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Volumn 13, Issue 6, 2012, Pages 6711-6729

8-oxoguanine DNA glycosylases: One lesion, three subfamilies

Author keywords

8 oxoguanine; 8 oxoguanine DNA glycosylase; Base excision repair; Crystallography; DNA repair; OGG; Protein DNA complex

Indexed keywords

8 HYDROXYGUANINE; 8 OXOGUANINE DNA DNA GLYCOSYLTRANSFERASE 2; 8 OXOGUANINE DNA GLYCOSYLTRANSFERASE; 8 OXOGUANINE DNA GLYCOSYLTRANSFERASE 1; ARCHAEAL 8 OXOGUANINE DNA GLYCOSYLTRANSFERASE; DNA BINDING PROTEIN; DNA GLYCOSYLTRANSFERASE; HELIX HAIRPIN HELIX PROTEIN; UNCLASSIFIED DRUG; 8-HYDROXYGUANINE; BACTERIAL PROTEIN; DNA; GUANINE; LIGAND; PROTEIN BINDING; REACTIVE OXYGEN METABOLITE;

EID: 84862497076     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms13066711     Document Type: Article
Times cited : (40)

References (61)
  • 1
    • 0025373259 scopus 로고
    • Oxidative damage to DNA during aging: 8-hydroxy-2'-deoxyguanosine in rat organ DNA and urine
    • Fraga, C.G.; Shigenaga, M.K.; Park, J.W.; Degan, P.; Ames, B.N. Oxidative damage to DNA during aging: 8-hydroxy-2'-deoxyguanosine in rat organ DNA and urine. Proc. Natl. Acad. Sci. USA 1990, 87, 4533-4537.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4533-4537
    • Fraga, C.G.1    Shigenaga, M.K.2    Park, J.W.3    Degan, P.4    Ames, B.N.5
  • 2
    • 0031027125 scopus 로고    scopus 로고
    • How easily oxidizable is DNA? One-electron reduction potentials of adenosine and guanosine radicals in aqueous solution
    • Steenken, S.; Jovanovic, S.V. How easily oxidizable is DNA? One-electron reduction potentials of adenosine and guanosine radicals in aqueous solution. J. Am. Chem. Soc. 1997, 119, 617-618.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 617-618
    • Steenken, S.1    Jovanovic, S.V.2
  • 3
    • 33646080824 scopus 로고    scopus 로고
    • Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products
    • Neeley, W.L.; Essigmann, J.M. Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products. Chem. Res. Toxicol. 2006, 19, 491-505.
    • (2006) Chem. Res. Toxicol , vol.19 , pp. 491-505
    • Neeley, W.L.1    Essigmann, J.M.2
  • 4
    • 0022809670 scopus 로고
    • Formation of 8-hydroxyguanine moiety in cellular DNA by agents producing oxygen radicals and evidence for its repair
    • Kasai, H.; Crain, P.F.; Kuchino, Y.; Nishimura, S.; Ootsuyama, A.; Tanooka, H. Formation of 8-hydroxyguanine moiety in cellular DNA by agents producing oxygen radicals and evidence for its repair. Carcinogenesis 1986, 7, 1849-1851.
    • (1986) Carcinogenesis , vol.7 , pp. 1849-1851
    • Kasai, H.1    Crain, P.F.2    Kuchino, Y.3    Nishimura, S.4    Ootsuyama, A.5    Tanooka, H.6
  • 5
    • 11244327638 scopus 로고    scopus 로고
    • Establishing the background level of base oxidation in human lymphocyte DNA: Results of an interlaboratory validation study
    • Gedik, C.M.; Collins, A. Establishing the background level of base oxidation in human lymphocyte DNA: Results of an interlaboratory validation study. FASEB J. 2005, 19, 82-84.
    • (2005) FASEB J , vol.19 , pp. 82-84
    • Gedik, C.M.1    Collins, A.2
  • 8
    • 0029773892 scopus 로고    scopus 로고
    • Theoretical studies of GC-specific photocleavage of DNA via electron transfer: Significant lowering of ionization potential and 5'-localization of HOMO of stacked GG bases in B-form DNA
    • Sugiyama, H.; Saito, I. Theoretical studies of GC-specific photocleavage of DNA via electron transfer: Significant lowering of ionization potential and 5'-localization of HOMO of stacked GG bases in B-form DNA. J. Am. Chem. Soc. 1996, 118, 7063-7068.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 7063-7068
    • Sugiyama, H.1    Saito, I.2
  • 9
    • 0035997345 scopus 로고    scopus 로고
    • Long-distance electron transfer through DNA
    • Giese, B. Long-distance electron transfer through DNA. Annu. Rev. Biochem. 2002, 71, 51-70.
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 51-70
    • Giese, B.1
  • 10
    • 0024841281 scopus 로고
    • Structural and conformational analyses of 8-hydroxy-2'-deoxyguanosine
    • Culp, S.J.; Cho, B.P.; Kadlubar, F.F.; Evans, F.E. Structural and conformational analyses of 8-hydroxy-2'-deoxyguanosine. Chem. Res. Toxicol. 1989, 2, 416-422.
    • (1989) Chem. Res. Toxicol , vol.2 , pp. 416-422
    • Culp, S.J.1    Cho, B.P.2    Kadlubar, F.F.3    Evans, F.E.4
  • 11
    • 0017772412 scopus 로고
    • Carbon-13 magnetic resonance spectra of 8-substituted purine nucleosides: Characteristic shifts for the syn conformation
    • Uesugi, S.; Ikehara, M. Carbon-13 magnetic resonance spectra of 8-substituted purine nucleosides: Characteristic shifts for the syn conformation. J. Am. Chem. Soc. 1977, 99, 3250-3253.
    • (1977) J. Am. Chem. Soc , vol.99 , pp. 3250-3253
    • Uesugi, S.1    Ikehara, M.2
  • 12
    • 0027324378 scopus 로고
    • Mutagenesis by 8-oxoguanine: An enemy within
    • Grollman, A.P.; Moriya, M. Mutagenesis by 8-oxoguanine: An enemy within. Trends Genet. 1993, 9, 246-249.
    • (1993) Trends Genet , vol.9 , pp. 246-249
    • Grollman, A.P.1    Moriya, M.2
  • 13
    • 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 1987, 327, 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
  • 14
    • 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 1991, 349, 431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 15
    • 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 1990, 29, 7024-7032.
    • (1990) Biochemistry , vol.29 , pp. 7024-7032
    • Wood, M.L.1    Dizdaroglu, M.2    Gajewski, E.3    Essigmann, J.M.4
  • 16
    • 0016391477 scopus 로고
    • Probing the interrelation between the glycosyl torsion, sugar pucker, and the backbone conformation in C(8) substituted adenine nucleotides by 1H and 1H-(31P) fast Fourier transform nuclear magnetic resonance methods and conformational energy calculations
    • Sarma, R.H.; Lee, C.H.; Evans, F.E.; Yathindra, N.; Sundaralingam, M. Probing the interrelation between the glycosyl torsion, sugar pucker, and the backbone conformation in C(8) substituted adenine nucleotides by 1H and 1H-(31P) fast Fourier transform nuclear magnetic resonance methods and conformational energy calculations. J. Am. Chem. Soc. 1974, 96, 7337-7348.
    • (1974) J. Am. Chem. Soc , vol.96 , pp. 7337-7348
    • Sarma, R.H.1    Lee, C.H.2    Evans, F.E.3    Yathindra, N.4    Sundaralingam, M.5
  • 17
    • 0014965547 scopus 로고
    • Crystal and molecular structure of 8-bromoguanosine and 8-bromoadenosine, two purine nucleosides in the syn conformation
    • Tavale, S.S.; Sobell, H.M. Crystal and molecular structure of 8-bromoguanosine and 8-bromoadenosine, two purine nucleosides in the syn conformation. J. Mol. Biol. 1970, 48, 109-123.
    • (1970) J. Mol. Biol , vol.48 , pp. 109-123
    • Tavale, S.S.1    Sobell, H.M.2
  • 18
    • 4644259458 scopus 로고    scopus 로고
    • Structural basis for the dual coding potential of 8-oxoguanosine by a high-fidelity DNA polymerase
    • Brieba, L.G.; Eichman, B.F.; Kokoska, R.J.; Doublié, S.; Kunkel, T.A.; Ellenberger, T. Structural basis for the dual coding potential of 8-oxoguanosine by a high-fidelity DNA polymerase. EMBO J. 2004, 23, 3452-3461.
    • (2004) EMBO J , vol.23 , pp. 3452-3461
    • Brieba, L.G.1    Eichman, B.F.2    Kokoska, R.J.3    Doublié, S.4    Kunkel, T.A.5    Ellenberger, T.6
  • 19
    • 4544273926 scopus 로고    scopus 로고
    • Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase
    • Hsu, G.W.; Ober, M.; Carell, T.; Beese, L.S. Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase. Nature 2004, 431, 217-221.
    • (2004) Nature , vol.431 , pp. 217-221
    • Hsu, G.W.1    Ober, M.2    Carell, T.3    Beese, L.S.4
  • 20
    • 3343022751 scopus 로고    scopus 로고
    • An evolutionary analysis of the helix-hairpin-helix superfamily of DNA repair glycosylases
    • Denver, D.R.; Swenson, S.L.; Lynch, M. An evolutionary analysis of the helix-hairpin-helix superfamily of DNA repair glycosylases. Mol. Biol. Evol. 2003, 20, 1603-1611.
    • (2003) Mol. Biol. Evol , vol.20 , pp. 1603-1611
    • Denver, D.R.1    Swenson, S.L.2    Lynch, M.3
  • 21
    • 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. Nucleic Acids Res. 1993, 21, 2899-2905.
    • (1993) Nucleic 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
  • 22
    • 0025871264 scopus 로고
    • MutM, a protein that prevents G.C→T.A transversions, is formamidopyrimidine-DNA glycosylase
    • Michaels, M.L.; Pham, L.; Cruz, C.; Miller, J.H. MutM, a protein that prevents G.C→T.A transversions, is formamidopyrimidine-DNA glycosylase. Nucleic Acids Res. 1991, 19, 3629-3632.
    • (1991) Nucleic Acids Res , vol.19 , pp. 3629-3632
    • Michaels, M.L.1    Pham, L.2    Cruz, C.3    Miller, J.H.4
  • 23
    • 0035339557 scopus 로고    scopus 로고
    • Escherichia coli Nth and human hNTH1 DNA glycosylases are involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA
    • Matsumoto, Y.; Zhang, Q.M.; Takao, M.; Yasui, A.; Yonei, S. Escherichia coli Nth and human hNTH1 DNA glycosylases are involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA. Nucleic Acids Res. 2001, 29, 1975-1981.
    • (2001) Nucleic Acids Res , vol.29 , pp. 1975-1981
    • Matsumoto, Y.1    Zhang, Q.M.2    Takao, M.3    Yasui, A.4    Yonei, S.5
  • 24
    • 47649118611 scopus 로고    scopus 로고
    • Clostridium acetobutylicum 8-oxoguanine DNA glycosylase (Ogg) differs from eukaryotic Oggs with respect to opposite base discrimination
    • Robey-Bond, S.M.; Barrantes-Reynolds, R.; Bond, J.P.; Wallace, S.S.; Bandaru, V. Clostridium acetobutylicum 8-oxoguanine DNA glycosylase (Ogg) differs from eukaryotic Oggs with respect to opposite base discrimination. Biochemistry 2008, 47, 7626-7636.
    • (2008) Biochemistry , vol.47 , pp. 7626-7636
    • Robey-Bond, S.M.1    Barrantes-Reynolds, R.2    Bond, J.P.3    Wallace, S.S.4    Bandaru, V.5
  • 25
    • 62049085266 scopus 로고    scopus 로고
    • Structural characterization of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase in its apo form and in complex with 8-oxodeoxyguanosine
    • Faucher, F.; Robey-Bond, S.M.; Wallace, S.S.; Doublié, S. Structural characterization of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase in its apo form and in complex with 8-oxodeoxyguanosine. J. Mol. Biol. 2009, 387, 669-679.
    • (2009) J. Mol. Biol , vol.387 , pp. 669-679
    • Faucher, F.1    Robey-Bond, S.M.2    Wallace, S.S.3    Doublié, S.4
  • 26
    • 0036290411 scopus 로고    scopus 로고
    • Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase
    • Bjørås, M.; Seeberg, E.; Luna, L.; Pearl, L.H.; Barrett, T.E. Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase. J. Mol. Biol. 2002, 317, 171-177.
    • (2002) J. Mol. Biol , vol.317 , pp. 171-177
    • Bjørås, M.1    Seeberg, E.2    Luna, L.3    Pearl, L.H.4    Barrett, T.E.5
  • 27
    • 65149095677 scopus 로고    scopus 로고
    • Crystal structures of two archaeal 8-oxoguanine DNA glycosylases provide structural insight into guanine/8-oxoguanine distinction
    • Faucher, F.; Duclos, S.; Bandaru, V.; Wallace, S.S.; Doublié, S. Crystal structures of two archaeal 8-oxoguanine DNA glycosylases provide structural insight into guanine/8-oxoguanine distinction. Structure 2009, 17, 703-712.
    • (2009) Structure , vol.17 , pp. 703-712
    • Faucher, F.1    Duclos, S.2    Bandaru, V.3    Wallace, S.S.4    Doublié, S.5
  • 28
    • 77249173864 scopus 로고    scopus 로고
    • The C-terminal lysine of Ogg2 DNA glycosylases is a major molecular determinant for guanine/8-oxoguanine distinction
    • Faucher, F.; Wallace, S.S.; Doublié, S. The C-terminal lysine of Ogg2 DNA glycosylases is a major molecular determinant for guanine/8-oxoguanine distinction. J. Mol. Biol. 2010, 397, 46-56.
    • (2010) J. Mol. Biol , vol.397 , pp. 46-56
    • Faucher, F.1    Wallace, S.S.2    Doublié, S.3
  • 29
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • Bruner, S.D.; Norman, D.P.; Verdine, G.L. Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature 2000, 403, 859-866.
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.2    Verdine, G.L.3
  • 30
    • 11844306632 scopus 로고    scopus 로고
    • A DNA glycosylase from Pyrobaculum aerophilum with an 8-oxoguanine binding mode and a noncanonical helix-hairpin-helix structure
    • Lingaraju, G.M.; Sartori, A.A.; Kostrewa, D.; Prota, A.E.; Jiricny, J.; Winkler, F.K. A DNA glycosylase from Pyrobaculum aerophilum with an 8-oxoguanine binding mode and a noncanonical helix-hairpin-helix structure. Structure 2005, 13, 87-98.
    • (2005) Structure , vol.13 , pp. 87-98
    • Lingaraju, G.M.1    Sartori, A.A.2    Kostrewa, D.3    Prota, A.E.4    Jiricny, J.5    Winkler, F.K.6
  • 32
    • 0036606464 scopus 로고    scopus 로고
    • Human OGG1 undergoes serine phosphorylation and associates with the nuclear matrix and mitotic chromatin in vivo
    • Dantzer, F.; Luna, L.; Bjørås, M.; Seeberg, E. Human OGG1 undergoes serine phosphorylation and associates with the nuclear matrix and mitotic chromatin in vivo. Nucleic Acids Res. 2002, 30, 2349-2357.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2349-2357
    • Dantzer, F.1    Luna, L.2    Bjørås, M.3    Seeberg, E.4
  • 33
    • 0032945268 scopus 로고    scopus 로고
    • Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs
    • Nishioka, K.; Ohtsubo, T.; Oda, H.; Fujiwara, T.; Kang, D.; Sugimachi, K.; Nakabeppu, Y. Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs. Mol. Biol. Cell 1999, 10, 1637-1652.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1637-1652
    • Nishioka, K.1    Ohtsubo, T.2    Oda, H.3    Fujiwara, T.4    Kang, D.5    Sugimachi, K.6    Nakabeppu, Y.7
  • 34
    • 0035869159 scopus 로고    scopus 로고
    • Inactivation of Saccharomyces cerevisiae OGG1 DNA repair gene leads to an increased frequency of mitochondrial mutants
    • Singh, K.K.; Sigala, B.; Sikder, H.A.; Schwimmer, C. Inactivation of Saccharomyces cerevisiae OGG1 DNA repair gene leads to an increased frequency of mitochondrial mutants. Nucleic Acids Res. 2001, 29, 1381-1388.
    • (2001) Nucleic Acids Res , vol.29 , pp. 1381-1388
    • Singh, K.K.1    Sigala, B.2    Sikder, H.A.3    Schwimmer, C.4
  • 35
    • 84862504457 scopus 로고    scopus 로고
    • The Human Protein Reference Database. Available online, accessed on 1 May
    • The Human Protein Reference Database. Available online: http://www.hprd.org/index_html (accessed on 1 May, 2012).
    • (2012)
  • 36
    • 0025995844 scopus 로고
    • A structural taxonomy of DNA-binding domains
    • Harrison, S.C. A structural taxonomy of DNA-binding domains. Nature 1991, 353, 715-719.
    • (1991) Nature , vol.353 , pp. 715-719
    • Harrison, S.C.1
  • 37
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer, M.M.; Ahern, H.; Xing, D.; Cunningham, R.P.; Tainer, J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 1995, 14, 4108-4120.
    • (1995) EMBO J , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 38
    • 0030220956 scopus 로고    scopus 로고
    • Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily
    • Nash, H.M.; Bruner, S.D.; Schärer, O.D.; Kawate, T.; Addona, T.A.; Spooner, E.; Lane, W.S.; Verdine, G.L. Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily. Curr. Biol. 1996, 6, 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
  • 39
    • 70349847564 scopus 로고    scopus 로고
    • Structural basis for the lack of opposite base specificity of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase
    • Faucher, F.; Wallace, S.S.; Doublié, S. Structural basis for the lack of opposite base specificity of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase. DNA Repair (Amst) 2009, 8, 1283-1289.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 1283-1289
    • Faucher, F.1    Wallace, S.S.2    Doublié, S.3
  • 40
    • 15844379169 scopus 로고    scopus 로고
    • Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA
    • Banerjee, A.; Yang, W.; Karplus, M.; Verdine, G.L. Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA. Nature 2005, 434, 612-618.
    • (2005) Nature , vol.434 , pp. 612-618
    • Banerjee, A.1    Yang, W.2    Karplus, M.3    Verdine, G.L.4
  • 41
    • 34247862129 scopus 로고    scopus 로고
    • Structural characterization of human 8-oxoguanine DNA glycosylase variants bearing active site mutations
    • Radom, C.T.; Banerjee, A.; Verdine, G.L. Structural characterization of human 8-oxoguanine DNA glycosylase variants bearing active site mutations. J. Biol. Chem. 2007, 282, 9182-9194.
    • (2007) J. Biol. Chem , vol.282 , pp. 9182-9194
    • Radom, C.T.1    Banerjee, A.2    Verdine, G.L.3
  • 42
    • 0141670355 scopus 로고    scopus 로고
    • Enzymatic properties of Escherichia coli and human 7,8-dihydro-8-oxoguanine DNA glycosylases
    • Asagoshi, K.; Yamada, T.; Terato, H.; Ohyama, Y.; Ide, H. Enzymatic properties of Escherichia coli and human 7,8-dihydro-8-oxoguanine DNA glycosylases. Nucleic Acids Symp. Ser. 2000, 11-12.
    • (2000) Nucleic Acids Symp. Ser , pp. 11-12
    • Asagoshi, K.1    Yamada, T.2    Terato, H.3    Ohyama, Y.4    Ide, H.5
  • 43
    • 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. 2000, 275, 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
  • 44
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • David, S.S.; O'Shea, V.L.; Kundu, S. Base-excision repair of oxidative DNA damage. Nature 2007, 447, 941-950.
    • (2007) Nature , vol.447 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 45
    • 34347264416 scopus 로고    scopus 로고
    • Substrate specificity of Fpg (MutM) and hOGG1, two repair glycosylases
    • Hamm, M.L.; Gill, T.J.; Nicolson, S.C.; Summers, M.R. Substrate specificity of Fpg (MutM) and hOGG1, two repair glycosylases. J. Am. Chem. Soc. 2007, 129, 7724-7725.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 7724-7725
    • Hamm, M.L.1    Gill, T.J.2    Nicolson, S.C.3    Summers, M.R.4
  • 46
    • 67349136743 scopus 로고    scopus 로고
    • Mutational studies of Pa-AGOG DNA glycosylase from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum
    • Lingaraju, G.M.; Prota, A.E.; Winkler, F.K. Mutational studies of Pa-AGOG DNA glycosylase from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. DNA Repair (Amst.) 2009, 8, 857-864.
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 857-864
    • Lingaraju, G.M.1    Prota, A.E.2    Winkler, F.K.3
  • 48
    • 84862489528 scopus 로고    scopus 로고
    • Enforced presentation of an extrahelical guanine to the lesion-recognition pocket of the human 8-oxoguanine DNA glycosylase, hOGG1
    • in press
    • Crenshaw, C.M.; Nam, K.; Oo, K.; Kutchukian, P.S.; Bowman, B.R.; Karplus, M.; Verdine, G.L. Enforced presentation of an extrahelical guanine to the lesion-recognition pocket of the human 8-oxoguanine DNA glycosylase, hOGG1. J. Biol. Chem. 2012, (in press).
    • (2012) J. Biol. Chem
    • Crenshaw, C.M.1    Nam, K.2    Oo, K.3    Kutchukian, P.S.4    Bowman, B.R.5    Karplus, M.6    Verdine, G.L.7
  • 49
    • 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. 1999, 274, 30447-30450.
    • (1999) J. Biol. Chem , vol.274 , pp. 30447-30450
    • Gogos, A.1    Clarke, N.D.2
  • 50
    • 42649085059 scopus 로고    scopus 로고
    • Transition-state analysis of the DNA repair enzyme MutY
    • McCann, J.A.; Berti, P.J. Transition-state analysis of the DNA repair enzyme MutY. J. Am. Chem. Soc. 2008, 130, 5789-5797.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 5789-5797
    • McCann, J.A.1    Berti, P.J.2
  • 51
    • 0034700259 scopus 로고    scopus 로고
    • Kinetic isotope effect studies of the reaction catalyzed by uracil DNA glycosylase: Evidence for an oxocarbenium ion-uracil anion intermediate
    • Werner, R.M.; Stivers, J.T. Kinetic isotope effect studies of the reaction catalyzed by uracil DNA glycosylase: Evidence for an oxocarbenium ion-uracil anion intermediate. Biochemistry 2000, 39, 14054-14064.
    • (2000) Biochemistry , vol.39 , pp. 14054-14064
    • Werner, R.M.1    Stivers, J.T.2
  • 52
    • 0032538337 scopus 로고    scopus 로고
    • Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: Mechanisms for nucleotide flipping and base excision
    • Lau, A.Y.; Schärer, O.D.; Samson, L.; Verdine, G.L.; Ellenberger, T. Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: Mechanisms for nucleotide flipping and base excision. Cell 1998, 95, 249-258.
    • (1998) Cell , vol.95 , pp. 249-258
    • Lau, A.Y.1    Schärer, O.D.2    Samson, L.3    Verdine, G.L.4    Ellenberger, T.5
  • 53
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
    • Mol, C.D.; Arvai, A.S.; Slupphaug, G.; Kavli, B.; Alseth, I.; Krokan, H.E.; Tainer, J.A. Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis. Cell 1995, 80, 869-878.
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 54
    • 0037452513 scopus 로고    scopus 로고
    • Structural and biochemical exploration of a critical amino acid in human 8-oxoguanine glycosylase
    • Norman, D.P.; Chung, S.J.; Verdine, G.L. Structural and biochemical exploration of a critical amino acid in human 8-oxoguanine glycosylase. Biochemistry 2003, 42, 1564-1572.
    • (2003) Biochemistry , vol.42 , pp. 1564-1572
    • Norman, D.P.1    Chung, S.J.2    Verdine, G.L.3
  • 55
    • 0031239573 scopus 로고    scopus 로고
    • The critical active-site amine of the human 8-oxoguanine DNA glycosylase, hOgg1: Direct identification, ablation and chemical reconstitution
    • Nash, H.M.; Lu, R.; Lane, W.S.; Verdine, G.L. The critical active-site amine of the human 8-oxoguanine DNA glycosylase, hOgg1: Direct identification, ablation and chemical reconstitution. Chem. Biol. 1997, 4, 693-702.
    • (1997) Chem. Biol , vol.4 , pp. 693-702
    • Nash, H.M.1    Lu, R.2    Lane, W.S.3    Verdine, G.L.4
  • 56
    • 0035900960 scopus 로고    scopus 로고
    • Coupling of substrate recognition and catalysis by a human base-excision DNA repair protein
    • Norman, D.P.; Bruner, S.D.; Verdine, G.L. Coupling of substrate recognition and catalysis by a human base-excision DNA repair protein. J. Am. Chem. Soc. 2001, 123, 359-360.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 359-360
    • Norman, D.P.1    Bruner, S.D.2    Verdine, G.L.3
  • 57
    • 12344307152 scopus 로고    scopus 로고
    • Product inhibition and magnesium modulate the dual reaction mode of hOgg1
    • Morland, I.; Luna, L.; Gustad, E.; Seeberg, E.; Bjørås, M. Product inhibition and magnesium modulate the dual reaction mode of hOgg1. DNA Repair (Amst.) 2005, 4, 381-387.
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 381-387
    • Morland, I.1    Luna, L.2    Gustad, E.3    Seeberg, E.4    Bjørås, M.5
  • 58
    • 0035803497 scopus 로고    scopus 로고
    • DNA polymerase beta is the major dRP lyase involved in repair of oxidative base lesions in DNA by mammalian cell extracts
    • Allinson, S.L.; Dianova, I.I.; Dianov, G.L. DNA polymerase beta is the major dRP lyase involved in repair of oxidative base lesions in DNA by mammalian cell extracts. EMBO J. 2001, 20, 6919-6926.
    • (2001) EMBO J , vol.20 , pp. 6919-6926
    • Allinson, S.L.1    Dianova, I.I.2    Dianov, G.L.3
  • 59
    • 0035863739 scopus 로고    scopus 로고
    • Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: Potential coordination of the initial steps in base excision repair
    • Hill, J.W.; Hazra, T.K.; Izumi, T.; Mitra, S. Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: Potential coordination of the initial steps in base excision repair. Nucleic Acids Res. 2001, 29, 430-438.
    • (2001) Nucleic Acids Res , vol.29 , pp. 430-438
    • Hill, J.W.1    Hazra, T.K.2    Izumi, T.3    Mitra, S.4
  • 60
    • 0035869114 scopus 로고    scopus 로고
    • Mechanism of stimulation of the DNA glycosylase activity of hOGG1 by the major human AP endonuclease: Bypass of the AP lyase activity step
    • Vidal, A.E.; Hickson, I.D.; Boiteux, S.; Radicella, J.P. Mechanism of stimulation of the DNA glycosylase activity of hOGG1 by the major human AP endonuclease: Bypass of the AP lyase activity step. Nucleic Acids Res. 2001, 29, 1285-1292.
    • (2001) Nucleic Acids Res , vol.29 , pp. 1285-1292
    • Vidal, A.E.1    Hickson, I.D.2    Boiteux, S.3    Radicella, J.P.4
  • 61
    • 0034661689 scopus 로고    scopus 로고
    • Effect of single mutations in the OGG1 gene found in human tumors on the substrate specificity of the Ogg1 protein
    • Audebert, M.; Radicella, J.P.; Dizdaroglu, M. Effect of single mutations in the OGG1 gene found in human tumors on the substrate specificity of the Ogg1 protein. Nucleic Acids Res. 2000, 28, 2672-2678.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2672-2678
    • Audebert, M.1    Radicella, J.P.2    Dizdaroglu, M.3


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