메뉴 건너뛰기




Volumn 531, Issue 1-2, 2003, Pages 37-80

Mutagenicity, toxicity and repair of DNA base damage induced by oxidation

Author keywords

DNA; Mutagenicity; Toxicity

Indexed keywords

5 METHYLCYTOSINE; ADENINE DERIVATIVE; CYTOSINE DERIVATIVE; DNA BASE; GUANINE DERIVATIVE; METHYL GROUP; MUTAGENIC AGENT; THYMINE DERIVATIVE;

EID: 0344586043     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2003.07.002     Document Type: Conference Paper
Times cited : (422)

References (410)
  • 2
    • 0023726166 scopus 로고
    • The repairability of oxidative free radical mediated damage to DNA: A review
    • Teebor G.W., Boorstein R.J., Cadet J. The repairability of oxidative free radical mediated damage to DNA: a review. Int. J. Radiat. Biol. 54:1988;131-150.
    • (1988) Int. J. Radiat. Biol. , vol.54 , pp. 131-150
    • Teebor, G.W.1    Boorstein, R.J.2    Cadet, J.3
  • 4
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • Imlay J.A., Linn S. DNA damage and oxygen radical toxicity. Science. 240:1988;1302-1309.
    • (1988) Science , vol.240 , pp. 1302-1309
    • Imlay, J.A.1    Linn, S.2
  • 6
    • 0030797051 scopus 로고    scopus 로고
    • Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide
    • Henle E.S., Linn S. Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide. J. Biol. Chem. 272:1997;19095-19098.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19095-19098
    • Henle, E.S.1    Linn, S.2
  • 7
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature. 362:1993;709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 10
    • 0030777056 scopus 로고    scopus 로고
    • Hypochlorous acid-induced base modifications in isolated calf thymus DNA
    • Whiteman M., Jenner A., Halliwell B. Hypochlorous acid-induced base modifications in isolated calf thymus DNA. Chem. Res. Toxicol. 10:1997;1240-1246.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 1240-1246
    • Whiteman, M.1    Jenner, A.2    Halliwell, B.3
  • 11
    • 0033584939 scopus 로고    scopus 로고
    • Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes produces 5-chlorocytosine in bacterial RNA
    • Henderson J.P., Byun J., Heinecke J.W. Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes produces 5-chlorocytosine in bacterial RNA. J. Biol. Chem. 274:1999;33440-33448.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33440-33448
    • Henderson, J.P.1    Byun, J.2    Heinecke, J.W.3
  • 13
    • 0033551167 scopus 로고    scopus 로고
    • Hypochlorous acid-induced DNA base modification: Potentiation by nitrite - Biomarkers of DNA damage by reactive oxygen species
    • Whiteman M., Spencer J.P.E., Jenner A., Halliwell B. Hypochlorous acid-induced DNA base modification: potentiation by nitrite - biomarkers of DNA damage by reactive oxygen species. Biochem. Biophys. Res. Commun. 257:1999;572-576.
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 572-576
    • Whiteman, M.1    Spencer, J.P.E.2    Jenner, A.3    Halliwell, B.4
  • 15
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan H.E., Standal R., Slupphaug G. DNA glycosylases in the base excision repair of DNA. Biochem. J. 325:1997;1-16.
    • (1997) Biochem. J. , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 16
    • 0001473891 scopus 로고    scopus 로고
    • Chemistry of glycosylases and endonucleases involved in base-excision repair
    • David S.S., Williams S.D. Chemistry of glycosylases and endonucleases involved in base-excision repair. Chem. Rev. 98:1998;1221-1261.
    • (1998) Chem. Rev. , vol.98 , pp. 1221-1261
    • David, S.S.1    Williams, S.D.2
  • 17
    • 0036628726 scopus 로고    scopus 로고
    • Biological consequences of free radical-damaged DNA bases
    • Wallace S.S. Biological consequences of free radical-damaged DNA bases. Free Radic. Biol. Med. 33:2002;1-14.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1-14
    • Wallace, S.S.1
  • 19
    • 0032836651 scopus 로고    scopus 로고
    • Initiation of base excision repair: Glycosylase mechanisms and structures
    • McCullough A.K., Dodson M.L., Lloyd R.S. Initiation of base excision repair: glycosylase mechanisms and structures. Annu. Rev. Biochem. 68:1999;255-285.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 255-285
    • McCullough, A.K.1    Dodson, M.L.2    Lloyd, R.S.3
  • 20
    • 0035163137 scopus 로고    scopus 로고
    • Complexities of the DNA base excision repair pathway for repair of oxidative DNA damage
    • Mitra S., Boldogh I., Izumi T., Hazra T.K. Complexities of the DNA base excision repair pathway for repair of oxidative DNA damage. Environ. Mol. Mutagen. 38:2001;180-190.
    • (2001) Environ. Mol. Mutagen. , vol.38 , pp. 180-190
    • Mitra, S.1    Boldogh, I.2    Izumi, T.3    Hazra, T.K.4
  • 21
    • 0025054962 scopus 로고
    • Nucleotide excision repair in Escherichia coli
    • Van Houten B. Nucleotide excision repair in Escherichia coli. Microbiol. Rev. 54:1990;18-51.
    • (1990) Microbiol. Rev. , vol.54 , pp. 18-51
    • Van Houten, B.1
  • 22
    • 0033197818 scopus 로고    scopus 로고
    • MSH2 and MSH6 are required for removal of adenine misincorporated opposite 8-oxo-guanine in S. cerevisiae
    • Ni T.T., Marsischky G.T., Kolodner R.D. MSH2 and MSH6 are required for removal of adenine misincorporated opposite 8-oxo-guanine in S. cerevisiae. Mol. Cell. 4:1999;439-444.
    • (1999) Mol. Cell , vol.4 , pp. 439-444
    • Ni, T.T.1    Marsischky, G.T.2    Kolodner, R.D.3
  • 25
    • 0028315896 scopus 로고
    • Thymidine hydroperoxides: Structural assignment, conformational features, and thermal decomposition in water
    • Wagner J.R., van Lier J.E., Berger M., Cadet J. Thymidine hydroperoxides: structural assignment, conformational features, and thermal decomposition in water. J. Am. Chem. Soc. 116:1994;2235-2242.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 2235-2242
    • Wagner, J.R.1    Van Lier, J.E.2    Berger, M.3    Cadet, J.4
  • 26
    • 0017668133 scopus 로고
    • Thymine fragment damage retained in the DNA polynucleotide chain after gamma irradiation in aerated solutions (II)
    • Téoule R., Bert C., Bonicel A. Thymine fragment damage retained in the DNA polynucleotide chain after gamma irradiation in aerated solutions (II). Radiat. Res. 72:1977;190-200.
    • (1977) Radiat. Res. , vol.72 , pp. 190-200
    • Téoule, R.1    Bert, C.2    Bonicel, A.3
  • 27
    • 0022432549 scopus 로고
    • Thymine glycols and urea residues in M13 DNA constitute replicative blocks in vitro
    • Ide H., Kow Y.W., Wallace S.S. Thymine glycols and urea residues in M13 DNA constitute replicative blocks in vitro. Nucl. Acids Res. 13:1985;8035-8052.
    • (1985) Nucl. Acids Res. , vol.13 , pp. 8035-8052
    • Ide, H.1    Kow, Y.W.2    Wallace, S.S.3
  • 28
    • 0023055848 scopus 로고
    • Sequence dependence for bypass of thymine glycols in DNA by DNA polymerase I
    • Hayes R.C., LeClerc J.E. Sequence dependence for bypass of thymine glycols in DNA by DNA polymerase I. Nucl. Acids Res. 14:1986;1045-1061.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 1045-1061
    • Hayes, R.C.1    Leclerc, J.E.2
  • 29
    • 0023055875 scopus 로고
    • Thymine glycol lesions terminate chain elongation by DNA polymerase I in vitro
    • Clark J.M., Beardsley G.P. Thymine glycol lesions terminate chain elongation by DNA polymerase I in vitro. Nucl. Acids Res. 14:1986;737-749.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 737-749
    • Clark, J.M.1    Beardsley, G.P.2
  • 30
    • 0023664796 scopus 로고
    • Functional effects of cis-thymine glycol lesions on DNA synthesis in vitro
    • Clark J.M., Beardsley G.P. Functional effects of cis-thymine glycol lesions on DNA synthesis in vitro. Biochemistry. 26:1987;5398-5403.
    • (1987) Biochemistry , vol.26 , pp. 5398-5403
    • Clark, J.M.1    Beardsley, G.P.2
  • 31
    • 0017456760 scopus 로고
    • Biological effect of thymine ring saturation in coliphage φx174-DNA
    • Hariharan P.V., Achey P.M., Cerutti P.A. Biological effect of thymine ring saturation in coliphage φX174-DNA. Radiat. Res. 69:1977;375-378.
    • (1977) Radiat. Res. , vol.69 , pp. 375-378
    • Hariharan, P.V.1    Achey, P.M.2    Cerutti, P.A.3
  • 32
    • 2642622799 scopus 로고
    • Genetic effects of thymine glycol: Site-specific mutagenesis and molecular modeling studies
    • Basu A.K., Loechler E.L., Leadon S.A., Essigmann J.M. Genetic effects of thymine glycol: site-specific mutagenesis and molecular modeling studies. Proc. Natl. Acad. Sci. U.S.A. 86:1989;7677-7681.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 7677-7681
    • Basu, A.K.1    Loechler, E.L.2    Leadon, S.A.3    Essigmann, J.M.4
  • 33
    • 0031859082 scopus 로고    scopus 로고
    • Replication inhibition and miscoding properties of DNA templates containing a site-specific cis-thymine glycol or urea residue
    • McNulty J.M., Jerkovic B., Bolton P.H., Basu A.K. Replication inhibition and miscoding properties of DNA templates containing a site-specific cis-thymine glycol or urea residue. Chem. Res. Toxicol. 11:1998;666-673.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 666-673
    • McNulty, J.M.1    Jerkovic, B.2    Bolton, P.H.3    Basu, A.K.4
  • 34
    • 0037076519 scopus 로고    scopus 로고
    • Translesion synthesis by human DNA polymerase η across thymine glycol lesions
    • Kusumoto R., Masutani C., Iwai S., Hanaoka F. Translesion synthesis by human DNA polymerase η across thymine glycol lesions. Biochemistry. 41:2002;6090-6099.
    • (2002) Biochemistry , vol.41 , pp. 6090-6099
    • Kusumoto, R.1    Masutani, C.2    Iwai, S.3    Hanaoka, F.4
  • 35
    • 0037020269 scopus 로고    scopus 로고
    • Human DNA polymerase κ bypasses and extends beyond thymine glycols during translesion synthesis in vitro, preferentially incorporating correct nucleotides
    • Fischhaber P.L., Gerlach V.L., Feaver W.J., Hatahet Z., Wallace S.S., Friedberg E.C. Human DNA polymerase κ bypasses and extends beyond thymine glycols during translesion synthesis in vitro, preferentially incorporating correct nucleotides. J. Biol. Chem. 277:2002;37604-37611.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37604-37611
    • Fischhaber, P.L.1    Gerlach, V.L.2    Feaver, W.J.3    Hatahet, Z.4    Wallace, S.S.5    Friedberg, E.C.6
  • 36
    • 0028138235 scopus 로고
    • Oxidative DNA lesions as blocks to in vitro transcription by phage T7 RNA polymerase
    • Hatahet Z., Purmal A.A., Wallace S.S. Oxidative DNA lesions as blocks to in vitro transcription by phage T7 RNA polymerase. Ann. N. Y. Acad. Sci. 726:1994;346-348.
    • (1994) Ann. N. Y. Acad. Sci. , vol.726 , pp. 346-348
    • Hatahet, Z.1    Purmal, A.A.2    Wallace, S.S.3
  • 37
    • 0027304370 scopus 로고
    • Characterization of the effects of a thymine glycol residue on the structure, dynamics, and stability of duplex DNA by NMR
    • Kao J.Y., Goljer I., Phan T.A., Bolton P.H. Characterization of the effects of a thymine glycol residue on the structure, dynamics, and stability of duplex DNA by NMR. J. Biol. Chem. 268:1993;17787-17793.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17787-17793
    • Kao, J.Y.1    Goljer, I.2    Phan, T.A.3    Bolton, P.H.4
  • 38
    • 0001195990 scopus 로고    scopus 로고
    • Structure of a duplex DNA containing a thymine glycol residue in solution
    • Kung H.C., Bolton P.H. Structure of a duplex DNA containing a thymine glycol residue in solution. J. Biol. Chem. 272:1997;9227-9236.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9227-9236
    • Kung, H.C.1    Bolton, P.H.2
  • 39
    • 0024468299 scopus 로고
    • A new mechanism for repairing oxidative damage to DNA: (A)BC excinuclease removes AP sites and thymine glycols from DNA
    • Lin J.-J., Sancar A. A new mechanism for repairing oxidative damage to DNA: (A)BC excinuclease removes AP sites and thymine glycols from DNA. Biochemistry. 28:1989;7979-7984.
    • (1989) Biochemistry , vol.28 , pp. 7979-7984
    • Lin, J.-J.1    Sancar, A.2
  • 40
    • 0025017257 scopus 로고
    • UvrABC nuclease complex repairs thymine glycol, an oxidative DNA base damage
    • Kow Y.W., Wallace S.S., Van Houten B. UvrABC nuclease complex repairs thymine glycol, an oxidative DNA base damage. Mutat. Res. 235:1990;147-156.
    • (1990) Mutat. Res. , vol.235 , pp. 147-156
    • Kow, Y.W.1    Wallace, S.S.2    Van Houten, B.3
  • 41
    • 0030745912 scopus 로고    scopus 로고
    • In vitro repair of oxidative DNA damage by human nucleotide excision repair system: Possible explanation for neurodegeneration in xeroderma pigmentosum patients
    • Reardon J.T., Bessho T., Kung H.C., Bolton P.H., Sancar A. In vitro repair of oxidative DNA damage by human nucleotide excision repair system: possible explanation for neurodegeneration in xeroderma pigmentosum patients. Proc. Natl. Acad. Sci. U.S.A. 94:1997;9463-9468.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 9463-9468
    • Reardon, J.T.1    Bessho, T.2    Kung, H.C.3    Bolton, P.H.4    Sancar, A.5
  • 42
    • 0034697012 scopus 로고    scopus 로고
    • Single nucleotide patch base excision repair is the major pathway for removal of thymine glycol from DNA in human cell extracts
    • Dianov G.L., Thybo T., Dianova I.I., Lipinski L.J., Bohr V.A. Single nucleotide patch base excision repair is the major pathway for removal of thymine glycol from DNA in human cell extracts. J. Biol. Chem. 275:2000;11809-11813.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11809-11813
    • Dianov, G.L.1    Thybo, T.2    Dianova, I.I.3    Lipinski, L.J.4    Bohr, V.A.5
  • 43
    • 0033557139 scopus 로고    scopus 로고
    • Nucleotide excision repair 3′ endonuclease XPG stimulates the activity of base excision repair enzyme thymine glycol DNA glycosylase
    • Bessho T. Nucleotide excision repair 3′ endonuclease XPG stimulates the activity of base excision repair enzyme thymine glycol DNA glycosylase. Nucl. Acids Res. 27:1999;979-983.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 979-983
    • Bessho, T.1
  • 44
    • 0034646516 scopus 로고    scopus 로고
    • Transcription-coupled repair of 8-oxoguanine: Requirement for XPG, TFIIH, and CSB and implications for Cockayne syndrome
    • Le Page F., Kwoh E.E., Avrutskaya A., Gentil A., Leadon S.A., Sarasin A., Cooper P.K. Transcription-coupled repair of 8-oxoguanine: requirement for XPG, TFIIH, and CSB and implications for Cockayne syndrome. Cell. 101:2000;159-171.
    • (2000) Cell , vol.101 , pp. 159-171
    • Le Page, F.1    Kwoh, E.E.2    Avrutskaya, A.3    Gentil, A.4    Leadon, S.A.5    Sarasin, A.6    Cooper, P.K.7
  • 45
    • 0034437623 scopus 로고    scopus 로고
    • Transcription-coupled repair of oxidative DNA damage in human cells: Mechanisms and consequences
    • Tsutakawa S.E., Cooper P.K. Transcription-coupled repair of oxidative DNA damage in human cells: mechanisms and consequences. Cold Spring Harb. Symp. Quant. Biol. 65:2000;201-215.
    • (2000) Cold Spring Harb. Symp. Quant. Biol. , vol.65 , pp. 201-215
    • Tsutakawa, S.E.1    Cooper, P.K.2
  • 47
    • 0035977062 scopus 로고    scopus 로고
    • Effect of thymine glycol on transcription elongation by T7 RNA polymerase and mammalian RNA polymerase II
    • Tornaletti S., Maeda L.S., Lloyd D.R., Reines D., Hanawalt P.C. Effect of thymine glycol on transcription elongation by T7 RNA polymerase and mammalian RNA polymerase II. J. Biol. Chem. 276:2001;45367-45371.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45367-45371
    • Tornaletti, S.1    Maeda, L.S.2    Lloyd, D.R.3    Reines, D.4    Hanawalt, P.C.5
  • 48
    • 0021106244 scopus 로고
    • Characterization of the Escherichia coli X-ray endonuclease, endonuclease III
    • Katcher H.L., Wallace S.S. Characterization of the Escherichia coli X-ray endonuclease, endonuclease III. Biochemistry. 22:1983;4071-4081.
    • (1983) Biochemistry , vol.22 , pp. 4071-4081
    • Katcher, H.L.1    Wallace, S.S.2
  • 49
  • 50
    • 0023710309 scopus 로고
    • Excision repair of thymine glycols, urea residues, and apurinic sites in Escherichia coli
    • Laspia M.F., Wallace S.S. Excision repair of thymine glycols, urea residues, and apurinic sites in Escherichia coli. J. Bacteriol. 170:1988;3359-3366.
    • (1988) J. Bacteriol. , vol.170 , pp. 3359-3366
    • Laspia, M.F.1    Wallace, S.S.2
  • 51
    • 0018926091 scopus 로고
    • DNA N-glycosylases and UV repair
    • Demple B., Linn S. DNA N-glycosylases and UV repair. Nature. 287:1980;203-208.
    • (1980) Nature , vol.287 , pp. 203-208
    • Demple, B.1    Linn, S.2
  • 52
    • 0021331957 scopus 로고
    • DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli
    • Breimer L.H., Lindahl T. DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli. J. Biol. Chem. 259:1984;5543-5548.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5543-5548
    • Breimer, L.H.1    Lindahl, T.2
  • 53
    • 0022392710 scopus 로고
    • Thymine lesions produced by ionizing radiation in double-stranded DNA
    • Breimer L.H., Lindahl T. Thymine lesions produced by ionizing radiation in double-stranded DNA. Biochemistry. 24:1985;4018-4022.
    • (1985) Biochemistry , vol.24 , pp. 4018-4022
    • Breimer, L.H.1    Lindahl, T.2
  • 55
    • 0028295382 scopus 로고
    • Isolation and characterization of endonuclease VIII from Escherichia coli
    • Melamede R.J., Hatahet Z., Kow Y.W., Ide H., Wallace S.S. Isolation and characterization of endonuclease VIII from Escherichia coli. Biochemistry. 33:1994;1255-1264.
    • (1994) Biochemistry , vol.33 , pp. 1255-1264
    • Melamede, R.J.1    Hatahet, Z.2    Kow, Y.W.3    Ide, H.4    Wallace, S.S.5
  • 56
    • 0034637604 scopus 로고    scopus 로고
    • Recognition of formamidopyrimidine by Escherichia coli and mammalian thymine glycol glycosylases. Distinctive paired base effects and biological and mechanistic implications
    • Asagoshi K., Yamada T., Okada Y., Terato H., Ohyama Y., Seki S., Ide H. Recognition of formamidopyrimidine by Escherichia coli and mammalian thymine glycol glycosylases. Distinctive paired base effects and biological and mechanistic implications. J. Biol. Chem. 275:2000;24781-24786.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24781-24786
    • Asagoshi, K.1    Yamada, T.2    Okada, Y.3    Terato, H.4    Ohyama, Y.5    Seki, S.6    Ide, H.7
  • 57
    • 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. Nucl. Acid Res. Mol. Biol. 68:2001;207-221.
    • (2001) Prog. Nucl. Acid Res. Mol. Biol. , vol.68 , pp. 207-221
    • Ide, H.1
  • 59
    • 0242418186 scopus 로고    scopus 로고
    • Endonuclease IV enhances base excision repair of endonuclease III from Methanobacterium thermoautotrophicum
    • Back J.H., Chung J.H., Park Y.I., Kim K.-S., Han Y.S. Endonuclease IV enhances base excision repair of endonuclease III from Methanobacterium thermoautotrophicum. DNA Repair. 2:2003;455-470.
    • (2003) DNA Repair , vol.2 , pp. 455-470
    • Back, J.H.1    Chung, J.H.2    Park, Y.I.3    Kim, K.-S.4    Han, Y.S.5
  • 60
    • 0033574208 scopus 로고    scopus 로고
    • Excision of 5,6-dihydroxy-5,6-dihydrothymine, 5,6-dihydrothymine, and 5-hydroxycytosine from defined sequence oligonucleotides by Escherichia coli endonuclease III and Fpg proteins: Kinetic and mechanistic aspects
    • D'Ham C., Romieu A., Jaquinod M., Gasparutto D., Cadet J. Excision of 5,6-dihydroxy-5,6-dihydrothymine, 5,6-dihydrothymine, and 5-hydroxycytosine from defined sequence oligonucleotides by Escherichia coli endonuclease III and Fpg proteins: kinetic and mechanistic aspects. Biochemistry. 38:1999;3335-3344.
    • (1999) Biochemistry , vol.38 , pp. 3335-3344
    • D'Ham, C.1    Romieu, A.2    Jaquinod, M.3    Gasparutto, D.4    Cadet, J.5
  • 61
    • 0032540240 scopus 로고    scopus 로고
    • Enzymatic processing of uracil glycol, a major oxidative product of DNA cytosine
    • Purmal A.A., Lampman G.W., Bond J.P., Hatahet Z., Wallace S.S. Enzymatic processing of uracil glycol, a major oxidative product of DNA cytosine. J. Biol. Chem. 273:1998;10026-10035.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10026-10035
    • Purmal, A.A.1    Lampman, G.W.2    Bond, J.P.3    Hatahet, Z.4    Wallace, S.S.5
  • 62
    • 0032519310 scopus 로고    scopus 로고
    • Multiply damaged sites in DNA: Interactions with Escherichia coli endonucleases III and VIII
    • Harrison L., Hatahet Z., Purmal A.A., Wallace S.S. Multiply damaged sites in DNA: interactions with Escherichia coli endonucleases III and VIII. Nucl. Acids Res. 26:1998;932-941.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 932-941
    • Harrison, L.1    Hatahet, Z.2    Purmal, A.A.3    Wallace, S.S.4
  • 63
    • 0037049975 scopus 로고    scopus 로고
    • Alternative nucleotide incision repair pathway for oxidative DNA damage
    • Ischenko A.A., Saparbaev M.K. Alternative nucleotide incision repair pathway for oxidative DNA damage. Nature. 415:2002;183-187.
    • (2002) Nature , vol.415 , pp. 183-187
    • Ischenko, A.A.1    Saparbaev, M.K.2
  • 64
    • 0032401931 scopus 로고    scopus 로고
    • Substrate specificities of the Ntg1 and Ntg2 proteins of Saccharomyces cerevisiae for oxidized DNA bases are not identical
    • Sentürker S., Auffret van der Kemp P., You H.J., Doetsch P.W., Dizdaroglu M., Boiteux S. Substrate specificities of the Ntg1 and Ntg2 proteins of Saccharomyces cerevisiae for oxidized DNA bases are not identical. Nucl. Acids Res. 26:1998;5270-5276.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 5270-5276
    • Sentürker, S.1    Auffret Van Der Kemp, P.2    You, H.J.3    Doetsch, P.W.4    Dizdaroglu, M.5    Boiteux, S.6
  • 65
    • 0032960862 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae homologues of endonuclease III from Escherichia coli, Ntg1 and Ntg2, are both required for efficient repair of spontaneous and induced oxidative DNA damage in yeast
    • Alseth I., Eide L., Pirovano M., Rognes T., Seeberg E., Bjørås M. The Saccharomyces cerevisiae homologues of endonuclease III from Escherichia coli, Ntg1 and Ntg2, are both required for efficient repair of spontaneous and induced oxidative DNA damage in yeast. Mol. Cell. Biol. 19:1999;3779-3787.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3779-3787
    • Alseth, I.1    Eide, L.2    Pirovano, M.3    Rognes, T.4    Seeberg, E.5    Bjørås, M.6
  • 67
    • 0038011100 scopus 로고    scopus 로고
    • A new Schizosaccharmyces pombe base excision repair mutant, nth1, reveals of overlapping pathways for repair of DNA base damage
    • Osman F., Bjørås M., Alseth I., Morland I., McCready S., Seeberg E., Tsaneva I. A new Schizosaccharmyces pombe base excision repair mutant, nth1, reveals of overlapping pathways for repair of DNA base damage. Mol. Microbiol. 48:2003;465-480.
    • (2003) Mol. Microbiol. , vol.48 , pp. 465-480
    • Osman, F.1    Bjørås, M.2    Alseth, I.3    Morland, I.4    McCready, S.5    Seeberg, E.6    Tsaneva, I.7
  • 68
    • 0029814011 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of a Schizosaccharomyces pombe homologue of Escherichia coli endonuclease III
    • Roldán-Arjona T., Anselmino C., Lindahl T. Molecular cloning and functional analysis of a Schizosaccharomyces pombe homologue of Escherichia coli endonuclease III. Nucl. Acids Res. 24:1996;3307-3312.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 3307-3312
    • Roldán-Arjona, T.1    Anselmino, C.2    Lindahl, T.3
  • 69
    • 0344734089 scopus 로고    scopus 로고
    • Substrate specificity of Schizosaccharomyces pombe Nth protein for products of oxidative DNA damage
    • Karahalil B., Roldán-Arjona T., Dizdaroglu M. Substrate specificity of Schizosaccharomyces pombe Nth protein for products of oxidative DNA damage. Biochemistry. 37:1998;590-595.
    • (1998) Biochemistry , vol.37 , pp. 590-595
    • Karahalil, B.1    Roldán-Arjona, T.2    Dizdaroglu, M.3
  • 71
    • 0034687125 scopus 로고    scopus 로고
    • Comparison of substrate specificities of Escherichia coli endonuclease III and its mouse homologue (mNth1) using defined oligonucleotide substrates
    • Asagoshi K., Odawara H., Nakano H., Miyano T., Terato H., Ohyama Y., Seki S., Ide H. Comparison of substrate specificities of Escherichia coli endonuclease III and its mouse homologue (mNth1) using defined oligonucleotide substrates. Biochemistry. 39:2000;11389-11398.
    • (2000) Biochemistry , vol.39 , pp. 11389-11398
    • Asagoshi, K.1    Odawara, H.2    Nakano, H.3    Miyano, T.4    Terato, H.5    Ohyama, Y.6    Seki, S.7    Ide, H.8
  • 73
    • 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., 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
  • 75
    • 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., Bond J.P. A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII. DNA Repair. 1:2002;517-529.
    • (2002) DNA Repair , vol.1 , pp. 517-529
    • Bandaru, V.1    Sunkara, S.2    Wallace, S.S.3    Bond, J.P.4
  • 76
    • 0026674158 scopus 로고
    • Inhibition of DNA polymerase activity by thymine hydrates
    • Ganguly T., Duker N.J. Inhibition of DNA polymerase activity by thymine hydrates. Mutat. Res. 293:1992;71-77.
    • (1992) Mutat. Res. , vol.293 , pp. 71-77
    • Ganguly, T.1    Duker, N.J.2
  • 77
    • 0030670509 scopus 로고    scopus 로고
    • -) catalyzed DNA polymerization by (5R)-5,6-dihydro-5-hydroxythymidine and structural analogue 5,6-dihydro-5-methylthymidine
    • -) catalyzed DNA polymerization by (5R)-5,6-dihydro-5- hydroxythymidine and structural analogue 5,6-dihydro-5-methylthymidine. Biochemistry. 36:1997;14071-14079.
    • (1997) Biochemistry , vol.36 , pp. 14071-14079
    • Greenberg, M.M.1    Matray, T.J.2
  • 78
    • 0033199511 scopus 로고    scopus 로고
    • The effects of 5R-5,6-dihydro-5-hydroxythymidine on duplex DNA stability and structure
    • Sambandam A., Greenberg M.M. The effects of 5R-5,6-dihydro-5- hydroxythymidine on duplex DNA stability and structure. Nucl. Acids Res. 27:1999;3597-3602.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 3597-3602
    • Sambandam, A.1    Greenberg, M.M.2
  • 79
    • 0027366974 scopus 로고
    • Substrate specificity of the Escherichia coli endonuclease III: Excision of thymine- and cytosine-derived lesions in DNA produced by radiation-generated free radicals
    • Dizdaroglu M., Laval J., Boiteux S. Substrate specificity of the Escherichia coli endonuclease III: excision of thymine- and cytosine-derived lesions in DNA produced by radiation-generated free radicals. Biochemistry. 32:1993;12105-12111.
    • (1993) Biochemistry , vol.32 , pp. 12105-12111
    • Dizdaroglu, M.1    Laval, J.2    Boiteux, S.3
  • 80
    • 0032511204 scopus 로고    scopus 로고
    • Gas chromatography-mass spectrometry with high-performance liquid chromatography prepurification for monitoring the endonuclease III-mediated excision of 5-hydroxy-5,6-dihydrothymine and 5,6-dihydrothymine from γ-irradiated DNA
    • D'Ham C., Ravanat J.-L., Cadet J. Gas chromatography-mass spectrometry with high-performance liquid chromatography prepurification for monitoring the endonuclease III-mediated excision of 5-hydroxy-5,6-dihydrothymine and 5,6-dihydrothymine from γ-irradiated DNA. J. Chromatogr. B: Biomed. Sci. Appl. 710:1998;67-74.
    • (1998) J. Chromatogr. B: Biomed. Sci. Appl. , vol.710 , pp. 67-74
    • D'Ham, C.1    Ravanat, J.-L.2    Cadet, J.3
  • 81
    • 0035833982 scopus 로고    scopus 로고
    • Substrate specificity and excision kinetics of Escherichia coli endonuclease VIII (Nei) for modified bases in DNA damaged by free radicals
    • Dizdaroglu M., Burgess S.M., Jaruga P., Hazra T.K., Rodriguez H., Lloyd R.S. Substrate specificity and excision kinetics of Escherichia coli endonuclease VIII (Nei) for modified bases in DNA damaged by free radicals. Biochemistry. 40:2001;12150-12156.
    • (2001) Biochemistry , vol.40 , pp. 12150-12156
    • Dizdaroglu, M.1    Burgess, S.M.2    Jaruga, P.3    Hazra, T.K.4    Rodriguez, H.5    Lloyd, R.S.6
  • 82
    • 0025333467 scopus 로고
    • Ultraviolet-induced thymine hydrates in DNA are excised by bacterial and human DNA glycosylase activities
    • Ganguly T., Weems K.M., Duker N.J. Ultraviolet-induced thymine hydrates in DNA are excised by bacterial and human DNA glycosylase activities. Biochemistry. 29:1990;7222-7228.
    • (1990) Biochemistry , vol.29 , pp. 7222-7228
    • Ganguly, T.1    Weems, K.M.2    Duker, N.J.3
  • 83
    • 0025834033 scopus 로고
    • Stability of DNA thymine hydrates
    • Ganguly T., Duker N.J. Stability of DNA thymine hydrates. Nucl. Acids Res. 19:1991;3319-3323.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 3319-3323
    • Ganguly, T.1    Duker, N.J.2
  • 85
    • 0032568654 scopus 로고    scopus 로고
    • The ring fragmentation product of thymidine C5-hydrate when present in DNA is repaired by the Escherichia coli Fpg and Nth proteins
    • Jurado J., Saparbaev M., Matray T.J., Greenberg M.M., Laval J. The ring fragmentation product of thymidine C5-hydrate when present in DNA is repaired by the Escherichia coli Fpg and Nth proteins. Biochemistry. 37:1998;7757-7763.
    • (1998) Biochemistry , vol.37 , pp. 7757-7763
    • Jurado, J.1    Saparbaev, M.2    Matray, T.J.3    Greenberg, M.M.4    Laval, J.5
  • 86
    • 0034700315 scopus 로고    scopus 로고
    • AlkA protein is the third Escherichia coli DNA repair protein excising a ring fragmentation product of thymine
    • Privezentzev C.V., Saparbaev M., Sambandam A., Greenberg M.M., Laval J. AlkA protein is the third Escherichia coli DNA repair protein excising a ring fragmentation product of thymine. Biochemistry. 39:2000;14263-14268.
    • (2000) Biochemistry , vol.39 , pp. 14263-14268
    • Privezentzev, C.V.1    Saparbaev, M.2    Sambandam, A.3    Greenberg, M.M.4    Laval, J.5
  • 87
    • 0033929846 scopus 로고    scopus 로고
    • Repair and coding properties of 5-hydroxy-5-methylhydantoin nucleosides inserted into DNA oligomers
    • Gasparutto D., Ait-Abbas M., Jaquinod M., Boiteux S., Cadet J. Repair and coding properties of 5-hydroxy-5-methylhydantoin nucleosides inserted into DNA oligomers. Chem. Res. Toxicol. 13:2000;575-584.
    • (2000) Chem. Res. Toxicol. , vol.13 , pp. 575-584
    • Gasparutto, D.1    Ait-Abbas, M.2    Jaquinod, M.3    Boiteux, S.4    Cadet, J.5
  • 89
    • 0023318603 scopus 로고
    • Radiation-induced DNA damage and its repair
    • Téoule R. Radiation-induced DNA damage and its repair. Int. J. Radiat. Biol. 51:1987;573-589.
    • (1987) Int. J. Radiat. Biol. , vol.51 , pp. 573-589
    • Téoule, R.1
  • 91
    • 0027182802 scopus 로고
    • Chemical synthesis and properties of an oligodeoxyribonucleotide containing a 2-deoxyribosylformamide residue
    • Shida T., Iwaori H., Arakawa M., Sekiguchi J. Chemical synthesis and properties of an oligodeoxyribonucleotide containing a 2-deoxyribosylformamide residue. Chem. Pharm. Bull. 41:1993;961-964.
    • (1993) Chem. Pharm. Bull. , vol.41 , pp. 961-964
    • Shida, T.1    Iwaori, H.2    Arakawa, M.3    Sekiguchi, J.4
  • 92
    • 0028291126 scopus 로고
    • Properties of DNA duplexes containing an abasic site: Effect of nucleotide residue of the opposite part of a 2-deoxyribosylformamide residue
    • Shida T., Arakawa M., Sekiguchi J. Properties of DNA duplexes containing an abasic site: effect of nucleotide residue of the opposite part of a 2-deoxyribosylformamide residue. Nucleos. Nucleot. 13:1994;1319-1326.
    • (1994) Nucleos. Nucleot. , vol.13 , pp. 1319-1326
    • Shida, T.1    Arakawa, M.2    Sekiguchi, J.3
  • 93
    • 0034624954 scopus 로고    scopus 로고
    • Solution structure by NMR and molecular dynamics of a duplex containing a guanine opposite a N-(2-deoxy-β-D-erythro-pentofuranosyl)formamide lesion
    • Maufrais C., Fazakerley G.V., Cadet J., Boulard Y. Solution structure by NMR and molecular dynamics of a duplex containing a guanine opposite a N-(2-deoxy-β-D-erythro-pentofuranosyl)formamide lesion. Biochemistry. 39:2000;5614-5621.
    • (2000) Biochemistry , vol.39 , pp. 5614-5621
    • Maufrais, C.1    Fazakerley, G.V.2    Cadet, J.3    Boulard, Y.4
  • 94
    • 0025943942 scopus 로고
    • Incorporation by chemical synthesis and characterization of deoxyribosylformylamine into DNA
    • Guy A., Duplaa A.-M., Ulrich J., Téoule R. Incorporation by chemical synthesis and characterization of deoxyribosylformylamine into DNA. Nucl. Acids Res. 19:1991;5815-5820.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 5815-5820
    • Guy, A.1    Duplaa, A.-M.2    Ulrich, J.3    Téoule, R.4
  • 95
    • 0034691679 scopus 로고    scopus 로고
    • Mutation spectra induced by replication of two vicinal oxidative DNA lesions in mammalian cells
    • Gentil A., Le Page F., Cadet J., Sarasin A. Mutation spectra induced by replication of two vicinal oxidative DNA lesions in mammalian cells. Mutat. Res. 452:2000;51-56.
    • (2000) Mutat. Res. , vol.452 , pp. 51-56
    • Gentil, A.1    Le Page, F.2    Cadet, J.3    Sarasin, A.4
  • 96
    • 0033557286 scopus 로고    scopus 로고
    • Synthesis and enzymatic processing of oligodeoxynucleotides containing tandem base damage
    • Bourdat A.-G., Gasparutto D., Cadet J. Synthesis and enzymatic processing of oligodeoxynucleotides containing tandem base damage. Nucl. Acids Res. 27:1999;1015-1024.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 1015-1024
    • Bourdat, A.-G.1    Gasparutto, D.2    Cadet, J.3
  • 98
    • 0034678995 scopus 로고    scopus 로고
    • Tandem base lesions are generated by hydroxyl radical within isolated DNA in aerated aqueous solution
    • Bourdat A.-G., Douki T., Frelon S., Gasparutto D., Cadet J. Tandem base lesions are generated by hydroxyl radical within isolated DNA in aerated aqueous solution. J. Am. Chem. Soc. 122:2000;4549-4556.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4549-4556
    • Bourdat, A.-G.1    Douki, T.2    Frelon, S.3    Gasparutto, D.4    Cadet, J.5
  • 101
    • 0036129039 scopus 로고    scopus 로고
    • DNA tandem lesions containing 8-oxo-7,8-dihydroguanine and formamido residues arise from intramolecular addition of thymine peroxyl radical to guanine
    • Douki T., Riviēre J., Cadet J. DNA tandem lesions containing 8-oxo-7,8-dihydroguanine and formamido residues arise from intramolecular addition of thymine peroxyl radical to guanine. Chem. Res. Toxicol. 15:2002;445-454.
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 445-454
    • Douki, T.1    Riviere, J.2    Cadet, J.3
  • 102
    • 0021115803 scopus 로고
    • Urea-DNA glycosylase in mammalian cells
    • Breimer L.H. Urea-DNA glycosylase in mammalian cells. Biochemistry. 22:1983;4192-4197.
    • (1983) Biochemistry , vol.22 , pp. 4192-4197
    • Breimer, L.H.1
  • 103
    • 0032570307 scopus 로고    scopus 로고
    • Solution structure of N-(2-deoxy-D-erythro-pentofuranosyl)urea frameshifts, one intrahelical and the other extrahelical, by nuclear magnetic resonance and molecular dynamics
    • Gervais V., Cognet J.A.H., Guy A., Cadet J., Tēoule R., Fazakerley G.V. Solution structure of N-(2-deoxy-D-erythro-pentofuranosyl)urea frameshifts, one intrahelical and the other extrahelical, by nuclear magnetic resonance and molecular dynamics. Biochemistry. 37:1998;1083-1093.
    • (1998) Biochemistry , vol.37 , pp. 1083-1093
    • Gervais, V.1    Cognet, J.A.H.2    Guy, A.3    Cadet, J.4    Teoule, R.5    Fazakerley, G.V.6
  • 104
    • 0028350136 scopus 로고
    • Pyrimidine ring fragmentation products. Effects of lesion structure and sequence context on mutagenesis
    • Maccabee M., Evans J.S., Glackin M.P., Hatahet Z., Wallace S.S. Pyrimidine ring fragmentation products. Effects of lesion structure and sequence context on mutagenesis. J. Mol. Biol. 236:1994;514-530.
    • (1994) J. Mol. Biol. , vol.236 , pp. 514-530
    • MacCabee, M.1    Evans, J.S.2    Glackin, M.P.3    Hatahet, Z.4    Wallace, S.S.5
  • 105
    • 0037154121 scopus 로고    scopus 로고
    • Oxidation of 7,8-dihydro-8-oxoguanine affords lesions that are potent sources of replication errors in vivo
    • Henderson P.T., Delaney J.C., Gu F., Tannenbaum S.R., Essigmann J.M. Oxidation of 7,8-dihydro-8-oxoguanine affords lesions that are potent sources of replication errors in vivo. Biochemistry. 41:2002;914-921.
    • (2002) Biochemistry , vol.41 , pp. 914-921
    • Henderson, P.T.1    Delaney, J.C.2    Gu, F.3    Tannenbaum, S.R.4    Essigmann, J.M.5
  • 106
    • 0019329947 scopus 로고
    • A DNA glycosylase from Escherichia coli that releases free urea from a polydeoxyribonucleotide containing fragments of base residues
    • Breimer L., Lindahl T. A DNA glycosylase from Escherichia coli that releases free urea from a polydeoxyribonucleotide containing fragments of base residues. Nucl. Acids Res. 8:1980;6199-6211.
    • (1980) Nucl. Acids Res. , vol.8 , pp. 6199-6211
    • Breimer, L.1    Lindahl, T.2
  • 108
    • 0010421759 scopus 로고
    • Exonuclease III recognizes urea residues in oxidized DNA
    • Kow Y.W., Wallace S.S. Exonuclease III recognizes urea residues in oxidized DNA. Proc. Natl. Acad. Sci. U.S.A. 82:1985;8354-8358.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 8354-8358
    • Kow, Y.W.1    Wallace, S.S.2
  • 109
    • 0028286268 scopus 로고
    • Purification and characterization of a novel deoxyinosine-specific enzyme, deoxyinosine 3′ endonuclease, from Escherichia coli
    • Yao M., Hatahet Z., Melamede R.J., Kow Y.W. Purification and characterization of a novel deoxyinosine-specific enzyme, deoxyinosine 3′ endonuclease, from Escherichia coli. J. Biol. Chem. 269:1994;16260-16268.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16260-16268
    • Yao, M.1    Hatahet, Z.2    Melamede, R.J.3    Kow, Y.W.4
  • 110
    • 0034721685 scopus 로고    scopus 로고
    • Chemical and biochemical properties of oligonucleotides that contain (5′S,6S)-cyclo-5,6-dihydro-2′-deoxyuridine and (5′S,6S)-cyclo- 5,6-dihydrothymidine, two main radiation-induced degradation products of pyrimidine 2′-deoxyribonucleosides
    • Muller E., Gasparutto D., Jaquinod M., Romieu A., Cadet J. Chemical and biochemical properties of oligonucleotides that contain (5′S,6S)-cyclo-5, 6-dihydro-2′-deoxyuridine and (5′S,6S)-cyclo-5,6-dihydrothymidine, two main radiation-induced degradation products of pyrimidine 2′-deoxyribonucleosides. Tetrahedron. 56:2000;8689-8701.
    • (2000) Tetrahedron , vol.56 , pp. 8689-8701
    • Muller, E.1    Gasparutto, D.2    Jaquinod, M.3    Romieu, A.4    Cadet, J.5
  • 111
    • 0006739604 scopus 로고
    • Ionizing radiation and tritium transmutation both cause formation of 5-hydroxymethyl-2′-deoxyuridine in cellular DNA
    • Teebor G.W., Frenkel K., Goldstein M.S. Ionizing radiation and tritium transmutation both cause formation of 5-hydroxymethyl-2′-deoxyuridine in cellular DNA. Proc. Natl. Acad. Sci. U.S.A. 81:1984;318-321.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 318-321
    • Teebor, G.W.1    Frenkel, K.2    Goldstein, M.S.3
  • 112
    • 0021931536 scopus 로고
    • Quantitative determination of the 5-(hydroxymethyl)uracil moiety in the DNA of γ-irradiated cells
    • Frenkel K., Cummings A., Solomon J., Cadet J., Steinberg J.J., Teebor G.W. Quantitative determination of the 5-(hydroxymethyl)uracil moiety in the DNA of γ-irradiated cells. Biochemistry. 24:1985;4527-4533.
    • (1985) Biochemistry , vol.24 , pp. 4527-4533
    • Frenkel, K.1    Cummings, A.2    Solomon, J.3    Cadet, J.4    Steinberg, J.J.5    Teebor, G.W.6
  • 113
    • 0023940833 scopus 로고
    • Metabolism, incorporation into DNA, and interactions with 1-β-D-arabinofuranosylcytosine of 5-hydroxymethyl-2′-deoxyuridine in human promyelocytic leukemia cells (HL-60)
    • Vilpo J.A., Vilpo L.M. Metabolism, incorporation into DNA, and interactions with 1-β-D-arabinofuranosylcytosine of 5-hydroxymethyl- 2′-deoxyuridine in human promyelocytic leukemia cells (HL-60). Cancer Res. 48:1988;3117-3122.
    • (1988) Cancer Res. , vol.48 , pp. 3117-3122
    • Vilpo, J.A.1    Vilpo, L.M.2
  • 114
    • 0001147412 scopus 로고
    • The new occurrence of a new pyrimidine base replacing thymine in a bacteriophage DNA: 5-hydroxymethyl uracil
    • Kallen R.G., Simon M., Marmur J. The new occurrence of a new pyrimidine base replacing thymine in a bacteriophage DNA: 5-hydroxymethyl uracil. J. Mol. Biol. 5:1962;248-250.
    • (1962) J. Mol. Biol. , vol.5 , pp. 248-250
    • Kallen, R.G.1    Simon, M.2    Marmur, J.3
  • 115
    • 0025737777 scopus 로고
    • Site directed substitution of 5-hydroxymethyluracil for thymine in replicating φ X-174am3 DNA via synthesis of 5-hydroxymethyl-2′- deoxyuridine-5′-triphosphate
    • Levy D.D., Teebor G.W. Site directed substitution of 5- hydroxymethyluracil for thymine in replicating φ X-174am3 DNA via synthesis of 5-hydroxymethyl-2′-deoxyuridine-5′-triphosphate. Nucl. Acids Res. 19:1991;3337-3343.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 3337-3343
    • Levy, D.D.1    Teebor, G.W.2
  • 116
    • 0035798827 scopus 로고    scopus 로고
    • 5-Formyluracil and its nucleoside derivatives confer toxicity and mutagenicity to mammalian cells by interfering with normal RNA and DNA metabolism
    • Klungland A., Paulsen R., Rolseth V., Yamada Y., Ueno Y., Wiik P., Matsuda A., Seeberg E., Bjelland S. 5-Formyluracil and its nucleoside derivatives confer toxicity and mutagenicity to mammalian cells by interfering with normal RNA and DNA metabolism. Toxicol. Lett. 119:2001;71-78.
    • (2001) Toxicol. Lett. , vol.119 , pp. 71-78
    • Klungland, A.1    Paulsen, R.2    Rolseth, V.3    Yamada, Y.4    Ueno, Y.5    Wiik, P.6    Matsuda, A.7    Seeberg, E.8    Bjelland, S.9
  • 117
    • 0022645241 scopus 로고
    • Comparison of the mutagenic activity of 5-hydroxymethyldeoxyuridine with 5-substituted 2′-deoxyuridine analogs in the Ames Salmonella/microsome test
    • Bilimoria M.H., Gupta S.V. Comparison of the mutagenic activity of 5-hydroxymethyldeoxyuridine with 5-substituted 2′-deoxyuridine analogs in the Ames Salmonella/microsome test. Mutat. Res. 169:1986;123-127.
    • (1986) Mutat. Res. , vol.169 , pp. 123-127
    • Bilimoria, M.H.1    Gupta, S.V.2
  • 118
    • 0023266255 scopus 로고
    • Genetic effects of 5-hydroxymethyl-2′-deoxyuridine, a product of ionizing radiation
    • Shirnamē-Morē L., Rossman T.G., Troll W., Teebor G.W., Frenkel K. Genetic effects of 5-hydroxymethyl-2′-deoxyuridine, a product of ionizing radiation. Mutat. Res. 178:1987;177-186.
    • (1987) Mutat. Res. , vol.178 , pp. 177-186
    • Shirname-More, L.1    Rossman, T.G.2    Troll, W.3    Teebor, G.W.4    Frenkel, K.5
  • 119
    • 0023684845 scopus 로고
    • Mutagenicity of 5-hydroxymethyl-2′-deoxyuridine to Chinese hamster cells
    • Boorstein R.J., Teebor G.W. Mutagenicity of 5-hydroxymethyl-2′- deoxyuridine to Chinese hamster cells. Cancer Res. 48:1988;5466-5470.
    • (1988) Cancer Res. , vol.48 , pp. 5466-5470
    • Boorstein, R.J.1    Teebor, G.W.2
  • 120
    • 0027257707 scopus 로고
    • Structures of base pairs with 5-(hydroxymethyl)-2′-deoxyuridine in DNA determined by NMR spectroscopy
    • Mellac S., Fazakerley G.V., Sowers L.C. Structures of base pairs with 5-(hydroxymethyl)-2′-deoxyuridine in DNA determined by NMR spectroscopy. Biochemistry. 32:1993;7779-7786.
    • (1993) Biochemistry , vol.32 , pp. 7779-7786
    • Mellac, S.1    Fazakerley, G.V.2    Sowers, L.C.3
  • 121
    • 0022538220 scopus 로고
    • Biochemical analysis of toxic effects of 5-hydroxymethyl-2′- deoxyuridine in mammalian cells
    • Kaufman E.R. Biochemical analysis of toxic effects of 5-hydroxymethyl-2′-deoxyuridine in mammalian cells. Somat. Cell Mol. Genet. 12:1986;501-512.
    • (1986) Somat. Cell Mol. Genet. , vol.12 , pp. 501-512
    • Kaufman, E.R.1
  • 122
    • 0026484396 scopus 로고
    • A mammalian cell line deficient in activity of the DNA repair enzyme 5-hydroxymethyluracil-DNA glycosylase is resistant to the toxic effects of the thymidine analog 5-hydroxymethyl-2′-deoxyuridine
    • Boorstein R.J., Chiu L.-N., Teebor G.W. A mammalian cell line deficient in activity of the DNA repair enzyme 5-hydroxymethyluracil-DNA glycosylase is resistant to the toxic effects of the thymidine analog 5-hydroxymethyl-2′- deoxyuridine. Mol. Cell. Biol. 12:1992;5536-5540.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5536-5540
    • Boorstein, R.J.1    Chiu, L.-N.2    Teebor, G.W.3
  • 123
    • 0037172798 scopus 로고    scopus 로고
    • Endogenous DNA lesions can inhibit the binding of the AP-1 (c-Jun) transcription factor
    • Rogstad D.K., Liu P., Burdzy A., Lin S.S., Sowers L.C. Endogenous DNA lesions can inhibit the binding of the AP-1 (c-Jun) transcription factor. Biochemistry. 41:2002;8093-8102.
    • (2002) Biochemistry , vol.41 , pp. 8093-8102
    • Rogstad, D.K.1    Liu, P.2    Burdzy, A.3    Lin, S.S.4    Sowers, L.C.5
  • 125
    • 0024332378 scopus 로고
    • Purification and characterization of 5-hydroxymethyluracil-DNA glycosylase from calf thymus. Its possible role in the maintenance of methylated cytosine residues
    • Cannon-Carlson S.V., Gokhale H., Teebor G.W. Purification and characterization of 5-hydroxymethyluracil-DNA glycosylase from calf thymus. Its possible role in the maintenance of methylated cytosine residues. J. Biol. Chem. 264:1989;13306-13312.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13306-13312
    • Cannon-Carlson, S.V.1    Gokhale, H.2    Teebor, G.W.3
  • 127
    • 18644363009 scopus 로고    scopus 로고
    • HUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup
    • Kavli B., Sundheim O., Akbari M., Otterlei M., Nilsen H., Skorpen F., Aas P.A., Hagen L., Krokan H.E., Slupphaug G. hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup. J. Biol. Chem. 277:2002;39926-39936.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39926-39936
    • Kavli, B.1    Sundheim, O.2    Akbari, M.3    Otterlei, M.4    Nilsen, H.5    Skorpen, F.6    Aas, P.A.7    Hagen, L.8    Krokan, H.E.9    Slupphaug, G.10
  • 128
    • 0037415368 scopus 로고    scopus 로고
    • Repair of the mutagenic DNA oxidation product, 5-formyluracil
    • Liu P., Burdzy A., Sowers L.C. Repair of the mutagenic DNA oxidation product, 5-formyluracil. DNA Repair. 2:2003;199-210.
    • (2003) DNA Repair , vol.2 , pp. 199-210
    • Liu, P.1    Burdzy, A.2    Sowers, L.C.3
  • 129
    • 0028045942 scopus 로고
    • DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the AlkA enzyme in Escherichia coli
    • Bjelland S., Birkeland N.-K., Benneche T., Volden G., Seeberg E. DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the AlkA enzyme in Escherichia coli. J. Biol. Chem. 269:1994;30489-30495.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30489-30495
    • Bjelland, S.1    Birkeland, N.-K.2    Benneche, T.3    Volden, G.4    Seeberg, E.5
  • 130
    • 0037743666 scopus 로고    scopus 로고
    • Mismatch uracil glycosylase from Escherichia coli: A general mismatch or a specific DNA glycosylase?
    • O'Neill R.J., Vorob'eva O.V., Shahbakhti H., Zmuda E., Bhagwat A.S., Baldwin G.S. Mismatch uracil glycosylase from Escherichia coli: a general mismatch or a specific DNA glycosylase? J. Biol. Chem. 278:2003;20526-20532.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20526-20532
    • O'Neill, R.J.1    Vorob'Eva, O.V.2    Shahbakhti, H.3    Zmuda, E.4    Bhagwat, A.S.5    Baldwin, G.S.6
  • 131
    • 0034687768 scopus 로고    scopus 로고
    • An unexpectedly high excision capacity for mispaired 5- hydroxymethyluracil in human cell extracts
    • Rusmintratip V., Sowers L.C. An unexpectedly high excision capacity for mispaired 5-hydroxymethyluracil in human cell extracts. Proc. Natl. Acad. Sci. U.S.A. 97:2000;14183-14187.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 14183-14187
    • Rusmintratip, V.1    Sowers, L.C.2
  • 132
    • 0037440695 scopus 로고    scopus 로고
    • Identification of high excision capacity for 5-hydroxymethyluracil mispaired with guanine in DNA of Escherichia coli MutM, Nei and Nth DNA glycosylases
    • Hori M., Yonei S., Sugiyama H., Kino K., Yamamoto K., Zhang Q.-M. Identification of high excision capacity for 5-hydroxymethyluracil mispaired with guanine in DNA of Escherichia coli MutM, Nei and Nth DNA glycosylases. Nucl. Acids Res. 31:2003;1191-1196.
    • (2003) Nucl. Acids Res. , vol.31 , pp. 1191-1196
    • Hori, M.1    Yonei, S.2    Sugiyama, H.3    Kino, K.4    Yamamoto, K.5    Zhang, Q.-M.6
  • 134
    • 0025220483 scopus 로고
    • 5-Formyldeoxyuridine: A new type of DNA damage induced by ionizing radiation and its mutagenicity to Salmonella strain TA102
    • Kasai H., Iida A., Yamaizumi Z., Nishimura S., Tanooka H. 5-Formyldeoxyuridine: a new type of DNA damage induced by ionizing radiation and its mutagenicity to Salmonella strain TA102. Mutat. Res. 243:1990;249-253.
    • (1990) Mutat. Res. , vol.243 , pp. 249-253
    • Kasai, H.1    Iida, A.2    Yamaizumi, Z.3    Nishimura, S.4    Tanooka, H.5
  • 135
    • 0030879145 scopus 로고    scopus 로고
    • Substrate and mispairing properties of 5-formyl-2′-deoxyuridine 5′-triphosphate assessed by in vitro DNA polymerase reactions
    • Yoshida M., Makino K., Morita H., Terato H., Ohyama Y., Ide H. Substrate and mispairing properties of 5-formyl-2′-deoxyuridine 5′- triphosphate assessed by in vitro DNA polymerase reactions. Nucl. Acids Res. 25:1997;1570-1577.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 1570-1577
    • Yoshida, M.1    Makino, K.2    Morita, H.3    Terato, H.4    Ohyama, Y.5    Ide, H.6
  • 136
    • 0035844134 scopus 로고    scopus 로고
    • Oxidation of thymine to 5-formyluracil in DNA promotes misincorporation of dGMP and subsequent elongation of a mismatched primer terminus by DNA polymerase
    • Masaoka A., Terato H., Kobayashi M., Ohyama Y., Ide H. Oxidation of thymine to 5-formyluracil in DNA promotes misincorporation of dGMP and subsequent elongation of a mismatched primer terminus by DNA polymerase. J. Biol. Chem. 276:2001;16501-16510.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16501-16510
    • Masaoka, A.1    Terato, H.2    Kobayashi, M.3    Ohyama, Y.4    Ide, H.5
  • 137
    • 0033609832 scopus 로고    scopus 로고
    • Enzymatic repair of 5-formyluracil. II. Mismatch formation between 5-formyluracil and guanine during DNA replication and its recognition by two proteins involved in base excision repair (AlkA) and mismatch repair (MutS)
    • Terato H., Masaoka A., Kobayashi M., Fukushima S., Ohyama Y., Yoshida M., Ide H. Enzymatic repair of 5-formyluracil. II. Mismatch formation between 5-formyluracil and guanine during DNA replication and its recognition by two proteins involved in base excision repair (AlkA) and mismatch repair (MutS). J. Biol. Chem. 274:1999;25144-25150.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25144-25150
    • Terato, H.1    Masaoka, A.2    Kobayashi, M.3    Fukushima, S.4    Ohyama, Y.5    Yoshida, M.6    Ide, H.7
  • 138
    • 0034176651 scopus 로고    scopus 로고
    • 2-Hydroxy-dATP is incorporated opposite G by Escherichia coli DNA polymerase III resulting in high mutagenicity
    • Kamiya H., Kasai H. 2-Hydroxy-dATP is incorporated opposite G by Escherichia coli DNA polymerase III resulting in high mutagenicity. Nucl. Acids Res. 28:2000;1640-1646.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 1640-1646
    • Kamiya, H.1    Kasai, H.2
  • 139
    • 0030791720 scopus 로고    scopus 로고
    • Replication of DNA templates containing 5-formyluracil, a major oxidative lesion of thymine in DNA
    • Zhang Q.-M., Sugiyama H., Miyabe I., Matsuda S., Saito I., Yonei S. Replication of DNA templates containing 5-formyluracil, a major oxidative lesion of thymine in DNA. Nucl. Acids Res. 25:1997;3969-3973.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3969-3973
    • Zhang, Q.-M.1    Sugiyama, H.2    Miyabe, I.3    Matsuda, S.4    Saito, I.5    Yonei, S.6
  • 140
    • 0032531758 scopus 로고    scopus 로고
    • The mutations induced by oxidatively damaged nucleotides, 5-formyl-dUTP and 5-hydroxy-dCTP, in Escherichia coli
    • Fujikawa K., Kamiya H., Kasai H. The mutations induced by oxidatively damaged nucleotides, 5-formyl-dUTP and 5-hydroxy-dCTP, in Escherichia coli. Nucl. Acids Res. 26:1998;4582-4587.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 4582-4587
    • Fujikawa, K.1    Kamiya, H.2    Kasai, H.3
  • 141
    • 0345549815 scopus 로고
    • A set of lacZ mutations in Escherichia coli that allow rapid detection of each of the six base substitutions
    • Cupples C.G., Miller J.H. A set of lacZ mutations in Escherichia coli that allow rapid detection of each of the six base substitutions. Proc. Natl. Acad. Sci. U.S.A. 86:1989;5345-5349.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5345-5349
    • Cupples, C.G.1    Miller, J.H.2
  • 142
    • 0035832365 scopus 로고    scopus 로고
    • Mutations induced by 5-formyl-2′-deoxyuridine in Escherichia coli include base substitutions that can arise from mispairs of 5-formyluracil with guanine, cytosine and thymine
    • Ånensen H., Provan F., Lian A.T., Reinertsen S.-H.H.S., Ueno Y., Matsuda A., Seeberg E., Bjelland S. Mutations induced by 5-formyl-2′- deoxyuridine in Escherichia coli include base substitutions that can arise from mispairs of 5-formyluracil with guanine, cytosine and thymine. Mutat. Res. 476:2001;99-107.
    • (2001) Mutat. Res. , vol.476 , pp. 99-107
    • Ånensen, H.1    Provan, F.2    Lian, A.T.3    Reinertsen, S.-H.H.S.4    Ueno, Y.5    Matsuda, A.6    Seeberg, E.7    Bjelland, S.8
  • 143
    • 0035863859 scopus 로고    scopus 로고
    • Induction of T → G and T → a transversions by 5-formyluracil in mammalian cells
    • Kamiya H., Murata-Kamiya N., Karino N., Ueno Y., Matsuda A., Kasai H. Induction of T → G and T → A transversions by 5-formyluracil in mammalian cells. Mutat. Res. 513:2002;213-222.
    • (2002) Mutat. Res. , vol.513 , pp. 213-222
    • Kamiya, H.1    Murata-Kamiya, N.2    Karino, N.3    Ueno, Y.4    Matsuda, A.5    Kasai, H.6
  • 144
    • 0030597970 scopus 로고    scopus 로고
    • A proposed mechanism for the mutagenicity of 5-formyluracil
    • Privat E.J., Sowers L.C. A proposed mechanism for the mutagenicity of 5-formyluracil. Mutat. Res. 354:1996;151-156.
    • (1996) Mutat. Res. , vol.354 , pp. 151-156
    • Privat, E.J.1    Sowers, L.C.2
  • 145
    • 0023790393 scopus 로고
    • Equilibrium between a wobble and ionized base pair formed between fluorouracil and guanine in DNA as studied by proton and fluorine NMR
    • Sowers L.C., Eritja R., Kaplan B., Goodman M.F., Fazakerley G.V. Equilibrium between a wobble and ionized base pair formed between fluorouracil and guanine in DNA as studied by proton and fluorine NMR. J. Biol. Chem. 263:1988;14794-14801.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14794-14801
    • Sowers, L.C.1    Eritja, R.2    Kaplan, B.3    Goodman, M.F.4    Fazakerley, G.V.5
  • 146
    • 0024565053 scopus 로고
    • Ionized and wobble base-pairing for bromouracil-guanine in equilibrium under physiological conditions. A nuclear magnetic resonance study on an oligonucleotide containing a bromouracil-guanine base-pair as a function of pH
    • Sowers L.C., Goodman M.F., Eritja R., Kaplan B., Fazakerley G.V. Ionized and wobble base-pairing for bromouracil-guanine in equilibrium under physiological conditions. A nuclear magnetic resonance study on an oligonucleotide containing a bromouracil-guanine base-pair as a function of pH. J. Mol. Biol. 205:1989;437-447.
    • (1989) J. Mol. Biol. , vol.205 , pp. 437-447
    • Sowers, L.C.1    Goodman, M.F.2    Eritja, R.3    Kaplan, B.4    Fazakerley, G.V.5
  • 148
    • 0037187794 scopus 로고    scopus 로고
    • Water mediated Dickerson-Drew-type crystal of DNA dodecamer containing 2′-deoxy-5-formyluridine
    • Tsunoda M., Kondo J., Karino N., Ueno Y., Matsuda A., Takenaka A. Water mediated Dickerson-Drew-type crystal of DNA dodecamer containing 2′-deoxy-5-formyluridine. Biophys. Chem. 95:2002;227-233.
    • (2002) Biophys. Chem. , vol.95 , pp. 227-233
    • Tsunoda, M.1    Kondo, J.2    Karino, N.3    Ueno, Y.4    Matsuda, A.5    Takenaka, A.6
  • 149
    • 0033609930 scopus 로고    scopus 로고
    • Enzymatic repair of 5-formyluracil. I. Excision of 5-formyluracil site-specifically incorporated into oligonucleotide substrates by AlkA protein (Escherichia coli 3-methyladenine DNA glycosylase II)
    • Masaoka A., Terato H., Kobayashi M., Honsho A., Ohyama Y., Ide H. Enzymatic repair of 5-formyluracil. I. Excision of 5-formyluracil site-specifically incorporated into oligonucleotide substrates by AlkA protein (Escherichia coli 3-methyladenine DNA glycosylase II). J. Biol. Chem. 274:1999;25136-25143.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25136-25143
    • Masaoka, A.1    Terato, H.2    Kobayashi, M.3    Honsho, A.4    Ohyama, Y.5    Ide, H.6
  • 150
    • 0034634691 scopus 로고    scopus 로고
    • Identification of repair enzymes for 5-formyluracil in DNA. Nth, Nei, and MutM proteins of Escherichia coli
    • Zhang Q.-M., Miyabe I., Matsumoto Y., Kino K., Sugiyama H., Yonei S. Identification of repair enzymes for 5-formyluracil in DNA. Nth, Nei, and MutM proteins of Escherichia coli. J. Biol. Chem. 275:2000;35471-35477.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35471-35477
    • Zhang, Q.-M.1    Miyabe, I.2    Matsumoto, Y.3    Kino, K.4    Sugiyama, H.5    Yonei, S.6
  • 152
    • 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., 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
  • 153
    • 0037509930 scopus 로고    scopus 로고
    • Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions
    • Masaoka A., Matsubara M., Hasegawa R., Tanaka T., Kurisu S., Terato H., Ohyama Y., Karino N., Matsuda A., Ide H. Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions. Biochemistry. 42:2003;5003-5012.
    • (2003) Biochemistry , vol.42 , pp. 5003-5012
    • Masaoka, A.1    Matsubara, M.2    Hasegawa, R.3    Tanaka, T.4    Kurisu, S.5    Terato, H.6    Ohyama, Y.7    Karino, N.8    Matsuda, A.9    Ide, H.10
  • 154
    • 0027967842 scopus 로고
    • Nucleosides and nucleotides. 131. Synthesis and properties of oligonucleotides containing 5-formyl-2′-deoxyuridine
    • Ono A., Okamoto T., Inada M., Nara H., Matsuda A. Nucleosides and nucleotides. 131. Synthesis and properties of oligonucleotides containing 5-formyl-2′-deoxyuridine. Chem. Pharm. Bull. (Tokyo). 42:1994;2231-2237.
    • (1994) Chem. Pharm. Bull. (Tokyo) , vol.42 , pp. 2231-2237
    • Ono, A.1    Okamoto, T.2    Inada, M.3    Nara, H.4    Matsuda, A.5
  • 155
    • 0029827166 scopus 로고    scopus 로고
    • Synthesis of oligonucleotides containing 5-carboxy-2′-deoxyuridine at defined sites
    • Berthod T., Pétillot Y., Guy A., Cadet J., Molko D. Synthesis of oligonucleotides containing 5-carboxy-2′-deoxyuridine at defined sites. J. Org. Chem. 61:1996;6075-6078.
    • (1996) J. Org. Chem. , vol.61 , pp. 6075-6078
    • Berthod, T.1    Pétillot, Y.2    Guy, A.3    Cadet, J.4    Molko, D.5
  • 156
    • 0027725120 scopus 로고
    • A non-heme iron protein with heme tendencies: An investigation of the substrate specificity of thymine hydroxylase
    • Thornburg L.D., Lai M.-T., Wishnok J.S., Stubbe J. A non-heme iron protein with heme tendencies: an investigation of the substrate specificity of thymine hydroxylase. Biochemistry. 32:1993;14023-14033.
    • (1993) Biochemistry , vol.32 , pp. 14023-14033
    • Thornburg, L.D.1    Lai, M.-T.2    Wishnok, J.S.3    Stubbe, J.4
  • 157
    • 0029812580 scopus 로고    scopus 로고
    • Oxidative damage to DNA constituents by iron-mediated Fenton reactions. The deoxycytidine family
    • Luo Y., Henle E.S., Linn S. Oxidative damage to DNA constituents by iron-mediated Fenton reactions. The deoxycytidine family. J. Biol. Chem. 271:1996;21167-21176.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21167-21176
    • Luo, Y.1    Henle, E.S.2    Linn, S.3
  • 158
    • 0022498726 scopus 로고
    • Formation of cytosine glycol and 5,6-dihydroxycytosine in deoxyribonucleic acid on treatment with osmium tetroxide
    • Dizdaroglu M., Holwitt E., Hagan M.P., Bcakely W.F. Formation of cytosine glycol and 5,6-dihydroxycytosine in deoxyribonucleic acid on treatment with osmium tetroxide. Biochem. J. 235:1986;531-536.
    • (1986) Biochem. J. , vol.235 , pp. 531-536
    • Dizdaroglu, M.1    Holwitt, E.2    Hagan, M.P.3    Bcakely, W.F.4
  • 159
    • 0033597782 scopus 로고    scopus 로고
    • 2′-Deoxycytidine glycols, a missing link in the free radical-mediated oxidation of DNA
    • Tremblay S., Douki T., Cadet J., Wagner J.R. 2′-Deoxycytidine glycols, a missing link in the free radical-mediated oxidation of DNA. J. Biol. Chem. 274:1999;20833-20838.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20833-20838
    • Tremblay, S.1    Douki, T.2    Cadet, J.3    Wagner, J.R.4
  • 161
    • 84914730814 scopus 로고
    • Acid hydrolysis of DNA. Analysis of modified bases after gamma: Irradiation
    • J. Broerse, G. Barendsen, H. Kal, A. van der Kogel (Eds.) Abstract A3.43, Martinus Nijhoff, Amsterdam
    • R. Téoule, A. Bonicel, N. Mariaggi, M. Polverelli, Acid hydrolysis of DNA. Analysis of modified bases after gamma: irradiation, in: J. Broerse, G. Barendsen, H. Kal, A. van der Kogel (Eds.), Proceedings of the Seventh International Congress on Radiation Research, Abstract A3.43, Martinus Nijhoff, Amsterdam, 1983.
    • (1983) Proceedings of the Seventh International Congress on Radiation Research
    • Téoule, R.1    Bonicel, A.2    Mariaggi, N.3    Polverelli, M.4
  • 162
    • 0032584107 scopus 로고    scopus 로고
    • Oxidized, deaminated cytosines are a source of C → T transitions in vivo
    • Kreutzer D.A., Essigmann J.M. Oxidized, deaminated cytosines are a source of C → T transitions in vivo. Proc. Natl. Acad. Sci. U.S.A. 95:1998;3578-3582.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3578-3582
    • Kreutzer, D.A.1    Essigmann, J.M.2
  • 163
    • 0032488631 scopus 로고    scopus 로고
    • Uracil glycol deoxynucleoside triphosphate is a better substrate for DNA polymerase I Klenow fragment than thymine glycol deoxynucleoside triphosphate
    • Purmal A.A., Bond J.P., Lyons B.A., Kow Y.W., Wallace S.S. Uracil glycol deoxynucleoside triphosphate is a better substrate for DNA polymerase I Klenow fragment than thymine glycol deoxynucleoside triphosphate. Biochemistry. 37:1998;330-338.
    • (1998) Biochemistry , vol.37 , pp. 330-338
    • Purmal, A.A.1    Bond, J.P.2    Lyons, B.A.3    Kow, Y.W.4    Wallace, S.S.5
  • 164
    • 0030061005 scopus 로고    scopus 로고
    • Excision of oxidative cytosine modifications from γ-irradiated DNA
    • Wagner J.R., Blount B.C., Weinfeld M. Excision of oxidative cytosine modifications from γ-irradiated DNA by Escherichia coli endonuclease III and human whole-cell extracts. Anal. Biochem. 233:1996;76-86.
    • (1996) Anal. Biochem. , vol.233 , pp. 76-86
    • Wagner, J.R.1    Blount, B.C.2    Weinfeld, M.3
  • 165
    • 0030793214 scopus 로고    scopus 로고
    • Kinetics of oxidized cytosine repair by endonuclease III of Escherichia coli
    • Wang D., Essigmann J.M. Kinetics of oxidized cytosine repair by endonuclease III of Escherichia coli. Biochemistry. 36:1997;8628-8633.
    • (1997) Biochemistry , vol.36 , pp. 8628-8633
    • Wang, D.1    Essigmann, J.M.2
  • 166
    • 0031307474 scopus 로고    scopus 로고
    • Incorporation of two deoxycytidine oxidation products into cellular DNA
    • Wagner J.R., Tremblay S., Gowans B., Hunting D.J. Incorporation of two deoxycytidine oxidation products into cellular DNA. Biochem. Cell Biol. 75:1997;377-381.
    • (1997) Biochem. Cell Biol. , vol.75 , pp. 377-381
    • Wagner, J.R.1    Tremblay, S.2    Gowans, B.3    Hunting, D.J.4
  • 167
    • 0028341311 scopus 로고
    • Major oxidative products of cytosine, 5-hydroxycytosine and 5-hydroxyuracil, exhibit sequence context-dependent mispairing in vitro
    • Purmal A.A., Kow Y.W., Wallace S.S. Major oxidative products of cytosine, 5-hydroxycytosine and 5-hydroxyuracil, exhibit sequence context-dependent mispairing in vitro. Nucl. Acids Res. 22:1994;72-78.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 72-78
    • Purmal, A.A.1    Kow, Y.W.2    Wallace, S.S.3
  • 168
    • 0027983621 scopus 로고
    • 5-Hydroxypyrimidine deoxynucleoside triphosphates are more efficiently incorporated into DNA by exonuclease-free Klenow fragment than 8-oxopurine deoxynucleoside triphosphates
    • Purmal A.A., Kow Y.W., Wallace S.S. 5-Hydroxypyrimidine deoxynucleoside triphosphates are more efficiently incorporated into DNA by exonuclease-free Klenow fragment than 8-oxopurine deoxynucleoside triphosphates. Nucl. Acids Res. 22:1994;3930-3935.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 3930-3935
    • Purmal, A.A.1    Kow, Y.W.2    Wallace, S.S.3
  • 169
    • 0028335058 scopus 로고
    • Reverse chemical mutagenesis: Identification of the mutagenic lesions resulting from reactive oxygen species-mediated damage to DNA
    • Feig D.I., Sowers L.C., Loeb L.A. Reverse chemical mutagenesis: identification of the mutagenic lesions resulting from reactive oxygen species-mediated damage to DNA. Proc. Natl. Acad. Sci. U.S.A. 91:1994;6609-6613.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 6609-6613
    • Feig, D.I.1    Sowers, L.C.2    Loeb, L.A.3
  • 170
    • 0035890302 scopus 로고    scopus 로고
    • Unique misinsertion specificity of polι may decrease the mutagenic potential of deaminated cytosines
    • Vaisman A., Woodgate R. Unique misinsertion specificity of polι may decrease the mutagenic potential of deaminated cytosines. EMBO J. 20:2001;6520-6529.
    • (2001) EMBO J. , vol.20 , pp. 6520-6529
    • Vaisman, A.1    Woodgate, R.2
  • 171
    • 0033605675 scopus 로고    scopus 로고
    • Induction of reversible complexes between eukaryotic DNA topoisomerase I and DNA-containing oxidative base damages. 7,8-Dihydro-8-oxoguanine and 5-hydroxycytosine
    • Pourquier P., Ueng L.-M., Fertala J., Wang D., Park H.-J., Essigmann J.M., Bjornsti M.-A., Pommier Y. Induction of reversible complexes between eukaryotic DNA topoisomerase I and DNA-containing oxidative base damages. 7,8-Dihydro-8-oxoguanine and 5-hydroxycytosine. J. Biol. Chem. 274:1999;8516-8523.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8516-8523
    • Pourquier, P.1    Ueng, L.-M.2    Fertala, J.3    Wang, D.4    Park, H.-J.5    Essigmann, J.M.6    Bjornsti, M.-A.7    Pommier, Y.8
  • 173
    • 0028305721 scopus 로고
    • New substrates for old enzymes. 5-Hydroxy-2′-deoxycytidine and 5-hydroxy-2′-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNA N-glycosylase
    • Hatahet Z., Kow Y.W., Purmal A.A., Cunningham R.P., Wallace S.S. New substrates for old enzymes. 5-Hydroxy-2′-deoxycytidine and 5-hydroxy-2′-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNA N-glycosylase. J. Biol. Chem. 269:1994;18814-18820.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18814-18820
    • Hatahet, Z.1    Kow, Y.W.2    Purmal, A.A.3    Cunningham, R.P.4    Wallace, S.S.5
  • 175
    • 0037112668 scopus 로고    scopus 로고
    • Human DNA glycosylases of the bacterial Fpg/MutM superfamily: An alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA
    • Morland I., Rolseth V., Luna L., Rognes T., Bjørås M., Seeberg E. Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA. Nucl. Acids Res. 30:2002;4926-4936.
    • (2002) Nucl. Acids Res. , vol.30 , pp. 4926-4936
    • Morland, I.1    Rolseth, V.2    Luna, L.3    Rognes, T.4    Bjørås, M.5    Seeberg, E.6
  • 177
    • 0033178917 scopus 로고    scopus 로고
    • Repair of oxidative DNA base lesions induced by fluorescent light is defective in xeroderma pigmentosum group a cells
    • Lipinski L.J., Hoehr N., Mazur S.J., Dianov G.L., Sentürker S., Dizdaroglu M., Bohr V.A. Repair of oxidative DNA base lesions induced by fluorescent light is defective in xeroderma pigmentosum group A cells. Nucl. Acids Res. 27:1999;3153-3158.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 3153-3158
    • Lipinski, L.J.1    Hoehr, N.2    Mazur, S.J.3    Dianov, G.L.4    Sentürker, S.5    Dizdaroglu, M.6    Bohr, V.A.7
  • 179
    • 0033579106 scopus 로고    scopus 로고
    • The mutagenic damaged DNA base, 5,6-dihydrouracil (DHU), incorporated into a 14-mer duplex: NMR evidence that DHU is intrahelical and causes minimal DNA distortion
    • Villanueva J.M., Pohl J., Doetsch P.W., Marzilli L.G. The mutagenic damaged DNA base, 5,6-dihydrouracil (DHU), incorporated into a 14-mer duplex: NMR evidence that DHU is intrahelical and causes minimal DNA distortion. J. Am. Chem. Soc. 121:1999;10652-10653.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10652-10653
    • Villanueva, J.M.1    Pohl, J.2    Doetsch, P.W.3    Marzilli, L.G.4
  • 180
    • 0028807735 scopus 로고
    • RNA polymerase bypass at sites of dihydrouracil: Implications for transcriptional mutagenesis
    • Liu J., Zhou W., Doetsch P.W. RNA polymerase bypass at sites of dihydrouracil: implications for transcriptional mutagenesis. Mol. Cell. Biol. 15:1995;6729-6735.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6729-6735
    • Liu, J.1    Zhou, W.2    Doetsch, P.W.3
  • 181
    • 0032052252 scopus 로고    scopus 로고
    • Escherichia coli RNA and DNA polymerase bypass of dihydrouracil: Mutagenic potential via transcription and replication
    • Liu J., Doetsch P.W. Escherichia coli RNA and DNA polymerase bypass of dihydrouracil: mutagenic potential via transcription and replication. Nucl. Acids Res. 26:1998;1707-1712.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 1707-1712
    • Liu, J.1    Doetsch, P.W.2
  • 182
    • 0032555571 scopus 로고    scopus 로고
    • Purification and characterization of human hNTH1, 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., Mitra S. Purification and characterization of human hNTH1, 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
  • 183
    • 0035863849 scopus 로고    scopus 로고
    • Enzymatic processing of DNA containing tandem dihydrouracil by endonucleases III and VIII
    • Venkhataraman R., Donald C.D., Roy R., You H.J., Doetsch P.W., Kow Y.W. Enzymatic processing of DNA containing tandem dihydrouracil by endonucleases III and VIII. Nucl. Acids Res. 29:2001;407-414.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 407-414
    • Venkhataraman, R.1    Donald, C.D.2    Roy, R.3    You, H.J.4    Doetsch, P.W.5    Kow, Y.W.6
  • 184
    • 0034623063 scopus 로고    scopus 로고
    • Characterization of a novel 8-oxoguanine-DNA glycosylase activity in Escherichia coli and identification of the enzyme as endonuclease VIII
    • Hazra T.K., Izumi T., Venkataraman R., Kow Y.W., Dizdaroglu M., Mitra S. Characterization of a novel 8-oxoguanine-DNA glycosylase activity in Escherichia coli and identification of the enzyme as endonuclease VIII. J. Biol. Chem. 275:2000;27762-27767.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27762-27767
    • Hazra, T.K.1    Izumi, T.2    Venkataraman, R.3    Kow, Y.W.4    Dizdaroglu, M.5    Mitra, S.6
  • 185
    • 0001409610 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae possesses two functional homologues of Escherichia coli endonuclease III
    • You H.J., Swanson R.L., Doetsch P.W. Saccharomyces cerevisiae possesses two functional homologues of Escherichia coli endonuclease III. Biochemistry. 37:1998;6033-6040.
    • (1998) Biochemistry , vol.37 , pp. 6033-6040
    • You, H.J.1    Swanson, R.L.2    Doetsch, P.W.3
  • 186
    • 0033151820 scopus 로고    scopus 로고
    • Substrate specificity of ultraviolet DNA endonuclease (UVDE/Uve1p) from Schizosaccharomyces pombe
    • Avery A.M., Kaur B., Taylor J.-S., Mello J.A., Essigmann J.M., Doetsch P.W. Substrate specificity of ultraviolet DNA endonuclease (UVDE/Uve1p) from Schizosaccharomyces pombe. Nucl. Acids Res. 27:1999;2256-2264.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 2256-2264
    • Avery, A.M.1    Kaur, B.2    Taylor, J.-S.3    Mello, J.A.4    Essigmann, J.M.5    Doetsch, P.W.6
  • 187
    • 0025242512 scopus 로고
    • Formation and stability of repairable pyrimidine photohydrates in DNA
    • Boorstein R.J., Hilbert T.P., Cunningham R.P., Teebor G.W. Formation and stability of repairable pyrimidine photohydrates in DNA. Biochemistry. 29:1990;10455-10460.
    • (1990) Biochemistry , vol.29 , pp. 10455-10460
    • Boorstein, R.J.1    Hilbert, T.P.2    Cunningham, R.P.3    Teebor, G.W.4
  • 188
    • 0024328839 scopus 로고
    • UV-induced pyrimidine hydrates in DNA are repaired by bacterial and mammalian DNA glycosylase activities
    • Boorstein R.J., Hilbert T.P., Cadet J., Cunningham R.P., Teebor G.W. UV-induced pyrimidine hydrates in DNA are repaired by bacterial and mammalian DNA glycosylase activities. Biochemistry. 28:1989;6164-6170.
    • (1989) Biochemistry , vol.28 , pp. 6164-6170
    • Boorstein, R.J.1    Hilbert, T.P.2    Cadet, J.3    Cunningham, R.P.4    Teebor, G.W.5
  • 189
    • 0025335882 scopus 로고
    • Excision of cytosine hydrates from Z-DNA
    • Duker N.J., Weems K.M. Excision of cytosine hydrates from Z-DNA. Nucl. Acids Res. 18:1990;2007-2010.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 2007-2010
    • Duker, N.J.1    Weems, K.M.2
  • 190
    • 0034625109 scopus 로고    scopus 로고
    • Novel substrates of Escherichia coli Nth protein and its kinetics for excision of modified bases from DNA damaged by free radicals
    • Dizdaroglu M., Bauche C., Rodriguez H., Laval J. Novel substrates of Escherichia coli Nth protein and its kinetics for excision of modified bases from DNA damaged by free radicals. Biochemistry. 39:2000;5586-5592.
    • (2000) Biochemistry , vol.39 , pp. 5586-5592
    • Dizdaroglu, M.1    Bauche, C.2    Rodriguez, H.3    Laval, J.4
  • 191
    • 0024335402 scopus 로고
    • Iron ion-dependent modification of bases in DNA by the superoxide radical-generating system hypoxanthine/xanthine oxidase
    • Aruoma O.I., Halliwell B., Dizdaroglu M. Iron ion-dependent modification of bases in DNA by the superoxide radical-generating system hypoxanthine/ xanthine oxidase. J. Biol. Chem. 264:1989;13024-13028.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13024-13028
    • Aruoma, O.I.1    Halliwell, B.2    Dizdaroglu, M.3
  • 192
    • 0025160599 scopus 로고
    • Modification of DNA bases in mammalian chromatin by radiation-generated free radicals
    • Gajewski E., Rao G., Nackerdien Z., Dizdaroglu M. Modification of DNA bases in mammalian chromatin by radiation-generated free radicals. Biochemistry. 29:1990;7876-7882.
    • (1990) Biochemistry , vol.29 , pp. 7876-7882
    • Gajewski, E.1    Rao, G.2    Nackerdien, Z.3    Dizdaroglu, M.4
  • 193
    • 0029008994 scopus 로고
    • A novel activity of E. coli uracil DNA N-glycosylase. Excision of isodialuric acid (5,6-dihydroxyuracil), a major product of oxidative DNA damage, from DNA
    • Zastawny T.H., Doetsch P.W., Dizdaroglu M. A novel activity of E. coli uracil DNA N-glycosylase. Excision of isodialuric acid (5,6-dihydroxyuracil), a major product of oxidative DNA damage, from DNA. FEBS Lett. 364:1995;255-258.
    • (1995) FEBS Lett. , vol.364 , pp. 255-258
    • Zastawny, T.H.1    Doetsch, P.W.2    Dizdaroglu, M.3
  • 194
    • 0029960063 scopus 로고    scopus 로고
    • Novel activities of human uracil DNA N-glycosylase for cytosine-derived products of oxidative DNA damage
    • Dizdaroglu M., Karakaya A., Jaruga P., Slupphaug G., Krokan H.E. Novel activities of human uracil DNA N-glycosylase for cytosine-derived products of oxidative DNA damage. Nucl. Acids Res. 24:1996;418-422.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 418-422
    • Dizdaroglu, M.1    Karakaya, A.2    Jaruga, P.3    Slupphaug, G.4    Krokan, H.E.5
  • 196
    • 0019506587 scopus 로고
    • Environmental pollutant 5-chlorouracil is incorporated in mouse liver and testes DNA
    • Pal B.C., Cumming R.B., Walton M.F., Preston R.J. Environmental pollutant 5-chlorouracil is incorporated in mouse liver and testes DNA. Mutat. Res. 91:1981;395-401.
    • (1981) Mutat. Res. , vol.91 , pp. 395-401
    • Pal, B.C.1    Cumming, R.B.2    Walton, M.F.3    Preston, R.J.4
  • 197
    • 0003240684 scopus 로고
    • Effects of 5-halogenated uracils on the growth of Escherichia coli and their incorporation into deoxyribonucleic acids
    • Dunn D.B., Smith J.D. Effects of 5-halogenated uracils on the growth of Escherichia coli and their incorporation into deoxyribonucleic acids. Biochem. J. 67:1957;494-506.
    • (1957) Biochem. J. , vol.67 , pp. 494-506
    • Dunn, D.B.1    Smith, J.D.2
  • 198
    • 0000529869 scopus 로고
    • Production of bacteriophage mutants by a disturbance of deoxyribonucleic acid metabolism
    • Litman R.M., Pardee A.B. Production of bacteriophage mutants by a disturbance of deoxyribonucleic acid metabolism. Nature. 178:1956;529-531.
    • (1956) Nature , vol.178 , pp. 529-531
    • Litman, R.M.1    Pardee, A.B.2
  • 199
    • 0017053206 scopus 로고
    • 5-Halogenated uracil base analog mutagenesis
    • Walton M.F., Cumming R.B. 5-Halogenated uracil base analog mutagenesis. Mutat. Res. 38:1976;371.
    • (1976) Mutat. Res. , vol.38 , pp. 371
    • Walton, M.F.1    Cumming, R.B.2
  • 200
    • 0017080824 scopus 로고
    • Mutagenicity of 5-halodeoxyuridines to diploid human lymphoblasts
    • Penman B.W., Wong M., Thilly W.G. Mutagenicity of 5-halodeoxyuridines to diploid human lymphoblasts. Life Sci. 19:1976;563-568.
    • (1976) Life Sci. , vol.19 , pp. 563-568
    • Penman, B.W.1    Wong, M.2    Thilly, W.G.3
  • 201
    • 0041431231 scopus 로고
    • The genetic toxicology of 5-fluoropyrimidines and 5-chlorouracil
    • Morris S.M. The genetic toxicology of 5-fluoropyrimidines and 5-chlorouracil. Mutat. Res. 297:1993;39-51.
    • (1993) Mutat. Res. , vol.297 , pp. 39-51
    • Morris, S.M.1
  • 202
    • 0020540215 scopus 로고
    • Sister-chromatid exchanges and gene mutations are induced by the replication of 5-bromo- and 5-chloro-deoxyuridine substituted DNA
    • O'Neill J.P., Heartlein M.W., Preston R.J. Sister-chromatid exchanges and gene mutations are induced by the replication of 5-bromo- and 5-chloro-deoxyuridine substituted DNA. Mutat. Res. 109:1983;259-270.
    • (1983) Mutat. Res. , vol.109 , pp. 259-270
    • O'Neill, J.P.1    Heartlein, M.W.2    Preston, R.J.3
  • 203
    • 0021344012 scopus 로고
    • In vivo SCE analysis using bromodeoxyuridine, iododeoxyuridine, and chlorodeoxyuridine
    • DuFrain R.J., McFee A.F., Linkous S., Jennings C.J., Lowe K.W. In vivo SCE analysis using bromodeoxyuridine, iododeoxyuridine, and chlorodeoxyuridine. Mutat. Res. 139:1984;57-60.
    • (1984) Mutat. Res. , vol.139 , pp. 57-60
    • Dufrain, R.J.1    McFee, A.F.2    Linkous, S.3    Jennings, C.J.4    Lowe, K.W.5
  • 204
    • 0020060972 scopus 로고
    • The induction of specific-locus mutations and sister-chromatid exchanges by 5-bromo- and 5-chloro-deoxyuridine
    • Heartlein M.W., O'Neill J.P., Pal B.C., Preston R.J. The induction of specific-locus mutations and sister-chromatid exchanges by 5-bromo- and 5-chloro-deoxyuridine. Mutat. Res. 92:1982;411-416.
    • (1982) Mutat. Res. , vol.92 , pp. 411-416
    • Heartlein, M.W.1    O'Neill, J.P.2    Pal, B.C.3    Preston, R.J.4
  • 205
    • 0034689142 scopus 로고    scopus 로고
    • 5-Chloro-2′-deoxyuridine cytotoxicity results from base excision repair of uracil subsequent to thymidylate synthase inhibition
    • Brandon M.L., Mi L.-J., Chaung W., Teebor G., Boorstein R.J. 5-Chloro-2′-deoxyuridine cytotoxicity results from base excision repair of uracil subsequent to thymidylate synthase inhibition. Mutat. Res. 459:2000;161-169.
    • (2000) Mutat. Res. , vol.459 , pp. 161-169
    • Brandon, M.L.1    Mi, L.-J.2    Chaung, W.3    Teebor, G.4    Boorstein, R.J.5
  • 206
    • 0036667452 scopus 로고    scopus 로고
    • Substrate recognition by a family of uracil-DNA glycosylases: UNG, MUG, and TDG
    • Liu P., Burdzy A., Sowers L.C. Substrate recognition by a family of uracil-DNA glycosylases: UNG, MUG, and TDG. Chem. Res. Toxicol. 15:2002;1001-1009.
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 1001-1009
    • Liu, P.1    Burdzy, A.2    Sowers, L.C.3
  • 207
    • 0345570144 scopus 로고
    • Incorporation of halogenated pyrimidines into the deoxyribonucleic acids of Bacterium coli and its bacteriophages
    • Dunn D.B., Smith J.D. Incorporation of halogenated pyrimidines into the deoxyribonucleic acids of Bacterium coli and its bacteriophages. Nature. 174:1954;305-306.
    • (1954) Nature , vol.174 , pp. 305-306
    • Dunn, D.B.1    Smith, J.D.2
  • 208
    • 0035916312 scopus 로고    scopus 로고
    • The eosinophil peroxidase-hydrogen peroxide-bromide system of human eosinophils generates 5-bromouracil, a mutagenic thymine analogue
    • Henderson J.P., Byun J., Mueller D.M., Heinecke J.W. The eosinophil peroxidase-hydrogen peroxide-bromide system of human eosinophils generates 5-bromouracil, a mutagenic thymine analogue. Biochemistry. 40:2001;2052-2059.
    • (2001) Biochemistry , vol.40 , pp. 2052-2059
    • Henderson, J.P.1    Byun, J.2    Mueller, D.M.3    Heinecke, J.W.4
  • 209
    • 0035896545 scopus 로고    scopus 로고
    • Production of brominating intermediates by myeloperoxidase. A transhalogenation pathway for generating mutagenic nucleobases during inflammation
    • Henderson J.P., Byun J., Williams M.V., Mueller D.M., McCormick M.L., Heinecke J.W. Production of brominating intermediates by myeloperoxidase. A transhalogenation pathway for generating mutagenic nucleobases during inflammation. J. Biol. Chem. 276:2001;7867-7875.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7867-7875
    • Henderson, J.P.1    Byun, J.2    Williams, M.V.3    Mueller, D.M.4    McCormick, M.L.5    Heinecke, J.W.6
  • 210
    • 0000724686 scopus 로고
    • Enzymatic synthesis of deoxyribonucleic acid. X. Influence of bromouracil substitutions on replication
    • Trautner T.A., Swartz M.N., Kornberg A. Enzymatic synthesis of deoxyribonucleic acid. X. Influence of bromouracil substitutions on replication. Proc. Natl. Acad. Sci. U.S.A. 48:1962;449-455.
    • (1962) Proc. Natl. Acad. Sci. U.S.A. , vol.48 , pp. 449-455
    • Trautner, T.A.1    Swartz, M.N.2    Kornberg, A.3
  • 211
    • 0021161792 scopus 로고
    • The biochemical basis of 5-bromouracil-induced mutagenesis. Heteroduplex base mispairs involving bromouracil in G·C → A·T and A·T → G·C mutational pathways
    • Lasken R.S., Goodman M.F. The biochemical basis of 5-bromouracil-induced mutagenesis. Heteroduplex base mispairs involving bromouracil in. G·C → A·T and A·T → G·C mutational pathways J. Biol. Chem. 259:1984;11491-11495.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11491-11495
    • Lasken, R.S.1    Goodman, M.F.2
  • 212
    • 0023677160 scopus 로고
    • The role of deoxyribonucleotide metabolism in 5-bromo-2′- deoxyuridine mutagenesis in mammalian cells
    • Kaufman E.R. The role of deoxyribonucleotide metabolism in 5-bromo-2′-deoxyuridine mutagenesis in mammalian cells. Mutat. Res. 200:1988;149-155.
    • (1988) Mutat. Res. , vol.200 , pp. 149-155
    • Kaufman, E.R.1
  • 213
    • 0027297046 scopus 로고
    • Ionization of bromouracil and fluorouracil stimulates base mispairing frequencies with guanine
    • Yu H., Eritja R., Bloom L.B., Goodman M.F. Ionization of bromouracil and fluorouracil stimulates base mispairing frequencies with guanine. J. Biol. Chem. 268:1993;15935-15943.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15935-15943
    • Yu, H.1    Eritja, R.2    Bloom, L.B.3    Goodman, M.F.4
  • 214
    • 0015260909 scopus 로고
    • The mutagenicity to mammalian cells of pyrimidine nucleoside analogs
    • Huberman E., Heidelberger C. The mutagenicity to mammalian cells of pyrimidine nucleoside analogs. Mutat. Res. 14:1972;130-132.
    • (1972) Mutat. Res. , vol.14 , pp. 130-132
    • Huberman, E.1    Heidelberger, C.2
  • 215
    • 0022218248 scopus 로고
    • Reversion analysis of mutations induced by 5-bromodeoxyuridine mutagenesis in mammalian cells
    • Kaufman E.R. Reversion analysis of mutations induced by 5-bromodeoxyuridine mutagenesis in mammalian cells. Mol. Cell. Biol. 5:1985;3092-3096.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3092-3096
    • Kaufman, E.R.1
  • 216
    • 0345588030 scopus 로고
    • Bromodeoxyuridine mutagenesis in mammalian cells: Mutagenesis is independent of the amount of bromouracil in DNA
    • Kaufman E.R., Davidson R.L. Bromodeoxyuridine mutagenesis in mammalian cells: mutagenesis is independent of the amount of bromouracil in DNA. Proc. Natl. Acad. Sci. U.S.A. 75:1978;4982-4986.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 4982-4986
    • Kaufman, E.R.1    Davidson, R.L.2
  • 217
    • 0036903711 scopus 로고    scopus 로고
    • Chemical synthesis and biochemical properties of oligonucleotides that contain the (5′S,5S,6S)-5′,6-cyclo-5-hydroxy-5,6-dihydro-2′- deoxyuridine DNA lesion
    • Muller E., Gasparutto D., Cadet J. Chemical synthesis and biochemical properties of oligonucleotides that contain the (5′S,5S,6S)-5′,6- cyclo-5-hydroxy-5,6-dihydro-2′-deoxyuridine DNA lesion. Chembiochem. 3:2002;534-542.
    • (2002) Chembiochem. , vol.3 , pp. 534-542
    • Muller, E.1    Gasparutto, D.2    Cadet, J.3
  • 218
    • 0019318994 scopus 로고
    • DNA methylation and gene function
    • Razin A., Riggs A.D. DNA methylation and gene function. Science. 210:1980;604-610.
    • (1980) Science , vol.210 , pp. 604-610
    • Razin, A.1    Riggs, A.D.2
  • 219
    • 0027280881 scopus 로고
    • Methylation and imprinting: From host defense to gene regulation?
    • Barlow D.P. Methylation and imprinting: from host defense to gene regulation? Science. 260:1993;309-310.
    • (1993) Science , vol.260 , pp. 309-310
    • Barlow, D.P.1
  • 220
    • 0028013240 scopus 로고
    • The flip side of DNA methylation
    • Verdine G.L. The flip side of DNA methylation. Cell. 76:1994;197-200.
    • (1994) Cell , vol.76 , pp. 197-200
    • Verdine, G.L.1
  • 222
    • 0019410144 scopus 로고
    • Activation of the Epstein-Barr virus genome by 5-aza-cytidine in latently infected human lymphoid lines
    • Ben-Sasson S.A., Klein G. Activation of the Epstein-Barr virus genome by 5-aza-cytidine in latently infected human lymphoid lines. Int. J. Cancer. 28:1981;131-135.
    • (1981) Int. J. Cancer , vol.28 , pp. 131-135
    • Ben-Sasson, S.A.1    Klein, G.2
  • 223
    • 0020967602 scopus 로고
    • Incorporation of 5-substituted analogs of deoxycytidine into DNA of herpes simplex virus-infected or -transformed cells without deamination to the thymidine analog
    • Fox L., Dobersen M.J., Greer S. Incorporation of 5-substituted analogs of deoxycytidine into DNA of herpes simplex virus-infected or -transformed cells without deamination to the thymidine analog. Antimicrob. Agents Chemother. 23:1983;465-476.
    • (1983) Antimicrob. Agents Chemother. , vol.23 , pp. 465-476
    • Fox, L.1    Dobersen, M.J.2    Greer, S.3
  • 224
    • 0025411135 scopus 로고
    • Inactivation of the HIV LTR by DNA CpG methylation: Evidence for a role in latency
    • Bednarik D.P., Cook J.A., Pitha P.M. Inactivation of the HIV LTR by DNA CpG methylation: evidence for a role in latency. EMBO J. 9:1990;1157-1164.
    • (1990) EMBO J. , vol.9 , pp. 1157-1164
    • Bednarik, D.P.1    Cook, J.A.2    Pitha, P.M.3
  • 226
    • 0026785391 scopus 로고
    • Awakenings, ..., UV light and HIV gene activation
    • Wallace B.M., Lasker J.S. Awakenings, ..., UV light and HIV gene activation. Science. 257:1992;1211-1212.
    • (1992) Science , vol.257 , pp. 1211-1212
    • Wallace, B.M.1    Lasker, J.S.2
  • 227
    • 0025059896 scopus 로고
    • Selection against CpG dinucleotides in lentiviral genes: A possible role of methylation in regulation of viral expression
    • Shpaer E.G., Mullins J.I. Selection against CpG dinucleotides in lentiviral genes: a possible role of methylation in regulation of viral expression. Nucl. Acids Res. 18:1990;5793-5797.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 5793-5797
    • Shpaer, E.G.1    Mullins, J.I.2
  • 228
    • 0020493818 scopus 로고
    • Heat- and alkali-induced deamination of 5-methylcytosine and cytosine residues in DNA
    • Wang R.Y.-H., Kuo K.C., Gehrke C.W., Huang L.-H., Ehrlich M. Heat- and alkali-induced deamination of 5-methylcytosine and cytosine residues in DNA. Biochim. Biophys. Acta. 697:1982;371-377.
    • (1982) Biochim. Biophys. Acta , vol.697 , pp. 371-377
    • Wang, R.Y.-H.1    Kuo, K.C.2    Gehrke, C.W.3    Huang, L.-H.4    Ehrlich, M.5
  • 230
    • 0028049859 scopus 로고
    • Excision of ultraviolet-induced photoproducts of 5-methylcytosine from DNA
    • Vairapandi M., Duker N.J. Excision of ultraviolet-induced photoproducts of 5-methylcytosine from DNA. Mutat. Res. 315:1994;85-94.
    • (1994) Mutat. Res. , vol.315 , pp. 85-94
    • Vairapandi, M.1    Duker, N.J.2
  • 231
    • 0029151273 scopus 로고
    • Oxidative damage to 5-methylcytosine in DNA
    • Zuo S., Boorstein R.J., Teebor G.W. Oxidative damage to 5-methylcytosine in DNA. Nucl. Acids Res. 23:1995;3239-3243.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 3239-3243
    • Zuo, S.1    Boorstein, R.J.2    Teebor, G.W.3
  • 232
    • 0016227181 scopus 로고
    • Preliminary characterization of minor bases from DNA fractionation, with discussion on 5-chlorocytosine as artifact or naturally occurring base
    • Lis A.W., McLaughlin R.K., McLaughlin D.I. Preliminary characterization of minor bases from DNA fractionation, with discussion on 5-chlorocytosine as artifact or naturally occurring base. Physiol. Chem. Phys. 6:1974;527-536.
    • (1974) Physiol. Chem. Phys. , vol.6 , pp. 527-536
    • Lis, A.W.1    McLaughlin, R.K.2    McLaughlin, D.I.3
  • 233
    • 0026548505 scopus 로고
    • Enzymatic shot-gun 5′-phosphorylation and 3′-sister phosphate exchange: A two-dimensional thin-layer chromatographic technique to measure DNA deoxynucleotide modification
    • Steinberg J.J., Cajigas A., Brownlee M. Enzymatic shot-gun 5′-phosphorylation and 3′-sister phosphate exchange: a two-dimensional thin-layer chromatographic technique to measure DNA deoxynucleotide modification. J. Chromatogr. 574:1992;41-55.
    • (1992) J. Chromatogr. , vol.574 , pp. 41-55
    • Steinberg, J.J.1    Cajigas, A.2    Brownlee, M.3
  • 234
    • 0023910144 scopus 로고
    • 5-Hydroxymethylcytosine DNA glycosylase activity in mammalian tissue
    • Cannon S.V., Cummings A., Teebor G.W. 5-Hydroxymethylcytosine DNA glycosylase activity in mammalian tissue. Biochem. Biophys. Res. Commun. 151:1988;1173-1179.
    • (1988) Biochem. Biophys. Res. Commun. , vol.151 , pp. 1173-1179
    • Cannon, S.V.1    Cummings, A.2    Teebor, G.W.3
  • 235
    • 0030842443 scopus 로고    scopus 로고
    • Solid phase synthesis and restriction endonuclease cleavage of oligodeoxynucleotides containing 5-(hydroxymethyl)-cytosine
    • Tardy-Planechaud S., Fujimoto J., Lin S.S., Sowers L.C. Solid phase synthesis and restriction endonuclease cleavage of oligodeoxynucleotides containing 5-(hydroxymethyl)-cytosine. Nucl. Acids Res. 25:1997;553-558.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 553-558
    • Tardy-Planechaud, S.1    Fujimoto, J.2    Lin, S.S.3    Sowers, L.C.4
  • 236
    • 0001129080 scopus 로고
    • The bases of the nucleic acids of some bacterial and animal viruses: The occurrence of 5-hydroxymethylcytosine
    • Wyatt G.R., Cohen S.S. The bases of the nucleic acids of some bacterial and animal viruses: the occurrence of 5-hydroxymethylcytosine. Biochem. J. 55:1953;774-782.
    • (1953) Biochem. J. , vol.55 , pp. 774-782
    • Wyatt, G.R.1    Cohen, S.S.2
  • 237
    • 0033571236 scopus 로고    scopus 로고
    • Formation of 5-formyl-2′-deoxycytidine from 5-methyl-2′- deoxycytidine in duplex DNA by Fenton-type reactions and γ-irradiation
    • Murata-Kamiya N., Kamiya H., Karino N., Ueno Y., Kaji H., Matsuda A., Kasai H. Formation of 5-formyl-2′-deoxycytidine from 5-methyl-2′- deoxycytidine in duplex DNA by Fenton-type reactions and γ-irradiation. Nucl. Acids Res. 27:1999;4385-4390.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 4385-4390
    • Murata-Kamiya, N.1    Kamiya, H.2    Karino, N.3    Ueno, Y.4    Kaji, H.5    Matsuda, A.6    Kasai, H.7
  • 238
    • 0035875297 scopus 로고    scopus 로고
    • Synthesis and properties of oligonucleotides containing 5-formyl-2′-deoxycytidine: In vitro DNA polymerase reactions on DNA templates containing 5-formyl-2′-deoxycytidine
    • Karino N., Ueno Y., Matsuda A. Synthesis and properties of oligonucleotides containing 5-formyl-2′-deoxycytidine: in vitro DNA polymerase reactions on DNA templates containing 5-formyl-2′- deoxycytidine. Nucl. Acids Res. 29:2001;2456-2463.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 2456-2463
    • Karino, N.1    Ueno, Y.2    Matsuda, A.3
  • 239
    • 0035413691 scopus 로고    scopus 로고
    • DNA molecular electrostatic potential: Novel perspectives for the mechanism of action of anticancer drugs involving electron transfer and oxidative stress
    • Kovacic P., Wakelin L.P.G. DNA molecular electrostatic potential: novel perspectives for the mechanism of action of anticancer drugs involving electron transfer and oxidative stress. Anti-Cancer Drug Des. 16:2001;175-184.
    • (2001) Anti-Cancer Drug Des. , vol.16 , pp. 175-184
    • Kovacic, P.1    Wakelin, L.P.G.2
  • 240
    • 0029833916 scopus 로고    scopus 로고
    • Oxidative DNA damage through long-range electron transfer
    • Hall D.B., Holmlin R.E., Barton J.K. Oxidative DNA damage through long-range electron transfer. Nature. 382:1996;731-735.
    • (1996) Nature , vol.382 , pp. 731-735
    • Hall, D.B.1    Holmlin, R.E.2    Barton, J.K.3
  • 241
    • 0021769722 scopus 로고
    • Hydroxylation of deoxyguanosine at the C-8 position by ascorbic acid and other reducing agents
    • Kasai H., Nishimura S. Hydroxylation of deoxyguanosine at the C-8 position by ascorbic acid and other reducing agents. Nucl. Acids Res. 12:1984;2137-2145.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 2137-2145
    • Kasai, H.1    Nishimura, S.2
  • 242
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani S., Takeshita M., Grollman A.P. Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature. 349:1991;431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 243
    • 0025334691 scopus 로고
    • Mechanistic studies of ionizing radiation and oxidative mutagenesis: Genetic effects of a single 8-hydroxyguanine (7-hydro-8-oxoguanine) residue inserted at a unique site in a viral genome
    • Wood M.L., Dizdaroglu M., Gajewski E., Essigmann J.M. Mechanistic studies of ionizing radiation and oxidative mutagenesis: genetic effects of a single 8-hydroxyguanine (7-hydro-8-oxoguanine) residue inserted at a unique site in a viral genome. Biochemistry. 29:1990;7024-7032.
    • (1990) Biochemistry , vol.29 , pp. 7024-7032
    • Wood, M.L.1    Dizdaroglu, M.2    Gajewski, E.3    Essigmann, J.M.4
  • 244
    • 0025802822 scopus 로고
    • Site-specific mutagenesis using a gapped duplex vector: A study of translesion synthesis past 8-oxodeoxyguanosine in E. coli
    • Moriya M., Ou C., Bodepudi V., Johnson F., Takeshita M., Grollman A.P. Site-specific mutagenesis using a gapped duplex vector: a study of translesion synthesis past 8-oxodeoxyguanosine in E. coli. Mutat. Res. 254:1991;281-288.
    • (1991) Mutat. Res. , vol.254 , pp. 281-288
    • Moriya, M.1    Ou, C.2    Bodepudi, V.3    Johnson, F.4    Takeshita, M.5    Grollman, A.P.6
  • 245
    • 0026592966 scopus 로고
    • 8-Hydroxyguanine, an abundant form of oxidative DNA damage, causes G → T and a → C substitutions
    • Cheng K.C., Cahill D.S., Kasai H., Nishimura S., Loeb L.A. 8-Hydroxyguanine, an abundant form of oxidative DNA damage, causes G → T and A → C substitutions. J. Biol. Chem. 267:1992;166-172.
    • (1992) J. Biol. Chem. , vol.267 , pp. 166-172
    • Cheng, K.C.1    Cahill, D.S.2    Kasai, H.3    Nishimura, S.4    Loeb, L.A.5
  • 246
    • 0023647116 scopus 로고
    • Misreading of DNA templates containing 8-hydroxydeoxyguanosine at the modified base and at adjacent residues
    • Kuchino Y., Mori F., Kasai H., Inoue H., Iwai S., Miura K., Ohtsuka E., Nishimura S. Misreading of DNA templates containing 8-hydroxydeoxyguanosine at the modified base and at adjacent residues. Nature. 327:1987;77-79.
    • (1987) Nature , vol.327 , pp. 77-79
    • Kuchino, Y.1    Mori, F.2    Kasai, H.3    Inoue, H.4    Iwai, S.5    Miura, K.6    Ohtsuka, E.7    Nishimura, S.8
  • 247
    • 0030986238 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen promotes DNA synthesis past template lesions by mammalian DNA polymerase δ
    • Mozzherin D.J., Shibutani S., Tan C.-K., Downey K.M., Fisher P.A. Proliferating cell nuclear antigen promotes DNA synthesis past template lesions by mammalian DNA polymerase δ Proc. Natl. Acad. Sci. U.S.A. 94:1997;6126-6131.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6126-6131
    • Mozzherin, D.J.1    Shibutani, S.2    Tan, C.-K.3    Downey, K.M.4    Fisher, P.A.5
  • 248
    • 0035830851 scopus 로고    scopus 로고
    • Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase δ. Steady-state and pre-steady-state kinetic analysis
    • Einolf H.J., Guengerich F.P. Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase δ. Steady-state and pre-steady-state kinetic analysis. J. Biol. Chem. 276:2001;3764-3771.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3764-3771
    • Einolf, H.J.1    Guengerich, F.P.2
  • 251
    • 0037058976 scopus 로고    scopus 로고
    • Role of human DNA polymerase κ as an extender in translesion synthesis
    • Haracska L., Prakash L., Prakash S. Role of human DNA polymerase κ as an extender in translesion synthesis. Proc. Natl. Acad. Sci. U.S.A. 99:2002;16000-16005.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16000-16005
    • Haracska, L.1    Prakash, L.2    Prakash, S.3
  • 255
    • 0034425754 scopus 로고    scopus 로고
    • Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase η
    • Haracska L., Yu S.-L., Johnson R.E., Prakash L., Prakash S. Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase η Nat. Genet. 25:2000;458-461.
    • (2000) Nat. Genet. , vol.25 , pp. 458-461
    • Haracska, L.1    Yu, S.-L.2    Johnson, R.E.3    Prakash, L.4    Prakash, S.5
  • 256
    • 0037013287 scopus 로고    scopus 로고
    • Yeast Rev1 protein is a G template-specific DNA polymerase
    • Haracska L., Prakash S., Prakash L. Yeast Rev1 protein is a G template-specific DNA polymerase. J. Biol. Chem. 277:2002;15546-15551.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15546-15551
    • Haracska, L.1    Prakash, S.2    Prakash, L.3
  • 259
    • 0027399969 scopus 로고
    • Single-stranded shuttle phagemid for mutagenesis studies in mammalian cells: 8-oxoguanine in DNA induces targeted G·C → T·A transversions in simian kidney cells
    • Moriya M. Single-stranded shuttle phagemid for mutagenesis studies in mammalian cells: 8-oxoguanine in DNA induces targeted. G·C → T·A transversions in simian kidney cells Proc. Natl. Acad. Sci. U.S.A. 90:1993;1122-1126.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 1122-1126
    • Moriya, M.1
  • 260
    • 0028848633 scopus 로고
    • Mutagenicity of a unique 8-oxoguanine in a human Ha-ras sequence in mammalian cells
    • Le Page F., Margot A., Grollman A.P., Sarasin A., Gentil A. Mutagenicity of a unique 8-oxoguanine in a human Ha-ras sequence in mammalian cells. Carcinogenesis. 16:1995;2779-2784.
    • (1995) Carcinogenesis , vol.16 , pp. 2779-2784
    • Le Page, F.1    Margot, A.2    Grollman, A.P.3    Sarasin, A.4    Gentil, A.5
  • 261
    • 0026650584 scopus 로고
    • 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., Ohtsuka E. c-Ha-ras containing 8-hydroxyguanine at codon 12 induces point mutations at the modified and adjacent positions. Cancer Res. 52:1992;3483-3485.
    • (1992) Cancer Res. , vol.52 , pp. 3483-3485
    • Kamiya, H.1    Miura, K.2    Ishikawa, H.3    Inoue, H.4    Nishimura, S.5    Ohtsuka, E.6
  • 262
    • 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., 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. 16:1995;883-889.
    • (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
  • 263
    • 0028266940 scopus 로고
    • DNA replication fidelity with 8-oxodeoxyguanosine triphosphate
    • Pavlov Y.I., Minnick D.T., Izuta S., Kunkel T.A. DNA replication fidelity with 8-oxodeoxyguanosine triphosphate. Biochemistry. 33:1994;4695-4701.
    • (1994) Biochemistry , vol.33 , pp. 4695-4701
    • Pavlov, Y.I.1    Minnick, D.T.2    Izuta, S.3    Kunkel, T.A.4
  • 264
    • 0028566564 scopus 로고
    • The fidelity of the human leading and lagging strand DNA replication apparatus with 8-oxodeoxyguanosine triphosphate
    • Minnick D.T., Pavlov Y.I., Kunkel T.A. The fidelity of the human leading and lagging strand DNA replication apparatus with 8-oxodeoxyguanosine triphosphate. Nucl. Acids Res. 22:1994;5658-5664.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 5658-5664
    • Minnick, D.T.1    Pavlov, Y.I.2    Kunkel, T.A.3
  • 265
    • 0032565577 scopus 로고    scopus 로고
    • Mutagenicity and repair of oxidative DNA damage: Insights from studies using defined lesions
    • Wang D., Kreutzer D.A., Essigmann J.M. Mutagenicity and repair of oxidative DNA damage: insights from studies using defined lesions. Mutat. Res. 400:1998;99-115.
    • (1998) Mutat. Res. , vol.400 , pp. 99-115
    • Wang, D.1    Kreutzer, D.A.2    Essigmann, J.M.3
  • 266
    • 0034193242 scopus 로고    scopus 로고
    • Sensitivity of human type II topoisomerases to DNA damage: Stimulation of enzyme-mediated DNA cleavage by abasic, oxidized and alkylated lesions
    • Sabourin M., Osheroff N. Sensitivity of human type II topoisomerases to DNA damage: stimulation of enzyme-mediated DNA cleavage by abasic, oxidized and alkylated lesions. Nucl. Acids Res. 28:2000;1947-1954.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 1947-1954
    • Sabourin, M.1    Osheroff, N.2
  • 267
    • 0025909996 scopus 로고
    • Escherichia coli Fpg protein and UvrABC endonuclease repair DNA damage induced by methylene blue plus visible light in vivo and in vitro
    • Czeczot H., Tudek B., Lambert B., Laval J., Boiteux S. Escherichia coli Fpg protein and UvrABC endonuclease repair DNA damage induced by methylene blue plus visible light in vivo and in vitro. J. Bacteriol. 173:1991;3419-3424.
    • (1991) J. Bacteriol. , vol.173 , pp. 3419-3424
    • Czeczot, H.1    Tudek, B.2    Lambert, B.3    Laval, J.4    Boiteux, S.5
  • 268
    • 0026701365 scopus 로고
    • The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)
    • Michaels M.L., Miller J.H. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8- oxoguanine). J. Bacteriol. 174:1992;6321-6325.
    • (1992) J. Bacteriol. , vol.174 , pp. 6321-6325
    • Michaels, M.L.1    Miller, J.H.2
  • 269
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
    • Maki H., Sekiguchi M. MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature. 355:1992;273-275.
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 274
    • 0027250070 scopus 로고
    • Properties and biological functions of the NTH and FPG proteins of Escherichia coli: Two DNA glycosylases that repair oxidative damage in DNA
    • Boiteux S. Properties and biological functions of the NTH and FPG proteins of Escherichia coli: two DNA glycosylases that repair oxidative damage in DNA. J. Photochem. Photobiol. B: Biol. 19:1993;87-96.
    • (1993) J. Photochem. Photobiol. B: Biol. , vol.19 , pp. 87-96
    • Boiteux, S.1
  • 275
    • 0027328401 scopus 로고
    • Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins
    • Castaing B., Geiger A., Seliger H., Nehls P., Laval J., Zelwer C., Boiteux S. Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins. Nucl. Acids Res. 21:1993;2899-2905.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 2899-2905
    • Castaing, B.1    Geiger, A.2    Seliger, H.3    Nehls, P.4    Laval, J.5    Zelwer, C.6    Boiteux, S.7
  • 276
    • 0028942512 scopus 로고
    • Repair of oxidative DNA damage in Gram-positive bacteria: The Lactococcus lactis Fpg protein
    • Duwat P., de Oliveira R., Ehrlich S.D., Boiteux S. Repair of oxidative DNA damage in Gram-positive bacteria: the Lactococcus lactis Fpg protein. Microbiology. 141:1995;411-417.
    • (1995) Microbiology , vol.141 , pp. 411-417
    • Duwat, P.1    De Oliveira, R.2    Ehrlich, S.D.3    Boiteux, S.4
  • 277
    • 0034681444 scopus 로고    scopus 로고
    • Distinct repair activities of human 7,8-dihydro-8-oxoguanine DNA glycosylase and formamidopyrimidine DNA glycosylase for formamidopyrimidine and 7,8-dihydro-8-oxoguanine
    • Asagoshi K., Yamada T., Terato H., Ohyama Y., Monden Y., Arai T., Nishimura S., Aburatani H., Lindahl T., Ide H. Distinct repair activities of human 7,8-dihydro-8-oxoguanine DNA glycosylase and formamidopyrimidine DNA glycosylase for formamidopyrimidine and 7,8-dihydro-8-oxoguanine. J. Biol. Chem. 275:2000;4956-4964.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4956-4964
    • Asagoshi, K.1    Yamada, T.2    Terato, H.3    Ohyama, Y.4    Monden, Y.5    Arai, T.6    Nishimura, S.7    Aburatani, H.8    Lindahl, T.9    Ide, H.10
  • 278
    • 0026684849 scopus 로고
    • Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA
    • Michaels M.L., Cruz C., Grollman A.P., Miller J.H. Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA. Proc. Natl. Acad. Sci. U.S.A. 89:1992;7022-7025.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7022-7025
    • Michaels, M.L.1    Cruz, C.2    Grollman, A.P.3    Miller, J.H.4
  • 279
    • 0028825742 scopus 로고
    • DNA determinants and substrate specificities of Escherichia coli MutY
    • Lu A.-L., Tsai-Wu J.-J., Cillo J. DNA determinants and substrate specificities of Escherichia coli MutY. J. Biol. Chem. 270:1995;23582-23588.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23582-23588
    • Lu, A.-L.1    Tsai-Wu, J.-J.2    Cillo, J.3
  • 281
    • 0032531869 scopus 로고    scopus 로고
    • Escherichia coli MutY protein has a guanine-DNA glycosylase that acts on 7,8-dihydro-8-oxoguanine:guanine mispair to prevent spontaneous G:C → C:G transversions
    • Zhang Q.-M., Ishikawa N., Nakahara T., Yonei S. Escherichia coli MutY protein has a guanine-DNA glycosylase that acts on 7,8-dihydro-8-oxoguanine: guanine mispair to prevent spontaneous G:C → C:G transversions. Nucl. Acids Res. 26:1998;4669-4675.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 4669-4675
    • Zhang, Q.-M.1    Ishikawa, N.2    Nakahara, T.3    Yonei, S.4
  • 282
    • 0024110769 scopus 로고
    • MutM, a second mutator locus in Escherichia coli that generates G·C → T·A transversions
    • Cabrera M., Nghiem Y., Miller J.H. mutM, a second mutator locus in Escherichia coli that generates. G·C → T·A transversions J. Bacteriol. 170:1988;5405-5407.
    • (1988) J. Bacteriol. , vol.170 , pp. 5405-5407
    • Cabrera, M.1    Nghiem, Y.2    Miller, J.H.3
  • 283
    • 0023992806 scopus 로고
    • The mutY gene: A mutator locus in Escherichia coli that generates G·C → T·A transversions
    • Nghiem Y., Cabrera M., Cupples C.G., Miller J.H. The mutY gene: a mutator locus in Escherichia coli that generates. G·C → T·A transversions Proc. Natl. Acad. Sci. U.S.A. 85:1988;2709-2713.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 2709-2713
    • Nghiem, Y.1    Cabrera, M.2    Cupples, C.G.3    Miller, J.H.4
  • 284
    • 0013882288 scopus 로고
    • The unusual mutagenic specificity of an E. coli mutator gene
    • Yanofsky C., Cox E.C., Horn V. The unusual mutagenic specificity of an E. coli mutator gene. Proc. Natl. Acad. Sci. U.S.A. 55:1966;274-281.
    • (1966) Proc. Natl. Acad. Sci. U.S.A. , vol.55 , pp. 274-281
    • Yanofsky, C.1    Cox, E.C.2    Horn, V.3
  • 285
    • 0032742730 scopus 로고    scopus 로고
    • A novel role for Escherichia coli endonuclease VIII in prevention of spontaneous G → T transversions
    • Blaisdell J.O., Hatahet Z., Wallace S.S. A novel role for Escherichia coli endonuclease VIII in prevention of spontaneous G → T transversions. J. Bacteriol. 181:1999;6396-6402.
    • (1999) J. Bacteriol. , vol.181 , pp. 6396-6402
    • Blaisdell, J.O.1    Hatahet, Z.2    Wallace, S.S.3
  • 286
    • 0030220956 scopus 로고    scopus 로고
    • Cloning of a yeast 8-oxo-guanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily
    • Nash H.M., Bruner S.D., Schärer O.D., Kawate T., Addona T.A., Spooner E., Lane W.S., Verdine G.L. Cloning of a yeast 8-oxo-guanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily. Curr. Biol. 6:1996;968-980.
    • (1996) Curr. Biol. , vol.6 , pp. 968-980
    • Nash, H.M.1    Bruner, S.D.2    Schärer, O.D.3    Kawate, T.4    Addona, T.A.5    Spooner, E.6    Lane, W.S.7    Verdine, G.L.8
  • 287
    • 0029896229 scopus 로고    scopus 로고
    • Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine
    • van der Kemp P.Auffret, Thomas D., Barbey R., de Oliveira R., Boiteux S. Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8- oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine. Proc. Natl. Acad. Sci. U.S.A. 93:1996;5197-5202.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5197-5202
    • Van Der Kemp, P.A.1    Thomas, D.2    Barbey, R.3    De Oliveira, R.4    Boiteux, S.5
  • 288
    • 0030750215 scopus 로고    scopus 로고
    • The Ogg1 protein of Saccharomyces cerevisiae: A 7,8-dihydro-8-oxoguanine DNA glycosylase/AP lyase whose lysine 241 is a critical residue for catalytic activity
    • Girard P.-M., Guibourt N., Boiteux S. The Ogg1 protein of Saccharomyces cerevisiae: a 7,8-dihydro-8-oxoguanine DNA glycosylase/AP lyase whose lysine 241 is a critical residue for catalytic activity. Nucl. Acids Res. 25:1997;3204-3211.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3204-3211
    • Girard, P.-M.1    Guibourt, N.2    Boiteux, S.3
  • 289
    • 0031926508 scopus 로고    scopus 로고
    • Opposite base-dependent excision of 7,8-dihydro-8-oxoadenine by the Ogg1 protein of Saccharomyces cerevisiae
    • Girard P.M., D'Ham C., Cadet J., Boiteux S. Opposite base-dependent excision of 7,8-dihydro-8-oxoadenine by the Ogg1 protein of Saccharomyces cerevisiae. Carcinogenesis. 19:1998;1299-1305.
    • (1998) Carcinogenesis , vol.19 , pp. 1299-1305
    • Girard, P.M.1    D'Ham, C.2    Cadet, J.3    Boiteux, S.4
  • 290
    • 0030929349 scopus 로고    scopus 로고
    • Inactivation of OGG1 increases the incidence of G·C → T·A transversions in Saccharomyces cerevisiae: Evidence for endogenous oxidative damage to DNA in eukaryotic cells
    • Thomas D., Scot A.D., Barbey R., Padula M., Boiteux S. Inactivation of OGG1 increases the incidence of. G·C → T·A transversions in Saccharomyces cerevisiae: evidence for endogenous oxidative damage to DNA in eukaryotic cells Mol. Gen. Genet. 254:1997;171-178.
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 171-178
    • Thomas, D.1    Scot, A.D.2    Barbey, R.3    Padula, M.4    Boiteux, S.5
  • 291
    • 0032568337 scopus 로고    scopus 로고
    • Repair of oxidatively damaged guanine in Saccharomyces cerevisiae by an alternative pathway
    • Bruner S.D., Nash H.M., Lane W.S., Verdine G.L. Repair of oxidatively damaged guanine in Saccharomyces cerevisiae by an alternative pathway. Curr. Biol. 8:1998;393-403.
    • (1998) Curr. Biol. , vol.8 , pp. 393-403
    • Bruner, S.D.1    Nash, H.M.2    Lane, W.S.3    Verdine, G.L.4
  • 295
    • 0030703177 scopus 로고    scopus 로고
    • Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites
    • Bjørås M., Luna L., Johnsen B., Hoff E., Haug T., Rognes T., Seeberg E. Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites. EMBO J. 16:1997;6314-6322.
    • (1997) EMBO J. , vol.16 , pp. 6314-6322
    • Bjørås, M.1    Luna, L.2    Johnsen, B.3    Hoff, E.4    Haug, T.5    Rognes, T.6    Seeberg, E.7
  • 296
    • 0031172802 scopus 로고    scopus 로고
    • A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer
    • Lu R., Nash H.M., Verdine G.L. A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer. Curr. Biol. 7:1997;397-407.
    • (1997) Curr. Biol. , vol.7 , pp. 397-407
    • Lu, R.1    Nash, H.M.2    Verdine, G.L.3
  • 297
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae
    • Radicella J.P., Dherin C., Desmaze C., Fox M.S., Boiteux S. Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 94:1997;8010-8015.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8010-8015
    • Radicella, J.P.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.4    Boiteux, S.5
  • 299
  • 300
    • 0000240354 scopus 로고    scopus 로고
    • Rat 7,8-dihydro-8-oxoguanine DNA glycosylase: Substrate specificity, kinetics and cleavage mechanism at an apurinic site
    • Prieto Alamo M.J., Jurado J., Francastel E., Laval F. Rat 7,8-dihydro-8-oxoguanine DNA glycosylase: substrate specificity, kinetics and cleavage mechanism at an apurinic site. Nucl. Acids Res. 26:1998;5199-5202.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 5199-5202
    • Prieto Alamo, M.J.1    Jurado, J.2    Francastel, E.3    Laval, F.4
  • 301
    • 0032566764 scopus 로고    scopus 로고
    • Characterization of the recombinant MutY homolog, an adenine DNA glycosylase, from yeast Schizosaccharomyces pombe
    • Lu A.-L., Fawcett W.P. Characterization of the recombinant MutY homolog, an adenine DNA glycosylase, from yeast Schizosaccharomyces pombe. J. Biol. Chem. 273:1998;25098-25105.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25098-25105
    • Lu, A.-L.1    Fawcett, W.P.2
  • 302
    • 0032840464 scopus 로고    scopus 로고
    • Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein
    • Slupska M.M., Luther W.M., Chiang J.-H., Yang H., Miller J.H. Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein. J. Bacteriol. 181:1999;6210-6213.
    • (1999) J. Bacteriol. , vol.181 , pp. 6210-6213
    • Slupska, M.M.1    Luther, W.M.2    Chiang, J.-H.3    Yang, H.4    Miller, J.H.5
  • 303
    • 0034654256 scopus 로고    scopus 로고
    • Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria
    • Ohtsubo T., Nishioka K., Imaiso Y., Iwai S., Shimokawa H., Oda H., Fujiwara T., Nakabeppu Y. Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria. Nucl. Acids Res. 28:2000;1355-1364.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 1355-1364
    • Ohtsubo, T.1    Nishioka, K.2    Imaiso, Y.3    Iwai, S.4    Shimokawa, H.5    Oda, H.6    Fujiwara, T.7    Nakabeppu, Y.8
  • 304
    • 0027368923 scopus 로고
    • Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis
    • Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 268:1993;23524-23530.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23524-23530
    • Sakumi, K.1    Furuichi, M.2    Tsuzuki, T.3    Kakuma, T.4    Kawabata, S.5    Maki, H.6    Sekiguchi, M.7
  • 305
    • 0028858586 scopus 로고
    • Mouse MTH1 protein with 8-oxo-7,8-dihydro-2′-deoxyguanosine 5′-triphosphatase activity that prevents transversion mutation; CDNA cloning and tissue distribution
    • Kakuma T., Nishida J., Tsuzuki T., Sekiguchi M. Mouse MTH1 protein with 8-oxo-7,8-dihydro-2′-deoxyguanosine 5′-triphosphatase activity that prevents transversion mutation; cDNA cloning and tissue distribution. J. Biol. Chem. 270:1995;25942-25948.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25942-25948
    • Kakuma, T.1    Nishida, J.2    Tsuzuki, T.3    Sekiguchi, M.4
  • 306
    • 0033603344 scopus 로고    scopus 로고
    • The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
    • Fujikawa K., Kamiya H., Yakushiji H., Fujii Y., Nakabeppu Y., Kasai H. The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein. J. Biol. Chem. 274:1999;18201-18205.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18201-18205
    • Fujikawa, K.1    Kamiya, H.2    Yakushiji, H.3    Fujii, Y.4    Nakabeppu, Y.5    Kasai, H.6
  • 310
    • 0038449261 scopus 로고    scopus 로고
    • A novel mechanism for preventing mutations caused by oxidation of guanine nucleotides
    • Ishibashi T., Hayakawa H., Sekiguchi M. A novel mechanism for preventing mutations caused by oxidation of guanine nucleotides. EMBO Rep. 4:2003;479-483.
    • (2003) EMBO Rep. , vol.4 , pp. 479-483
    • Ishibashi, T.1    Hayakawa, H.2    Sekiguchi, M.3
  • 311
    • 0035393812 scopus 로고    scopus 로고
    • HMYH cell cycle-dependent expression, subcellular localization and association with replication foci: Evidence suggesting replication-coupled repair of adenine:8-oxoguanine mispairs
    • Boldogh I., Milligan D., Lee M.S., Bassett H., Lloyd R.S., McCullough A.K. hMYH cell cycle-dependent expression, subcellular localization and association with replication foci: evidence suggesting replication-coupled repair of adenine:8-oxoguanine mispairs. Nucl. Acids Res. 29:2001;2802-2809.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 2802-2809
    • Boldogh, I.1    Milligan, D.2    Lee, M.S.3    Bassett, H.4    Lloyd, R.S.5    McCullough, A.K.6
  • 313
    • 0027171181 scopus 로고
    • Evidence for two DNA repair enzymes for 8-hydroxyguanine (7,8-dihydro-8-oxoguanine) in human cells
    • Bessho T., Tano K., Kasai H., Ohtsuka E., Nishimura S. Evidence for two DNA repair enzymes for 8-hydroxyguanine (7,8-dihydro-8-oxoguanine) in human cells. J. Biol. Chem. 268:1993;19416-19421.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19416-19421
    • Bessho, T.1    Tano, K.2    Kasai, H.3    Ohtsuka, E.4    Nishimura, S.5
  • 316
    • 0031455583 scopus 로고    scopus 로고
    • Characterization and mechanism of action of Drosophila ribosomal protein S3 DNA glycosylase activity for the removal of oxidatively damaged DNA bases
    • Deutsch W.A., Yacoub A., Jaruga P., Zastawny T.H., Dizdaroglu M. Characterization and mechanism of action of Drosophila ribosomal protein S3 DNA glycosylase activity for the removal of oxidatively damaged DNA bases. J. Biol. Chem. 272:1997;32857-32860.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32857-32860
    • Deutsch, W.A.1    Yacoub, A.2    Jaruga, P.3    Zastawny, T.H.4    Dizdaroglu, M.5
  • 317
    • 0034556627 scopus 로고    scopus 로고
    • Repair of oxidative DNA damage in Drosophila melanogaster: Identification and characterization of dOgg1, a second DNA glycosylase activity for 8-hydroxyguanine and formamidopyrimidines
    • Dherin C., Dizdaroglu M., Doerflinger H., Boiteux S., Radicella J.P. Repair of oxidative DNA damage in Drosophila melanogaster: identification and characterization of dOgg1, a second DNA glycosylase activity for 8-hydroxyguanine and formamidopyrimidines. Nucl. Acids Res. 28:2000;4583-4592.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 4583-4592
    • Dherin, C.1    Dizdaroglu, M.2    Doerflinger, H.3    Boiteux, S.4    Radicella, J.P.5
  • 318
    • 0031796813 scopus 로고    scopus 로고
    • Molecular cloning of AtMMH, an Arabidopsis thaliana ortholog of the Escherichia coli mutM gene, and analysis of functional domains of its product
    • Ohtsubo T., Matsuda O., Iba K., Terashima I., Sekiguchi M., Nakabeppu Y. Molecular cloning of AtMMH, an Arabidopsis thaliana ortholog of the Escherichia coli mutM gene, and analysis of functional domains of its product. Mol. Gen. Genet. 259:1998;577-590.
    • (1998) Mol. Gen. Genet. , vol.259 , pp. 577-590
    • Ohtsubo, T.1    Matsuda, O.2    Iba, K.3    Terashima, I.4    Sekiguchi, M.5    Nakabeppu, Y.6
  • 319
    • 0035044549 scopus 로고    scopus 로고
    • A functional OGG1 homologue from Arabidopsis thaliana
    • Dany A.L., Tissier A. A functional OGG1 homologue from Arabidopsis thaliana. Mol. Genet. Genom. 265:2001;293-301.
    • (2001) Mol. Genet. Genom. , vol.265 , pp. 293-301
    • Dany, A.L.1    Tissier, A.2
  • 320
    • 0038939282 scopus 로고    scopus 로고
    • Substrate specificity of Deinococcus radiodurans Fpg protein
    • Sentürker S., Bauche C., Laval J., Dizdaroglu M. Substrate specificity of Deinococcus radiodurans Fpg protein. Biochemistry. 38:1999;9435-9439.
    • (1999) Biochemistry , vol.38 , pp. 9435-9439
    • Sentürker, S.1    Bauche, C.2    Laval, J.3    Dizdaroglu, M.4
  • 321
    • 0032519382 scopus 로고    scopus 로고
    • Thermostable repair enzyme for oxidative DNA damage from extremely thermophilic bacterium, Thermus thermophilus HB8
    • Mikawa T., Kato R., Sugahara M., Kuramitsu S. Thermostable repair enzyme for oxidative DNA damage from extremely thermophilic bacterium, Thermus thermophilus HB8. Nucl. Acids Res. 26:1998;903-910.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 903-910
    • Mikawa, T.1    Kato, R.2    Sugahara, M.3    Kuramitsu, S.4
  • 322
    • 0032698574 scopus 로고    scopus 로고
    • Characterization of an 8-oxoguanine DNA glycosylase from Methanococcus jannaschii
    • Gogos A., Clarke N.D. Characterization of an 8-oxoguanine DNA glycosylase from Methanococcus jannaschii. J. Biol. Chem. 274:1999;30447-30450.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30447-30450
    • Gogos, A.1    Clarke, N.D.2
  • 323
    • 0035850219 scopus 로고    scopus 로고
    • Repair activities of 8-oxoguanine DNA glycosylase from Archaeoglobus fulgidus, a hyperthermophilic archaeon
    • Chung J.H., Suh M.-J., Park Y.I., Tainer J.A., Han Y.S. Repair activities of 8-oxoguanine DNA glycosylase from Archaeoglobus fulgidus, a hyperthermophilic archaeon. Mutat. Res. 486:2001;99-111.
    • (2001) Mutat. Res. , vol.486 , pp. 99-111
    • Chung, J.H.1    Suh, M.-J.2    Park, Y.I.3    Tainer, J.A.4    Han, Y.S.5
  • 324
    • 0035339672 scopus 로고    scopus 로고
    • A functional interaction of Ku with Werner exonuclease facilitates digestion of damaged DNA
    • Orren D.K., Machwe A., Karmakar P., Piotrowski J., Cooper M.P., Bohr V.A. A functional interaction of Ku with Werner exonuclease facilitates digestion of damaged DNA. Nucl. Acids Res. 29:2001;1926-1934.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 1926-1934
    • Orren, D.K.1    MacHwe, A.2    Karmakar, P.3    Piotrowski, J.4    Cooper, M.P.5    Bohr, V.A.6
  • 325
    • 0032516880 scopus 로고    scopus 로고
    • Effects of nonbulky DNA base damages on Escherichia coli RNA polymerase-mediated elongation and promoter clearance
    • Viswanathan A., Doetsch P.W. Effects of nonbulky DNA base damages on Escherichia coli RNA polymerase-mediated elongation and promoter clearance. J. Biol. Chem. 273:1998;21276-21281.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21276-21281
    • Viswanathan, A.1    Doetsch, P.W.2
  • 326
    • 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., 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
  • 329
    • 0033178246 scopus 로고    scopus 로고
    • Effect of oxidative DNA damage in promoter elements on transcription factor binding
    • Ghosh R., Mitchell D.L. Effect of oxidative DNA damage in promoter elements on transcription factor binding. Nucl. Acids Res. 27:1999;3213-3218.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 3213-3218
    • Ghosh, R.1    Mitchell, D.L.2
  • 330
    • 0032831460 scopus 로고    scopus 로고
    • Effects of 8-oxo-7,8-dihydro-2′-deoxyguanosine on the binding of the transcription factor Sp1 to its cognate target DNA sequence (GC box)
    • Ramon O., Sauvaigo S., Gasparutto D., Faure P., Favier A., Cadet J. Effects of 8-oxo-7,8-dihydro-2′-deoxyguanosine on the binding of the transcription factor Sp1 to its cognate target DNA sequence (GC box). Free Radic. Res. 31:1999;217-229.
    • (1999) Free Radic. Res. , vol.31 , pp. 217-229
    • Ramon, O.1    Sauvaigo, S.2    Gasparutto, D.3    Faure, P.4    Favier, A.5    Cadet, J.6
  • 331
    • 0033024623 scopus 로고    scopus 로고
    • DNA damage in deoxynucleosides and oligonucleotides treated with peroxynitrite
    • Burney S., Niles J.C., Dedon P.C., Tannenbaum S.R. DNA damage in deoxynucleosides and oligonucleotides treated with peroxynitrite. Chem. Res. Toxicol. 12:1999;513-520.
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 513-520
    • Burney, S.1    Niles, J.C.2    Dedon, P.C.3    Tannenbaum, S.R.4
  • 333
    • 0033914329 scopus 로고    scopus 로고
    • Peroxynitrite-induced secondary oxidative lesions at guanine nucleobases: Chemical stability and recognition by the Fpg DNA repair enzyme
    • Tretyakova N.Y., Wishnok J.S., Tannenbaum S.R. Peroxynitrite-induced secondary oxidative lesions at guanine nucleobases: chemical stability and recognition by the Fpg DNA repair enzyme. Chem. Res. Toxicol. 13:2000;658-664.
    • (2000) Chem. Res. Toxicol. , vol.13 , pp. 658-664
    • Tretyakova, N.Y.1    Wishnok, J.S.2    Tannenbaum, S.R.3
  • 334
    • 0029990148 scopus 로고    scopus 로고
    • Photosensitized reaction of 8-oxo-7,8-dihydro-2′-deoxyguanosine: Identification of 1-(2-deoxy-β-D-erythro-pentofuranosyl)cyanuric acid as the major singlet oxygen oxidation product
    • Raoul S., Cadet J. Photosensitized reaction of 8-oxo-7,8-dihydro- 2′-deoxyguanosine: identification of 1-(2-deoxy-β-D-erythro- pentofuranosyl)cyanuric acid as the major singlet oxygen oxidation product. J. Am. Chem. Soc. 118:1996;1892-1898.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1892-1898
    • Raoul, S.1    Cadet, J.2
  • 335
    • 0032839543 scopus 로고    scopus 로고
    • Synthesis and biochemical properties of cyanuric acid nucleoside-containing DNA oligomers
    • Gasparutto D., Da Cruz S., Bourdat A.-G., Jaquinod M., Cadet J. Synthesis and biochemical properties of cyanuric acid nucleoside-containing DNA oligomers. Chem. Res. Toxicol. 12:1999;630-638.
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 630-638
    • Gasparutto, D.1    Da Cruz, S.2    Bourdat, A.-G.3    Jaquinod, M.4    Cadet, J.5
  • 337
    • 0035157221 scopus 로고    scopus 로고
    • Repair and mutagenic potential of oxaluric acid, a major product of singlet oxygen-mediated oxidation of 8-oxo-7,8-dihydroguanine
    • Duarte V., Gasparutto D., Jaquinod M., Ravanat J.-L., Cadet J. Repair and mutagenic potential of oxaluric acid, a major product of singlet oxygen-mediated oxidation of 8-oxo-7,8-dihydroguanine. Chem. Res. Toxicol. 14:2001;46-53.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 46-53
    • Duarte, V.1    Gasparutto, D.2    Jaquinod, M.3    Ravanat, J.-L.4    Cadet, J.5
  • 338
    • 0033555373 scopus 로고    scopus 로고
    • Insertion of dGMP and dAMP during in vitro DNA synthesis opposite an oxidized form of 7,8-dihydro-8-oxoguanine
    • Duarte V., Muller J.G., Burrows C.J. Insertion of dGMP and dAMP during in vitro DNA synthesis opposite an oxidized form of 7,8-dihydro-8-oxoguanine. Nucl. Acids Res. 27:1999;496-502.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 496-502
    • Duarte, V.1    Muller, J.G.2    Burrows, C.J.3
  • 339
    • 0034932109 scopus 로고    scopus 로고
    • Characterization of hydantoin products from one-electron oxidation of 8-oxo-7,8-dihydroguanosine in a nucleoside model
    • Luo W., Muller J.G., Rachlin E.M., Burrows C.J. Characterization of hydantoin products from one-electron oxidation of 8-oxo-7,8-dihydroguanosine in a nucleoside model. Chem. Res. Toxicol. 14:2001;927-938.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 927-938
    • Luo, W.1    Muller, J.G.2    Rachlin, E.M.3    Burrows, C.J.4
  • 340
    • 0034610403 scopus 로고    scopus 로고
    • Removal of hydantoin products of 8-oxoguanine oxidation by the Escherichia coli DNA repair enzyme, FPG
    • Leipold M.D., Muller J.G., Burrows C.J., David S.S. Removal of hydantoin products of 8-oxoguanine oxidation by the Escherichia coli DNA repair enzyme, FPG. Biochemistry. 39:2000;14984-14992.
    • (2000) Biochemistry , vol.39 , pp. 14984-14992
    • Leipold, M.D.1    Muller, J.G.2    Burrows, C.J.3    David, S.S.4
  • 341
    • 0035339684 scopus 로고    scopus 로고
    • Repair of hydantoins, one electron oxidation product of 8-oxoguanine, by DNA glycosylases of Escherichia coli
    • Hazra T.K., Muller J.G., Manuel R.C., Burrows C.J., Lloyd R.S., Mitra S. Repair of hydantoins, one electron oxidation product of 8-oxoguanine, by DNA glycosylases of Escherichia coli. Nucl. Acids Res. 29:2001;1967-1974.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 1967-1974
    • Hazra, T.K.1    Muller, J.G.2    Manuel, R.C.3    Burrows, C.J.4    Lloyd, R.S.5    Mitra, S.6
  • 342
    • 0037168491 scopus 로고    scopus 로고
    • In vitro nucleotide misinsertion opposite the oxidized guanosine lesions spiroiminodihydantoin and guanidinohydantoin and DNA synthesis past the lesions using Escherichia coli DNA polymerase I (Klenow fragment)
    • Kornyushyna O., Berges A.M., Muller J.G., Burrows C.J. In vitro nucleotide misinsertion opposite the oxidized guanosine lesions spiroiminodihydantoin and guanidinohydantoin and DNA synthesis past the lesions using Escherichia coli DNA polymerase I (Klenow fragment). Biochemistry. 41:2002;15304-15314.
    • (2002) Biochemistry , vol.41 , pp. 15304-15314
    • Kornyushyna, O.1    Berges, A.M.2    Muller, J.G.3    Burrows, C.J.4
  • 343
    • 0036802909 scopus 로고    scopus 로고
    • Structure and potential mutagenicity of new hydantoin products from guanosine and 8-oxo-7,8-dihydroguanine oxidation by transition metals
    • Burrows C.J., Muller J.G., Kornyushyna O., Luo W., Duarte V., Leipold M.D., David S.S. Structure and potential mutagenicity of new hydantoin products from guanosine and 8-oxo-7,8-dihydroguanine oxidation by transition metals. Environ. Health Perspect. 110(Suppl. 5):2002;713-717.
    • (2002) Environ. Health Perspect. , vol.110 , Issue.SUPPL. 5 , pp. 713-717
    • Burrows, C.J.1    Muller, J.G.2    Kornyushyna, O.3    Luo, W.4    Duarte, V.5    Leipold, M.D.6    David, S.S.7
  • 344
    • 0035039434 scopus 로고    scopus 로고
    • Possible cause of G·C → C·G transversion mutation by guanine oxidation product, imidazolone
    • Kino K., Sugiyama H. Possible cause of G·C → C·G transversion mutation by guanine oxidation product, imidazolone. Chem. Biol. 8:2001;369-378.
    • (2001) Chem. Biol. , vol.8 , pp. 369-378
    • Kino, K.1    Sugiyama, H.2
  • 345
    • 0032578191 scopus 로고    scopus 로고
    • Product analysis of GG-specific photooxidation of DNA via electron transfer: 2-aminoimidazolone as a major guanine oxidation product
    • Kino K., Saito I., Sugiyama H. Product analysis of GG-specific photooxidation of DNA via electron transfer: 2-aminoimidazolone as a major guanine oxidation product. J. Am. Chem. Soc. 120:1998;7373-7374.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7373-7374
    • Kino, K.1    Saito, I.2    Sugiyama, H.3
  • 346
    • 0033601092 scopus 로고    scopus 로고
    • 8-Methoxydeoxyguanosine as an effective precursor of 2-aminoimidazolone, a major guanine oxidation product in one-electron oxidation of DNA
    • Ikeda H., Saito I. 8-Methoxydeoxyguanosine as an effective precursor of 2-aminoimidazolone, a major guanine oxidation product in one-electron oxidation of DNA. J. Am. Chem. Soc. 121:1999;10836-10837.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10836-10837
    • Ikeda, H.1    Saito, I.2
  • 347
    • 0029960714 scopus 로고    scopus 로고
    • Photooxidation of 8-oxo-7,8-dihydro-2′-deoxyguanosine by thermally generated triplet-excited ketones from 3-(hydroxymethyl)-3,4,4-trimethyl-1,2- dioxetane and comparison with type I and type II photosensitizers
    • Adam W., Saha-Möller C.R., Schönberger A. Photooxidation of 8-oxo-7,8-dihydro-2′-deoxyguanosine by thermally generated triplet-excited ketones from 3-(hydroxymethyl)-3,4,4-trimethyl-1,2-dioxetane and comparison with type I and type II photosensitizers. J. Am. Chem. Soc. 118:1996;9233-9238.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9233-9238
    • Adam, W.1    Saha-Möller, C.R.2    Schönberger, A.3
  • 348
    • 0030010723 scopus 로고    scopus 로고
    • Peroxynitrite mediated oxidation of purine bases of nucleosides and isolated DNA
    • Douki T., Cadet J. Peroxynitrite mediated oxidation of purine bases of nucleosides and isolated DNA. Free Radic. Res. 24:1996;369-380.
    • (1996) Free Radic. Res. , vol.24 , pp. 369-380
    • Douki, T.1    Cadet, J.2
  • 350
    • 0034177417 scopus 로고    scopus 로고
    • In vitro DNA synthesis opposite oxazolone and repair of this DNA damage using modified oligonucleotides
    • Duarte V., Gasparutto D., Jaquinod M., Cadet J. In vitro DNA synthesis opposite oxazolone and repair of this DNA damage using modified oligonucleotides. Nucl. Acids Res. 28:2000;1555-1563.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 1555-1563
    • Duarte, V.1    Gasparutto, D.2    Jaquinod, M.3    Cadet, J.4
  • 351
    • 0024367977 scopus 로고
    • Damage to the bases in DNA induced by hydrogen peroxide and ferric ion chelates
    • Aruoma O.I., Halliwell B., Gajewski E., Dizdaroglu M. Damage to the bases in DNA induced by hydrogen peroxide and ferric ion chelates. J. Biol. Chem. 264:1989;20509-20512.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20509-20512
    • Aruoma, O.I.1    Halliwell, B.2    Gajewski, E.3    Dizdaroglu, M.4
  • 353
    • 0042527365 scopus 로고    scopus 로고
    • Repair of DNA containing fapy·dG and its β-C-nucleoside analogue by formamidopyrimidine DNA glycosylase and MutY
    • Wiederholt C.J., Delaney M.O., Pope M.A., David S.S., Greenberg M.M. Repair of DNA containing fapy·dG and its β-C-nucleoside analogue by formamidopyrimidine DNA glycosylase and MutY. Biochemistry. 42:2003;9755-9760.
    • (2003) Biochemistry , vol.42 , pp. 9755-9760
    • Wiederholt, C.J.1    Delaney, M.O.2    Pope, M.A.3    David, S.S.4    Greenberg, M.M.5
  • 354
    • 0026533905 scopus 로고
    • Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): Excision of purine lesions in DNA produced by ionizing radiation or photosensitization
    • Boiteux S., Gajewski E., Laval J., Dizdaroglu M. Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): excision of purine lesions in DNA produced by ionizing radiation or photosensitization. Biochemistry. 31:1992;106-110.
    • (1992) Biochemistry , vol.31 , pp. 106-110
    • Boiteux, S.1    Gajewski, E.2    Laval, J.3    Dizdaroglu, M.4
  • 355
  • 356
    • 0032029919 scopus 로고    scopus 로고
    • Substrate specificity of the Ogg1 protein of Saccharomyces cerevisiae: Excision of guanine lesions produced in DNA by ionizing radiation- or hydrogen peroxide/metal ion-generated free radicals
    • Karahalil B., Girard P.-M., Boiteux S., Dizdaroglu M. Substrate specificity of the Ogg1 protein of Saccharomyces cerevisiae: excision of guanine lesions produced in DNA by ionizing radiation- or hydrogen peroxide/metal ion-generated free radicals. Nucl. Acids Res. 26:1998;1228-1232.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 1228-1232
    • Karahalil, B.1    Girard, P.-M.2    Boiteux, S.3    Dizdaroglu, M.4
  • 358
    • 0028785105 scopus 로고
    • Formation of 8-nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination
    • Yermilov V., Rubio J., Ohshima H. Formation of 8-nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination. FEBS Lett. 376:1995;207-210.
    • (1995) FEBS Lett. , vol.376 , pp. 207-210
    • Yermilov, V.1    Rubio, J.2    Ohshima, H.3
  • 359
    • 0029979758 scopus 로고    scopus 로고
    • Base modification and strand breakage in isolated calf thymus DNA and in DNA from human skin epidermal keratinocytes exposed to peroxynitrite or 3-morpholinosydnonimine
    • Spencer J.P.E., Wong J., Jenner A., Aruoma O.I., Cross C.E., Halliwell B. Base modification and strand breakage in isolated calf thymus DNA and in DNA from human skin epidermal keratinocytes exposed to peroxynitrite or 3-morpholinosydnonimine. Chem. Res. Toxicol. 9:1996;1152-1158.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 1152-1158
    • Spencer, J.P.E.1    Wong, J.2    Jenner, A.3    Aruoma, O.I.4    Cross, C.E.5    Halliwell, B.6
  • 360
    • 0033596750 scopus 로고    scopus 로고
    • 8-Nitro-2′-deoxyguanosine, a specific marker of oxidation by reactive nitrogen species, is generated by the myeloperoxidase-hydrogen peroxide-nitrite system of activated human phagocytes
    • Byun J., Henderson J.P., Mueller D.M., Heinecke J.W. 8-Nitro-2′- deoxyguanosine, a specific marker of oxidation by reactive nitrogen species, is generated by the myeloperoxidase-hydrogen peroxide-nitrite system of activated human phagocytes. Biochemistry. 38:1999;2590-2600.
    • (1999) Biochemistry , vol.38 , pp. 2590-2600
    • Byun, J.1    Henderson, J.P.2    Mueller, D.M.3    Heinecke, J.W.4
  • 362
    • 0035341318 scopus 로고    scopus 로고
    • Gaseous nitric oxide-induced 8-nitroguanine formation in human lung fibroblast cells and cell-free DNA
    • Hsieh Y.-S., Wang H.-C., Tseng T.-H., Chang W.-C., Wang C.-J. Gaseous nitric oxide-induced 8-nitroguanine formation in human lung fibroblast cells and cell-free DNA. Toxicol. Appl. Pharmacol. 172:2001;210-216.
    • (2001) Toxicol. Appl. Pharmacol. , vol.172 , pp. 210-216
    • Hsieh, Y.-S.1    Wang, H.-C.2    Tseng, T.-H.3    Chang, W.-C.4    Wang, C.-J.5
  • 363
    • 0034997674 scopus 로고    scopus 로고
    • 8-Nitroxanthine, an adduct derived from 2′-deoxyguanosine or DNA reaction with nitryl chloride
    • Chen H.-J.C., Chen Y.-M., Wang T.-F., Wang K.-S., Shiea J. 8-Nitroxanthine, an adduct derived from 2′-deoxyguanosine or DNA reaction with nitryl chloride. Chem. Res. Toxicol. 14:2001;536-546.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 536-546
    • Chen, H.-J.C.1    Chen, Y.-M.2    Wang, T.-F.3    Wang, K.-S.4    Shiea, J.5
  • 364
    • 0037062625 scopus 로고    scopus 로고
    • Peroxynitrite-induced reactions of synthetic oligo 2′- deoxynucleotides and DNA containing guanine: Formation and stability of a 5-guanidino-4-nitroimidazole lesion
    • Gu F., Stillwell W.G., Wishnok J.S., Shallop A.J., Jones R.A., Tannenbaum S.R. Peroxynitrite-induced reactions of synthetic oligo 2′-deoxynucleotides and DNA containing guanine: formation and stability of a 5-guanidino-4-nitroimidazole lesion. Biochemistry. 41:2002;7508-7518.
    • (2002) Biochemistry , vol.41 , pp. 7508-7518
    • Gu, F.1    Stillwell, W.G.2    Wishnok, J.S.3    Shallop, A.J.4    Jones, R.A.5    Tannenbaum, S.R.6
  • 365
    • 0037133531 scopus 로고    scopus 로고
    • Mass spectrometric assays for the tandem lesion 8,5′-cyclo- 2′-deoxyguanosine in mammalian DNA
    • Jaruga P., Birincioglu M., Rodriguez H., Dizdaroglu M. Mass spectrometric assays for the tandem lesion 8,5′-cyclo-2′- deoxyguanosine in mammalian DNA. Biochemistry. 41:2002;3703-3711.
    • (2002) Biochemistry , vol.41 , pp. 3703-3711
    • Jaruga, P.1    Birincioglu, M.2    Rodriguez, H.3    Dizdaroglu, M.4
  • 366
    • 0022518370 scopus 로고
    • Free-radical-induced formation of an 8,5′-cyclo-2′- deoxyguanosine moiety in deoxyribonucleic acid
    • Dizdaroglu M. Free-radical-induced formation of an 8,5′-cyclo- 2′-deoxyguanosine moiety in deoxyribonucleic acid. Biochem. J. 238:1986;247-254.
    • (1986) Biochem. J. , vol.238 , pp. 247-254
    • Dizdaroglu, M.1
  • 367
    • 0023097587 scopus 로고
    • Ionizing-radiation-induced damage in the DNA of cultured human cells. Identification of 8,5-cyclo-2-deoxyguanosine
    • Dizdaroglu M., Dirksen M.-L., Jiang H., Robbins J.H. Ionizing-radiation- induced damage in the DNA of cultured human cells. Identification of 8,5-cyclo-2-deoxyguanosine. Biochem. J. 241:1987;929-932.
    • (1987) Biochem. J. , vol.241 , pp. 929-932
    • Dizdaroglu, M.1    Dirksen, M.-L.2    Jiang, H.3    Robbins, J.H.4
  • 368
    • 0034636004 scopus 로고    scopus 로고
    • Removal of oxygen free-radical-induced 5′,8-purine cyclodeoxynucleosides from DNA by the nucleotide excision-repair pathway in human cells
    • Kuraoka I., Bender C., Romieu A., Cadet J., Wood R.D., Lindahl T. Removal of oxygen free-radical-induced 5′,8-purine cyclodeoxynucleosides from DNA by the nucleotide excision-repair pathway in human cells. Proc. Natl. Acad. Sci. U.S.A. 97:2000;3832-3837.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3832-3837
    • Kuraoka, I.1    Bender, C.2    Romieu, A.3    Cadet, J.4    Wood, R.D.5    Lindahl, T.6
  • 370
    • 0018837482 scopus 로고
    • In vitro γ irradiation of DNA: Identification of radioinduced chemical modifications of the adenine moiety
    • Bonicel A., Mariaggi N., Hughes E., Téoule R. In vitro γ irradiation of DNA: identification of radioinduced chemical modifications of the adenine moiety. Radiat. Res. 83:1980;19-26.
    • (1980) Radiat. Res. , vol.83 , pp. 19-26
    • Bonicel, A.1    Mariaggi, N.2    Hughes, E.3    Téoule, R.4
  • 371
    • 0025906777 scopus 로고
    • Structure and in vitro replication of DNA templates containing 7,8-dihydro-8-oxoadenine
    • Guschlbauer W., Duplaa A.-M., Guy A., Téoule R., Fazakerley G.V. Structure and in vitro replication of DNA templates containing 7,8-dihydro-8-oxoadenine. Nucl. Acids Res. 19:1991;1753-1758.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 1753-1758
    • Guschlbauer, W.1    Duplaa, A.-M.2    Guy, A.3    Téoule, R.4    Fazakerley, G.V.5
  • 372
    • 0027160522 scopus 로고
    • Translesional synthesis on DNA templates containing 8-oxo-7,8- dihydrodeoxyadenosine
    • Shibutani S., Bodepudi V., Johnson F., Grollman A.P. Translesional synthesis on DNA templates containing 8-oxo-7,8-dihydrodeoxyadenosine. Biochemistry. 32:1993;4615-4621.
    • (1993) Biochemistry , vol.32 , pp. 4615-4621
    • Shibutani, S.1    Bodepudi, V.2    Johnson, F.3    Grollman, A.P.4
  • 374
    • 0026452281 scopus 로고
    • Genetic effects of oxidative DNA damage: Comparative mutagenesis of 7,8-dihydro-8-oxoguanine and 7,8-dihydro-8-oxoadenine in Escherichia coli
    • Wood M.L., Esteve A., Morningstar M.L., Kuziemko G.M., Essigmann J.M. Genetic effects of oxidative DNA damage: comparative mutagenesis of 7,8-dihydro-8-oxoguanine and 7,8-dihydro-8-oxoadenine in Escherichia coli. Nucl. Acids Res. 20:1992;6023-6032.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 6023-6032
    • Wood, M.L.1    Esteve, A.2    Morningstar, M.L.3    Kuziemko, G.M.4    Essigmann, J.M.5
  • 375
    • 0036155859 scopus 로고    scopus 로고
    • Influence of an 8-oxoadenine lesion on the structural and dynamic features of a 30-mer DNA fragment with and without a mismatch
    • Barone F., Cellai L., Giordano C., La Sala G., Mazzei F. Influence of an 8-oxoadenine lesion on the structural and dynamic features of a 30-mer DNA fragment with and without a mismatch. Int. J. Radiat. Biol. 78:2002;9-16.
    • (2002) Int. J. Radiat. Biol. , vol.78 , pp. 9-16
    • Barone, F.1    Cellai, L.2    Giordano, C.3    La Sala, G.4    Mazzei, F.5
  • 376
    • 0021084610 scopus 로고
    • A dose-response study on opening of imidazole ring of adenine in DNA by ionizing radiation
    • Chetsanga C.J., Grigorian C. A dose-response study on opening of imidazole ring of adenine in DNA by ionizing radiation. Int. J. Radiat. Biol. 44:1983;321-331.
    • (1983) Int. J. Radiat. Biol. , vol.44 , pp. 321-331
    • Chetsanga, C.J.1    Grigorian, C.2
  • 380
    • 0036494773 scopus 로고    scopus 로고
    • Fapy·dA induces nucleotide misincorporation translesionally by a DNA polymerase
    • Delaney M.O., Wiederholt C.J., Greenberg M.M. Fapy·dA induces nucleotide misincorporation translesionally by a DNA polymerase. Angew. Chem. Int. Ed. 41:2002;771-773.
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 771-773
    • Delaney, M.O.1    Wiederholt, C.J.2    Greenberg, M.M.3
  • 381
    • 0021769936 scopus 로고
    • Enzymatic excision from γ-irradiated polydeoxyribonucleotides of adenine residues whose imidazole rings have been ruptured
    • Breimer L.H. Enzymatic excision from γ-irradiated polydeoxyribonucleotides of adenine residues whose imidazole rings have been ruptured. Nucl. Acids Res. 12:1984;6359-6367.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 6359-6367
    • Breimer, L.H.1
  • 382
    • 0037207138 scopus 로고    scopus 로고
    • Interaction of DNA containing Fapy·dA or its C-nucleoside analogues with base excision repair enzymes. Implications for mutagenesis and enzyme inhibition
    • Wiederholt C.J., Delaney M.O., Greenberg M.M. Interaction of DNA containing Fapy·dA or its C-nucleoside analogues with base excision repair enzymes. Implications for mutagenesis and enzyme inhibition. Biochemistry. 41:2002;15838-15844.
    • (2002) Biochemistry , vol.41 , pp. 15838-15844
    • Wiederholt, C.J.1    Delaney, M.O.2    Greenberg, M.M.3
  • 383
    • 0030069384 scopus 로고    scopus 로고
    • A novel DNA N-glycosylase activity of E. coli T4 endonuclease V that excises 4,6-diamino-5-formamidopyrimidine from DNA, a UV-radiation- and hydroxyl radical-induced product of adenine
    • Dizdaroglu M., Zastawny T.H., Carmical J.R., Lloyd R.S. A novel DNA N-glycosylase activity of E. coli T4 endonuclease V that excises 4,6-diamino-5-formamidopyrimidine from DNA, a UV-radiation- and hydroxyl radical-induced product of adenine. Mutat. Res. 362:1996;1-8.
    • (1996) Mutat. Res. , vol.362 , pp. 1-8
    • Dizdaroglu, M.1    Zastawny, T.H.2    Carmical, J.R.3    Lloyd, R.S.4
  • 384
    • 0017198622 scopus 로고
    • Tautomerism of isoguanosine and solvent-induced keto-enol equilibrium
    • Sepiol J., Kazimierczuk Z., Shugar D. Tautomerism of isoguanosine and solvent-induced keto-enol equilibrium. Z. Naturforsch. 31:1976;361-370.
    • (1976) Z. Naturforsch. , vol.31 , pp. 361-370
    • Sepiol, J.1    Kazimierczuk, Z.2    Shugar, D.3
  • 385
    • 0026354762 scopus 로고
    • Nickel(II)- and cobalt(II)-dependent damage by hydrogen peroxide to the DNA bases in isolated human chromatin
    • Nackerdien Z., Kasprzak K.S., Rao G., Halliwell B., Dizdaroglu M. Nickel(II)- and cobalt(II)-dependent damage by hydrogen peroxide to the DNA bases in isolated human chromatin. Cancer Res. 51:1991;5837-5842.
    • (1991) Cancer Res. , vol.51 , pp. 5837-5842
    • Nackerdien, Z.1    Kasprzak, K.S.2    Rao, G.3    Halliwell, B.4    Dizdaroglu, M.5
  • 386
    • 0027136806 scopus 로고
    • DNA base damage generated in vivo in hepatic chromatin of mice upon whole body γ-irradiation
    • Mori T., Hori Y., Dizdaroglu M. DNA base damage generated in vivo in hepatic chromatin of mice upon whole body γ-irradiation. Int. J. Radiat. Biol. 64:1993;645-650.
    • (1993) Int. J. Radiat. Biol. , vol.64 , pp. 645-650
    • Mori, T.1    Hori, Y.2    Dizdaroglu, M.3
  • 387
    • 0029133347 scopus 로고
    • Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation
    • Kamiya H., Kasai H. Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation. J. Biol. Chem. 270:1995;19446-19450.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19446-19450
    • Kamiya, H.1    Kasai, H.2
  • 388
    • 0034622582 scopus 로고    scopus 로고
    • Two DNA polymerases of Escherichia coli display distinct misinsertion specificities for 2-hydroxy-dATP during DNA synthesis
    • Kamiya H., Maki H., Kasai H. Two DNA polymerases of Escherichia coli display distinct misinsertion specificities for 2-hydroxy-dATP during DNA synthesis. Biochemistry. 39:2000;9508-9513.
    • (2000) Biochemistry , vol.39 , pp. 9508-9513
    • Kamiya, H.1    Maki, H.2    Kasai, H.3
  • 389
    • 0028929892 scopus 로고
    • Misincorporation of dAMP opposite 2-hydroxyadenine, an oxidative form of adenine
    • Kamiya H., Ueda T., Ohgi T., Matsukage A., Kasai H. Misincorporation of dAMP opposite 2-hydroxyadenine, an oxidative form of adenine. Nucl. Acids Res. 23:1995;761-766.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 761-766
    • Kamiya, H.1    Ueda, T.2    Ohgi, T.3    Matsukage, A.4    Kasai, H.5
  • 390
    • 0030570568 scopus 로고    scopus 로고
    • Effects of sequence contexts on misincorporation of nucleotides opposite 2-hydroxyadenine
    • Kamiya H., Kasai H. Effects of sequence contexts on misincorporation of nucleotides opposite 2-hydroxyadenine. FEBS Lett. 391:1996;113-116.
    • (1996) FEBS Lett. , vol.391 , pp. 113-116
    • Kamiya, H.1    Kasai, H.2
  • 391
    • 0040162339 scopus 로고    scopus 로고
    • 2-Hydroxyadenine in DNA is a very poor substrate of the Escherichia coli MutY protein
    • Kamiya H., Kasai H. 2-Hydroxyadenine in DNA is a very poor substrate of the Escherichia coli MutY protein. J. Radiat. Res. (Tokyo). 41:2000;349-354.
    • (2000) J. Radiat. Res. (Tokyo) , vol.41 , pp. 349-354
    • Kamiya, H.1    Kasai, H.2
  • 392
    • 0036297160 scopus 로고    scopus 로고
    • Characterization of 2-hydroxyadenine DNA glycosylase activity of Escherichia coli MutY protein
    • Hashiguchi K., Zhang Q.M., Sugiyama H., Ikeda S., Yonei S. Characterization of 2-hydroxyadenine DNA glycosylase activity of Escherichia coli MutY protein. Int. J. Radiat. Biol. 78:2002;585-592.
    • (2002) Int. J. Radiat. Biol. , vol.78 , pp. 585-592
    • Hashiguchi, K.1    Zhang, Q.M.2    Sugiyama, H.3    Ikeda, S.4    Yonei, S.5
  • 393
    • 0032532285 scopus 로고    scopus 로고
    • Oxidation of DNA bases, deoxyribonucleosides and homopolymers by peroxyl radicals
    • Simandan T., Sun J., Dix T.A. Oxidation of DNA bases, deoxyribonucleosides and homopolymers by peroxyl radicals. Biochem. J. 335:1998;233-240.
    • (1998) Biochem. J. , vol.335 , pp. 233-240
    • Simandan, T.1    Sun, J.2    Dix, T.A.3
  • 394
    • 0022373343 scopus 로고
    • An immunochemical probe for 8,5′-cycloadenosine-5′- monophosphate and its deoxy analog in irradiated nucleic acids
    • Fuciarelli A.F., Miller G.G., Raleigh J.A. An immunochemical probe for 8,5′-cycloadenosine-5′-monophosphate and its deoxy analog in irradiated nucleic acids. Radiat. Res. 104:1985;272-283.
    • (1985) Radiat. Res. , vol.104 , pp. 272-283
    • Fuciarelli, A.F.1    Miller, G.G.2    Raleigh, J.A.3
  • 395
    • 0023710238 scopus 로고
    • Effect of DNA conformation on the hydroxyl radical-induced formation of 8,5′-cyclopurine 2′-deoxyribonucleoside residues in DNA
    • Dirksen M.-L., Blakely W.F., Holwitt E., Dizdaroglu M. Effect of DNA conformation on the hydroxyl radical-induced formation of 8,5′- cyclopurine 2′-deoxyribonucleoside residues in DNA. Int. J. Radiat. Biol. 54:1988;195-204.
    • (1988) Int. J. Radiat. Biol. , vol.54 , pp. 195-204
    • Dirksen, M.-L.1    Blakely, W.F.2    Holwitt, E.3    Dizdaroglu, M.4
  • 396
    • 0035929666 scopus 로고    scopus 로고
    • 32P -postlabeling assay for the oxidative DNA lesion 8,5′-cyclo-2′-deoxyadenosine in mammalian tissues: Evidence that four type II I-compounds are dinucleotides containing the lesion in the 3′ nucleotide
    • 32P -postlabeling assay for the oxidative DNA lesion 8,5′-cyclo-2′-deoxyadenosine in mammalian tissues: evidence that four type II I-compounds are dinucleotides containing the lesion in the 3′ nucleotide J. Biol. Chem. 276:2001;36051-36057.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36051-36057
    • Randerath, K.1    Zhou, G.-D.2    Somers, R.L.3    Robbins, J.H.4    Brooks, P.J.5
  • 397
    • 0000964269 scopus 로고    scopus 로고
    • Site-specific introduction of (5′S)-5′,8-cyclo-2′- deoxyadenosine into oligodeoxyribonucleotides
    • Romieu A., Gasparutto D., Molko D., Cadet J. Site-specific introduction of (5′S)-5′,8-cyclo-2′-deoxyadenosine into oligodeoxyribonucleotides. J. Org. Chem. 63:1998;5245-5249.
    • (1998) J. Org. Chem. , vol.63 , pp. 5245-5249
    • Romieu, A.1    Gasparutto, D.2    Molko, D.3    Cadet, J.4
  • 399
    • 0035966003 scopus 로고    scopus 로고
    • Oxygen free radical damage to DNA. Translesion synthesis by human DNA polymerase η and resistance to exonuclease action at cyclopurine deoxynucleoside residues
    • Kuraoka I., Robins P., Masutani C., Hanaoka F., Gasparutto D., Cadet J., Wood R.D., Lindahl T. Oxygen free radical damage to DNA. Translesion synthesis by human DNA polymerase η and resistance to exonuclease action at cyclopurine deoxynucleoside residues. J. Biol. Chem. 276:2001;49283-49288.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49283-49288
    • Kuraoka, I.1    Robins, P.2    Masutani, C.3    Hanaoka, F.4    Gasparutto, D.5    Cadet, J.6    Wood, R.D.7    Lindahl, T.8
  • 400
    • 0036837134 scopus 로고    scopus 로고
    • A single 8,5′-cyclo-2′-deoxyadenosine lesion in a TATA box prevents binding of the TATA binding protein and strongly reduces transcription in vivo
    • Marietta C., Gulam H., Brooks P.J. A single 8,5′-cyclo-2′- deoxyadenosine lesion in a TATA box prevents binding of the TATA binding protein and strongly reduces transcription in vivo. DNA Repair. 1:2002;967-975.
    • (2002) DNA Repair , vol.1 , pp. 967-975
    • Marietta, C.1    Gulam, H.2    Brooks, P.J.3
  • 401
    • 0032782017 scopus 로고    scopus 로고
    • Synthesis and characterization of oligonucleotides containing 5′,8-cyclopurine 2′-deoxyribonucleosides: (5′R)-5′,8- cyclo-2′-deoxyadenosine, (5′S)-5′,8-cyclo-2′- deoxyguanosine, and (5′R)-5′,8-cyclo-2′-deoxyguanosine
    • Romieu A., Gasparutto D., Cadet J. Synthesis and characterization of oligonucleotides containing 5′,8-cyclopurine 2′- deoxyribonucleosides: (5′R)-5′,8-cyclo-2′-deoxyadenosine, (5′S)-5′,8-cyclo-2′-deoxyguanosine, and (5′R)-5′, 8-cyclo-2′-deoxyguanosine. Chem. Res. Toxicol. 12:1999;412-421.
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 412-421
    • Romieu, A.1    Gasparutto, D.2    Cadet, J.3
  • 402
    • 0025228603 scopus 로고
    • Formation of α-deoxyadenosine in polydeoxynucleotides exposed to ionizing radiation under anoxic conditions
    • Lesiak K.B., Wheeler K.T. Formation of α-deoxyadenosine in polydeoxynucleotides exposed to ionizing radiation under anoxic conditions. Radiat. Res. 121:1990;328-337.
    • (1990) Radiat. Res. , vol.121 , pp. 328-337
    • Lesiak, K.B.1    Wheeler, K.T.2
  • 404
    • 0028181135 scopus 로고
    • α-Deoxyadenosine, a major anoxic radiolysis product of adenine in DNA, is a substrate for Escherichia coli endonuclease IV
    • Ide H., Tedzuka K., Shimzu H., Kimura Y., Purmal A.A., Wallace S.S., Kow Y.W. α-Deoxyadenosine, a major anoxic radiolysis product of adenine in DNA, is a substrate for Escherichia coli endonuclease IV. Biochemistry. 33:1994;7842-7847.
    • (1994) Biochemistry , vol.33 , pp. 7842-7847
    • Ide, H.1    Tedzuka, K.2    Shimzu, H.3    Kimura, Y.4    Purmal, A.A.5    Wallace, S.S.6    Kow, Y.W.7
  • 405
    • 0030802872 scopus 로고    scopus 로고
    • Replication bypass and mutagenic effect of α-deoxyadenosine site-specifically incorporated into single-stranded vectors
    • Shimizu H., Yagi R., Kimura Y., Makino K., Terato H., Ohyama Y., Ide H. Replication bypass and mutagenic effect of α-deoxyadenosine site-specifically incorporated into single-stranded vectors. Nucl. Acids Res. 25:1997;597-603.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 597-603
    • Shimizu, H.1    Yagi, R.2    Kimura, Y.3    Makino, K.4    Terato, H.5    Ohyama, Y.6    Ide, H.7
  • 406
    • 0021280347 scopus 로고
    • Synthetic nucleosides and nucleotides. XXI. On the synthesis and biological evaluations of 2′-deoxy-α-D-ribofuranosyl nucleosides and nucleotides
    • Yamaguchi T., Saneyoshi M. Synthetic nucleosides and nucleotides. XXI. On the synthesis and biological evaluations of 2′-deoxy-α-D- ribofuranosyl nucleosides and nucleotides. Chem. Pharm. Bull. (Tokyo). 32:1984;1441-1450.
    • (1984) Chem. Pharm. Bull. (Tokyo) , vol.32 , pp. 1441-1450
    • Yamaguchi, T.1    Saneyoshi, M.2
  • 407
    • 0025198541 scopus 로고
    • 32P -postlabeling measurement of adenine N-1-oxide in cellular DNA exposed to hydrogen peroxide
    • 32P -postlabeling measurement of adenine N-1-oxide in cellular DNA exposed to hydrogen peroxide Chem. Res. Toxicol. 3:1990;102-110.
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 102-110
    • Mouret, J.F.1    Odin, F.2    Polverelli, M.3    Cadet, J.4
  • 409
    • 0036229483 scopus 로고    scopus 로고
    • Cross-linked thymine-purine base tandem lesions: Synthesis, characterization, and measurement in γ-irradiated isolated DNA
    • Bellon S., Ravanat J.-L., Gasparutto D., Cadet J. Cross-linked thymine-purine base tandem lesions: synthesis, characterization, and measurement in γ-irradiated isolated DNA. Chem. Res. Toxicol. 15:2002;598-606.
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 598-606
    • Bellon, S.1    Ravanat, J.-L.2    Gasparutto, D.3    Cadet, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.