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Volumn 129, Issue 7-8, 2008, Pages 366-382

Base excision repair, aging and health span

Author keywords

Aging; Base excision repair; DNA damage; Health span; Mutagenesis

Indexed keywords

DNA DIRECTED DNA POLYMERASE BETA; DNA GLYCOSYLTRANSFERASE; GUANINE;

EID: 46149083468     PISSN: 00476374     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mad.2008.03.001     Document Type: Article
Times cited : (96)

References (273)
  • 3
    • 0014040945 scopus 로고
    • The role of DNA lesions in the processes leading to aging in mice
    • Alexander P. The role of DNA lesions in the processes leading to aging in mice. Symp. Soc. Exp. Biol. 21 (1967) 29-50
    • (1967) Symp. Soc. Exp. Biol. , vol.21 , pp. 29-50
    • Alexander, P.1
  • 4
    • 34247599335 scopus 로고    scopus 로고
    • A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification
    • Almeida K.H., and Sobol R.W. A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification. DNA Repair (Amst.) 6 (2007) 695-711
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 695-711
    • Almeida, K.H.1    Sobol, R.W.2
  • 6
    • 21844464297 scopus 로고    scopus 로고
    • C → T mutagenesis and gamma-radiation sensitivity due to deficiency in the Smug1 and Ung DNA glycosylases
    • An Q., Robins P., Lindahl T., and Barnes D.E. C → T mutagenesis and gamma-radiation sensitivity due to deficiency in the Smug1 and Ung DNA glycosylases. EMBO J. 24 (2005) 2205-2213
    • (2005) EMBO J. , vol.24 , pp. 2205-2213
    • An, Q.1    Robins, P.2    Lindahl, T.3    Barnes, D.E.4
  • 7
    • 33847057392 scopus 로고    scopus 로고
    • 5-Fluorouracil incorporated into DNA is excised by the Smug1 DNA glycosylase to reduce drug cytotoxicity
    • An Q., Robins P., Lindahl T., and Barnes D.E. 5-Fluorouracil incorporated into DNA is excised by the Smug1 DNA glycosylase to reduce drug cytotoxicity. Cancer Res. 67 (2007) 940-945
    • (2007) Cancer Res. , vol.67 , pp. 940-945
    • An, Q.1    Robins, P.2    Lindahl, T.3    Barnes, D.E.4
  • 8
    • 33646183367 scopus 로고    scopus 로고
    • DNA damage responses and their many interactions with the replication fork
    • Andreassen P.R., Ho G.P.H., and D'Andrea A.D. DNA damage responses and their many interactions with the replication fork. Carcinogenesis 27 (2006) 883-892
    • (2006) Carcinogenesis , vol.27 , pp. 883-892
    • Andreassen, P.R.1    Ho, G.P.H.2    D'Andrea, A.D.3
  • 10
    • 0141670355 scopus 로고    scopus 로고
    • Enzymatic properties of Escherichia coli and human 7,8-dihydro-8-oxoguanine DNA glycosylases
    • Asagoshi K., Yamada T., Terato H., Ohyama Y., and Ide H. Enzymatic properties of Escherichia coli and human 7,8-dihydro-8-oxoguanine DNA glycosylases. Nucleic Acids Symp. Ser. (2000) 11-12
    • (2000) Nucleic Acids Symp. Ser. , pp. 11-12
    • Asagoshi, K.1    Yamada, T.2    Terato, H.3    Ohyama, Y.4    Ide, H.5
  • 11
    • 0034681176 scopus 로고    scopus 로고
    • A method for detecting abasic sites in living cells: age-dependent changes in base excision repair
    • Atamna H., Cheung I., and Ames B.N. A method for detecting abasic sites in living cells: age-dependent changes in base excision repair. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 686-691
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 686-691
    • Atamna, H.1    Cheung, I.2    Ames, B.N.3
  • 12
    • 0346243565 scopus 로고    scopus 로고
    • Functional characterization of polymorphisms in DNA repair genes using cytogenetic challenge assays
    • Au W.W., Salama S.A., and Sierra-Torres C.H. Functional characterization of polymorphisms in DNA repair genes using cytogenetic challenge assays. Environ. Health Perspect. 111 (2003) 1843-1850
    • (2003) Environ. Health Perspect. , vol.111 , pp. 1843-1850
    • Au, W.W.1    Salama, S.A.2    Sierra-Torres, C.H.3
  • 14
    • 0036151695 scopus 로고    scopus 로고
    • Characterization of the substrate specificity of a human 5-hydroxymethyluracil glycosylase activity
    • Baker D., Liu P., Burdzy A., and Sowers L.C. Characterization of the substrate specificity of a human 5-hydroxymethyluracil glycosylase activity. Chem. Res. Toxicol. 15 (2002) 33-39
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 33-39
    • Baker, D.1    Liu, P.2    Burdzy, A.3    Sowers, L.C.4
  • 15
    • 0037125133 scopus 로고    scopus 로고
    • A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII
    • Bandaru V., Sunkara S., Wallace S.S., and Bond J.P. A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII. DNA Repair (Amst.) 1 (2002) 517-529
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 517-529
    • Bandaru, V.1    Sunkara, S.2    Wallace, S.S.3    Bond, J.P.4
  • 16
    • 0032498302 scopus 로고    scopus 로고
    • Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions
    • Barrett T.E., Savva R., Panayotou G., Barlow T., Brown T., Jiricny J., and Pearl L.H. Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92 (1998) 117-129
    • (1998) Cell , vol.92 , pp. 117-129
    • Barrett, T.E.1    Savva, R.2    Panayotou, G.3    Barlow, T.4    Brown, T.5    Jiricny, J.6    Pearl, L.H.7
  • 20
    • 0034192265 scopus 로고    scopus 로고
    • The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis
    • Boiteux S., and Radicella J.P. The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis. Arch. Biochem. Biophys. 377 (2000) 1-8
    • (2000) Arch. Biochem. Biophys. , vol.377 , pp. 1-8
    • Boiteux, S.1    Radicella, J.P.2
  • 21
    • 33745222090 scopus 로고    scopus 로고
    • First AID (activation-induced cytidine deaminase) is needed to produce high affinity isotype-switched antibodies
    • Bransteitter R., Sneeden J.L., Allen S., Pham P., and Goodman M.F. First AID (activation-induced cytidine deaminase) is needed to produce high affinity isotype-switched antibodies. J. Biol. Chem. 281 (2006) 16833-16836
    • (2006) J. Biol. Chem. , vol.281 , pp. 16833-16836
    • Bransteitter, R.1    Sneeden, J.L.2    Allen, S.3    Pham, P.4    Goodman, M.F.5
  • 23
    • 0037139232 scopus 로고    scopus 로고
    • Attenuation of DNA polymerase beta-dependent base excision repair and increased DMS-induced mutagenicity in aged mice
    • Cabelof D.C., Raffoul J.J., Yanamadala S., Ganir C., Guo Z., and Heydari A.R. Attenuation of DNA polymerase beta-dependent base excision repair and increased DMS-induced mutagenicity in aged mice. Mutat. Res. 500 (2002) 135-145
    • (2002) Mutat. Res. , vol.500 , pp. 135-145
    • Cabelof, D.C.1    Raffoul, J.J.2    Yanamadala, S.3    Ganir, C.4    Guo, Z.5    Heydari, A.R.6
  • 24
    • 0037353433 scopus 로고    scopus 로고
    • Caloric restriction promotes genomic stability by induction of base excision repair and reversal of its age-related decline
    • Cabelof D.C., Yanamadala S., Raffoul J.J., Guo Z., Soofi A., and Heydari A.R. Caloric restriction promotes genomic stability by induction of base excision repair and reversal of its age-related decline. DNA Repair (Amst.) 2 (2003) 295-307
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 295-307
    • Cabelof, D.C.1    Yanamadala, S.2    Raffoul, J.J.3    Guo, Z.4    Soofi, A.5    Heydari, A.R.6
  • 26
  • 27
    • 33846782890 scopus 로고    scopus 로고
    • UVA irradiation induces relocalisation of the DNA repair protein hOGG1 to nuclear speckles
    • Campalans A., Amouroux R., Bravard A., Epe B., and Radicella J.P. UVA irradiation induces relocalisation of the DNA repair protein hOGG1 to nuclear speckles. J. Cell. Sci. 120 (2007) 23-32
    • (2007) J. Cell. Sci. , vol.120 , pp. 23-32
    • Campalans, A.1    Amouroux, R.2    Bravard, A.3    Epe, B.4    Radicella, J.P.5
  • 28
    • 34548186667 scopus 로고    scopus 로고
    • Cellular senescence: when bad things happen to good cells
    • Campisi J., and d'Adda di Fagagna F. Cellular senescence: when bad things happen to good cells. Nat. Rev. Mol. Cell. Biol. 8 (2007) 729-740
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , pp. 729-740
    • Campisi, J.1    d'Adda di Fagagna, F.2
  • 30
    • 0033555450 scopus 로고    scopus 로고
    • Frequencies of chromosomal abnormalities at amniocentesis: over 20 years of cytogenetic analyses in one laboratory
    • Caron L., Tihy F., and Dallaire L. Frequencies of chromosomal abnormalities at amniocentesis: over 20 years of cytogenetic analyses in one laboratory. Am. J. Med. Genet. 82 (1999) 149-154
    • (1999) Am. J. Med. Genet. , vol.82 , pp. 149-154
    • Caron, L.1    Tihy, F.2    Dallaire, L.3
  • 31
    • 0025949662 scopus 로고
    • Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase
    • Chakravarti D., Ibeanu G.C., Tano K., 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 (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
  • 32
    • 35948952747 scopus 로고    scopus 로고
    • Base excision repair of ionizing radiation-induced DNA damage in G1 and G2 cell cycle phases
    • Chaudhry M.A. Base excision repair of ionizing radiation-induced DNA damage in G1 and G2 cell cycle phases. Cancer Cell Int. 7 (2007) 15
    • (2007) Cancer Cell Int. , vol.7 , pp. 15
    • Chaudhry, M.A.1
  • 33
    • 0141960200 scopus 로고    scopus 로고
    • Exposing the MYtH about base excision repair and human inherited disease
    • Cheadle J.P., and Sampson J.R. Exposing the MYtH about base excision repair and human inherited disease. Hum. Mol. Genet. 12 Spec No 2 (2003) R159-R165
    • (2003) Hum. Mol. Genet. , vol.12 , Issue.Spec No 2
    • Cheadle, J.P.1    Sampson, J.R.2
  • 34
    • 0036316413 scopus 로고    scopus 로고
    • Age-dependent decline of DNA repair activity for oxidative lesions in rat brain mitochondria
    • Chen D., Cao G., Hastings T., Feng Y., Pei W., O'Horo C., and Chen J. Age-dependent decline of DNA repair activity for oxidative lesions in rat brain mitochondria. J. Neurochem. 81 (2002) 1273-1284
    • (2002) J. Neurochem. , vol.81 , pp. 1273-1284
    • Chen, D.1    Cao, G.2    Hastings, T.3    Feng, Y.4    Pei, W.5    O'Horo, C.6    Chen, J.7
  • 35
    • 0037216491 scopus 로고    scopus 로고
    • Upregulation of mitochondrial base-excision repair capability within rat brain after brief ischemia
    • Chen D., Minami M., Henshall D.C., Meller R., Kisby G., and Simon R.P. Upregulation of mitochondrial base-excision repair capability within rat brain after brief ischemia. J. Cereb. Blood Flow Metab. 23 (2003) 88-98
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 88-98
    • Chen, D.1    Minami, M.2    Henshall, D.C.3    Meller, R.4    Kisby, G.5    Simon, R.P.6
  • 36
    • 0242608423 scopus 로고    scopus 로고
    • Association between polymorphism of human oxoguanine glycosylase 1 and risk of prostate cancer
    • Chen L., Elahi A., Pow-Sang J., Lazarus P., and Park J. Association between polymorphism of human oxoguanine glycosylase 1 and risk of prostate cancer. J. Urol. 170 (2003) 2471-2474
    • (2003) J. Urol. , vol.170 , pp. 2471-2474
    • Chen, L.1    Elahi, A.2    Pow-Sang, J.3    Lazarus, P.4    Park, J.5
  • 37
    • 0036054272 scopus 로고    scopus 로고
    • DNA repair gene XRCC1 and XPD polymorphisms and risk of lung cancer in a Chinese population
    • Chen S., Tang D., Xue K., Xu L., Ma G., Hsu Y., and Cho S.S. DNA repair gene XRCC1 and XPD polymorphisms and risk of lung cancer in a Chinese population. Carcinogenesis 23 (2002) 1321-1325
    • (2002) Carcinogenesis , vol.23 , pp. 1321-1325
    • Chen, S.1    Tang, D.2    Xue, K.3    Xu, L.4    Ma, G.5    Hsu, Y.6    Cho, S.S.7
  • 38
    • 2942571939 scopus 로고    scopus 로고
    • Age-associated decrease of oxidative repair enzymes, human 8-oxoguanine DNA glycosylases (hOgg1), in human aging
    • Chen S.K., Hsieh W.A., Tsai M.H., Chen C.C., Hong A.I., Wei Y.H., and Chang W.P. Age-associated decrease of oxidative repair enzymes, human 8-oxoguanine DNA glycosylases (hOgg1), in human aging. J. Radiat. Res. (Tokyo) 44 (2003) 31-35
    • (2003) J. Radiat. Res. (Tokyo) , vol.44 , pp. 31-35
    • Chen, S.K.1    Hsieh, W.A.2    Tsai, M.H.3    Chen, C.C.4    Hong, A.I.5    Wei, Y.H.6    Chang, W.P.7
  • 43
    • 0030582551 scopus 로고    scopus 로고
    • There is substantial agreement among interspecies estimates of DNA repair activity
    • Cortopassi G.A., and Wang E. There is substantial agreement among interspecies estimates of DNA repair activity. Mech. Ageing Dev. 91 (1996) 211-218
    • (1996) Mech. Ageing Dev. , vol.91 , pp. 211-218
    • Cortopassi, G.A.1    Wang, E.2
  • 46
    • 0034303523 scopus 로고    scopus 로고
    • The origins, patterns and implications of human spontaneous mutation
    • Crow J.F. The origins, patterns and implications of human spontaneous mutation. Nat. Rev. Genet. 1 (2000) 40-47
    • (2000) Nat. Rev. Genet. , vol.1 , pp. 40-47
    • Crow, J.F.1
  • 51
  • 52
    • 33846957403 scopus 로고    scopus 로고
    • A novel interaction between DNA ligase III and DNA polymerase gamma plays an essential role in mitochondrial DNA stability
    • De A., and Campbell C. A novel interaction between DNA ligase III and DNA polymerase gamma plays an essential role in mitochondrial DNA stability. Biochem. J. 402 (2007) 175-186
    • (2007) Biochem. J. , vol.402 , pp. 175-186
    • De, A.1    Campbell, C.2
  • 54
    • 0035878869 scopus 로고    scopus 로고
    • Repair of 8-oxodeoxyguanosine lesions in mitochondrial DNA depends on the oxoguanine DNA glycosylase (OGG1) gene and 8-oxoguanine accumulates in the mitochondrial dna of OGG1-defective mice
    • de Souza-Pinto N.C., Eide L., Hogue B.A., Thybo T., Stevnsner T., Seeberg E., Klungland A., and Bohr V.A. Repair of 8-oxodeoxyguanosine lesions in mitochondrial DNA depends on the oxoguanine DNA glycosylase (OGG1) gene and 8-oxoguanine accumulates in the mitochondrial dna of OGG1-defective mice. Cancer Res. 61 (2001) 5378-5381
    • (2001) Cancer Res. , vol.61 , pp. 5378-5381
    • de Souza-Pinto, N.C.1    Eide, L.2    Hogue, B.A.3    Thybo, T.4    Stevnsner, T.5    Seeberg, E.6    Klungland, A.7    Bohr, V.A.8
  • 55
    • 0035871706 scopus 로고    scopus 로고
    • DNA repair and aging in mouse liver: 8-oxodG glycosylase activity increase in mitochondrial but not in nuclear extracts
    • de Souza-Pinto N.C., Hogue B.A., and Bohr V.A. DNA repair and aging in mouse liver: 8-oxodG glycosylase activity increase in mitochondrial but not in nuclear extracts. Free Radic. Biol. Med. 30 (2001) 916-923
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 916-923
    • de Souza-Pinto, N.C.1    Hogue, B.A.2    Bohr, V.A.3
  • 56
    • 1642331382 scopus 로고    scopus 로고
    • Excision by the human methylpurine DNA N-glycosylase of cyanuric acid, a stable and mutagenic oxidation product of 8-oxo-7,8-dihydroguanine
    • Dherin C., Gasparutto D., O'Connor T.R., Cadet J., and Boiteux S. Excision by the human methylpurine DNA N-glycosylase of cyanuric acid, a stable and mutagenic oxidation product of 8-oxo-7,8-dihydroguanine. Int. J. Radiat. Biol. 80 (2004) 21-27
    • (2004) Int. J. Radiat. Biol. , vol.80 , pp. 21-27
    • Dherin, C.1    Gasparutto, D.2    O'Connor, T.R.3    Cadet, J.4    Boiteux, S.5
  • 60
    • 33847630719 scopus 로고    scopus 로고
    • Co-ordination of DNA single strand break repair
    • Dianov G.L., and Parsons J.L. Co-ordination of DNA single strand break repair. DNA Repair (Amst.) 6 (2007) 454-460
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 454-460
    • Dianov, G.L.1    Parsons, J.L.2
  • 62
    • 0030699271 scopus 로고    scopus 로고
    • Rapid accumulation of genome rearrangements in liver but not in brain of old mice
    • Dolle M.E., Giese H., Hopkins C.L., Martus H.J., Hausdorff J.M., and Vijg J. Rapid accumulation of genome rearrangements in liver but not in brain of old mice. Nat. Genet. 17 (1997) 431-434
    • (1997) Nat. Genet. , vol.17 , pp. 431-434
    • Dolle, M.E.1    Giese, H.2    Hopkins, C.L.3    Martus, H.J.4    Hausdorff, J.M.5    Vijg, J.6
  • 67
    • 0036904660 scopus 로고    scopus 로고
    • Rat MYH, a glycosylase for repair of oxidatively damaged DNA, has brain-specific isoforms that localize to neuronal mitochondria
    • Englander E.W., Hu Z., Sharma A., Lee H.M., Wu Z.H., and Greeley G.H. Rat MYH, a glycosylase for repair of oxidatively damaged DNA, has brain-specific isoforms that localize to neuronal mitochondria. J. Neurochem. 83 (2002) 1471-1480
    • (2002) J. Neurochem. , vol.83 , pp. 1471-1480
    • Englander, E.W.1    Hu, Z.2    Sharma, A.3    Lee, H.M.4    Wu, Z.H.5    Greeley, G.H.6
  • 68
    • 28244466766 scopus 로고    scopus 로고
    • Differential modulation of base excision repair activities during brain ontogeny: implications for repair of transcribed DNA
    • Englander E.W., and Ma H. Differential modulation of base excision repair activities during brain ontogeny: implications for repair of transcribed DNA. Mech. Ageing Dev. 127 (2006) 64-69
    • (2006) Mech. Ageing Dev. , vol.127 , pp. 64-69
    • Englander, E.W.1    Ma, H.2
  • 71
    • 0000572335 scopus 로고
    • The aging process and cancerogenesis
    • Failla G. The aging process and cancerogenesis. Ann. N.Y. Acad. Sci. 71 (1958) 1124-1140
    • (1958) Ann. N.Y. Acad. Sci. , vol.71 , pp. 1124-1140
    • Failla, G.1
  • 74
    • 33847625356 scopus 로고    scopus 로고
    • Base damage and single-strand break repair: mechanisms and functional significance of short- and long-patch repair subpathways
    • Fortini P., and Dogliotti E. Base damage and single-strand break repair: mechanisms and functional significance of short- and long-patch repair subpathways. DNA Repair (Amst.) 6 (2007) 398-409
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 398-409
    • Fortini, P.1    Dogliotti, E.2
  • 75
    • 30344455023 scopus 로고    scopus 로고
    • Database of mouse strains carrying targeted mutations in genes affecting biological responses to DNA damage Version 7
    • Friedberg E.C., and Meira L.B. Database of mouse strains carrying targeted mutations in genes affecting biological responses to DNA damage Version 7. DNA Repair 5 (2006) 189-209
    • (2006) DNA Repair , vol.5 , pp. 189-209
    • Friedberg, E.C.1    Meira, L.B.2
  • 76
    • 0032745303 scopus 로고    scopus 로고
    • Early decrease of XRCC1, a DNA base excision repair protein, may contribute to DNA fragmentation after transient focal cerebral ischemia in mice
    • (discussion 2463)
    • Fujimura M., Morita-Fujimura Y., Sugawara T., and Chan P.H. Early decrease of XRCC1, a DNA base excision repair protein, may contribute to DNA fragmentation after transient focal cerebral ischemia in mice. Stroke 30 (1999) 2456-2462 (discussion 2463)
    • (1999) Stroke , vol.30 , pp. 2456-2462
    • Fujimura, M.1    Morita-Fujimura, Y.2    Sugawara, T.3    Chan, P.H.4
  • 77
    • 0033548096 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen facilitates excision in long-patch base excision repair
    • Gary R., Kim K., Cornelius H.L., Park M.S., and Matsumoto Y. Proliferating cell nuclear antigen facilitates excision in long-patch base excision repair. J. Biol. Chem. 274 (1999) 4354-4363
    • (1999) J. Biol. Chem. , vol.274 , pp. 4354-4363
    • Gary, R.1    Kim, K.2    Cornelius, H.L.3    Park, M.S.4    Matsumoto, Y.5
  • 78
    • 0142059634 scopus 로고    scopus 로고
    • The paternal-age effect in Apert syndrome is due, in part, to the increased frequency of mutations in sperm
    • Glaser R.L., Broman K.W., Schulman R.L., Eskenazi B., Wyrobek A.J., and Jabs E.W. The paternal-age effect in Apert syndrome is due, in part, to the increased frequency of mutations in sperm. Am. J. Hum. Genet. 73 (2003) 939-947
    • (2003) Am. J. Hum. Genet. , vol.73 , pp. 939-947
    • Glaser, R.L.1    Broman, K.W.2    Schulman, R.L.3    Eskenazi, B.4    Wyrobek, A.J.5    Jabs, E.W.6
  • 79
  • 80
    • 0042490798 scopus 로고    scopus 로고
    • Evidence for selective advantage of pathogenic FGFR2 mutations in the male germ line
    • Goriely A., McVean G.A., Rojmyr M., Ingemarsson B., and Wilkie A.O. Evidence for selective advantage of pathogenic FGFR2 mutations in the male germ line. Science 301 (2003) 643-646
    • (2003) Science , vol.301 , pp. 643-646
    • Goriely, A.1    McVean, G.A.2    Rojmyr, M.3    Ingemarsson, B.4    Wilkie, A.O.5
  • 82
    • 0027081044 scopus 로고
    • Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span
    • Grube K., and Burkle A. Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 11759-11763
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 11759-11763
    • Grube, K.1    Burkle, A.2
  • 83
    • 0028059099 scopus 로고
    • Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting
    • Gu H., Marth J.D., Orban P.C., Mossmann H., and Rajewsky K. Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting. Science 265 (1994) 103-106
    • (1994) Science , vol.265 , pp. 103-106
    • Gu, H.1    Marth, J.D.2    Orban, P.C.3    Mossmann, H.4    Rajewsky, K.5
  • 85
    • 0037192812 scopus 로고    scopus 로고
    • Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6
    • Gu Y., Parker A., Wilson T.M., Bai H., Chang D.Y., and Lu A.L. Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6. J. Biol. Chem. 277 (2002) 11135-11142
    • (2002) J. Biol. Chem. , vol.277 , pp. 11135-11142
    • Gu, Y.1    Parker, A.2    Wilson, T.M.3    Bai, H.4    Chang, D.Y.5    Lu, A.L.6
  • 86
    • 34250361079 scopus 로고    scopus 로고
    • The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates NEIL1 glycosylase
    • Guan X., Bai H., Shi G., Theriot C.A., Hazra T.K., Mitra S., and Lu A.L. The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates NEIL1 glycosylase. Nucleic Acids Res. 35 (2007) 2463-2472
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2463-2472
    • Guan, X.1    Bai, H.2    Shi, G.3    Theriot, C.A.4    Hazra, T.K.5    Mitra, S.6    Lu, A.L.7
  • 88
    • 7944222565 scopus 로고    scopus 로고
    • Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2
    • Hailer M.K., Slade P.G., Martin B.D., Rosenquist T.A., and Sugden K.D. Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2. DNA Repair (Amst.) 4 (2005) 41-50
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 41-50
    • Hailer, M.K.1    Slade, P.G.2    Martin, B.D.3    Rosenquist, T.A.4    Sugden, K.D.5
  • 94
    • 0011555560 scopus 로고
    • Correlation between deoxyribonucleic acid excision-repair and life-span in a number of mammalian species
    • Hart R.W., and Setlow R.B. Correlation between deoxyribonucleic acid excision-repair and life-span in a number of mammalian species. Proc. Natl. Acad. Sci. U.S.A. 71 (1974) 2169-2173
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 2169-2173
    • Hart, R.W.1    Setlow, R.B.2
  • 95
    • 10244255214 scopus 로고    scopus 로고
    • Futile short-patch DNA base excision repair of adenine:8-oxoguanine mispair
    • Hashimoto K., Tominaga Y., Nakabeppu Y., and Moriya M. Futile short-patch DNA base excision repair of adenine:8-oxoguanine mispair. Nucleic Acids Res. 32 (2004) 5928-5934
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5928-5934
    • Hashimoto, K.1    Tominaga, Y.2    Nakabeppu, Y.3    Moriya, M.4
  • 97
    • 0037162995 scopus 로고    scopus 로고
    • Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions
    • Hazra T.K., Kow Y.W., Hatahet Z., Imhoff B., Boldogh I., Mokkapati S.K., Mitra S., and Izumi T. Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions. J. Biol. Chem. 277 (2002) 30417-30420
    • (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
  • 98
    • 33745186677 scopus 로고    scopus 로고
    • Purification and characterization of NEIL1 and NEIL2, members of a distinct family of mammalian DNA glycosylases for repair of oxidized bases
    • Hazra T.K., and Mitra S. Purification and characterization of NEIL1 and NEIL2, members of a distinct family of mammalian DNA glycosylases for repair of oxidized bases. Methods Enzymol. 408 (2006) 33-48
    • (2006) Methods Enzymol. , vol.408 , pp. 33-48
    • Hazra, T.K.1    Mitra, S.2
  • 101
    • 0033575886 scopus 로고    scopus 로고
    • The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites
    • Hendrich B., Hardeland U., Ng H.H., Jiricny J., and Bird A. The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites. Nature 401 (1999) 301-304
    • (1999) Nature , vol.401 , pp. 301-304
    • Hendrich, B.1    Hardeland, U.2    Ng, H.H.3    Jiricny, J.4    Bird, A.5
  • 103
    • 33847673237 scopus 로고    scopus 로고
    • The intricate structural chemistry of base excision repair machinery: implications for DNA damage recognition, removal, and repair
    • Hitomi K., Iwai S., and Tainer J.A. The intricate structural chemistry of base excision repair machinery: implications for DNA damage recognition, removal, and repair. DNA Repair (Amst.) 6 (2007) 410-428
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 410-428
    • Hitomi, K.1    Iwai, S.2    Tainer, J.A.3
  • 104
    • 0034283066 scopus 로고    scopus 로고
    • Age-associated DNA damage is accelerated in the senescence-accelerated mice
    • Hosokawa M., Fujisawa H., Ax S., Zahn-Daimler G., and Zahn R.K. Age-associated DNA damage is accelerated in the senescence-accelerated mice. Mech. Ageing Dev. 118 (2000) 61-70
    • (2000) Mech. Ageing Dev. , vol.118 , pp. 61-70
    • Hosokawa, M.1    Fujisawa, H.2    Ax, S.3    Zahn-Daimler, G.4    Zahn, R.K.5
  • 106
    • 3242891383 scopus 로고    scopus 로고
    • PARP-1, PARP-2 and ATM in the DNA damage response: functional synergy in mouse development
    • Huber A., Bai P., de Murcia J.M., and de Murcia G. PARP-1, PARP-2 and ATM in the DNA damage response: functional synergy in mouse development. DNA Repair (Amst.) 3 (2004) 1103-1108
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 1103-1108
    • Huber, A.1    Bai, P.2    de Murcia, J.M.3    de Murcia, G.4
  • 107
    • 27744531188 scopus 로고    scopus 로고
    • Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review
    • Hung R.J., Hall J., Brennan P., and Boffetta P. Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review. Am. J. Epidemiol. 162 (2005) 925-942
    • (2005) Am. J. Epidemiol. , vol.162 , pp. 925-942
    • Hung, R.J.1    Hall, J.2    Brennan, P.3    Boffetta, P.4
  • 108
    • 0035236781 scopus 로고    scopus 로고
    • DNA substrates containing defined oxidative base lesions and their application to study substrate specificities of base excision repair enzymes
    • Ide H. DNA substrates containing defined oxidative base lesions and their application to study substrate specificities of base excision repair enzymes. Prog. Nucleic Acid Res. Mol. Biol. 68 (2001) 207-221
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.68 , pp. 207-221
    • Ide, H.1
  • 109
    • 7444266619 scopus 로고    scopus 로고
    • Human DNA glycosylases involved in the repair of oxidatively damaged DNA
    • Ide H., and Kotera M. Human DNA glycosylases involved in the repair of oxidatively damaged DNA. Biol. Pharm. Bull. 27 (2004) 480-485
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 480-485
    • Ide, H.1    Kotera, M.2
  • 110
    • 0036942993 scopus 로고    scopus 로고
    • Expression of 8-oxoguanine DNA glycosylase is reduced and associated with neurofibrillary tangles in Alzheimer's disease brain
    • Iida T., Furuta A., Nishioka K., Nakabeppu Y., and Iwaki T. Expression of 8-oxoguanine DNA glycosylase is reduced and associated with neurofibrillary tangles in Alzheimer's disease brain. Acta Neuropathol. 103 (2002) 20-25
    • (2002) Acta Neuropathol. , vol.103 , pp. 20-25
    • Iida, T.1    Furuta, A.2    Nishioka, K.3    Nakabeppu, Y.4    Iwaki, T.5
  • 111
    • 0032555571 scopus 로고    scopus 로고
    • Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue
    • Ikeda S., Biswas T., Roy R., Izumi T., Boldogh I., Kurosky A., Sarker A.H., Seki S., and Mitra S. Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue. J. Biol. Chem. 273 (1998) 21585-21593
    • (1998) J. Biol. Chem. , vol.273 , pp. 21585-21593
    • Ikeda, S.1    Biswas, T.2    Roy, R.3    Izumi, T.4    Boldogh, I.5    Kurosky, A.6    Sarker, A.H.7    Seki, S.8    Mitra, S.9
  • 112
    • 33744912521 scopus 로고    scopus 로고
    • Mitochondrial and nuclear DNA-repair capacity of various brain regions in mouse is altered in an age-dependent manner
    • Imam S.Z., Karahalil B., Hogue B.A., Souza-Pinto N.C., and Bohr V.A. Mitochondrial and nuclear DNA-repair capacity of various brain regions in mouse is altered in an age-dependent manner. Neurobiol. Aging 27 (2006) 1129-1136
    • (2006) Neurobiol. Aging , vol.27 , pp. 1129-1136
    • Imam, S.Z.1    Karahalil, B.2    Hogue, B.A.3    Souza-Pinto, N.C.4    Bohr, V.A.5
  • 113
    • 0035869149 scopus 로고    scopus 로고
    • Mixed spermatogenic germ cell nuclear extracts exhibit high base excision repair activity
    • Intano G.W., McMahan C.A., Walter R.B., McCarrey J.R., and Walter C.A. Mixed spermatogenic germ cell nuclear extracts exhibit high base excision repair activity. Nucleic Acids Res. 29 (2001) 1366-1372
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1366-1372
    • Intano, G.W.1    McMahan, C.A.2    Walter, R.B.3    McCarrey, J.R.4    Walter, C.A.5
  • 114
    • 0036118571 scopus 로고    scopus 로고
    • Base excision repair is limited by different proteins in male germ cell nuclear extracts prepared from young and old mice
    • Intano G.W. Base excision repair is limited by different proteins in male germ cell nuclear extracts prepared from young and old mice. Mol. Cell. Biol. 22 (2002) 2410-2418
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2410-2418
    • Intano, G.W.1
  • 117
    • 0021335930 scopus 로고
    • Influence of age on sperm production and testicular weights in men
    • Johnson L., Petty C.S., and Neaves W.B. Influence of age on sperm production and testicular weights in men. J. Reprod. Fertil. 70 (1984) 211-218
    • (1984) J. Reprod. Fertil. , vol.70 , pp. 211-218
    • Johnson, L.1    Petty, C.S.2    Neaves, W.B.3
  • 120
    • 0036904776 scopus 로고    scopus 로고
    • Base excision repair capacity in mitochondria and nuclei: tissue-specific variations
    • Karahalil B., Hogue B.A., de Souza-Pinto N.C., and Bohr V.A. Base excision repair capacity in mitochondria and nuclei: tissue-specific variations. FASEB J. 16 (2002) 1895-1902
    • (2002) FASEB J. , vol.16 , pp. 1895-1902
    • Karahalil, B.1    Hogue, B.A.2    de Souza-Pinto, N.C.3    Bohr, V.A.4
  • 122
    • 0035140143 scopus 로고    scopus 로고
    • Effects of male age on semen quality and fertility: a review of the literature
    • Kidd S.A., Eskenazi B., and Wyrobek A.J. Effects of male age on semen quality and fertility: a review of the literature. Fertil. Steril. 75 (2001) 237-248
    • (2001) Fertil. Steril. , vol.75 , pp. 237-248
    • Kidd, S.A.1    Eskenazi, B.2    Wyrobek, A.J.3
  • 123
    • 0030916372 scopus 로고    scopus 로고
    • Evidence of reduced DNA repair in amyotrophic lateral sclerosis brain tissue
    • Kisby G.E., Milne J., and Sweatt C. Evidence of reduced DNA repair in amyotrophic lateral sclerosis brain tissue. Neuroreport 8 (1997) 1337-1340
    • (1997) Neuroreport , vol.8 , pp. 1337-1340
    • Kisby, G.E.1    Milne, J.2    Sweatt, C.3
  • 124
    • 0028787248 scopus 로고
    • Two maternally derived missense mutations in the tyrosine kinase domain of the RET protooncogene in a patient with de novo MEN 2B
    • Kitamura Y., Scavarda N., Wells Jr. S.A., Jackson C.E., and Goodfellow P.J. Two maternally derived missense mutations in the tyrosine kinase domain of the RET protooncogene in a patient with de novo MEN 2B. Hum. Mol. Genet. 4 (1995) 1987-1988
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 1987-1988
    • Kitamura, Y.1    Scavarda, N.2    Wells Jr., S.A.3    Jackson, C.E.4    Goodfellow, P.J.5
  • 125
    • 33750311904 scopus 로고    scopus 로고
    • Association of genetic polymorphisms in the base excision repair pathway with lung cancer risk: a meta-analysis
    • Kiyohara C., Takayama K., and Nakanishi Y. Association of genetic polymorphisms in the base excision repair pathway with lung cancer risk: a meta-analysis. Lung Cancer 54 (2006) 267-283
    • (2006) Lung Cancer , vol.54 , pp. 267-283
    • Kiyohara, C.1    Takayama, K.2    Nakanishi, Y.3
  • 128
    • 0025309553 scopus 로고
    • Development of a short-term, in vivo mutagenesis assay: the effects of methylation on the recovery of a lambda phage shuttle vector from transgenic mice
    • Kohler S.W., Provost G.S., Kretz P.L., Dycaico M.J., Sorge J.A., and Short J.M. Development of a short-term, in vivo mutagenesis assay: the effects of methylation on the recovery of a lambda phage shuttle vector from transgenic mice. Nucleic Acids Res. 18 (1990) 3007-3013
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3007-3013
    • Kohler, S.W.1    Provost, G.S.2    Kretz, P.L.3    Dycaico, M.J.4    Sorge, J.A.5    Short, J.M.6
  • 129
    • 34249337762 scopus 로고    scopus 로고
    • OGG1 initiates age-dependent CAG trinucleotide expansion in somatic cells
    • Kovtun I.V., Liu Y., Bjoras M., Klungland A., Wilson S.H., and McMurray C.T. OGG1 initiates age-dependent CAG trinucleotide expansion in somatic cells. Nature 447 (2007) 447-452
    • (2007) Nature , vol.447 , pp. 447-452
    • Kovtun, I.V.1    Liu, Y.2    Bjoras, M.3    Klungland, A.4    Wilson, S.H.5    McMurray, C.T.6
  • 130
    • 33646563727 scopus 로고    scopus 로고
    • Possible association of the X-ray cross complementing gene 1 (XRCC1) Arg280His polymorphism as a risk for rheumatoid arthritis
    • Koyama A., Kubota Y., Shimamura T., and Horiuchi S. Possible association of the X-ray cross complementing gene 1 (XRCC1) Arg280His polymorphism as a risk for rheumatoid arthritis. Rheumatol. Int. 26 (2006) 749-751
    • (2006) Rheumatol. Int. , vol.26 , pp. 749-751
    • Koyama, A.1    Kubota, Y.2    Shimamura, T.3    Horiuchi, S.4
  • 131
    • 13644271465 scopus 로고    scopus 로고
    • Reduced DNA gap repair in aging rat neuronal extracts and its restoration by DNA polymerase beta and DNA-ligase
    • Krishna T.H., Mahipal S., Sudhakar A., Sugimoto H., Kalluri R., and Rao K.S. Reduced DNA gap repair in aging rat neuronal extracts and its restoration by DNA polymerase beta and DNA-ligase. J. Neurochem. 92 (2005) 818-823
    • (2005) J. Neurochem. , vol.92 , pp. 818-823
    • Krishna, T.H.1    Mahipal, S.2    Sudhakar, A.3    Sugimoto, H.4    Kalluri, R.5    Rao, K.S.6
  • 133
    • 0037115911 scopus 로고    scopus 로고
    • Uracil in DNA-occurrence, consequences and repair
    • Krokan H.E., Drablos F., and Slupphaug G. Uracil in DNA-occurrence, consequences and repair. Oncogene 21 (2002) 8935-8948
    • (2002) Oncogene , vol.21 , pp. 8935-8948
    • Krokan, H.E.1    Drablos, F.2    Slupphaug, G.3
  • 135
    • 0242490147 scopus 로고    scopus 로고
    • Inducible repair of oxidative DNA lesions in the rat brain after transient focal ischemia and reperfusion
    • Lan J., Li W., Zhang F., Sun F.Y., Nagayama T., O'Horo C., and Chen J. Inducible repair of oxidative DNA lesions in the rat brain after transient focal ischemia and reperfusion. J. Cereb. Blood Flow Metab. 23 (2003) 1324-1339
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 1324-1339
    • Lan, J.1    Li, W.2    Zhang, F.3    Sun, F.Y.4    Nagayama, T.5    O'Horo, C.6    Chen, J.7
  • 136
    • 0042091947 scopus 로고    scopus 로고
    • Proliferation failure and gamma radiation sensitivity of Fen1 null mutant mice at the blastocyst stage
    • Larsen E., Gran C., Saether B.E., Seeberg E., and Klungland A. Proliferation failure and gamma radiation sensitivity of Fen1 null mutant mice at the blastocyst stage. Mol. Cell. Biol. 23 (2003) 5346-5353
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5346-5353
    • Larsen, E.1    Gran, C.2    Saether, B.E.3    Seeberg, E.4    Klungland, A.5
  • 137
    • 0032543425 scopus 로고    scopus 로고
    • Antimutagenic role of base-excision repair enzymes upon free radical-induced DNA damage
    • Laval J., Jurado J., Saparbaev M., and Sidorkina O. Antimutagenic role of base-excision repair enzymes upon free radical-induced DNA damage. Mutat. Res. 402 (1998) 93-102
    • (1998) Mutat. Res. , vol.402 , pp. 93-102
    • Laval, J.1    Jurado, J.2    Saparbaev, M.3    Sidorkina, O.4
  • 138
    • 0034682518 scopus 로고    scopus 로고
    • Transcription coupled repair of 8-oxoguanine in murine cells: the ogg1 protein is required for repair in nontranscribed sequences but not in transcribed sequences
    • Le Page F., Klungland A., Barnes D.E., Sarasin A., and Boiteux S. Transcription coupled repair of 8-oxoguanine in murine cells: the ogg1 protein is required for repair in nontranscribed sequences but not in transcribed sequences. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 8397-8402
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8397-8402
    • Le Page, F.1    Klungland, A.2    Barnes, D.E.3    Sarasin, A.4    Boiteux, S.5
  • 139
    • 0028217661 scopus 로고
    • Comparative analysis of DNA mutations in lacI transgenic mice with age
    • Lee A.T., DeSimone C., Cerami A., and Bucala R. Comparative analysis of DNA mutations in lacI transgenic mice with age. FASEB J. 8 (1994) 545-550
    • (1994) FASEB J. , vol.8 , pp. 545-550
    • Lee, A.T.1    DeSimone, C.2    Cerami, A.3    Bucala, R.4
  • 140
    • 0347717730 scopus 로고    scopus 로고
    • Developmental changes in expression and subcellular localization of the DNA repair glycosylase, MYH, in the rat brain
    • Lee H.M., Hu Z., Ma H., Greeley Jr. G.H., Wang C., and Englander E.W. Developmental changes in expression and subcellular localization of the DNA repair glycosylase, MYH, in the rat brain. J. Neurochem. 88 (2004) 394-400
    • (2004) J. Neurochem. , vol.88 , pp. 394-400
    • Lee, H.M.1    Hu, Z.2    Ma, H.3    Greeley Jr., G.H.4    Wang, C.5    Englander, E.W.6
  • 142
    • 34547787147 scopus 로고    scopus 로고
    • Ischemic preconditioning induces XRCC1, DNA polymerase-beta, and DNA ligase III and correlates with enhanced base excision repair
    • Li N., Wu H., Yang S., and Chen D. Ischemic preconditioning induces XRCC1, DNA polymerase-beta, and DNA ligase III and correlates with enhanced base excision repair. DNA Repair (Amst.) 6 (2007) 1297-1306
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 1297-1306
    • Li, N.1    Wu, H.2    Yang, S.3    Chen, D.4
  • 143
    • 31444450139 scopus 로고    scopus 로고
    • Ischemic preconditioning in the rat brain enhances the repair of endogenous oxidative DNA damage by activating the base-excision repair pathway
    • Li W., Luo Y., Zhang F., Signore A.P., Gobbel G.T., Simon R.P., and Chen J. Ischemic preconditioning in the rat brain enhances the repair of endogenous oxidative DNA damage by activating the base-excision repair pathway. J. Cereb. Blood Flow Metab. 26 (2006) 181-198
    • (2006) J. Cereb. Blood Flow Metab. , vol.26 , pp. 181-198
    • Li, W.1    Luo, Y.2    Zhang, F.3    Signore, A.P.4    Gobbel, G.T.5    Simon, R.P.6    Chen, J.7
  • 144
    • 33846909036 scopus 로고    scopus 로고
    • Association of Dnmt3a and thymine DNA glycosylase links DNA methylation with base-excision repair
    • Li Y.Q., Zhou P.Z., Zheng X.D., Walsh C.P., and Xu G.L. Association of Dnmt3a and thymine DNA glycosylase links DNA methylation with base-excision repair. Nucleic Acids Res. 35 (2007) 390-400
    • (2007) Nucleic Acids Res. , vol.35 , pp. 390-400
    • Li, Y.Q.1    Zhou, P.Z.2    Zheng, X.D.3    Walsh, C.P.4    Xu, G.L.5
  • 145
    • 0037415368 scopus 로고    scopus 로고
    • Repair of the mutagenic DNA oxidation product, 5-formyluracil
    • Liu P., Burdzy A., and Sowers L.C. Repair of the mutagenic DNA oxidation product, 5-formyluracil. DNA Repair (Amst.) 2 (2003) 199-210
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 199-210
    • Liu, P.1    Burdzy, A.2    Sowers, L.C.3
  • 146
    • 13544261768 scopus 로고    scopus 로고
    • DNA polymerase beta and flap endonuclease 1 enzymatic specificities sustain DNA synthesis for long patch base excision repair
    • Liu Y., Beard W.A., Shock D.D., Prasad R., Hou E.W., and Wilson S.H. DNA polymerase beta and flap endonuclease 1 enzymatic specificities sustain DNA synthesis for long patch base excision repair. J. Biol. Chem. 280 (2005) 3665-3674
    • (2005) J. Biol. Chem. , vol.280 , pp. 3665-3674
    • Liu, Y.1    Beard, W.A.2    Shock, D.D.3    Prasad, R.4    Hou, E.W.5    Wilson, S.H.6
  • 147
    • 0032933750 scopus 로고    scopus 로고
    • Increased DNA oxidation and decreased levels of repair products in Alzheimer's disease ventricular CSF
    • Lovell M.A., Gabbita S.P., and Markesbery W.R. Increased DNA oxidation and decreased levels of repair products in Alzheimer's disease ventricular CSF. J. Neurochem. 72 (1999) 771-776
    • (1999) J. Neurochem. , vol.72 , pp. 771-776
    • Lovell, M.A.1    Gabbita, S.P.2    Markesbery, W.R.3
  • 148
    • 38049010515 scopus 로고    scopus 로고
    • Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer's disease
    • Lovell M.A., and Markesbery W.R. Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer's disease. Nucleic Acids Res. (2007)
    • (2007) Nucleic Acids Res.
    • Lovell, M.A.1    Markesbery, W.R.2
  • 149
    • 0033152748 scopus 로고    scopus 로고
    • XRCC1 polymorphisms: effects on aflatoxin B1-DNA adducts and glycophorin A variant frequency
    • Lunn R.M., Langlois R.G., Hsieh L.L., Thompson C.L., and Bell D.A. XRCC1 polymorphisms: effects on aflatoxin B1-DNA adducts and glycophorin A variant frequency. Cancer Res. 59 (1999) 2557-2561
    • (1999) Cancer Res. , vol.59 , pp. 2557-2561
    • Lunn, R.M.1    Langlois, R.G.2    Hsieh, L.L.3    Thompson, C.L.4    Bell, D.A.5
  • 150
    • 34247581131 scopus 로고    scopus 로고
    • Impaired DNA repair via the base-excision repair pathway after focal ischemic brain injury: a protein phosphorylation-dependent mechanism reversed by hypothermic neuroprotection
    • Luo Y., Ji X., Ling F., Li W., Zhang F., Cao G., and Chen J. Impaired DNA repair via the base-excision repair pathway after focal ischemic brain injury: a protein phosphorylation-dependent mechanism reversed by hypothermic neuroprotection. Front. Biosci. 12 (2007) 1852-1862
    • (2007) Front. Biosci. , vol.12 , pp. 1852-1862
    • Luo, Y.1    Ji, X.2    Ling, F.3    Li, W.4    Zhang, F.5    Cao, G.6    Chen, J.7
  • 153
    • 0034949224 scopus 로고    scopus 로고
    • Mutation frequency and type during ageing in mouse seminiferous tubules
    • Martin S.L., Hopkins C.L., Naumer A., Dolle M.E., and Vijg J. Mutation frequency and type during ageing in mouse seminiferous tubules. Mech. Ageing Dev. 122 (2001) 1321-1331
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 1321-1331
    • Martin, S.L.1    Hopkins, C.L.2    Naumer, A.3    Dolle, M.E.4    Vijg, J.5
  • 154
    • 0141611988 scopus 로고    scopus 로고
    • Subfield history: caloric restriction, slowing aging, and extending life
    • Masoro E.J. Subfield history: caloric restriction, slowing aging, and extending life. Sci. Aging Knowl. Environ. 2003 (2003) re2
    • (2003) Sci. Aging Knowl. Environ. , vol.2003
    • Masoro, E.J.1
  • 155
    • 0038185257 scopus 로고    scopus 로고
    • Mammalian 5-formyluracil-DNA glycosylase. 1. Identification and characterization of a novel activity that releases 5-formyluracil from DNA
    • Matsubara M., Masaoka A., Tanaka T., Miyano T., Kato N., Terato H., Ohyama Y., Iwai S., and Ide H. Mammalian 5-formyluracil-DNA glycosylase. 1. Identification and characterization of a novel activity that releases 5-formyluracil from DNA. Biochemistry 42 (2003) 4993-5002
    • (2003) Biochemistry , vol.42 , pp. 4993-5002
    • Matsubara, M.1    Masaoka, A.2    Tanaka, T.3    Miyano, T.4    Kato, N.5    Terato, H.6    Ohyama, Y.7    Iwai, S.8    Ide, H.9
  • 156
    • 5144220241 scopus 로고    scopus 로고
    • Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase
    • Matsubara M., Tanaka T., Terato H., Ohmae E., Izumi S., Katayanagi K., and Ide H. Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase. Nucleic Acids Res. 32 (2004) 5291-5302
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5291-5302
    • Matsubara, M.1    Tanaka, T.2    Terato, H.3    Ohmae, E.4    Izumi, S.5    Katayanagi, K.6    Ide, H.7
  • 158
    • 0028831129 scopus 로고
    • Characterization of a mammalian homolog of the Escherichia coli MutY mismatch repair protein
    • McGoldrick J.P., Yeh Y.C., Solomon M., Essigmann J.M., and Lu A.L. Characterization of a mammalian homolog of the Escherichia coli MutY mismatch repair protein. Mol. Cell. Biol. 15 (1995) 989-996
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 989-996
    • McGoldrick, J.P.1    Yeh, Y.C.2    Solomon, M.3    Essigmann, J.M.4    Lu, A.L.5
  • 162
    • 0032169406 scopus 로고    scopus 로고
    • Interaction of the recombinant human methylpurine-DNA glycosylase (MPG protein) with oligodeoxyribonucleotides containing either hypoxanthine or abasic sites
    • Miao F., Bouziane M., and O'Connor T.R. Interaction of the recombinant human methylpurine-DNA glycosylase (MPG protein) with oligodeoxyribonucleotides containing either hypoxanthine or abasic sites. Nucleic Acids Res. 26 (1998) 4034-4041
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4034-4041
    • Miao, F.1    Bouziane, M.2    O'Connor, T.R.3
  • 166
    • 33845733594 scopus 로고    scopus 로고
    • SUMO-1-dependent allosteric regulation of thymine DNA glycosylase alters subnuclear localization and CBP/p300 recruitment
    • Mohan R.D., Rao A., Gagliardi J., and Tini M. SUMO-1-dependent allosteric regulation of thymine DNA glycosylase alters subnuclear localization and CBP/p300 recruitment. Mol. Cell. Biol. 27 (2007) 229-243
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 229-243
    • Mohan, R.D.1    Rao, A.2    Gagliardi, J.3    Tini, M.4
  • 168
    • 10644282845 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase deaminates 5-methylcytosine in DNA and is expressed in pluripotent tissues: implications for epigenetic reprogramming
    • Morgan H.D., Dean W., Coker H.A., Reik W., and Petersen-Mahrt S.K. Activation-induced cytidine deaminase deaminates 5-methylcytosine in DNA and is expressed in pluripotent tissues: implications for epigenetic reprogramming. J. Biol. Chem. 279 (2004) 52353-52360
    • (2004) J. Biol. Chem. , vol.279 , pp. 52353-52360
    • Morgan, H.D.1    Dean, W.2    Coker, H.A.3    Reik, W.4    Petersen-Mahrt, S.K.5
  • 170
    • 0141723585 scopus 로고    scopus 로고
    • Mammalian longevity under the protection of PARP-1's multi-facets
    • Muiras M.L. Mammalian longevity under the protection of PARP-1's multi-facets. Ageing Res. Rev. 2 (2003) 129-148
    • (2003) Ageing Res. Rev. , vol.2 , pp. 129-148
    • Muiras, M.L.1
  • 172
    • 34247880172 scopus 로고    scopus 로고
    • Early decrease of mitochondrial DNA repair enzymes in spinal motor neurons of presymptomatic transgenic mice carrying a mutant SOD1 gene
    • Murakami T., Nagai M., Miyazaki K., Morimoto N., Ohta Y., Kurata T., Takehisa Y., Kamiya T., and Abe K. Early decrease of mitochondrial DNA repair enzymes in spinal motor neurons of presymptomatic transgenic mice carrying a mutant SOD1 gene. Brain Res. 1150 (2007) 182-189
    • (2007) Brain Res. , vol.1150 , pp. 182-189
    • Murakami, T.1    Nagai, M.2    Miyazaki, K.3    Morimoto, N.4    Ohta, Y.5    Kurata, T.6    Takehisa, Y.7    Kamiya, T.8    Abe, K.9
  • 173
    • 0035237612 scopus 로고    scopus 로고
    • Regulation of intracellular localization of human MTH1, OGG1, and MYH proteins for repair of oxidative DNA damage
    • Nakabeppu Y. Regulation of intracellular localization of human MTH1, OGG1, and MYH proteins for repair of oxidative DNA damage. Prog. Nucleic Acid Res. Mol. Biol. 68 (2001) 75-94
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.68 , pp. 75-94
    • Nakabeppu, Y.1
  • 176
    • 0036141390 scopus 로고    scopus 로고
    • The XRCC1 Arg399Gln polymorphism, sunburn, and non-melanoma skin cancer: evidence of gene-environment interaction
    • Nelson H.H., Kelsey K.T., Mott L.A., and Karagas M.R. The XRCC1 Arg399Gln polymorphism, sunburn, and non-melanoma skin cancer: evidence of gene-environment interaction. Cancer Res. 62 (2002) 152-155
    • (2002) Cancer Res. , vol.62 , pp. 152-155
    • Nelson, H.H.1    Kelsey, K.T.2    Mott, L.A.3    Karagas, M.R.4
  • 182
    • 0032945268 scopus 로고    scopus 로고
    • Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs
    • Nishioka K., Ohtsubo T., Oda H., Fujiwara T., Kang D., Sugimachi K., and Nakabeppu Y. Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs. Mol. Biol. Cell. 10 (1999) 1637-1652
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 1637-1652
    • Nishioka, K.1    Ohtsubo, T.2    Oda, H.3    Fujiwara, T.4    Kang, D.5    Sugimachi, K.6    Nakabeppu, Y.7
  • 183
    • 27844492836 scopus 로고    scopus 로고
    • Modulation of oxidative mutagenesis and carcinogenesis by polymorphic forms of human DNA repair enzymes
    • Nohmi T., Kim S.R., and Yamada M. Modulation of oxidative mutagenesis and carcinogenesis by polymorphic forms of human DNA repair enzymes. Mutat. Res. 591 (2005) 60-73
    • (2005) Mutat. Res. , vol.591 , pp. 60-73
    • Nohmi, T.1    Kim, S.R.2    Yamada, M.3
  • 185
    • 0032567807 scopus 로고    scopus 로고
    • Mutant AP endonuclease in patients with amyotrophic lateral sclerosis
    • Olkowski Z.L. Mutant AP endonuclease in patients with amyotrophic lateral sclerosis. Neuroreport 9 (1998) 239-242
    • (1998) Neuroreport , vol.9 , pp. 239-242
    • Olkowski, Z.L.1
  • 186
    • 0034646079 scopus 로고    scopus 로고
    • Age-associated increase of spontaneous mutant frequency and molecular nature of mutation in newborn and old lacZ-transgenic mouse
    • Ono T., Ikehata H., Nakamura S., Saito Y., Hosoi Y., Takai Y., Yamada S., Onodera J., and Yamamoto K. Age-associated increase of spontaneous mutant frequency and molecular nature of mutation in newborn and old lacZ-transgenic mouse. Mutat. Res. 447 (2000) 165-177
    • (2000) Mutat. Res. , vol.447 , pp. 165-177
    • Ono, T.1    Ikehata, H.2    Nakamura, S.3    Saito, Y.4    Hosoi, Y.5    Takai, Y.6    Yamada, S.7    Onodera, J.8    Yamamoto, K.9
  • 187
    • 0034812540 scopus 로고    scopus 로고
    • Age-related and tissue-specific accumulation of oxidative DNA base damage in 7,8-dihydro-8-oxoguanine-DNA glycosylase (Ogg1) deficient mice
    • Osterod M., Hollenbach S., Hengstler J.G., Barnes D.E., Lindahl T., and Epe B. Age-related and tissue-specific accumulation of oxidative DNA base damage in 7,8-dihydro-8-oxoguanine-DNA glycosylase (Ogg1) deficient mice. Carcinogenesis 22 (2001) 1459-1463
    • (2001) Carcinogenesis , vol.22 , pp. 1459-1463
    • Osterod, M.1    Hollenbach, S.2    Hengstler, J.G.3    Barnes, D.E.4    Lindahl, T.5    Epe, B.6
  • 188
    • 33645067629 scopus 로고    scopus 로고
    • XRCC1 genotype and breast cancer: functional studies and epidemiologic data show interactions between XRCC1 codon 280 His and smoking
    • Pachkowski B.F., Winkel S., Kubota Y., Swenberg J.A., Millikan R.C., and Nakamura J. XRCC1 genotype and breast cancer: functional studies and epidemiologic data show interactions between XRCC1 codon 280 His and smoking. Cancer Res. 66 (2006) 2860-2868
    • (2006) Cancer Res. , vol.66 , pp. 2860-2868
    • Pachkowski, B.F.1    Winkel, S.2    Kubota, Y.3    Swenberg, J.A.4    Millikan, R.C.5    Nakamura, J.6
  • 190
    • 34247128593 scopus 로고    scopus 로고
    • Human base excision repair complex is physically associated to DNA replication and cell cycle regulatory proteins
    • Parlanti E., Locatelli G., Maga G., and Dogliotti E. Human base excision repair complex is physically associated to DNA replication and cell cycle regulatory proteins. Nucleic Acids Res. 35 (2007) 1569-1577
    • (2007) Nucleic Acids Res. , vol.35 , pp. 1569-1577
    • Parlanti, E.1    Locatelli, G.2    Maga, G.3    Dogliotti, E.4
  • 191
    • 0034734383 scopus 로고    scopus 로고
    • Structure and function in the uracil-DNA glycosylase superfamily
    • Pearl L.H. Structure and function in the uracil-DNA glycosylase superfamily. Mutat. Res. 460 (2000) 165-181
    • (2000) Mutat. Res. , vol.460 , pp. 165-181
    • Pearl, L.H.1
  • 192
    • 50449119163 scopus 로고
    • Parental age and mutation
    • Penrose L.S. Parental age and mutation. Lancet 269 (1955) 312-313
    • (1955) Lancet , vol.269 , pp. 312-313
    • Penrose, L.S.1
  • 193
    • 2542457893 scopus 로고    scopus 로고
    • ATP-dependent selection between single nucleotide and long patch base excision repair
    • Petermann E., Ziegler M., and Oei S.L. ATP-dependent selection between single nucleotide and long patch base excision repair. DNA Repair (Amst.) 2 (2003) 1101-1114
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 1101-1114
    • Petermann, E.1    Ziegler, M.2    Oei, S.L.3
  • 194
    • 34547645005 scopus 로고    scopus 로고
    • Uracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanisms
    • Pettersen H.S., Sundheim O., Gilljam K.M., Slupphaug G., Krokan H.E., and Kavli B. Uracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanisms. Nucleic Acids Res. 35 (2007) 3879-3892
    • (2007) Nucleic Acids Res. , vol.35 , pp. 3879-3892
    • Pettersen, H.S.1    Sundheim, O.2    Gilljam, K.M.3    Slupphaug, G.4    Krokan, H.E.5    Kavli, B.6
  • 196
    • 0034635403 scopus 로고    scopus 로고
    • FEN1 stimulation of DNA polymerase beta mediates an excision step in mammalian long patch base excision repair
    • Prasad R., Dianov G.L., Bohr V.A., and Wilson S.H. FEN1 stimulation of DNA polymerase beta mediates an excision step in mammalian long patch base excision repair. J. Biol. Chem. 275 (2000) 4460-4466
    • (2000) J. Biol. Chem. , vol.275 , pp. 4460-4466
    • Prasad, R.1    Dianov, G.L.2    Bohr, V.A.3    Wilson, S.H.4
  • 197
    • 15244341766 scopus 로고    scopus 로고
    • Micronuclei in EM9 cells expressing polymorphic forms of human XRCC1
    • Qu T., Morii E., Oboki K., Lu Y., and Morimoto K. Micronuclei in EM9 cells expressing polymorphic forms of human XRCC1. Cancer Lett. 221 (2005) 91-95
    • (2005) Cancer Lett. , vol.221 , pp. 91-95
    • Qu, T.1    Morii, E.2    Oboki, K.3    Lu, Y.4    Morimoto, K.5
  • 198
    • 20044379872 scopus 로고    scopus 로고
    • Exercise and hormesis: oxidative stress-related adaptation for successful aging
    • Radak Z., Chung H.Y., and Goto S. Exercise and hormesis: oxidative stress-related adaptation for successful aging. Biogerontology 6 (2005) 71-75
    • (2005) Biogerontology , vol.6 , pp. 71-75
    • Radak, Z.1    Chung, H.Y.2    Goto, S.3
  • 199
    • 34147111884 scopus 로고    scopus 로고
    • 8-Oxoguanosine and uracil repair of nuclear and mitochondrial DNA in red and white skeletal muscle of exercise-trained old rats
    • Radak Z., Kumagai S., Nakamoto H., and Goto S. 8-Oxoguanosine and uracil repair of nuclear and mitochondrial DNA in red and white skeletal muscle of exercise-trained old rats. J. Appl. Physiol. 102 (2007) 1696-1701
    • (2007) J. Appl. Physiol. , vol.102 , pp. 1696-1701
    • Radak, Z.1    Kumagai, S.2    Nakamoto, H.3    Goto, S.4
  • 201
    • 0029805533 scopus 로고    scopus 로고
    • Reproductive parameters of older compared to younger men of infertile couples
    • Rolf C., Behre H.M., and Nieschlag E. Reproductive parameters of older compared to younger men of infertile couples. Int. J. Androl. 19 (1996) 135-142
    • (1996) Int. J. Androl. , vol.19 , pp. 135-142
    • Rolf, C.1    Behre, H.M.2    Nieschlag, E.3
  • 203
    • 33845407758 scopus 로고    scopus 로고
    • Different DNA repair strategies to combat the threat from 8-oxoguanine
    • Russo M.T., De Luca G., Degan P., and Bignami M. Different DNA repair strategies to combat the threat from 8-oxoguanine. Mutat. Res. 614 (2007) 69-76
    • (2007) Mutat. Res. , vol.614 , pp. 69-76
    • Russo, M.T.1    De Luca, G.2    Degan, P.3    Bignami, M.4
  • 206
    • 0000885942 scopus 로고
    • A case of authentic fertility in a man of 94
    • Seymour F., Duffy C., and Korner A. A case of authentic fertility in a man of 94. JAMA (1935) 1423-1424
    • (1935) JAMA , pp. 1423-1424
    • Seymour, F.1    Duffy, C.2    Korner, A.3
  • 207
    • 0036357310 scopus 로고    scopus 로고
    • DNA base-excision repair enzyme apurinic/apyrimidinic endonuclease/redox factor-1 is increased and competent in the brain and spinal cord of individuals with amyotrophic lateral sclerosis
    • Shaikh A.Y., and Martin L.J. DNA base-excision repair enzyme apurinic/apyrimidinic endonuclease/redox factor-1 is increased and competent in the brain and spinal cord of individuals with amyotrophic lateral sclerosis. Neuromol. Med. 2 (2002) 47-60
    • (2002) Neuromol. Med. , vol.2 , pp. 47-60
    • Shaikh, A.Y.1    Martin, L.J.2
  • 208
    • 0034733928 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model?
    • Shall S., and de Murcia G. Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model?. Mutat. Res. 460 (2000) 1-15
    • (2000) Mutat. Res. , vol.460 , pp. 1-15
    • Shall, S.1    de Murcia, G.2
  • 209
    • 0037726504 scopus 로고    scopus 로고
    • Decline of nuclear and mitochondrial oxidative base excision repair activity in late passage human diploid fibroblasts
    • Shen G.P., Galick H., Inoue M., and Wallace S.S. Decline of nuclear and mitochondrial oxidative base excision repair activity in late passage human diploid fibroblasts. DNA Repair (Amst.) 2 (2003) 673-693
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 673-693
    • Shen, G.P.1    Galick, H.2    Inoue, M.3    Wallace, S.S.4
  • 210
    • 0035837651 scopus 로고    scopus 로고
    • Somatic mutations and single nucleotide polymorphisms of base excision repair genes involved in the repair of 8-hydroxyguanine in damaged DNA
    • Shinmura K., Yamaguchi S., Saitoh T., Kohno T., and Yokota J. Somatic mutations and single nucleotide polymorphisms of base excision repair genes involved in the repair of 8-hydroxyguanine in damaged DNA. Cancer Lett. 166 (2001) 65-69
    • (2001) Cancer Lett. , vol.166 , pp. 65-69
    • Shinmura, K.1    Yamaguchi, S.2    Saitoh, T.3    Kohno, T.4    Yokota, J.5
  • 211
    • 0034283847 scopus 로고    scopus 로고
    • In vivo repair of methylation damage in Aag 3-methyladenine DNA glycosylase null mouse cells
    • Smith S.A., and Engelward B.P. In vivo repair of methylation damage in Aag 3-methyladenine DNA glycosylase null mouse cells. Nucleic Acids Res. 28 (2000) 3294-3300
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3294-3300
    • Smith, S.A.1    Engelward, B.P.2
  • 212
    • 0034976379 scopus 로고    scopus 로고
    • Effects of age on testicular function and consequences of testosterone treatment
    • Snyder P.J. Effects of age on testicular function and consequences of testosterone treatment. J. Clin. Endocrinol. Metab. 86 (2001) 2369-2372
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 2369-2372
    • Snyder, P.J.1
  • 214
    • 0033561246 scopus 로고    scopus 로고
    • Age-associated increase in 8-oxo-deoxyguanosine glycosylase/AP lyase activity in rat mitochondria
    • Souza-Pinto N.C., Croteau D.L., Hudson E.K., Hansford R.G., and Bohr V.A. Age-associated increase in 8-oxo-deoxyguanosine glycosylase/AP lyase activity in rat mitochondria. Nucleic Acids Res. 27 (1999) 1935-1942
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1935-1942
    • Souza-Pinto, N.C.1    Croteau, D.L.2    Hudson, E.K.3    Hansford, R.G.4    Bohr, V.A.5
  • 215
    • 0031888181 scopus 로고    scopus 로고
    • Effect of parental age on fertilization and pregnancy characteristics in couples treated by intracytoplasmic sperm injection
    • Spandorfer S.D., Avrech O.M., Colombero L.T., Palermo G.D., and Rosenwaks Z. Effect of parental age on fertilization and pregnancy characteristics in couples treated by intracytoplasmic sperm injection. Hum. Reprod. 13 (1998) 334-338
    • (1998) Hum. Reprod. , vol.13 , pp. 334-338
    • Spandorfer, S.D.1    Avrech, O.M.2    Colombero, L.T.3    Palermo, G.D.4    Rosenwaks, Z.5
  • 216
    • 17144410054 scopus 로고    scopus 로고
    • Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation
    • Steinacher R., and Schar P. Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation. Curr. Biol. 15 (2005) 616-623
    • (2005) Curr. Biol. , vol.15 , pp. 616-623
    • Steinacher, R.1    Schar, P.2
  • 217
    • 0035174375 scopus 로고    scopus 로고
    • A polymorphism of the XRCC1 gene predicts for response to platinum based treatment in advanced colorectal cancer
    • Stoehlmacher J., Ghaderi V., Iobal S., Groshen S., Tsao-Wei D., Park D., and Lenz H.J. A polymorphism of the XRCC1 gene predicts for response to platinum based treatment in advanced colorectal cancer. Anticancer Res. 21 (2001) 3075-3079
    • (2001) Anticancer Res. , vol.21 , pp. 3075-3079
    • Stoehlmacher, J.1    Ghaderi, V.2    Iobal, S.3    Groshen, S.4    Tsao-Wei, D.5    Park, D.6    Lenz, H.J.7
  • 218
    • 0033924885 scopus 로고    scopus 로고
    • Through a glass, darkly: reflections of mutation from lacI transgenic mice
    • Stuart G.R., and Glickman B.W. Through a glass, darkly: reflections of mutation from lacI transgenic mice. Genetics 155 (2000) 1359-1367
    • (2000) Genetics , vol.155 , pp. 1359-1367
    • Stuart, G.R.1    Glickman, B.W.2
  • 219
    • 0034006159 scopus 로고    scopus 로고
    • Mutation frequency and specificity with age in liver, bladder and brain of lacI transgenic mice
    • Stuart G.R., Oda Y., de Boer J.G., and Glickman B.W. Mutation frequency and specificity with age in liver, bladder and brain of lacI transgenic mice. Genetics 154 (2000) 1291-1300
    • (2000) Genetics , vol.154 , pp. 1291-1300
    • Stuart, G.R.1    Oda, Y.2    de Boer, J.G.3    Glickman, B.W.4
  • 220
    • 2442695594 scopus 로고    scopus 로고
    • Mitochondrial and nuclear DNA base excision repair are affected differently by caloric restriction
    • Stuart J.A., Karahalil B., Hogue B.A., Souza-Pinto N.C., and Bohr V.A. Mitochondrial and nuclear DNA base excision repair are affected differently by caloric restriction. FASEB J. 18 (2004) 595-597
    • (2004) FASEB J. , vol.18 , pp. 595-597
    • Stuart, J.A.1    Karahalil, B.2    Hogue, B.A.3    Souza-Pinto, N.C.4    Bohr, V.A.5
  • 221
    • 22244476422 scopus 로고    scopus 로고
    • Localization of mitochondrial DNA base excision repair to an inner membrane-associated particulate fraction
    • Stuart J.A., Mayard S., Hashiguchi K., Souza-Pinto N.C., and Bohr V.A. Localization of mitochondrial DNA base excision repair to an inner membrane-associated particulate fraction. Nucleic Acids Res. 33 (2005) 3722-3732
    • (2005) Nucleic Acids Res. , vol.33 , pp. 3722-3732
    • Stuart, J.A.1    Mayard, S.2    Hashiguchi, K.3    Souza-Pinto, N.C.4    Bohr, V.A.5
  • 223
    • 0034654379 scopus 로고    scopus 로고
    • Neonatal lethality with abnormal neurogenesis in mice deficient in DNA polymerase beta
    • Sugo N., Aratani Y., Nagashima Y., Kubota Y., and Koyama H. Neonatal lethality with abnormal neurogenesis in mice deficient in DNA polymerase beta. EMBO J. 19 (2000) 1397-1404
    • (2000) EMBO J. , vol.19 , pp. 1397-1404
    • Sugo, N.1    Aratani, Y.2    Nagashima, Y.3    Kubota, Y.4    Koyama, H.5
  • 224
    • 3042842128 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 inhibits strand-displacement synthesis of DNA catalyzed by DNA polymerase beta
    • Sukhanova M.V., Khodyreva S.N., and Lavrik O.I. Poly(ADP-ribose) polymerase-1 inhibits strand-displacement synthesis of DNA catalyzed by DNA polymerase beta. Biochemistry (Mosc) 69 (2004) 558-568
    • (2004) Biochemistry (Mosc) , vol.69 , pp. 558-568
    • Sukhanova, M.V.1    Khodyreva, S.N.2    Lavrik, O.I.3
  • 225
    • 34047135111 scopus 로고    scopus 로고
    • Suppression of base excision repair reactions by apoptotic 24 kDa-fragment of poly(ADP-ribose) polymerase 1 in bovine testis nuclear extract
    • Sukhanova M., Khodyreva S., and Lavrik O. Suppression of base excision repair reactions by apoptotic 24 kDa-fragment of poly(ADP-ribose) polymerase 1 in bovine testis nuclear extract. DNA Repair (Amst.) 6 (2007) 615-625
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 615-625
    • Sukhanova, M.1    Khodyreva, S.2    Lavrik, O.3
  • 226
    • 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 (2005) 1071-1078
    • (2005) Mech. Ageing Dev. , vol.126 , pp. 1071-1078
    • Szczesny, B.1    Mitra, S.2
  • 227
    • 0002235236 scopus 로고
    • On the Nature of the Aging Process
    • Szilard L. On the Nature of the Aging Process. Proc. Natl. Acad. Sci. U.S.A. 45 (1959) 30-45
    • (1959) Proc. Natl. Acad. Sci. U.S.A. , vol.45 , pp. 30-45
    • Szilard, L.1
  • 228
    • 14044278774 scopus 로고    scopus 로고
    • Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein
    • Takahashi H., Hatakeyama S., Saitoh H., and Nakayama K.I. Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein. J. Biol. Chem. 280 (2005) 5611-5621
    • (2005) J. Biol. Chem. , vol.280 , pp. 5611-5621
    • Takahashi, H.1    Hatakeyama, S.2    Saitoh, H.3    Nakayama, K.I.4
  • 229
    • 15244361447 scopus 로고    scopus 로고
    • The Arg280His polymorphism in X-ray repair cross-complementing gene 1 impairs DNA repair ability
    • Takanami T., Nakamura J., Kubota Y., and Horiuchi S. The Arg280His polymorphism in X-ray repair cross-complementing gene 1 impairs DNA repair ability. Mutat. Res. 582 (2005) 135-145
    • (2005) Mutat. Res. , vol.582 , pp. 135-145
    • Takanami, T.1    Nakamura, J.2    Kubota, Y.3    Horiuchi, S.4
  • 230
    • 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 (1998) 2917-2922
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2917-2922
    • Takao, M.1    Aburatani, H.2    Kobayashi, K.3    Yasui, A.4
  • 231
  • 233
    • 0036208101 scopus 로고    scopus 로고
    • Central role for the XRCC1 BRCT I domain in mammalian DNA single-strand break repair
    • Taylor R.M., Thistlethwaite A., and Caldecott K.W. Central role for the XRCC1 BRCT I domain in mammalian DNA single-strand break repair. Mol. Cell. Biol. 22 (2002) 2556-2563
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2556-2563
    • Taylor, R.M.1    Thistlethwaite, A.2    Caldecott, K.W.3
  • 235
    • 14044269479 scopus 로고    scopus 로고
    • The Intracellular Localization of APE1/Ref-1: More than a Passive Phenomenon?
    • Tell G., Damante G., Caldwell D., and Kelley M.R. The Intracellular Localization of APE1/Ref-1: More than a Passive Phenomenon?. Antioxidants Redox Signal. 7 (2005) 367-384
    • (2005) Antioxidants Redox Signal. , vol.7 , pp. 367-384
    • Tell, G.1    Damante, G.2    Caldwell, D.3    Kelley, M.R.4
  • 237
    • 0024241304 scopus 로고
    • Mitochondrial endonuclease activities specific for apurinic/apyrimidinic sites in DNA from mouse cells
    • Tomkinson A.E., Bonk R.T., and Linn S. Mitochondrial endonuclease activities specific for apurinic/apyrimidinic sites in DNA from mouse cells. J. Biol. Chem. 263 (1988) 12532-12537
    • (1988) J. Biol. Chem. , vol.263 , pp. 12532-12537
    • Tomkinson, A.E.1    Bonk, R.T.2    Linn, S.3
  • 239
    • 32944471308 scopus 로고    scopus 로고
    • Hematopoietic tissue-specific expression of mouse Neil3 for endonuclease VIII-like protein
    • Torisu K., Tsuchimoto D., Ohnishi Y., and Nakabeppu Y. Hematopoietic tissue-specific expression of mouse Neil3 for endonuclease VIII-like protein. J. Biochem. (Tokyo) 138 (2005) 763-772
    • (2005) J. Biochem. (Tokyo) , vol.138 , pp. 763-772
    • Torisu, K.1    Tsuchimoto, D.2    Ohnishi, Y.3    Nakabeppu, Y.4
  • 240
    • 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 (2001) 2349-2360
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2349-2360
    • Tsuchimoto, D.1    Sakai, Y.2    Sakumi, K.3    Nishioka, K.4    Sasaki, M.5    Fujiwara, T.6    Nakabeppu, Y.7
  • 242
    • 0028979570 scopus 로고
    • Ageing of the hypothalamo-pituitary-testicular axis in men
    • Vermeulen A., and Kaufman J.M. Ageing of the hypothalamo-pituitary-testicular axis in men. Horm. Res. 43 (1995) 25-28
    • (1995) Horm. Res. , vol.43 , pp. 25-28
    • Vermeulen, A.1    Kaufman, J.M.2
  • 243
    • 0035890069 scopus 로고    scopus 로고
    • XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions
    • Vidal A.E., Boiteux S., Hickson I.D., and Radicella J.P. XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions. EMBO J. 20 (2001) 6530-6539
    • (2001) EMBO J. , vol.20 , pp. 6530-6539
    • Vidal, A.E.1    Boiteux, S.2    Hickson, I.D.3    Radicella, J.P.4
  • 247
    • 0032544120 scopus 로고    scopus 로고
    • Mutation frequency declines during spermatogenesis in young mice but increases in old mice
    • Walter C.A. Mutation frequency declines during spermatogenesis in young mice but increases in old mice. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 10015-10019
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 10015-10019
    • Walter, C.A.1
  • 250
    • 0034658267 scopus 로고    scopus 로고
    • Mitochondrial DNA damage and a hypoxic response are induced by CoCl(2) in rat neuronal PC12 cells
    • Wang G., Hazra T.K., Mitra S., Lee H.M., and Englander E.W. Mitochondrial DNA damage and a hypoxic response are induced by CoCl(2) in rat neuronal PC12 cells. Nucleic Acids Res. 28 (2000) 2135-2140
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2135-2140
    • Wang, G.1    Hazra, T.K.2    Mitra, S.3    Lee, H.M.4    Englander, E.W.5
  • 251
    • 0142124401 scopus 로고    scopus 로고
    • From genotype to phenotype: correlating XRCC1 polymorphisms with mutagen sensitivity
    • Wang Y., Spitz M.R., Zhu Y., Dong Q., Shete S., and Wu X. From genotype to phenotype: correlating XRCC1 polymorphisms with mutagen sensitivity. DNA Repair (Amst.) 2 (2003) 901-908
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 901-908
    • Wang, Y.1    Spitz, M.R.2    Zhu, Y.3    Dong, Q.4    Shete, S.5    Wu, X.6
  • 255
    • 13944281044 scopus 로고    scopus 로고
    • Polymorphic variation in hOGG1 and risk of cancer: a review of the functional and epidemiologic literature
    • Weiss J.M., Goode E.L., Ladiges W.C., and Ulrich C.M. Polymorphic variation in hOGG1 and risk of cancer: a review of the functional and epidemiologic literature. Mol. Carcinog. 42 (2005) 127-141
    • (2005) Mol. Carcinog. , vol.42 , pp. 127-141
    • Weiss, J.M.1    Goode, E.L.2    Ladiges, W.C.3    Ulrich, C.M.4
  • 257
    • 34548802393 scopus 로고    scopus 로고
    • Defective DNA base excision repair in brain from individuals with Alzheimer's disease and amnestic mild cognitive impairment
    • Weissman L., Jo D.G., Sorensen M.M., de Souza-Pinto N.C., Markesbery W.R., Mattson M.P., and Bohr V.A. Defective DNA base excision repair in brain from individuals with Alzheimer's disease and amnestic mild cognitive impairment. Nucleic Acids Res. 35 (2007) 5545-5555
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5545-5555
    • Weissman, L.1    Jo, D.G.2    Sorensen, M.M.3    de Souza-Pinto, N.C.4    Markesbery, W.R.5    Mattson, M.P.6    Bohr, V.A.7
  • 258
    • 0024541790 scopus 로고
    • In vitro correction of G.T mispairs to G.C pairs in nuclear extracts from human cells
    • Wiebauer K., and Jiricny J. In vitro correction of G.T mispairs to G.C pairs in nuclear extracts from human cells. Nature 339 (1989) 234-236
    • (1989) Nature , vol.339 , pp. 234-236
    • Wiebauer, K.1    Jiricny, J.2
  • 261
    • 0035837587 scopus 로고    scopus 로고
    • The major human abasic endonuclease: formation, consequences and repair of abasic lesions in DNA
    • Wilson III D.M., and Barsky D. The major human abasic endonuclease: formation, consequences and repair of abasic lesions in DNA. Mutat. Res. 485 (2001) 283-307
    • (2001) Mutat. Res. , vol.485 , pp. 283-307
    • Wilson III, D.M.1    Barsky, D.2
  • 263
    • 33847007529 scopus 로고    scopus 로고
    • The mechanics of base excision repair, and its relationship to aging and disease
    • Wilson III D.M., and Bohr V.A. The mechanics of base excision repair, and its relationship to aging and disease. DNA Repair (Amst.) 6 (2007) 544-559
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 544-559
    • Wilson III, D.M.1    Bohr, V.A.2
  • 266
    • 13844280351 scopus 로고    scopus 로고
    • Human 3-methyladenine-DNA glycosylase: effect of sequence context on excision, association with PCNA, and stimulation by AP endonuclease
    • Xia L., Zheng L., Lee H.W., Bates S.E., Federico L., Shen B., and O'Connor T.R. Human 3-methyladenine-DNA glycosylase: effect of sequence context on excision, association with PCNA, and stimulation by AP endonuclease. J. Mol. Biol. 346 (2005) 1259-1274
    • (2005) J. Mol. Biol. , vol.346 , pp. 1259-1274
    • Xia, L.1    Zheng, L.2    Lee, H.W.3    Bates, S.E.4    Federico, L.5    Shen, B.6    O'Connor, T.R.7
  • 268
    • 0344875199 scopus 로고    scopus 로고
    • Human thymine DNA glycosylase (TDG) and methyl-CpG-binding protein 4 (MBD4) excise thymine glycol (Tg) from a Tg:G mispair
    • Yoon J.H., Iwai S., O'Connor T.R., and Pfeifer G.P. Human thymine DNA glycosylase (TDG) and methyl-CpG-binding protein 4 (MBD4) excise thymine glycol (Tg) from a Tg:G mispair. Nucleic Acids Res. 31 (2003) 5399-5404
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5399-5404
    • Yoon, J.H.1    Iwai, S.2    O'Connor, T.R.3    Pfeifer, G.P.4
  • 270
    • 0028101170 scopus 로고
    • Somatic and MEN 2A de novo mutations identified in the RET proto-oncogene by screening of sporadic MTC:s
    • Zedenius J., Wallin G., Hamberger B., Nordenskjold M., Weber G., and Larsson C. Somatic and MEN 2A de novo mutations identified in the RET proto-oncogene by screening of sporadic MTC:s. Hum. Mol. Genet. 3 (1994) 1259-1262
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1259-1262
    • Zedenius, J.1    Wallin, G.2    Hamberger, B.3    Nordenskjold, M.4    Weber, G.5    Larsson, C.6
  • 271
    • 7944227532 scopus 로고    scopus 로고
    • DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells
    • Zhang Q.M., Yonekura S., Takao M., Yasui A., Sugiyama H., and Yonei S. DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells. DNA Repair (Amst.) 4 (2005) 71-79
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 71-79
    • Zhang, Q.M.1    Yonekura, S.2    Takao, M.3    Yasui, A.4    Sugiyama, H.5    Yonei, S.6
  • 272
    • 0028838395 scopus 로고
    • Expression of the DNA repair gene XRCC1 in baboon tissues
    • Zhou Z.Q., and Walter C.A. Expression of the DNA repair gene XRCC1 in baboon tissues. Mutat. Res. 348 (1995) 111-116
    • (1995) Mutat. Res. , vol.348 , pp. 111-116
    • Zhou, Z.Q.1    Walter, C.A.2


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