460 scopus 로고
    • Homogeneous Escherichia coli endonuclease IV. Characterization of an enzyme that recognizes oxidative damage in DNA
    • [76] J.D. Levin, A.W. Johnson, B. Demple, Homogeneous Escherichia coli endonuclease IV. Characterization of an enzyme that recognizes oxidative damage in DNA, J. Biol. Chem. 263 (1988) 8066-8071.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8066-8071
    • Levin, J.D.1    Johnson, A.W.2    Demple, B.3
  • 77
    • 0017701231 scopus 로고
    • A new endonuclease from Escherichia coli acting at apurinic sites in DNA
    • [77] S. Ljungquist, A new endonuclease from Escherichia coli acting at apurinic sites in DNA, J. Biol. Chem. 252 (1977) 2808-2814.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2808-2814
    • Ljungquist, S.1
  • 78
    • 0028181135 scopus 로고
    • α-Deoxyadenosine, a major anoxic radiolysis product of adenine in DNA, is a substrate for Escherichia coli endonuclease IV
    • [78] H. Ide, K. Tedzuka, H. Shimzu, Y. Kimura, A.A. Purmal, S.S. Wallace, Y.W. Kow, α-Deoxyadenosine, a major anoxic radiolysis product of adenine in DNA, is a substrate for Escherichia coli endonuclease IV, Biochemistry 33 (1994) 7842-7847.
    • (1994) Biochemistry , vol.33 , pp. 7842-7847
    • Ide, H.1    Tedzuka, K.2    Shimzu, H.3    Kimura, Y.4    Purmal, A.A.5    Wallace, S.S.6    Kow, Y.W.7
  • 79
    • 0030474259 scopus 로고    scopus 로고
    • An unusual mechanism for the major human apurinic/apyrimidinic (AP) endonuclease involving 5′ cleavage of DNA containing a benzene-derived exocyclic adduct in the absence of an AP-site
    • [79] B. Hang, A. Chenna, H. Fraenkel-Conrat, B. Singer, An unusual mechanism for the major human apurinic/apyrimidinic (AP) endonuclease involving 5′ cleavage of DNA containing a benzene-derived exocyclic adduct in the absence of an AP-site, Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 13737-13741.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13737-13741
    • Hang, B.1    Chenna, A.2    Fraenkel-Conrat, H.3    Singer, B.4
  • 80
    • 0000973806 scopus 로고
    • A deoxiribonucleic acid phosphatase-exonuclease from Escherichia coli: II. Characterization of the exonuclease activity
    • [80] C.C. Richardson, I.R. Lehman, A. Kornberg, A deoxiribonucleic acid phosphatase-exonuclease from Escherichia coli: II. Characterization of the exonuclease activity, J. Biol. Chem. 239 (1964) 251-258.
    • (1964) J. Biol. Chem. , vol.239 , pp. 251-258
    • Richardson, C.C.1    Lehman, I.R.2    Kornberg, A.3
  • 81
    • 0000973807 scopus 로고
    • A deoxiribonucleic acid phosphatase-exonuclease from Escherichia coli: I. Purification and characterization of the phosphatase activity
    • [81] C.C. Richardson, A. Kornberg, A deoxiribonucleic acid phosphatase-exonuclease from Escherichia coli: I. Purification and characterization of the phosphatase activity, J. Biol. Chem. 239 (1964) 242-250.
    • (1964) J. Biol. Chem. , vol.239 , pp. 242-250
    • Richardson, C.C.1    Kornberg, A.2
  • 83
    • 0017255036 scopus 로고
    • Endonuclease II of Escherichia coli is exonuclease III
    • [83] B. Weiss, Endonuclease II of Escherichia coli is exonuclease III, J. Biol. Chem. 251 (1976) 1896-1901.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1896-1901
    • Weiss, B.1
  • 84
    • 0017819269 scopus 로고
    • Properties of the main endonuclease specific for apurinic sites of Escherichia coli (endonuclease VI). Mechanism of apurinic site excision from DNA
    • [84] F. Grossard, W.G. Verly, Properties of the main endonuclease specific for apurinic sites of Escherichia coli (endonuclease VI). Mechanism of apurinic site excision from DNA, Eur. J. Biochem. 82 (1978) 321-332.
    • (1978) Eur. J. Biochem. , vol.82 , pp. 321-332
    • Grossard, F.1    Verly, W.G.2
  • 85
    • 0019142844 scopus 로고
    • Cloning of the exonuclease III gene of Escherichia coli
    • [85] S.G. Rogers, B. Weiss, Cloning of the exonuclease III gene of Escherichia coli, Gene 11 (1980) 187-195.
    • (1980) Gene , vol.11 , pp. 187-195
    • Rogers, S.G.1    Weiss, B.2
  • 86
    • 0019051753 scopus 로고
    • Apurinic/apyrimidinic endonucleases in repair of pyrimidine dimers and other lesions in DNA
    • [86] H.R. Warner, B.F. Demple, W.A. Deutsch, C.M. Kane, S. Linn, Apurinic/apyrimidinic endonucleases in repair of pyrimidine dimers and other lesions in DNA, Proc. Natl. Acad. Sci. U.S.A. 77 (1980) 4602-4606.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 4602-4606
    • Warner, H.R.1    Demple, B.F.2    Deutsch, W.A.3    Kane, C.M.4    Linn, S.5
  • 88
    • 0020974525 scopus 로고
    • Escherichia coli xthA mutants are sensitive to inactivation by broad-spectrum near-UV (300-to 400-nm) radiation
    • [88] L.J. Sammartano, R.W. Tuveson, Escherichia coli xthA mutants are sensitive to inactivation by broad-spectrum near-UV (300-to 400-nm) radiation, J. Bacteriol. 156 (1983) 904-906.
    • (1983) J. Bacteriol. , vol.156 , pp. 904-906
    • Sammartano, L.J.1    Tuveson, R.W.2
  • 89
    • 0028923440 scopus 로고
    • Structure and function of the multifunctional DNA-repair enzyme exonuclease III
    • [89] C.D. Mol, C.F. Kuo, M.M. Thayer, R.P. Cunningham, J.A. Tainer, Structure and function of the multifunctional DNA-repair enzyme exonuclease III, Nature 374 (1995) 381-386.
    • (1995) Nature , vol.374 , pp. 381-386
    • Mol, C.D.1    Kuo, C.F.2    Thayer, M.M.3    Cunningham, R.P.4    Tainer, J.A.5
  • 90
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • [90] M.M. Thayer, H. Ahern, D. Xing, R.P. Cunningham, J.A. Tainer, Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure, EMBO J. 14 (1995) 4108-4120.
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 92
    • 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
    • [92] P. Auffret van der Kemp, D. Thomas, R. Barbey, R. de Oliveira, S. Boiteux, 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
    • Auffret Van Der Kemp, P.1    Thomas, D.2    Barbey, R.3    De Oliveira, R.4    Boiteux, S.5
  • 93
    • 0030220956 scopus 로고    scopus 로고
    • Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily
    • [93] H.M. Nash, S.D. Bruner, O.D. Schärer, T. Kawate, T.A. Addona, E. Spooner, W.S. Lane, G.L. Verdine, Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily, Curr. Biol. 6 (1996) 968-980.
    • (1996) Curr. Biol. , vol.6 , pp. 968-980
    • Nash, H.M.1    Bruner, S.D.2    Schärer, O.D.3    Kawate, T.4    Addona, T.A.5    Spooner, E.6    Lane, W.S.7    Verdine, G.L.8
  • 94
    • 0030738194 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase
    • [94] T.A. Rosenquist, D.O. Zharkov, A.P. Grollman, Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase, Proc. Natl. Acad. Sci. 94 (1997) 7429-7434.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 7429-7434
    • Rosenquist, T.A.1    Zharkov, D.O.2    Grollman, A.P.3
  • 95
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae
    • [95] J.P. Radicella, C. Dherin, C. Desmaze, M.S. Fox, S. Boiteux, Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae, Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 8010-8015.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8010-8015
    • Radicella, J.P.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.4    Boiteux, S.5
  • 97
    • 0031172802 scopus 로고    scopus 로고
    • A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer
    • [97] R. Lu, H.M. Nash, G.L. Verdine, A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer, Curr. Biol. 7 (1997) 397-407.
    • (1997) Curr. Biol. , vol.7 , pp. 397-407
    • Lu, R.1    Nash, H.M.2    Verdine, G.L.3
  • 98
  • 100
    • 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
    • [100] L. Eide, M. Bjoras, M. Pirovano, I. Alseth, K.G. Berdal, E. Seeberg, 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. 93 (1996) 10735-10740.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 10735-10740
    • Eide, L.1    Bjoras, M.2    Pirovano, M.3    Alseth, I.4    Berdal, K.G.5    Seeberg, E.6
  • 101
    • 0029814011 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of a Schizosaccharomyces pombe homologue of Escherichia coli endonuclease III
    • [101] T. Roldan-Arjona, C. Anselmino, T. Lindahl, Molecular cloning and functional analysis of a Schizosaccharomyces pombe homologue of Escherichia coli endonuclease III, Nucleic Acids Res. 24 (1996) 3307-3312.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3307-3312
    • Roldan-Arjona, T.1    Anselmino, C.2    Lindahl, T.3
  • 103
    • 0030890419 scopus 로고    scopus 로고
    • Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme Escherichia coli endonuclease III
    • [103] T.P. Hilbert, W. Chaung, R.J. Boorstein, R.P. Cunningham, G.W. Teebor, Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme Escherichia coli endonuclease III, J. Biol. Chem. 272 (1997) 6733-6740.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6733-6740
    • Hilbert, T.P.1    Chaung, W.2    Boorstein, R.J.3    Cunningham, R.P.4    Teebor, G.W.5
  • 104
    • 0025324303 scopus 로고
    • Yeast structural gene (APN1) for the major apurinic endonuclease: Homology to Escherichia coli endonuclease IV
    • [104] S.C. Popoff, A.I. Spira, A.W. Johnson, B. Demple, Yeast structural gene (APN1) for the major apurinic endonuclease: homology to Escherichia coli endonuclease IV, Proc. Natl. Acad. Sci. U.S.A. 87 (1990) 4193-4197.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4193-4197
    • Popoff, S.C.1    Spira, A.I.2    Johnson, A.W.3    Demple, B.4
  • 105
    • 0024279616 scopus 로고
    • Yeast DNA 3′-repair diesterase is the major cellular apurinic/apyrimidinic endonuclease: Substrate specificity and kinetics
    • [105] A.W. Johnson, B. Demple, Yeast DNA 3′-repair diesterase is the major cellular apurinic/apyrimidinic endonuclease: substrate specificity and kinetics, J. Biol. Chem. 263 (1988) 18017-18022.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18017-18022
    • Johnson, A.W.1    Demple, B.2
  • 106
    • 0024404908 scopus 로고
    • Drosophila melanogaster strand transferase. A protein that forms heteroduplex DNA in the absence of both ATP and single-strand DNA binding protein
    • [106] K. Lowenhaupt, M. Sander, C. Hauser, A. Rich, Drosophila melanogaster strand transferase. A protein that forms heteroduplex DNA in the absence of both ATP and single-strand DNA binding protein, J. Biol. Chem. 264 (1989) 20568-20575.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20568-20575
    • Lowenhaupt, K.1    Sander, M.2    Hauser, C.3    Rich, A.4
  • 107
    • 0026070597 scopus 로고
    • Isolation of cDNA clones encoding an enzyme from bovine cells that repairs oxidative DNA damage in vitro: Homology with bacterial repair enzymes
    • [107] C.N. Robson, I.D. Hickson, Isolation of cDNA clones encoding an enzyme from bovine cells that repairs oxidative DNA damage in vitro: homology with bacterial repair enzymes, Nucleic Acids Res. 19 (1991) 1087-1092.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1087-1092
    • Robson, C.N.1    Hickson, I.D.2
  • 108
    • 0025718595 scopus 로고
    • cDNA and deduced amino acid sequence of a mouse DNA repair enzyme (APEX nuclease) with significant homology to Escherichia coli exonuclease III
    • [108] S. Seki, K. Akiyama, S. Watanabe, M. Hatsushika, S. Ikeda, K. Tsutsui, cDNA and deduced amino acid sequence of a mouse DNA repair enzyme (APEX nuclease) with significant homology to Escherichia coli exonuclease III, J. Biol. Chem. 266 (1991) 20797-20802.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20797-20802
    • Seki, S.1    Akiyama, K.2    Watanabe, S.3    Hatsushika, M.4    Ikeda, S.5    Tsutsui, K.6
  • 109
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: Definition of a family of DNA repair enzymes
    • [109] B. Demple, T. Herman, D.S. Chen, 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 (1991) 10450-10454.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10450-10454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 110
    • 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
    • [110] C.N. Robson, A.M. Milne, D.J.C. Pappin, I.D. Hickson, 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 (1991) 5519-5523.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5519-5523
    • Robson, C.N.1    Milne, A.M.2    Pappin, D.J.C.3    Hickson, I.D.4
  • 111
    • 0026683715 scopus 로고
    • cDNA cloning, sequencing, expression and possible domain structure of human nuclease homologous to Escherichia coli exonuclease III
    • [111] S. Seki, M. Hatsushika, S. Watanabe, K. Akiyama, K. Nagao, K. Tsutsui, cDNA cloning, sequencing, expression and possible domain structure of human nuclease homologous to Escherichia coli exonuclease III, Biochim. Biophys. Acta 1131 (1992) 287-299.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 287-299
    • Seki, S.1    Hatsushika, M.2    Watanabe, S.3    Akiyama, K.4    Nagao, K.5    Tsutsui, K.6
  • 112
    • 0025784273 scopus 로고
    • Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine
    • [112] T.R. O'Connor, J. Laval J, Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine, Biochem. Biophys. Res. Commun. 176 (1991) 1170-1177.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1170-1177
    • O'Connor, T.R.1    Laval, J.2
  • 113
    • 0025949662 scopus 로고
    • Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase
    • [113] D. Chakravarti, G.C. Ibeanu, K. Tano, S. Mitra, Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase, J. Biol. Chem. 266 (1991) 15710-15715.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15710-15715
    • Chakravarti, D.1    Ibeanu, G.C.2    Tano, K.3    Mitra, S.4
  • 114
    • 0025990209 scopus 로고
    • Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16
    • [114] L. Samson, B. Derfler, M. Boosalis, K. Call, 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 (1991) 9127-9131.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9127-9131
    • Samson, L.1    Derfler, B.2    Boosalis, M.3    Call, K.4
  • 115
    • 0027759522 scopus 로고
    • Purification and characterization of human 3-methyladenine-DNA glycosylase
    • [115] T.R. O'Connor, 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'Connor, T.R.1
  • 116
    • 0027538469 scopus 로고
    • Structure of the human 3-methyladenine DNA glycosylase gene and localization close to the 16p telomere
    • [116] M.A. Vickers, P. Vyas, P.C. Harris, D.L. Simmons, D.R. Higgs, Structure of the human 3-methyladenine DNA glycosylase gene and localization close to the 16p telomere, Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 3437-3441.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 3437-3441
    • Vickers, M.A.1    Vyas, P.2    Harris, P.C.3    Simmons, D.L.4    Higgs, D.R.5
  • 117
    • 0028844785 scopus 로고
    • Oxidation of thymine to 5-formyluracil in DNA: Mechanisms of formation, structural implications, and base excision by human cell free extracts
    • [117] S. Bjelland, L. Eide, R.W. Time, R. Stote, I. Eftedal, G. Volden, E. Seeberg, Oxidation of thymine to 5-formyluracil in DNA: mechanisms of formation, structural implications, and base excision by human cell free extracts, Biochemistry 34 (1995) 14758-14764.
    • (1995) Biochemistry , vol.34 , pp. 14758-14764
    • Bjelland, S.1    Eide, L.2    Time, R.W.3    Stote, R.4    Eftedal, I.5    Volden, G.6    Seeberg, E.7
  • 119
    • 0026684849 scopus 로고
    • Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA
    • [119] L.M. Michaels, C. Cruz, A.P. Grollman, J.H. Miller, Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA, Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 7022-7025.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7022-7025
    • Michaels, L.M.1    Cruz, C.2    Grollman, A.P.3    Miller, J.H.4
  • 120
    • 0028942512 scopus 로고
    • Repair of oxidative DNA damage in gram-positive bacteria: The Lactococcus lactis Fpg protein
    • [120] P. Duwat, R. de Oliveira, S.D. Ehrlich, S. Boiteux, Repair of oxidative DNA damage in gram-positive bacteria: the Lactococcus lactis Fpg protein, Microbiology 141 (1995) 411-417.
    • (1995) Microbiology , vol.141 , pp. 411-417
    • Duwat, P.1    De Oliveira, R.2    Ehrlich, S.D.3    Boiteux, S.4
  • 121
    • 0020693158 scopus 로고
    • Escherichia coli xth mutants are hypersensitive to hydrogen peroxide
    • [121] B. Demple, J.H. Halbrook, S. Linn, Escherichia coli xth mutants are hypersensitive to hydrogen peroxide, J. Bacteriol. 153 (1983) 1079-1082.
    • (1983) J. Bacteriol. , vol.153 , pp. 1079-1082
    • Demple, B.1    Halbrook, J.H.2    Linn, S.3


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