메뉴 건너뛰기




Volumn 20, Issue 4, 2014, Pages 708-726

Repair of oxidative DNA damage and cancer: Recent progress in DNA base excision repair

Author keywords

[No Author keywords available]

Indexed keywords

8 HYDROXYGUANINE; APE1 ENZYME; DEOXYRIBONUCLEASE I; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA BASE; GLYCOSYLTRANSFERASE; NEIL2 GLYCOSYLASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 84887383501     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2013.5529     Document Type: Review
Times cited : (120)

References (182)
  • 2
    • 40649109989 scopus 로고    scopus 로고
    • Mitochondrial base excision repair of uracil and AP sites takes place by single-nucleotide insertion and long-patch DNA synthesis
    • Akbari M, Visnes T, Krokan HE, and Otterlei M. Mitochondrial base excision repair of uracil and AP sites takes place by single-nucleotide insertion and long-patch DNA synthesis. DNA Repair (Amst) 7: 605-616, 2008.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 605-616
    • Akbari, M.1    Visnes, T.2    Krokan, H.E.3    Otterlei, M.4
  • 4
    • 33645288241 scopus 로고    scopus 로고
    • The study using wild-type and Ogg1 knockout mice exposed to potassium bromate shows no tumor induction despite an extensive accumulation of 8-hydroxyguanine in kidney DNA
    • Arai T, Kelly VP, Minowa O, Noda T, and Nishimura S. The study using wild-type and Ogg1 knockout mice exposed to potassium bromate shows no tumor induction despite an extensive accumulation of 8-hydroxyguanine in kidney DNA. Toxicology 221: 179-186, 2006.
    • (2006) Toxicology , vol.221 , pp. 179-186
    • Arai, T.1    Kelly, V.P.2    Minowa, O.3    Noda, T.4    Nishimura, S.5
  • 5
    • 0024332124 scopus 로고
    • Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs
    • Au KG, Clark S, Miller JH, and Modrich P. Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs. Proc Natl Acad Sci USA 86: 8877-8881, 1989.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8877-8881
    • Au, K.G.1    Clark, S.2    Miller, J.H.3    Modrich, P.4
  • 8
    • 84871716320 scopus 로고    scopus 로고
    • Down-regulation of 8-oxoguanine DNA glycosylase 1 expression in the airway epithelium ameliorates allergic lung inflammation
    • Bacsi A, Aguilera-Aguirre L, Szczesny B, Radak Z, Hazra TK, Sur S, Ba X, and Boldogh I. Down-regulation of 8-oxoguanine DNA glycosylase 1 expression in the airway epithelium ameliorates allergic lung inflammation. DNA Repair (Amst) 12: 18-26, 2013.
    • (2013) DNA Repair (Amst) , vol.12 , pp. 18-26
    • Bacsi, A.1    Aguilera-Aguirre, L.2    Szczesny, B.3    Radak, Z.4    Hazra, T.K.5    Sur, S.6    Ba, X.7    Boldogh, I.8
  • 10
    • 0023127167 scopus 로고
    • Escherichia coli endonuclease III is not an endonuclease but a beta-elimination catalyst
    • Bailly V and Verly WG. Escherichia coli endonuclease III is not an endonuclease but a beta-elimination catalyst. Biochem J 242: 565-572, 1987.
    • (1987) Biochem J , vol.242 , pp. 565-572
    • Bailly, V.1    Verly, W.G.2
  • 11
    • 67651149733 scopus 로고    scopus 로고
    • Of Apurinic/apyrimidinic endonuclease 1 (APE1) as the endoribonuclease that cleaves c-myc mRNA
    • CH. Identification
    • Barnes T, Kim WC, Mantha AK, Kim SE, Izumi T, Mitra S, and Lee CH. Identification of Apurinic/apyrimidinic endonuclease 1 (APE1) as the endoribonuclease that cleaves c-myc mRNA. Nucleic Acids Res 37: 3946-3958, 2009.
    • (2009) Nucleic Acids Res , vol.37 , pp. 3946-3958
    • Barnes, T.1    Kim, W.C.2    Mantha, A.K.3    Kim, S.E.4    Izumi, T.5    Lee, M.S.6
  • 12
    • 0029010778 scopus 로고
    • Sitedirected mutagenesis of the human DNA repair enzyme HAP1: Identification of residues important for AP endonuclease and RNase H activity
    • Barzilay G, Walker LJ, Robson CN, and Hickson ID. Sitedirected mutagenesis of the human DNA repair enzyme HAP1: identification of residues important for AP endonuclease and RNase H activity. Nucleic Acids Res 23: 1544-1550, 1995.
    • (1995) Nucleic Acids Res , vol.23 , pp. 1544-1550
    • Barzilay, G.1    Walker, L.J.2    Robson, C.N.3    Hickson, I.D.4
  • 14
    • 0347504848 scopus 로고    scopus 로고
    • Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene
    • Bhakat KK, Izumi T, Yang SH, Hazra TK, and Mitra S. Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene. EMBO J 22: 6299-6309, 2003.
    • (2003) EMBO J , vol.22 , pp. 6299-6309
    • Bhakat, K.K.1    Izumi, T.2    Yang, S.H.3    Hazra, T.K.4    Mitra, S.5
  • 15
    • 18744416025 scopus 로고    scopus 로고
    • Quantification of random genomic mutations
    • Bielas JH and Loeb LA. Quantification of random genomic mutations. Nat Methods 2: 285-290, 2005.
    • (2005) Nat Methods , vol.2 , pp. 285-290
    • Bielas, J.H.1    Loeb, L.A.2
  • 17
    • 0035176178 scopus 로고    scopus 로고
    • Apurinic/apyrimidinic endonuclease activity is elevated in human adult gliomas
    • Bobola MS, Blank A, Berger MS, Stevens BA, and Silber JR. Apurinic/apyrimidinic endonuclease activity is elevated in human adult gliomas. Clin Cancer Res 7: 3510-3518, 2001.
    • (2001) Clin Cancer Res , vol.7 , pp. 3510-3518
    • Bobola, M.S.1    Blank, A.2    Berger, M.S.3    Stevens, B.A.4    Silber, J.R.5
  • 19
    • 0028927261 scopus 로고
    • Reactions of oxyl radicals with DNA
    • Breen AP and Murphy JA. Reactions of oxyl radicals with DNA. Free Radic Biol Med 18: 1033-1077, 1995.
    • (1995) Free Radic Biol Med , vol.18 , pp. 1033-1077
    • Breen, A.P.1    Murphy, J.A.2
  • 21
    • 67949109632 scopus 로고    scopus 로고
    • Role of PCNA-dependent stimulation of 3¢-phosphodiesterase and 3¢-5¢ exonuclease activities of human Ape2 in repair of oxidative DNA damage
    • Burkovics P, Hajdu I, Szukacsov V, Unk I, and Haracska L. Role of PCNA-dependent stimulation of 3¢-phosphodiesterase and 3¢-5¢ exonuclease activities of human Ape2 in repair of oxidative DNA damage. Nucleic Acids Res 37: 4247-4255, 2009.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4247-4255
    • Burkovics, P.1    Hajdu, I.2    Szukacsov, V.3    Unk, I.4    Haracska, L.5
  • 22
    • 64049110265 scopus 로고    scopus 로고
    • Ubiquitination of mammalian AP endonuclease (APE1) regulated by the p53-MDM2 signaling pathway
    • Busso CS, Iwakuma T, and Izumi T. Ubiquitination of mammalian AP endonuclease (APE1) regulated by the p53-MDM2 signaling pathway. Oncogene 28: 1616-1625, 2009.
    • (2009) Oncogene , vol.28 , pp. 1616-1625
    • Busso, C.S.1    Iwakuma, T.2    Izumi, T.3
  • 23
    • 78149428468 scopus 로고    scopus 로고
    • Posttranslational modification of mammalian AP endonuclease (APE1)
    • Busso CS, Lake MW, and Izumi T. Posttranslational modification of mammalian AP endonuclease (APE1). Cell Mol Life Sci 67: 3609-3620, 2010.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3609-3620
    • Busso, C.S.1    Lake, M.W.2    Izumi, T.3
  • 24
    • 80054083892 scopus 로고    scopus 로고
    • Ubiquitination of human AP-endonuclease 1 (APE1) enhanced by T233E substitution and by CDK5
    • Busso CS, Wedgeworth CM, and Izumi T. Ubiquitination of human AP-endonuclease 1 (APE1) enhanced by T233E substitution and by CDK5. Nucleic Acids Res 39: 8017-8028, 2011.
    • (2011) Nucleic Acids Res , vol.39 , pp. 8017-8028
    • Busso, C.S.1    Wedgeworth, C.M.2    Izumi, T.3
  • 25
    • 48249095920 scopus 로고    scopus 로고
    • Single-strand break repair and genetic disease
    • Caldecott KW. Single-strand break repair and genetic disease. Nat Rev Genet 9: 619-631, 2008.
    • (2008) Nat Rev Genet , vol.9 , pp. 619-631
    • Caldecott, K.W.1
  • 26
    • 0033986948 scopus 로고    scopus 로고
    • Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha
    • Carrero P, Okamoto K, Coumailleau P, O'Brien S, Tanaka H, Poellinger L. Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Mol Cell Biol 20: 402-415, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 402-415
    • Carrero, P.1    Okamoto, K.2    Coumailleau, P.3    O'Brien, S.4    Tanaka, H.5    Poellinger, L.6
  • 27
    • 12644298684 scopus 로고    scopus 로고
    • Neutrophil-derived superoxide anion induces lipid peroxidation and stimulates collagen synthesis in human hepatic stellate cells: Role of nitric oxide
    • Casini A, Ceni E, Salzano R, Biondi P, Parola M, Galli A, Foschi M, Caligiuri A, Pinzani M, and Surrenti C. Neutrophil-derived superoxide anion induces lipid peroxidation and stimulates collagen synthesis in human hepatic stellate cells: role of nitric oxide. Hepatology 25: 361-367, 1997.
    • (1997) Hepatology , vol.25 , pp. 361-367
    • Casini, A.1    Ceni, E.2    Salzano, R.3    Biondi, P.4    Parola, M.5    Galli, A.6    Foschi, M.7    Caligiuri, A.8    Pinzani, M.9    Surrenti, C.10
  • 28
    • 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 GC, Tano K, and 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: 15710-15715, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 15710-15715
    • Chakravarti, D.1    Ibeanu, G.C.2    Tano, K.3    Mitra, S.4
  • 30
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: Central role of complex III
    • Chen Q, Vazquez EJ, Moghaddas S, Hoppel CL, and Lesnefsky EJ. Production of reactive oxygen species by mitochondria: central role of complex III. J Biol Chem 278: 36027-36031, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 31
    • 76649092342 scopus 로고    scopus 로고
    • Quantitative nanoproteomics for protein complexes (QNanoPX) related to estrogen transcriptional action
    • Cheng PC, Chang HK, Chen SH. Quantitative nanoproteomics for protein complexes (QNanoPX) related to estrogen transcriptional action. Mol Cell Proteomics 9: 209-224, 2010.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 209-224
    • Cheng, P.C.1    Chang, H.K.2    Chen, S.H.3
  • 33
    • 70350065725 scopus 로고    scopus 로고
    • Disorders of nucleotide excision repair: The genetic and molecular basis of heterogeneity
    • Cleaver JE, Lam ET, and Revet I. Disorders of nucleotide excision repair: the genetic and molecular basis of heterogeneity. Nat Rev Genet 10: 756-768, 2009.
    • (2009) Nat Rev Genet , vol.10 , pp. 756-768
    • Cleaver, J.E.1    Lam, E.T.2    Revet, I.3
  • 37
    • 0019976340 scopus 로고
    • Regulation of DNA ligase activity by poly(ADP-ribose)
    • Creissen D and Shall S. Regulation of DNA ligase activity by poly(ADP-ribose). Nature 296: 271-272, 1982.
    • (1982) Nature , vol.296 , pp. 271-272
    • Creissen, D.1    Shall, S.2
  • 38
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours D, Desnoyers S, D'Silva I, and Poirier GG. Poly(ADP-ribosyl) ation reactions in the regulation of nuclear functions. Biochem J 342(Pt 2): 249-268, 1999.
    • (1999) Biochem J , vol.342 , Issue.PART. 2 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 42
    • 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, and Chen DS. 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 USA 88: 11450-11454, 1991.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 44
    • 0035940441 scopus 로고    scopus 로고
    • Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair
    • Dianova, II, Bohr VA, Dianov GL. Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair. Biochemistry 40: 12639-12644, 2001.
    • (2001) Biochemistry , vol.40 , pp. 12639-12644
    • Dianova, I.I.1    Bohr, V.A.2    Dianov, G.L.3
  • 47
    • 0029042393 scopus 로고
    • Biochemical, physiological and medical aspects of ubiquinone function
    • Ernster L and Dallner G. Biochemical, physiological and medical aspects of ubiquinone function. Biochim Biophys Acta 1271: 195-204, 1995.
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 195-204
    • Ernster, L.1    Dallner, G.2
  • 48
    • 4444339833 scopus 로고    scopus 로고
    • Oxidative DNA damage and disease: Induction, repair and significance
    • Evans MD, Dizdaroglu M, and Cooke MS. Oxidative DNA damage and disease: induction, repair and significance. Mutat Res 567: 1-61, 2004.
    • (2004) Mutat Res , vol.567 , pp. 1-61
    • Evans, M.D.1    Dizdaroglu, M.2    Cooke, M.S.3
  • 51
    • 57749097697 scopus 로고    scopus 로고
    • Coordinating the initial steps of base excision repair. Apurinic/apyrimidinic endonuclease 1 actively stimulates thymine DNA glycosylase by disrupting the product complex
    • Fitzgerald ME and Drohat AC. Coordinating the initial steps of base excision repair. Apurinic/apyrimidinic endonuclease 1 actively stimulates thymine DNA glycosylase by disrupting the product complex. J Biol Chem 283: 32680-32690, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 32680-32690
    • Fitzgerald, M.E.1    Drohat, A.C.2
  • 52
    • 0033611583 scopus 로고    scopus 로고
    • Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1
    • Fritz G and Kaina B. Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1. Oncogene 18: 1033-1040, 1999.
    • (1999) Oncogene , vol.18 , pp. 1033-1040
    • Fritz, G.1    Kaina, B.2
  • 54
    • 49049087691 scopus 로고    scopus 로고
    • Evolution of the redox function in mammalian apurinic/apyrimidinic endonuclease
    • Georgiadis MM, Luo M, Gaur RK, Delaplane S, Li X, and Kelley MR. Evolution of the redox function in mammalian apurinic/apyrimidinic endonuclease. Mutat Res 643: 54-63, 2008.
    • (2008) Mutat Res , vol.643 , pp. 54-63
    • Georgiadis, M.M.1    Luo, M.2    Gaur, R.K.3    Delaplane, S.4    Li, X.5    Kelley, M.R.6
  • 56
    • 84862757952 scopus 로고    scopus 로고
    • Evolutionary dynamics of carcinogenesis and why targeted therapy does not work
    • Gillies RJ, Verduzco D, and Gatenby RA. Evolutionary dynamics of carcinogenesis and why targeted therapy does not work. Nat Rev Cancer 12: 487-493, 2012.
    • (2009) Nat Rev Cancer , vol.12 , pp. 487-493
    • Gillies, R.J.1    Verduzco, D.2    Gatenby, R.A.3
  • 58
    • 78649774638 scopus 로고    scopus 로고
    • Identification of SUMOylated proteins in neuroblastoma cells after treatment with hydrogen peroxide or ascorbat
    • Grant MM. Identification of SUMOylated proteins in neuroblastoma cells after treatment with hydrogen peroxide or ascorbate. BMB Rep 43: 720-725, 2010.
    • (2010) BMB Rep , vol.43 , pp. 720-725
    • Grant, M.M.1
  • 59
    • 18844444774 scopus 로고    scopus 로고
    • HIF-1alpha, STAT3, CBP/p300 and Ref-1/APE are components of a transcriptional complex that regulates Src-dependent hypoxia-induced expression of VEGF in pancreatic and prostate carcinomas
    • Gray MJ, Zhang J, Ellis LM, Semenza GL, Evans DB, Watowich SS, Gallick GE. HIF-1alpha, STAT3, CBP/p300 and Ref-1/APE are components of a transcriptional complex that regulates Src-dependent hypoxia-induced expression of VEGF in pancreatic and prostate carcinomas. Oncogene 24: 3110-3120, 2005.
    • (2005) Oncogene , vol.24 , pp. 3110-3120
    • Gray, M.J.1    Zhang, J.2    Ellis, L.M.3    Semenza, G.L.4    Evans, D.B.5    Watowich, S.S.6    Gallick, G.E.7
  • 60
    • 0028059099 scopus 로고
    • Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting
    • Gu H, Marth JD, Orban PC, Mossmann H, and Rajewsky K. Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting. Science 265: 103-106, 1994.
    • (1994) Science , vol.265 , pp. 103-106
    • Gu, H.1    Marth, J.D.2    Orban, P.C.3    Mossmann, H.4    Rajewsky, K.5
  • 62
    • 77954345408 scopus 로고    scopus 로고
    • Genome-wide reprogramming in the mouse germ line entails the base excision repair pathway
    • Hajkova P, Jeffries SJ, Lee C, Miller N, Jackson SP, and Surani MA. Genome-wide reprogramming in the mouse germ line entails the base excision repair pathway. Science 329: 78-82, 2010.
    • (2010) Science , vol.329 , pp. 78-82
    • Hajkova, P.1    Jeffries, S.J.2    Lee, C.3    Miller, N.4    Jackson, S.P.5    Surani, M.A.6
  • 63
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • Hardeland U, Steinacher R, Jiricny J, and Schar P. Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J 21: 1456-1464, 2002.
    • (2002) EMBO J , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schar, P.4
  • 66
    • 0037162995 scopus 로고    scopus 로고
    • Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions
    • Hazra TK, Kow YW, Hatahet Z, Imhoff B, Boldogh I, Mokkapati SK, Mitra S, and Izumi T. Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions. J Biol Chem 277: 30417-30420, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 30417-30420
    • Hazra, T.K.1    Kow, Y.W.2    Hatahet, Z.3    Imhoff, B.4    Boldogh, I.5    Mokkapati, S.K.6    Mitra, S.7    Izumi, T.8
  • 67
    • 78149469033 scopus 로고    scopus 로고
    • Functions of disordered regions in mammalian early base excision repair proteins
    • Hegde ML, Hazra TK, and Mitra S. Functions of disordered regions in mammalian early base excision repair proteins. Cell Mol Life Sci 67: 3573-3587, 2010.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3573-3587
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 68
    • 84862978423 scopus 로고    scopus 로고
    • Oxidized base damage and single-strand break repair in Mammalian genomes: Role of disordered regions and posttranslational modifications in early enzymes
    • Hegde ML, Izumi T, and Mitra S. Oxidized base damage and single-strand break repair in Mammalian genomes: role of disordered regions and posttranslational modifications in early enzymes. Prog Mol Biol Transl Sci 110: 123-153, 2012.
    • (2012) Prog Mol Biol Transl Sci , vol.110 , pp. 123-153
    • Hegde, M.L.1    Izumi, T.2    Mitra, S.3
  • 69
    • 0035863739 scopus 로고    scopus 로고
    • Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: Potential coordination of the initial steps in base excision repair
    • Hill JW, Hazra TK, Izumi T, and Mitra S. Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: potential coordination of the initial steps in base excision repair. Nucleic Acids Res 29: 430-438, 2001.
    • (2001) Nucleic Acids Res , vol.29 , pp. 430-438
    • Hill, J.W.1    Hazra, T.K.2    Izumi, T.3    Mitra, S.4
  • 70
    • 20444487725 scopus 로고    scopus 로고
    • Phosphorylation of human oxoguanine DNA glycosylase (alpha-OGG1) modulates its function
    • Hu J, Imam SZ, Hashiguchi K, de Souza-Pinto NC, and Bohr VA. Phosphorylation of human oxoguanine DNA glycosylase (alpha-OGG1) modulates its function. Nucleic Acids Res 33: 3271-3282, 2005.
    • (2005) Nucleic Acids Res , vol.33 , pp. 3271-3282
    • Hu, J.1    Imam, S.Z.2    Hashiguchi, K.3    De Souza-Pinto, N.C.4    Bohr, V.A.5
  • 71
    • 0034981858 scopus 로고    scopus 로고
    • Amino acid substitution variants of APE1 and XRCC1 genes associated with ionizing radiation sensitivity
    • Hu JJ, Smith TR, Miller MS, Mohrenweiser HW, Golden A, and Case LD. Amino acid substitution variants of APE1 and XRCC1 genes associated with ionizing radiation sensitivity. Carcinogenesis 22: 917-922, 2001.
    • (2001) Carcinogenesis , vol.22 , pp. 917-922
    • Hu, J.J.1    Smith, T.R.2    Miller, M.S.3    Mohrenweiser, H.W.4    Golden, A.5    Case, L.D.6
  • 72
    • 77956994293 scopus 로고    scopus 로고
    • Identification of RING finger protein 4 (RNF4) as a modulator of DNA demethylation through a functional genomics screen
    • Hu XV, Rodrigues TM, Tao H, Baker RK, Miraglia L, Orth AP, Lyons GE, Schultz PG, Wu X.
    • Hu XV, Rodrigues TM, Tao H, Baker RK, Miraglia L, Orth AP, Lyons GE, Schultz PG, Wu X. Identification of RING finger protein 4 (RNF4) as a modulator of DNA demethylation through a functional genomics screen. Proc Natl Acad Sci USA 107: 15087-15092, 2010.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 15087-15092
  • 73
    • 82655187105 scopus 로고    scopus 로고
    • Generation and replication-dependent dilution of 5fC and 5caC during mouse preimplantation development
    • Inoue A, Shen L, Dai Q, He C, and Zhang Y. Generation and replication-dependent dilution of 5fC and 5caC during mouse preimplantation development. Cell Res 21: 1670-1676, 2011.
    • (2011) Cell Res , vol.21 , pp. 1670-1676
    • Inoue, A.1    Shen, L.2    Dai, Q.3    He, C.4    Zhang, Y.5
  • 74
    • 0037049975 scopus 로고    scopus 로고
    • Alternative nucleotide incision repair pathway for oxidative DNA damage
    • Ischenko AA and Saparbaev MK. Alternative nucleotide incision repair pathway for oxidative DNA damage. Nature 415: 183-187, 2002.
    • (2002) Nature , vol.415 , pp. 183-187
    • Ischenko, A.A.1    Saparbaev, M.K.2
  • 75
    • 33644546374 scopus 로고    scopus 로고
    • Uncoupling of the base excision and nucleotide incision repair pathways reveals their respective biological roles
    • Ishchenko AA, Deprez E, Maksimenko A, Brochon JC, Tauc P, and Saparbaev MK. Uncoupling of the base excision and nucleotide incision repair pathways reveals their respective biological roles. Proc Natl Acad Sci USA 103: 2564-2569, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2564-2569
    • Ishchenko, A.A.1    Deprez, E.2    Maksimenko, A.3    Brochon, J.C.4    Tauc, P.5    Saparbaev, M.K.6
  • 76
    • 0242268065 scopus 로고    scopus 로고
    • Mammalian DNA base excision repair proteins: Their interactions and role in repair of oxidative DNA damage
    • Izumi T, Wiederhold LR, Roy G, Roy R, Jaiswal A, Bhakat KK, Mitra S, and Hazra TK. Mammalian DNA base excision repair proteins: their interactions and role in repair of oxidative DNA damage. Toxicology 193: 43-65, 2003.
    • (2003) Toxicology , vol.193 , pp. 43-65
    • Izumi, T.1    Wiederhold, L.R.2    Roy, G.3    Roy, R.4    Jaiswal, A.5    Bhakat, K.K.6    Mitra, S.7    Hazra, T.K.8
  • 77
    • 20444490757 scopus 로고    scopus 로고
    • Analysis of nuclear transport signals in the human apurinic/apyrimidinic endonuclease (APE1/Ref1)
    • Jackson EB, Theriot CA, Chattopadhyay R, Mitra S, and Izumi T. Analysis of nuclear transport signals in the human apurinic/apyrimidinic endonuclease (APE1/Ref1). Nucleic Acids Res 33: 3303-3312, 2005.
    • (2005) Nucleic Acids Res , vol.33 , pp. 3303-3312
    • Jackson, E.B.1    Theriot, C.A.2    Chattopadhyay, R.3    Mitra, S.4    Izumi, T.5
  • 78
    • 0344442405 scopus 로고    scopus 로고
    • 8-Hydroxyguanine in a mutational hotspot of the c-Ha-ras gene causes misreplication 'action-at-adistance' mutagenesis and inhibition of replication
    • Jaloszynski P, Masutani C, Hanaoka F, Perez AB, and Nishimura S. 8-Hydroxyguanine in a mutational hotspot of the c-Ha-ras gene causes misreplication, 'action-at-adistance' mutagenesis and inhibition of replication. Nucleic Acids Res 31: 6085-6095, 2003.
    • (2003) Nucleic Acids Res , vol.31 , pp. 6085-6095
    • Jaloszynski, P.1    Masutani, C.2    Hanaoka, F.3    Perez, A.B.4    Nishimura, S.5
  • 82
    • 0026650584 scopus 로고
    • And Ohtsuka E c-Ha-ras containing 8-hydroxyguanine at codon 12 induces point mutations at the modified and adjacent positions
    • Kamiya H, Miura K, Ishikawa H, Inoue H, Nishimura S, and Ohtsuka E. c-Ha-ras containing 8-hydroxyguanine at codon 12 induces point mutations at the modified and adjacent positions. Cancer Res 52: 3483-3485, 1992.
    • (1992) Cancer Res , vol.52 , pp. 3483-3485
    • Kamiya, H.1    Miura, K.2    Ishikawa, H.3    Inoue, H.4    Nishimura, S.5
  • 83
    • 0028944525 scopus 로고
    • 8-Hydroxyguanine (7,8-dihydro-8-oxoguanine) in hot spots of the c-Ha-ras gene: Effects of sequence contexts on mutation spectra
    • Kamiya H, Murata-Kamiya N, Koizume S, Inoue H, Nishimura S, and Ohtsuka E. 8-Hydroxyguanine (7,8-dihydro-8-oxoguanine) in hot spots of the c-Ha-ras gene: effects of sequence contexts on mutation spectra. Carcinogenesis 16: 883-889, 1995.
    • (1995) Carcinogenesis , vol.16 , pp. 883-889
    • Kamiya, H.1    Murata-Kamiya, N.2    Koizume, S.3    Inoue, H.4    Nishimura, S.5    Ohtsuka, E.6
  • 84
    • 0021008815 scopus 로고
    • Hydroxylation of the C-8 position of deoxyguanosine by reducing agents in the presence of oxygen
    • Kasai H and Nishimura S. Hydroxylation of the C-8 position of deoxyguanosine by reducing agents in the presence of oxygen. Nucleic Acids Symp Ser 12: 165-167, 1983.
    • (1983) Nucleic Acids Symp ser , vol.12 , pp. 165-167
    • Kasai, H.1    Nishimura, S.2
  • 85
    • 84860346892 scopus 로고    scopus 로고
    • An evolutionary view of the mechanism for immune and genome diversity
    • Kato L, Stanlie A, Begum NA, Kobayashi M, Aida M, and Honjo T. An evolutionary view of the mechanism for immune and genome diversity. J Immunol 188: 3559-3566, 2012.
    • (2012) J Immunol , vol.188 , pp. 3559-3566
    • Kato, L.1    Stanlie, A.2    Begum, N.A.3    Kobayashi, M.4    Aida, M.5    Honjo, T.6
  • 87
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1)
    • Klungland A and Lindahl T. Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). EMBO J 16: 3341-3348, 1997.
    • (1997) EMBO J , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 90
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan HE, Standal R, and Slupphaug G. DNA glycosylases in the base excision repair of DNA. Biochem J 325(Pt 1): 1-16, 1997.
    • (1997) Biochem J , vol.325 , Issue.PART. 1 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 91
    • 84866134921 scopus 로고    scopus 로고
    • A high-throughput approach for measuring temporal changes in the interactome
    • Kristensen AR, Gsponer J, Foster LJ. A high-throughput approach for measuring temporal changes in the interactome. Nature Methods 9: 907-909, 2012.
    • (2012) Nature Methods , vol.9 , pp. 907-909
    • Kristensen, A.R.1    Gsponer, J.2    Foster, L.J.3
  • 92
    • 71049180608 scopus 로고    scopus 로고
    • Complementary quantitative proteomics reveals that transcription factor AP-4 mediates E-box-dependent complex formation for transcriptional repression of HDM2
    • Ku WC, Chiu SK, Chen YJ, Huang HH, Wu WG, Chen YJ. Complementary quantitative proteomics reveals that transcription factor AP-4 mediates E-box-dependent complex formation for transcriptional repression of HDM2. Mol Cell Proteomics 8: 2034-2050, 2009.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2034-2050
    • Ku, W.C.1    Chiu, S.K.2    Chen, Y.J.3    Huang, H.H.4    Wu, W.G.5    Chen, Y.J.6
  • 93
    • 0036464533 scopus 로고    scopus 로고
    • Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter
    • Kuninger DT, Izumi T, Papaconstantinou J, Mitra S. Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter. Nucleic Acids Res 30: 823-829, 2002.
    • (2002) Nucleic Acids Res , vol.3 , pp. 823-829
    • Kuninger, D.T.1    Izumi, T.2    Papaconstantinou, J.3    Mitra, S.4
  • 94
    • 79953212976 scopus 로고    scopus 로고
    • Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells
    • (doi: 10.1074/mcp.M110.001628)
    • Lee OH, Kim H, He Q, Baek HJ, Yang D, Chen LY, Liang J, Chae HK, Safari A, Liu D, Songyang Z. Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells. Mol Cell Proteomics 10: M110 001628, 2011. (doi: 10.1074/mcp.M110.001628).
    • (2011) Mol Cell Proteomics , vol.10
    • Lee, O.H.1    Kim, H.2    He, Q.3    Baek, H.J.4    Yang, D.5    Chen, L.Y.6    Liang, J.7    Chae, H.K.8    Safari, A.9    Liu, D.10    Songyang, Z.11
  • 95
    • 77950519512 scopus 로고    scopus 로고
    • OGG1 is a novel prognostic indicator in acute myeloid leukaemia
    • Liddiard K, Hills R, Burnett AK, Darley RL, and Tonks A. OGG1 is a novel prognostic indicator in acute myeloid leukaemia. Oncogene 29: 2005-2012, 2010.
    • (2010) Oncogene , vol.29 , pp. 2005-2012
    • Liddiard, K.1    Hills, R.2    Burnett, A.K.3    Darley, R.L.4    Tonks, A.5
  • 96
    • 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: 709-715, 1993.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 97
  • 101
    • 84856019858 scopus 로고    scopus 로고
    • The DNA damage response and cancer therapy
    • Lord CJ and Ashworth A. The DNA damage response and cancer therapy. Nature 481: 287-294, 2012.
    • (2012) Nature , vol.481 , pp. 287-294
    • Lord, C.J.1    Ashworth, A.2
  • 102
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
    • Maki H and Sekiguchi M. MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature 355: 273-275, 1992.
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 103
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair
    • Matsumoto Y and Kim K. Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair. Science 269: 699-702, 1995.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 105
    • 0029092218 scopus 로고
    • Origin of a negative calcium response element in an ALU-repeat: Implications for regulation of gene expression by extracellular calcium
    • McHaffie GS and Ralston SH. Origin of a negative calcium response element in an ALU-repeat: implications for regulation of gene expression by extracellular calcium. Bone 17: 11-14, 1995.
    • (1995) Bone , vol.17 , pp. 11-14
    • McHaffie, G.S.1    Ralston, S.H.2
  • 106
    • 55949136614 scopus 로고    scopus 로고
    • Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry
    • Meierhofer D, Wang X, Huang L, Kaiser P. Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res 7: 4566-4576, 2008.
    • (2008) J Proteome Res , vol.7 , pp. 4566-4576
    • Meierhofer, D.1    Wang, X.2    Huang, L.3    Kaiser, P.4
  • 109
    • 34548227894 scopus 로고    scopus 로고
    • TRAF2 and p38 are involved in B cells CD40-mediated APE/Ref-1 nuclear translocation: A novel pathway in B cell activatio
    • Merluzzi S, D'Orlando O, Leonardi A, Vitale G, Pucillo C. TRAF2 and p38 are involved in B cells CD40-mediated APE/Ref-1 nuclear translocation: a novel pathway in B cell activation. Mol Immunol 45: 76-86, 2008.
    • (2008) Mol Immunol , vol.45 , pp. 76-86
    • Merluzzi, S.1    D'Orlando, O.2    Leonardi, A.3    Vitale, G.4    Pucillo, C.5
  • 110
    • 0026684849 scopus 로고
    • Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA
    • Michaels ML, Cruz C, Grollman AP, and Miller JH. Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA. Proc Natl Acad Sci USA 89: 7022-7025, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7022-7025
    • Michaels, M.L.1    Cruz, C.2    Grollman, A.P.3    Miller, J.H.4
  • 111
    • 0028170326 scopus 로고
    • Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress
    • Michiels C, Raes M, Toussaint O, and Remacle J. Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radic Biol Med 17: 235-248, 1994.
    • (1994) Free Radic Biol Med , vol.17 , pp. 235-248
    • Michiels, C.1    Raes, M.2    Toussaint, O.3    Remacle, J.4
  • 112
    • 77950347722 scopus 로고    scopus 로고
    • Opposing regulatory roles of phosphorylation and acetylation in DNA mispair processing by thymine DNA glycosylase
    • Mohan RD, Litchfield DW, Torchia J, and Tini M. Opposing regulatory roles of phosphorylation and acetylation in DNA mispair processing by thymine DNA glycosylase. Nucleic Acids Res 38: 1135-1148, 2010.
    • (2010) Nucleic Acids Res , vol.38 , pp. 1135-1148
    • Mohan, R.D.1    Litchfield, D.W.2    Torchia, J.3    Tini, M.4
  • 113
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected]
    • Mol CD, Izumi T, Mitra S, and Tainer JA. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected]. Nature 403: 451-456, 2000.
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 115
    • 0023992806 scopus 로고
    • The mutY gene: Amutator locus in Escherichia coli that generatesG.C-T.A transversions
    • Nghiem Y, Cabrera M, Cupples CG, and Miller JH. The mutY gene: amutator locus in Escherichia coli that generatesG.C-T.A transversions. Proc Natl Acad Sci USA 85: 2709-2713, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2709-2713
    • Nghiem, Y.1    Cabrera, M.2    Cupples, C.G.3    Miller, J.H.4
  • 116
    • 84857375721 scopus 로고    scopus 로고
    • 8-Hydroxyguanine: A base for discovery
    • Nishimura S. 8-Hydroxyguanine: a base for discovery. DNA Repair (Amst) 10: 1078-1083, 2011.
    • (2011) DNA Repair (Amst) , vol.10 , pp. 1078-1083
    • Nishimura, S.1
  • 118
    • 84867853849 scopus 로고    scopus 로고
    • Mitochondrial defect drives non-autonomous tumour progression through Hippo signalling in Drosophila
    • Ohsawa S, Sato Y, Enomoto M, Nakamura M, Betsumiya A, and Igaki T. Mitochondrial defect drives non-autonomous tumour progression through Hippo signalling in Drosophila. Nature 490: 547-551, 2012.
    • (2012) Nature , vol.490 , pp. 547-551
    • Ohsawa, S.1    Sato, Y.2    Enomoto, M.3    Nakamura, M.4    Betsumiya, A.5    Igaki, T.6
  • 120
    • 0036716827 scopus 로고    scopus 로고
    • Detection of mitochondrial DNA alterations in the serum of hepatocellular carcinoma patients
    • Okochi O, Hibi K, Uemura T, Inoue S, Takeda S, Kaneko T, and Nakao A. Detection of mitochondrial DNA alterations in the serum of hepatocellular carcinoma patients. Clin Cancer Res 8: 2875-2878, 2002.
    • (2002) Clin Cancer Res , vol.8 , pp. 2875-2878
    • Okochi, O.1    Hibi, K.2    Uemura, T.3    Inoue, S.4    Takeda, S.5    Kaneko, T.6    Nakao, A.7
  • 123
    • 0035937102 scopus 로고    scopus 로고
    • Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair
    • Parker A, Gu Y, Mahoney W, Lee SH, Singh KK, Lu AL. Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair. J Biol Chem 276: 5547-5555, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 5547-5555
    • Parker, A.1    Gu, Y.2    Mahoney, W.3    Lee, S.H.4    Singh, K.K.5    Lu, A.L.6
  • 124
    • 0034734383 scopus 로고    scopus 로고
    • Structure and function in the uracil-DNA glycosylase superfamily
    • Pearl LH. Structure and function in the uracil-DNA glycosylase superfamily. Mutat Res 460: 165-181, 2000.
    • (2000) Mutat Res , vol.460 , pp. 165-181
    • Pearl, L.H.1
  • 125
    • 34250357205 scopus 로고    scopus 로고
    • Nitric oxide controls nuclear export of APE1/Ref-1 through S-nitrosation of cysteines 93 and 310
    • Qu J, Liu GH, Huang B, and Chen C. Nitric oxide controls nuclear export of APE1/Ref-1 through S-nitrosation of cysteines 93 and 310. Nucleic Acids Res 35: 2522-2532, 2007.
    • (2007) Nucleic Acids Res , vol.35 , pp. 2522-2532
    • Qu, J.1    Liu, G.H.2    Huang, B.3    Chen, C.4
  • 126
    • 0242380642 scopus 로고    scopus 로고
    • Mitochondria-mediated nuclear mutator phenotype in Saccharomyces cerevisiae
    • Rasmussen AK, Chatterjee A, Rasmussen LJ, and Singh KK. Mitochondria-mediated nuclear mutator phenotype in Saccharomyces cerevisiae. Nucleic Acids Res 31: 3909-3917, 2003.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3909-3917
    • Rasmussen, A.K.1    Chatterjee, A.2    Rasmussen, L.J.3    Singh, K.K.4
  • 127
    • 34248215322 scopus 로고    scopus 로고
    • Actions of aprataxin in multiple DNA repair pathways
    • Rass U, Ahel I, and West SC. Actions of aprataxin in multiple DNA repair pathways. J Biol Chem 282: 9469-9474, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 9469-9474
    • Rass, U.1    Ahel, I.2    West, S.C.3
  • 131
    • 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 CN and Hickson ID. 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: 5519-5523, 1991.
    • (1991) Nucleic Acids Res , vol.19 , pp. 5519-5523
    • Robson, C.N.1    Hickson, I.D.2
  • 133
    • 80053379755 scopus 로고
    • Involvement of DNA ligase III and ribonuclease H1 in mitochondrial DNA replication in cultured human cells
    • Ruhanen H, Ushakov K, and Yasukawa T. Involvement of DNA ligase III and ribonuclease H1 in mitochondrial DNA replication in cultured human cells. Biochim Biophys Acta 1813: 2000-2007, 2011.
    • (1813) Biochim Biophys Acta , pp. 2000-2007
    • Ruhanen, H.1    Ushakov, K.2    Yasukawa, T.3
  • 137
    • 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, and 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 USA 88: 9127-9131, 1991.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9127-9131
    • Samson, L.1    Derfler, B.2    Boosalis, M.3    Call, K.4
  • 139
    • 0026507413 scopus 로고
    • Role of poly(ADP-ribose) formation in DNA repair
    • Satoh MS and Lindahl T. Role of poly(ADP-ribose) formation in DNA repair. Nature 356: 356-358, 1992.
    • (1992) Nature , vol.356 , pp. 356-358
    • Satoh, M.S.1    Lindahl, T.2
  • 140
    • 20544433877 scopus 로고    scopus 로고
    • Roles of thioredoxin reductase 1 and APE/Ref-1 in the control of basal p53 stability and activity
    • Seemann S, Hainaut P. Roles of thioredoxin reductase 1 and APE/Ref-1 in the control of basal p53 stability and activity. Oncogene 24: 3853-3863, 2005.
    • (2005) Oncogene , vol.24 , pp. 3853-4386
    • Seemann, S.1    Hainaut, P.2
  • 141
    • 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
    • Seki S, Akiyama K, Watanabe S, Hatsushika M, Ikeda S, and Tsutsui K. 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: 20797-20802, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 20797-20802
    • Seki, S.1    Akiyama, K.2    Watanabe, S.3    Hatsushika, M.4    Ikeda Tsutsui, S.K.5
  • 142
    • 79251647522 scopus 로고    scopus 로고
    • Human AP endonuclease (APE1/Ref-1) and its acetylation regulate YB-1-p300 recruitment and RNA polymerase II loading in the drug-induced activation of multidrug resistance gene MDR1
    • Sengupta S, Mantha AK, Mitra S, Bhakat KK. Human AP endonuclease (APE1/Ref-1) and its acetylation regulate YB-1-p300 recruitment and RNA polymerase II loading in the drug-induced activation of multidrug resistance gene MDR1. Oncogene 30: 482-493, 2011.
    • (2011) Oncogene , vol.30 , pp. 482-493
    • Sengupta, S.1    Mantha, A.K.2    Mitra, S.3    Bhakat, K.K.4
  • 144
    • 84876946045 scopus 로고    scopus 로고
    • Genome-wide analysis reveals TET-and TDG-dependent 5-methylcytosine oxidation dynamics
    • Shen L, Wu H, Diep D, Yamaguchi S, D'Alessio AC, Fung HL, Zhang K, and Zhang Y. Genome-wide analysis reveals TET-and TDG-dependent 5-methylcytosine oxidation dynamics. Cell 153: 692-706, 2013.
    • (2013) Cell , vol.153 , pp. 692-706
    • Shen, L.1    Wu, H.2    Diep, D.3    Yamaguchi, S.4    D'Alessio, A.C.5    Fung, H.L.6    Zhang, K.7    Zhang, Y.8
  • 145
    • 0027179827 scopus 로고
    • Short gap-filling synthesis by DNA polymerase beta is processive
    • Singhal RK and Wilson SH. Short gap-filling synthesis by DNA polymerase beta is processive. J Biol Chem 268: 15906-15911, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 15906-15911
    • Singhal, R.K.1    Wilson, S.H.2
  • 146
    • 0028966181 scopus 로고
    • DNA polymerase beta conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract
    • Singhal RK, Prasad R, and Wilson SH. DNA polymerase beta conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract. J Biol Chem 270: 949-957, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 949-957
    • Singhal, R.K.1    Prasad, R.2    Wilson, S.H.3
  • 148
    • 0034254724 scopus 로고    scopus 로고
    • Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8
    • Sugahara M, Mikawa T, Kumasaka T, Yamamoto M, Kato R, Fukuyama K, Inoue Y, and Kuramitsu S. Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8. EMBO J 19: 3857-3869, 2000.
    • (2000) EMBO J , vol.19 , pp. 3857-3869
    • Sugahara, M.1    Mikawa, T.2    Kumasaka, T.3    Yamamoto, M.4    Kato, R.5    Fukuyama, K.6    Inoue, Y.7    Kuramitsu, S.8
  • 149
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics
    • Szabo C, Ischiropoulos H, and Radi R. Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat Rev Drug Discov 6: 662-680, 2007.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 150
    • 24344436378 scopus 로고    scopus 로고
    • Effect of aging on intracellular distribution of abasic (AP) endonuclease 1 in the mouse liver
    • Szczesny B and Mitra S. Effect of aging on intracellular distribution of abasic (AP) endonuclease 1 in the mouse liver. Mech Ageing Dev 126: 1071-1078, 2005.
    • (2005) Mech Ageing Dev , vol.126 , pp. 1071-1078
    • Szczesny, B.1    Mitra, S.2
  • 151
    • 55049124777 scopus 로고    scopus 로고
    • Long patch base excision repair in mammalian mitochondrial genomes
    • Szczesny B, Tann AW, Longley MJ, Copeland WC, and Mitra S. Long patch base excision repair in mammalian mitochondrial genomes. J Biol Chem 283: 26349-26356, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 26349-26356
    • Szczesny, B.1    Tann, A.W.2    Longley, M.J.3    Copeland, W.C.4    Mitra, S.5
  • 152
    • 0032526616 scopus 로고    scopus 로고
    • Mitochondrial targeting of human DNA glycosylases for repair of oxidative DNA damage
    • Takao M, Aburatani H, Kobayashi K, and Yasui A. Mitochondrial targeting of human DNA glycosylases for repair of oxidative DNA damage. Nucleic Acids Res 26: 2917-2922, 1998.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2917-2922
    • Takao, M.1    Aburatani, H.2    Kobayashi, K.3    Yasui, A.4
  • 153
    • 80052698492 scopus 로고    scopus 로고
    • Apoptosis induced by persistent single-strand breaks in mitochondrial genome: Critical role of EXOG (5¢-EXO/endonuclease) in their repair
    • Tann AW, Boldogh I, Meiss G, Qian W, Van Houten B, Mitra S, and Szczesny B. Apoptosis induced by persistent single-strand breaks in mitochondrial genome: critical role of EXOG (5¢-EXO/endonuclease) in their repair. J Biol Chem 286: 31975-31983, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 31975-31983
    • Tann, A.W.1    Boldogh, I.2    Meiss, G.3    Qian, W.4    Van Houten, B.5    Mitra, S.6    Szczesny, B.7
  • 154
    • 0025105041 scopus 로고
    • Collier J, Foote RS, and Mitra S. Isolation and structural characterization of a cDNA clone encoding the human DNA repair protein for O6-alkylguanine. Proc Natl Acad Sci USA
    • Tano K, Shiota S, Collier J, Foote RS, and Mitra S. Isolation and structural characterization of a cDNA clone encoding the human DNA repair protein for O6-alkylguanine. Proc Natl Acad Sci USA 87: 686-690, 1990.
    • (1990) , vol.87 , pp. 686-690
    • Tano, K.1    Shiota, S.2
  • 157
    • 0024241304 scopus 로고
    • Mitochondrial endonuclease activities specific for apurinic/apyrimidinic sites in DNA from mouse cells
    • Tomkinson AE, Bonk RT, and Linn S. Mitochondrial endonuclease activities specific for apurinic/apyrimidinic sites in DNA from mouse cells. J Biol Chem 263: 12532-12537, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 12532-12537
    • Tomkinson, A.E.1    Bonk, R.T.2    Linn, S.3
  • 159
    • 0035369734 scopus 로고    scopus 로고
    • Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen
    • Tsuchimoto D, Sakai Y, Sakumi K, Nishioka K, Sasaki M, Fujiwara T, and Nakabeppu Y. Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen. Nucleic Acids Res 29: 2349-2660, 2001.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2349-2660
    • Tsuchimoto, D.1    Sakai, Y.2    Sakumi, K.3    Nishioka, K.4    Sasaki, M.5    Fujiwara, T.6    Nakabeppu, Y.7
  • 163
    • 0035890069 scopus 로고    scopus 로고
    • XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions
    • Vidal AE, Boiteux S, Hickson ID, Radicella JP. XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions. EMBO J 20: 6530-6539, 2001.
    • (2001) EMBO J , vol.20 , pp. 6530-6539
    • Vidal, A.E.1    Boiteux, S.2    Hickson, I.D.3    Radicella, J.P.4
  • 165
    • 0027324056 scopus 로고
    • Identification of residues in the human DNA repair enzyme HAP1 (Ref-1) that are essential for redox regulation of Jun DNA binding
    • Walker LJ, Robson CN, Black E, Gillespie D, and Hickson ID. Identification of residues in the human DNA repair enzyme HAP1 (Ref-1) that are essential for redox regulation of Jun DNA binding. Mol Cell Biol 13: 5370-5376, 1993.
    • (1993) Mol Cell Biol , vol.13 , pp. 5370-5376
    • Walker, L.J.1    Robson, C.N.2    Black, E.3    Gillespie, D.4    Hickson, I.D.5
  • 166
  • 167
    • 84875181661 scopus 로고    scopus 로고
    • Oxidants, antioxidants and the current incurability of metastatic cancers
    • Watson J. Oxidants, antioxidants and the current incurability of metastatic cancers. Open Biol 3: 120144, 2013.
    • (2013) Open Biol , vol.3 , pp. 120144
    • Watson, J.1
  • 168
    • 84875392806 scopus 로고    scopus 로고
    • Association between the OGG1 Ser326Cys and APEX1 Asp148Glu polymorphisms and lung cancer risk: A meta-analysis
    • Wei W, He XF, Qin JB, Su J, Li SX, Liu Y, Zhang Y, and Wang W. Association between the OGG1 Ser326Cys and APEX1 Asp148Glu polymorphisms and lung cancer risk: a meta-analysis. Mol Biol Rep 39: 11249-11262, 2012.
    • (2012) Mol Biol Rep , vol.39 , pp. 11249-11262
    • Wei, W.1    He, X.F.2    Qin, J.B.3    Su, J.4    Li, S.X.5    Liu, Y.6    Zhang, Y.7    Wang, W.8
  • 170
    • 0034093291 scopus 로고    scopus 로고
    • Passing the baton in base excision repair
    • Wilson SH and Kunkel TA. Passing the baton in base excision repair. Nat Struct Biol 7: 176-178, 2000.
    • (2000) Nat Struct Biol , vol.7 , pp. 176-178
    • Wilson, S.H.1    Kunkel, T.A.2
  • 171
    • 77955174568 scopus 로고    scopus 로고
    • Subcellular localization of apurinic endonuclease 1 promotes lung tumor aggressiveness via NF-kappaB activation
    • Wu HH, Cheng YW, Chang JT, Wu TC, Liu WS, Chen CY, and Lee H. Subcellular localization of apurinic endonuclease 1 promotes lung tumor aggressiveness via NF-kappaB activation. Oncogene 29: 4330-4340, 2010.
    • (2010) Oncogene , vol.29 , pp. 4330-4340
    • Wu, H.H.1    Cheng, Y.W.2    Chang, J.T.3    Wu, T.C.4    Liu, W.S.5    Chen, C.Y.6    Lee, H.7
  • 172
    • 84892784526 scopus 로고    scopus 로고
    • Cytoplasmic Ape1 expression elevated by p53 aberration may predict survival and relapse in resected non-small cell lung cancer
    • Epub ahead of print DOI: 10.1245/s10434-012-2431-2
    • Wu HH, Chu YC,Wang L, Tsai LH, LeeMC, Chen CY, Shieh SH, Cheng YW, and Lee H. Cytoplasmic Ape1 expression elevated by p53 aberration may predict survival and relapse in resected non-small cell lung cancer. Ann Surg Oncol 2012 [Epub ahead of print]; DOI: 10.1245/s10434-012-2431-2.
    • (2012) Ann Surg Oncol
    • Wu, H.H.1    Chu Ycwang, L.2    Tsai, L.H.3    Leemc Chen, C.Y.4    Shieh, S.H.5    Cheng, Y.W.6    Lee, H.7
  • 173
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis S, Miao G, Wang F, Pan YC, and Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J 11: 3323-3335, 1992.
    • (1992) EMBO J , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.C.4    Curran, T.5
  • 174
    • 0029829265 scopus 로고    scopus 로고
    • The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice
    • Xanthoudakis S, Smeyne RJ, Wallace JD, and Curran T. The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice. Proc Natl Acad Sci USA 93: 8919-8923, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8919-8923
    • Xanthoudakis, S.1    Smeyne, R.J.2    Wallace, J.D.3    Curran, T.4
  • 176
    • 0031439356 scopus 로고    scopus 로고
    • The DNA repair activity of human redox/repair protein APE/Ref-1 is inactivated by phosphorylation
    • Yacoub A, Kelley MR, and Deutsch WA. The DNA repair activity of human redox/repair protein APE/Ref-1 is inactivated by phosphorylation. Cancer Res 57: 5457-5459, 1997.
    • (1997) Cancer Res , vol.57 , pp. 5457-5459
    • Yacoub, A.1    Kelley, M.R.2    Deutsch, W.A.3
  • 178
    • 0035253515 scopus 로고    scopus 로고
    • Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatch
    • Yang H, Clendenin WM, Wong D, Demple B, Slupska MM, Chiang JH, and Miller JH. Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatch. Nucleic Acids Res 29: 743-752, 2001.
    • (2001) Nucleic Acids Res , vol.29 , pp. 743-752
    • Yang, H.1    Clendenin, W.M.2    Wong, D.3    Demple, B.4    Slupska, M.M.5    Chiang, J.H.6    Miller, J.H.7
  • 179
    • 43049102429 scopus 로고    scopus 로고
    • Alteration of APE1/ref-1 expression in non-small cell lung cancer: The implications of impaired extracellular superoxide dismutase and catalase antioxidant systems
    • Yoo DG, Song YJ, Cho EJ, Lee SK, Park JB, Yu JH, Lim SP, Kim JM, and Jeon BH. Alteration of APE1/ref-1 expression in non-small cell lung cancer: the implications of impaired extracellular superoxide dismutase and catalase antioxidant systems. Lung Cancer 60: 277-284, 2008.
    • (2008) Lung Cancer , vol.60 , pp. 277-284
    • Yoo, D.G.1    Song, Y.J.2    Cho, E.J.3    Lee, S.K.4    Park, J.B.5    Yu, J.H.6    Lim, S.P.7    Kim, J.M.8    Jeon, B.H.9
  • 181
    • 0022359332 scopus 로고
    • Inhibition of DNA polymerase alpha, DNA polymerase beta, terminal deoxynucleotidyl transferase, and DNA ligase II by poly(-ADP-ribosyl)ation reaction in vitro
    • Yoshihara K, Itaya A, Tanaka Y, Ohashi Y, Ito K, Teraoka H, Tsukada K, Matsukage A, and Kamiya T. Inhibition of DNA polymerase alpha, DNA polymerase beta, terminal deoxynucleotidyl transferase, and DNA ligase II by poly(-ADP-ribosyl)ation reaction in vitro. Biochem Biophys Res Commun 128: 61-67, 1985.
    • (1985) Biochem Biophys Res Commun , vol.128 , pp. 61-67
    • Yoshihara, K.1    Itaya, A.2    Tanaka, Y.3    Ohashi, Y.4    Ito, K.5    Teraoka, H.6    Tsukada, K.7    Matsukage, A.8    Kamiya, T.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.