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Volumn 275, Issue 15, 2008, Pages 3747-3760

Ionic strength and magnesium affect the specificity of Escherichia coli and human 8-oxoguanine-DNA glycosylases

Author keywords

8 oxoguanine; DNA damage; DNA glycosylase; DNA repair; Substrate specificity

Indexed keywords

8 HYDROXYGUANINE; 8 OXOGUANINE DNA GLYCOSYLASE; ANION; BIOTIN; CAFFEINE; CHLORIDE ION; DNA FORMAMIDOPYRIMIDINE GLYCOSYLASE; DNA GLYCOSYLTRANSFERASE; GLUTAMIC ACID; MAGNESIUM ION; POLYAMIDE; PROTEIN; PROTEIN OGG1;

EID: 47249106541     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06521.x     Document Type: Article
Times cited : (7)

References (72)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T (1993) Instability and decay of the primary structure of DNA. Nature 362, 709 715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 2
    • 11244327638 scopus 로고    scopus 로고
    • Establishing the background level of base oxidation in human lymphocyte DNA: Results of an interlaboratory validation study
    • European Standards Committee on Oxidative DNA Damage (ESCODD)
    • European Standards Committee on Oxidative DNA Damage (ESCODD), Gedik CM Collins A (2005) Establishing the background level of base oxidation in human lymphocyte DNA: results of an interlaboratory validation study. FASEB J 19, 82 84.
    • (2005) FASEB J , vol.19 , pp. 82-84
    • Gedik, C.M.1    Collins, A.2
  • 3
    • 0025891866 scopus 로고
    • NMR structural studies of the ionizing radiation adduct 7-hydro-8-oxodeoxyguanosine (8-oxo-7H-dG) opposite deoxyadenosine in a DNA duplex. 8-Oxo-7H-dG(syn)·dA(anti) alignment at lesion site
    • Kouchakdjian M, Bodepudi V, Shibutani S, Eisenberg M, Johnson F, Grollman AP Patel DJ (1991) NMR structural studies of the ionizing radiation adduct 7-hydro-8-oxodeoxyguanosine (8-oxo-7H-dG) opposite deoxyadenosine in a DNA duplex. 8-Oxo-7H-dG(syn)·dA(anti) alignment at lesion site. Biochemistry 30, 1403 1412.
    • (1991) Biochemistry , vol.30 , pp. 1403-1412
    • Kouchakdjian, M.1    Bodepudi, V.2    Shibutani, S.3    Eisenberg, M.4    Johnson, F.5    Grollman, A.P.6    Patel, D.J.7
  • 4
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani S, Takeshita M Grollman AP (1991) Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature 349, 431 434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 7
    • 0026701365 scopus 로고
    • The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)
    • Michaels ML Miller JH (1992) The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8- oxoguanine). J Bacteriol 174, 6321 6325.
    • (1992) J Bacteriol , vol.174 , pp. 6321-6325
    • Michaels, M.L.1    Miller, J.H.2
  • 8
    • 0027528412 scopus 로고
    • Repair of DNA containing the oxidatively damaged base, 8-oxoguanine
    • Tchou J Grollman AP (1993) Repair of DNA containing the oxidatively damaged base, 8-oxoguanine. Mutat Res 299, 277 287.
    • (1993) Mutat Res , vol.299 , pp. 277-287
    • Tchou, J.1    Grollman, A.P.2
  • 9
    • 34147174320 scopus 로고    scopus 로고
    • Significance of error-avoiding mechanisms for oxidative DNA damage in carcinogenesis
    • Tsuzuki T, Nakatsu Y Nakabeppu Y (2007) Significance of error-avoiding mechanisms for oxidative DNA damage in carcinogenesis. Cancer Sci 98, 465 470.
    • (2007) Cancer Sci , vol.98 , pp. 465-470
    • Tsuzuki, T.1    Nakatsu, Y.2    Nakabeppu, Y.3
  • 10
    • 33847007529 scopus 로고    scopus 로고
    • The mechanics of base excision repair, and its relationship to aging and disease
    • Wilson DM III Bohr VA (2007) The mechanics of base excision repair, and its relationship to aging and disease. DNA Repair 6, 544 559.
    • (2007) DNA Repair , vol.6 , pp. 544-559
    • Wilson III, D.M.1    Bohr, V.A.2
  • 11
    • 0028933674 scopus 로고
    • Functional cooperation of MutT, MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotide in Escherichia coli
    • Tajiri T, Maki H Sekiguchi M (1995) Functional cooperation of MutT, MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotide in Escherichia coli. Mutat Res 336, 257 267.
    • (1995) Mutat Res , vol.336 , pp. 257-267
    • Tajiri, T.1    Maki, H.2    Sekiguchi, M.3
  • 13
    • 2342520175 scopus 로고    scopus 로고
    • Deficiencies in mouse myh and ogg1 result in tumor predisposition and G to T mutations in codon 12 of the k-ras oncogene in lung tumors
    • Xie Y, Yang H, Cunanan C, Okamoto K, Shibata D, Pan J, Barnes DE, Lindahl T, McIlhatton M, Fishel R et al. (2004) Deficiencies in mouse myh and ogg1 result in tumor predisposition and G to T mutations in codon 12 of the k-ras oncogene in lung tumors. Cancer Res 64, 3096 3102.
    • (2004) Cancer Res , vol.64 , pp. 3096-3102
    • Xie, Y.1    Yang, H.2    Cunanan, C.3    Okamoto, K.4    Shibata, D.5    Pan, J.6    Barnes, D.E.7    Lindahl, T.8    McIlhatton, M.9    Fishel, R.10
  • 15
    • 13944281044 scopus 로고    scopus 로고
    • Polymorphic variation in hOGG1 and risk of cancer: A review of the functional and epidemiologic literature
    • Weiss JM, Goode EL, Ladiges WC Ulrich CM (2005) Polymorphic variation in hOGG1 and risk of cancer: a review of the functional and epidemiologic literature. Mol Carcinogen 42, 127 141.
    • (2005) Mol Carcinogen , vol.42 , pp. 127-141
    • Weiss, J.M.1    Goode, E.L.2    Ladiges, W.C.3    Ulrich, C.M.4
  • 16
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • Bruner SD, Norman DPG Verdine GL (2000) Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature 403, 859 866.
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.G.2    Verdine, G.L.3
  • 18
    • 0036294464 scopus 로고    scopus 로고
    • Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM
    • Fromme JC Verdine GL (2002) Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM. Nat Struct Biol 9, 544 552.
    • (2002) Nat Struct Biol , vol.9 , pp. 544-552
    • Fromme, J.C.1    Verdine, G.L.2
  • 22
    • 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 (1993) Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins. Nucleic Acids Res 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
  • 24
    • 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
    • Auffret van der Kemp P, Thomas D, Barbey R, de Oliveira R Boiteux S (1996) 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 USA 93, 5197 5202.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5197-5202
    • Auffret Van Der Kemp, P.1    Thomas, D.2    Barbey, R.3    De Oliveira, R.4    Boiteux, S.5
  • 25
    • 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 (1997) 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, 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
  • 26
    • 0034666313 scopus 로고    scopus 로고
    • Substrate specificity and reaction mechanism of murine 8-oxoguanine-DNA glycosylase
    • Zharkov DO, Rosenquist TA, Gerchman SE Grollman AP (2000) Substrate specificity and reaction mechanism of murine 8-oxoguanine-DNA glycosylase. J Biol Chem 275, 28607 28617.
    • (2000) J Biol Chem , vol.275 , pp. 28607-28617
    • Zharkov, D.O.1    Rosenquist, T.A.2    Gerchman, S.E.3    Grollman, A.P.4
  • 27
    • 0345863934 scopus 로고    scopus 로고
    • The CyberCell Database (CCDB): A comprehensive, self-updating, relational database to coordinate and facilitate in silico modeling of Escherichia coli
    • Sundararaj S, Guo A, Habibi-Nazhad B, Rouani M, Stothard P, Ellison M Wishart DS (2004) The CyberCell Database (CCDB): a comprehensive, self-updating, relational database to coordinate and facilitate in silico modeling of Escherichia coli. Nucleic Acids Res 32, D293 D295.
    • (2004) Nucleic Acids Res , vol.32
    • Sundararaj, S.1    Guo, A.2    Habibi-Nazhad, B.3    Rouani, M.4    Stothard, P.5    Ellison, M.6    Wishart, D.S.7
  • 28
    • 0024462459 scopus 로고
    • Mechanism of DNA strand nicking at apurinic/apyrimidinic sites by Escherichia coli [formamidopyrimidine]DNA glycosylase
    • Bailly V, Verly WG, O'Connor T Laval J (1989) Mechanism of DNA strand nicking at apurinic/apyrimidinic sites by Escherichia coli [formamidopyrimidine] DNA glycosylase. Biochem J 262, 581 589.
    • (1989) Biochem J , vol.262 , pp. 581-589
    • Bailly, V.1    Verly, W.G.2    O'Connor, T.3    Laval, J.4
  • 29
    • 0027403859 scopus 로고
    • Structure of the B-DNA decamer C-C-A-A-C-I-T-T-G-G in two different space groups: Conformational flexibility of B-DNA
    • Lipanov A, Kopka ML, Kaczor-Grzeskowiak M, Quintana J Dickerson RE (1993) Structure of the B-DNA decamer C-C-A-A-C-I-T-T-G-G in two different space groups: conformational flexibility of B-DNA. Biochemistry 32, 1373 1389.
    • (1993) Biochemistry , vol.32 , pp. 1373-1389
    • Lipanov, A.1    Kopka, M.L.2    Kaczor-Grzeskowiak, M.3    Quintana, J.4    Dickerson, R.E.5
  • 30
    • 0035863739 scopus 로고    scopus 로고
    • Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: Potential coordination of the initial steps in base excision repair
    • Hill JW, Hazra TK, Izumi T Mitra S (2001) Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: potential coordination of the initial steps in base excision repair. Nucleic Acids Res 29, 430 438.
    • (2001) Nucleic Acids Res , vol.29 , pp. 430-438
    • Hill, J.W.1    Hazra, T.K.2    Izumi, T.3    Mitra, S.4
  • 31
    • 33847293432 scopus 로고    scopus 로고
    • Mechanism of interaction between human 8-oxoguanine-DNA glycosylase and AP endonuclease
    • Sidorenko VS, Nevinsky GA Zharkov DO (2007) Mechanism of interaction between human 8-oxoguanine-DNA glycosylase and AP endonuclease. DNA Repair 6, 317 328.
    • (2007) DNA Repair , vol.6 , pp. 317-328
    • Sidorenko, V.S.1    Nevinsky, G.A.2    Zharkov, D.O.3
  • 32
    • 0027462131 scopus 로고
    • Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role
    • O'Connor TR, Graves RJ, de Murcia G, Castaing B Laval J (1993) Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role. J Biol Chem 268, 9063 9070.
    • (1993) J Biol Chem , vol.268 , pp. 9063-9070
    • O'Connor, T.R.1    Graves, R.J.2    De Murcia, G.3    Castaing, B.4    Laval, J.5
  • 33
    • 0031034183 scopus 로고    scopus 로고
    • Mechanism of bypass synthesis through an abasic site analog by DNA polymerase I
    • Paz-Elizur T, Takeshita M Livneh Z (1997) Mechanism of bypass synthesis through an abasic site analog by DNA polymerase I. Biochemistry 36, 1766 1773.
    • (1997) Biochemistry , vol.36 , pp. 1766-1773
    • Paz-Elizur, T.1    Takeshita, M.2    Livneh, Z.3
  • 34
    • 15344340623 scopus 로고    scopus 로고
    • Polyamines: Metabolism and implications in human diseases
    • Moinard C, Cynober L de Bandt J-P (2005) Polyamines: metabolism and implications in human diseases. Clin Nutr 24, 184 197.
    • (2005) Clin Nutr , vol.24 , pp. 184-197
    • Moinard, C.1    Cynober, L.2    De Bandt, J.-P.3
  • 36
    • 14244266841 scopus 로고    scopus 로고
    • The fidelity of DNA synthesis by human immunodeficiency virus type 1 reverse transcriptase increases in the presence of polyamines
    • Bakhanashvili M, Novitsky E, Levy I Rahav G (2005) The fidelity of DNA synthesis by human immunodeficiency virus type 1 reverse transcriptase increases in the presence of polyamines. FEBS Lett 579, 1435 1440.
    • (2005) FEBS Lett , vol.579 , pp. 1435-1440
    • Bakhanashvili, M.1    Novitsky, E.2    Levy, I.3    Rahav, G.4
  • 37
    • 0020491243 scopus 로고
    • Polyamine-induced hydrolysis of apurinic sites in DNA and nucleosomes
    • Male R, Fosse VM Kleppe K (1982) Polyamine-induced hydrolysis of apurinic sites in DNA and nucleosomes. Nucleic Acids Res 10, 6305 6318.
    • (1982) Nucleic Acids Res , vol.10 , pp. 6305-6318
    • Male, R.1    Fosse, V.M.2    Kleppe, K.3
  • 38
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis RJ (2001) Macromolecular crowding: obvious but underappreciated. Trends Biochem Sci 26, 597 604.
    • (2001) Trends Biochem Sci , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 39
    • 0021112785 scopus 로고
    • Polymer-stimulated ligation: Enhanced blunt- or cohesive-end ligation of DNA or deoxyribooligonucleotides by T4 DNA ligase in polymer solutions
    • Pheiffer BH Zimmerman SB (1983) Polymer-stimulated ligation: enhanced blunt- or cohesive-end ligation of DNA or deoxyribooligonucleotides by T4 DNA ligase in polymer solutions. Nucleic Acids Res 11, 7853 7871.
    • (1983) Nucleic Acids Res , vol.11 , pp. 7853-7871
    • Pheiffer, B.H.1    Zimmerman, S.B.2
  • 40
    • 0032762645 scopus 로고    scopus 로고
    • Crowding effects on EcoRV kinetics and binding
    • Wenner JR Bloomfield VA (1999) Crowding effects on EcoRV kinetics and binding. Biophys J 77, 3234 3241.
    • (1999) Biophys J , vol.77 , pp. 3234-3241
    • Wenner, J.R.1    Bloomfield, V.A.2
  • 41
    • 0031984418 scopus 로고    scopus 로고
    • Direct detection of 8-oxodeoxyguanosine and 8-oxoguanine by avidin and its analogues
    • Struthers L, Patel R, Clark J Thomas S (1998) Direct detection of 8-oxodeoxyguanosine and 8-oxoguanine by avidin and its analogues. Anal Biochem 255, 20 31.
    • (1998) Anal Biochem , vol.255 , pp. 20-31
    • Struthers, L.1    Patel, R.2    Clark, J.3    Thomas, S.4
  • 42
    • 33644754088 scopus 로고    scopus 로고
    • Recognition of oxidatively modified bases within the biotin-binding site of avidin
    • Conners R, Hooley E, Clarke AR, Thomas S Brady RL (2006) Recognition of oxidatively modified bases within the biotin-binding site of avidin. J Mol Biol 357, 263 274.
    • (2006) J Mol Biol , vol.357 , pp. 263-274
    • Conners, R.1    Hooley, E.2    Clarke, A.R.3    Thomas, S.4    Brady, R.L.5
  • 43
    • 0038584912 scopus 로고    scopus 로고
    • Coffee drinking: The rationale for treating it as a potential effect modifier of carcinogenic exposures
    • Porta M, Vioque J, Ayude D, Alguacil J, Jariod M, Ruiz L Murillo JA (2003) Coffee drinking: the rationale for treating it as a potential effect modifier of carcinogenic exposures. Eur J Epidemiol 18, 289 298.
    • (2003) Eur J Epidemiol , vol.18 , pp. 289-298
    • Porta, M.1    Vioque, J.2    Ayude, D.3    Alguacil, J.4    Jariod, M.5    Ruiz, L.6    Murillo, J.A.7
  • 44
    • 0142187125 scopus 로고    scopus 로고
    • Structural characterization of the Fpg family of DNA glycosylases
    • Zharkov DO, Shoham G Grollman AP (2003) Structural characterization of the Fpg family of DNA glycosylases. DNA Repair 2, 839 862.
    • (2003) DNA Repair , vol.2 , pp. 839-862
    • Zharkov, D.O.1    Shoham, G.2    Grollman, A.P.3
  • 45
    • 0023433565 scopus 로고
    • Formamidopyrimidine-DNA glycosylase of Escherichia coli: Cloning and sequencing of the fpg structural gene and overproduction of the protein
    • Boiteux S, O'Connor TR Laval J (1987) Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein. EMBO J 6, 3177 3183.
    • (1987) EMBO J , vol.6 , pp. 3177-3183
    • Boiteux, S.1    O'Connor, T.R.2    Laval, J.3
  • 47
    • 24044492241 scopus 로고    scopus 로고
    • The DNA trackwalkers: Principles of lesion search and recognition by DNA glycosylases
    • Zharkov DO Grollman AP (2005) The DNA trackwalkers: principles of lesion search and recognition by DNA glycosylases. Mutat Res 577, 24 54.
    • (2005) Mutat Res , vol.577 , pp. 24-54
    • Zharkov, D.O.1    Grollman, A.P.2
  • 48
    • 33749568015 scopus 로고    scopus 로고
    • Magnesium, essential for base excision repair enzymes, inhibits substrate binding of N-methylpurine-DNA glycosylase
    • Adhikari S, Toretsky JA, Yuan L Roy R (2006) Magnesium, essential for base excision repair enzymes, inhibits substrate binding of N-methylpurine-DNA glycosylase. J Biol Chem 281, 29525 29532.
    • (2006) J Biol Chem , vol.281 , pp. 29525-29532
    • Adhikari, S.1    Toretsky, J.A.2    Yuan, L.3    Roy, R.4
  • 50
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae
    • Radicella JP, Dherin C, Desmaze C, Fox MS Boiteux S (1997) Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae. Proc Natl Acad Sci USA 94, 8010 8015.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8010-8015
    • Radicella, J.P.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.4    Boiteux, S.5
  • 51
    • 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 GL (2005) Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA. Nature 434, 612 618.
    • (2005) Nature , vol.434 , pp. 612-618
    • Banerjee, A.1    Yang, W.2    Karplus, M.3    Verdine, G.L.4
  • 52
    • 33644511436 scopus 로고    scopus 로고
    • Structure of a DNA glycosylase searching for lesions
    • Banerjee A, Santos WL Verdine GL (2006) Structure of a DNA glycosylase searching for lesions. Science 311, 1153 1157.
    • (2006) Science , vol.311 , pp. 1153-1157
    • Banerjee, A.1    Santos, W.L.2    Verdine, G.L.3
  • 53
    • 0019887628 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory
    • Berg OG, Winter RB von Hippel PH (1981) Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory. Biochemistry 20, 6929 6948.
    • (1981) Biochemistry , vol.20 , pp. 6929-6948
    • Berg, O.G.1    Winter, R.B.2    Von Hippel, P.H.3
  • 56
    • 0028783875 scopus 로고
    • Influence of the oxidatively damaged adduct 8-oxodeoxyguanosine on the conformation, energetics, and thermodynamic stability of a DNA duplex
    • Plum GE, Grollman AP, Johnson F Breslauer KJ (1995) Influence of the oxidatively damaged adduct 8-oxodeoxyguanosine on the conformation, energetics, and thermodynamic stability of a DNA duplex. Biochemistry 34, 16148 16160.
    • (1995) Biochemistry , vol.34 , pp. 16148-16160
    • Plum, G.E.1    Grollman, A.P.2    Johnson, F.3    Breslauer, K.J.4
  • 59
    • 0043037215 scopus 로고    scopus 로고
    • Cations as hydrogen bond donors: A view of electrostatic interactions in DNA
    • Subirana JA Soler-López M (2003) Cations as hydrogen bond donors: a view of electrostatic interactions in DNA. Annu Rev Biophys Biomol Struct 32, 27 45.
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 27-45
    • Subirana, J.A.1    Soler-López, M.2
  • 60
    • 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 (2005) Product inhibition and magnesium modulate the dual reaction mode of hOgg1. DNA Repair 4, 381 387.
    • (2005) DNA Repair , vol.4 , pp. 381-387
    • Morland, I.1    Luna, L.2    Gustad, E.3    Seeberg, E.4    Bjørås, M.5
  • 62
    • 0019878052 scopus 로고
    • Uracil DNA-glycosylase from HeLa cells: General properties, substrate specificity and effect of uracil analogs
    • Krokan H Wittwer CU (1981) Uracil DNA-glycosylase from HeLa cells: general properties, substrate specificity and effect of uracil analogs. Nucleic Acids Res 9, 2599 2613.
    • (1981) Nucleic Acids Res , vol.9 , pp. 2599-2613
    • Krokan, H.1    Wittwer, C.U.2
  • 63
    • 0020060168 scopus 로고
    • Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine
    • Thomas L, Yang CH Goldthwait DA (1982) Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine. Biochemistry 21, 1162 1169.
    • (1982) Biochemistry , vol.21 , pp. 1162-1169
    • Thomas, L.1    Yang, C.H.2    Goldthwait, D.A.3
  • 64
    • 0023649611 scopus 로고
    • Purification and characterization of 3-methyladenine DNA glycosylase I from Escherichia coli
    • Bjelland S Seeberg E (1987) Purification and characterization of 3-methyladenine DNA glycosylase I from Escherichia coli. Nucleic Acids Res 15, 2787 2801.
    • (1987) Nucleic Acids Res , vol.15 , pp. 2787-2801
    • Bjelland, S.1    Seeberg, E.2
  • 65
    • 0028657625 scopus 로고
    • Purification and biochemical characterization of recombinant N-methylpurine-DNA glycosylase of the mouse
    • Roy R, Brooks C Mitra S (1994) Purification and biochemical characterization of recombinant N-methylpurine-DNA glycosylase of the mouse. Biochemistry 33, 15131 15140.
    • (1994) Biochemistry , vol.33 , pp. 15131-15140
    • Roy, R.1    Brooks, C.2    Mitra, S.3
  • 68
    • 0035997351 scopus 로고    scopus 로고
    • Active site tightness and substrate fit in DNA replication
    • Kool ET (2002) Active site tightness and substrate fit in DNA replication. Annu Rev Biochem 71, 191 219.
    • (2002) Annu Rev Biochem , vol.71 , pp. 191-219
    • Kool, E.T.1
  • 69
    • 0030911133 scopus 로고    scopus 로고
    • Recognition and cleavage of DNA by type-II restriction endonucleases
    • Pingoud A Jeltsch A (1997) Recognition and cleavage of DNA by type-II restriction endonucleases. Eur J Biochem 246, 1 22.
    • (1997) Eur J Biochem , vol.246 , pp. 1-22
    • Pingoud, A.1    Jeltsch, A.2
  • 71
    • 0032497404 scopus 로고    scopus 로고
    • MutY DNA glycosylase: Base release and intermediate complex formation
    • Zharkov DO Grollman AP (1998) MutY DNA glycosylase: base release and intermediate complex formation. Biochemistry 37, 12384 12394.
    • (1998) Biochemistry , vol.37 , pp. 12384-12394
    • Zharkov, D.O.1    Grollman, A.P.2


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