메뉴 건너뛰기




Volumn 392, Issue 3, 2009, Pages 602-613

Functional Study of the P32T ITPA Variant Associated with Drug Sensitivity in Humans

Author keywords

base analogs; drug sensitivity; ITPA; nucleotide pools

Indexed keywords

6 N HYDROXYADENINE; INORGANIC PYROPHOSPHATASE; INOSINE TRIPHOSPHATE PYROPHOSPHATASE; PROLINE; PURINE DERIVATIVE; THREONINE; UNCLASSIFIED DRUG;

EID: 69349100176     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.07.051     Document Type: Article
Times cited : (53)

References (63)
  • 1
    • 0000773895 scopus 로고
    • Regulation of amino acid and nucleotide biosynthesis in yeast
    • Strathern J.N., Jones E.W., and Broach J.R. (Eds), Cold Spring Harbor Press, Cold Spring Harbor, NY
    • Jones E.W., and Fink G. Regulation of amino acid and nucleotide biosynthesis in yeast. In: Strathern J.N., Jones E.W., and Broach J.R. (Eds). Molecular Biology of the Yeast Saccharomyces. Metabolism and Gene Expression (1982), Cold Spring Harbor Press, Cold Spring Harbor, NY 181-299
    • (1982) Molecular Biology of the Yeast Saccharomyces. Metabolism and Gene Expression , pp. 181-299
    • Jones, E.W.1    Fink, G.2
  • 3
    • 0038575033 scopus 로고    scopus 로고
    • RdgB acts to avoid chromosome fragmentation in Escherichia coli
    • Bradshaw J.S., and Kuzminov A. RdgB acts to avoid chromosome fragmentation in Escherichia coli. Mol. Microbiol. 48 (2003) 1711-1725
    • (2003) Mol. Microbiol. , vol.48 , pp. 1711-1725
    • Bradshaw, J.S.1    Kuzminov, A.2
  • 4
    • 0038304303 scopus 로고    scopus 로고
    • Repair system for noncanonical purines in Escherichia coli
    • Burgis N.E., Brucker J.J., and Cunningham R.P. Repair system for noncanonical purines in Escherichia coli. J. Bacteriol. 185 (2003) 3101-3110
    • (2003) J. Bacteriol. , vol.185 , pp. 3101-3110
    • Burgis, N.E.1    Brucker, J.J.2    Cunningham, R.P.3
  • 5
    • 0030971874 scopus 로고    scopus 로고
    • Clastogenic activity in the plasma of scleroderma patients: a biomarker of oxidative stress
    • Emerit I., Filipe P., Meunier P., Auclair C., Freitas J., Deroussent A., et al. Clastogenic activity in the plasma of scleroderma patients: a biomarker of oxidative stress. Dermatology 194 (1997) 140-146
    • (1997) Dermatology , vol.194 , pp. 140-146
    • Emerit, I.1    Filipe, P.2    Meunier, P.3    Auclair, C.4    Freitas, J.5    Deroussent, A.6
  • 6
    • 0029941438 scopus 로고    scopus 로고
    • Intracellular targets for nitric oxide toxicity to pancreatic β-cells
    • Delaney C.A., and Eizirik D.L. Intracellular targets for nitric oxide toxicity to pancreatic β-cells. Braz. J. Med. Biol. Res. 29 (1996) 569-579
    • (1996) Braz. J. Med. Biol. Res. , vol.29 , pp. 569-579
    • Delaney, C.A.1    Eizirik, D.L.2
  • 8
    • 33748767935 scopus 로고    scopus 로고
    • Hypoxanthine incorporation is nonmutagenic in Escherichia coli
    • Budke B., and Kuzminov A. Hypoxanthine incorporation is nonmutagenic in Escherichia coli. J. Bacteriol. 188 (2006) 6553-6560
    • (2006) J. Bacteriol. , vol.188 , pp. 6553-6560
    • Budke, B.1    Kuzminov, A.2
  • 9
    • 0032544198 scopus 로고    scopus 로고
    • Misincorporation of 2′-deoxyoxanosine 5′-triphosphate by DNA polymerases and its implication for mutagenesis
    • Suzuki T., Yoshida M., Yamada M., Ide H., Kobayashi M., Kanaori K., et al. Misincorporation of 2′-deoxyoxanosine 5′-triphosphate by DNA polymerases and its implication for mutagenesis. Biochemistry 37 (1998) 11592-11598
    • (1998) Biochemistry , vol.37 , pp. 11592-11598
    • Suzuki, T.1    Yoshida, M.2    Yamada, M.3    Ide, H.4    Kobayashi, M.5    Kanaori, K.6
  • 11
    • 0022993948 scopus 로고
    • Site-specific mutagenesis in vivo by single methylated or deaminated purine bases
    • Hill-Perkins M., Jones M.D., and Karran P. Site-specific mutagenesis in vivo by single methylated or deaminated purine bases. Mutat. Res. 162 (1986) 153-163
    • (1986) Mutat. Res. , vol.162 , pp. 153-163
    • Hill-Perkins, M.1    Jones, M.D.2    Karran, P.3
  • 12
    • 36048950551 scopus 로고    scopus 로고
    • Analyses of PCR products using DNA templates containing a consecutive deoxyinosine sequence
    • Kobayashi A., Kitaoka M., and Hayashi K. Analyses of PCR products using DNA templates containing a consecutive deoxyinosine sequence. Nucleic Acids Symp. Ser. (2004) 225-226
    • (2004) Nucleic Acids Symp. Ser. , pp. 225-226
    • Kobayashi, A.1    Kitaoka, M.2    Hayashi, K.3
  • 13
    • 0242380643 scopus 로고    scopus 로고
    • Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V
    • Moe A., Ringvoll J., Nordstrand L.M., Eide L., Bjoras M., Seeberg E., et al. Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V. Nucleic Acids Res. 31 (2003) 3893-3900
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3893-3900
    • Moe, A.1    Ringvoll, J.2    Nordstrand, L.M.3    Eide, L.4    Bjoras, M.5    Seeberg, E.6
  • 14
    • 0037440169 scopus 로고    scopus 로고
    • Mutagenic potentials of damaged nucleic acids produced by reactive oxygen/nitrogen species: approaches using synthetic oligonucleotides and nucleotides: survey and summary
    • Kamiya H. Mutagenic potentials of damaged nucleic acids produced by reactive oxygen/nitrogen species: approaches using synthetic oligonucleotides and nucleotides: survey and summary. Nucleic Acids Res. 31 (2003) 517-531
    • (2003) Nucleic Acids Res. , vol.31 , pp. 517-531
    • Kamiya, H.1
  • 15
    • 33644783699 scopus 로고    scopus 로고
    • Chromosomal fragmentation is the major consequence of the rdgB defect in Escherichia coli
    • Lukas L., and Kuzminov A. Chromosomal fragmentation is the major consequence of the rdgB defect in Escherichia coli. Genetics 172 (2006) 1359-1362
    • (2006) Genetics , vol.172 , pp. 1359-1362
    • Lukas, L.1    Kuzminov, A.2
  • 16
    • 0032543424 scopus 로고    scopus 로고
    • Multiple antimutagenesis mechanisms affect mutagenic activity and specificity of the base analog 6-N-hydroxylaminopurine in bacteria and yeast
    • Kozmin S.G., Schaaper R.M., Shcherbakova P.V., Kulikov V.N., Noskov V.N., Guetsova M.L., et al. Multiple antimutagenesis mechanisms affect mutagenic activity and specificity of the base analog 6-N-hydroxylaminopurine in bacteria and yeast. Mutat. Res. 402 (1998) 41-50
    • (1998) Mutat. Res. , vol.402 , pp. 41-50
    • Kozmin, S.G.1    Schaaper, R.M.2    Shcherbakova, P.V.3    Kulikov, V.N.4    Noskov, V.N.5    Guetsova, M.L.6
  • 17
    • 34047247010 scopus 로고    scopus 로고
    • Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T
    • Stenmark P., Kursula P., Flodin S., Graslund S., Landry R., Nordlund P., and Schuler H. Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T. J. Biol. Chem. 282 (2007) 3182-3187
    • (2007) J. Biol. Chem. , vol.282 , pp. 3182-3187
    • Stenmark, P.1    Kursula, P.2    Flodin, S.3    Graslund, S.4    Landry, R.5    Nordlund, P.6    Schuler, H.7
  • 18
    • 17444452114 scopus 로고
    • [Mutants of Saccharomyces cerevisiae supersensitive to the mutagenic effect of 6-N-hydroxylaminopurine]
    • Pavlov Iu I. [Mutants of Saccharomyces cerevisiae supersensitive to the mutagenic effect of 6-N-hydroxylaminopurine]. Genetika 22 (1986) 2235-2243
    • (1986) Genetika , vol.22 , pp. 2235-2243
    • Pavlov Iu, I.1
  • 19
    • 0030068703 scopus 로고    scopus 로고
    • HAM1, the gene controlling 6-N-hydroxylaminopurine sensitivity and mutagenesis in the yeast Saccharomyces cerevisiae
    • Noskov V.N., Staak K., Shcherbakova P.V., Kozmin S.G., Negishi K., Ono B.C., et al. HAM1, the gene controlling 6-N-hydroxylaminopurine sensitivity and mutagenesis in the yeast Saccharomyces cerevisiae. Yeast 12 (1996) 17-29
    • (1996) Yeast , vol.12 , pp. 17-29
    • Noskov, V.N.1    Staak, K.2    Shcherbakova, P.V.3    Kozmin, S.G.4    Negishi, K.5    Ono, B.C.6
  • 20
    • 0023405085 scopus 로고
    • Escherichia coli K-12 mutants in which viability is dependent on recA function
    • Clyman J., and Cunningham R.P. Escherichia coli K-12 mutants in which viability is dependent on recA function. J. Bacteriol. 169 (1987) 4203-4210
    • (1987) J. Bacteriol. , vol.169 , pp. 4203-4210
    • Clyman, J.1    Cunningham, R.P.2
  • 21
    • 0034129708 scopus 로고    scopus 로고
    • Hypersensitivity of Escherichia coli D(uvrB-bio) mutants to 6-hydroxylaminopurine and other base analogs is due to a defect in molybdenum cofactor biosynthesis
    • Kozmin S.G., Pavlov Y.I., Dunn R.L., and Schaaper R.M. Hypersensitivity of Escherichia coli D(uvrB-bio) mutants to 6-hydroxylaminopurine and other base analogs is due to a defect in molybdenum cofactor biosynthesis. J. Bacteriol. 182 (2000) 3361-3367
    • (2000) J. Bacteriol. , vol.182 , pp. 3361-3367
    • Kozmin, S.G.1    Pavlov, Y.I.2    Dunn, R.L.3    Schaaper, R.M.4
  • 22
    • 40549106101 scopus 로고    scopus 로고
    • YcbX and yiiM, two novel determinants for resistance of Escherichia coli to N-hydroxylated base analogues
    • Kozmin S.G., Leroy P., Pavlov Y.I., and Schaaper R.M. YcbX and yiiM, two novel determinants for resistance of Escherichia coli to N-hydroxylated base analogues. Mol. Microbiol. 68 (2008) 51-65
    • (2008) Mol. Microbiol. , vol.68 , pp. 51-65
    • Kozmin, S.G.1    Leroy, P.2    Pavlov, Y.I.3    Schaaper, R.M.4
  • 23
    • 17444398048 scopus 로고    scopus 로고
    • Structure-based identification of a novel NTPase from Methanococcus jannaschii
    • Hwang K.Y., Chung J.H., Kim S.H., Han Y.S., and Cho Y. Structure-based identification of a novel NTPase from Methanococcus jannaschii. Nat. Struct. Biol. 6 (1999) 691-696
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 691-696
    • Hwang, K.Y.1    Chung, J.H.2    Kim, S.H.3    Han, Y.S.4    Cho, Y.5
  • 24
    • 0035879027 scopus 로고    scopus 로고
    • Biochemical characterization of a novel hypoxanthine/xanthine dNTP pyrophosphatase from Methanococcus jannaschii
    • Chung J.H., Back J.H., Park Y.I., and Han Y.S. Biochemical characterization of a novel hypoxanthine/xanthine dNTP pyrophosphatase from Methanococcus jannaschii. Nucleic Acids Res. 29 (2001) 3099-3107
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3099-3107
    • Chung, J.H.1    Back, J.H.2    Park, Y.I.3    Han, Y.S.4
  • 25
    • 0035379753 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene
    • Lin S., McLennan A.G., Ying K., Wang Z., Gu S., Jin H., et al. Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene. J. Biol. Chem. 276 (2001) 18695-18701
    • (2001) J. Biol. Chem. , vol.276 , pp. 18695-18701
    • Lin, S.1    McLennan, A.G.2    Ying, K.3    Wang, Z.4    Gu, S.5    Jin, H.6
  • 26
    • 18244379589 scopus 로고    scopus 로고
    • Characterization of the structure and expression of mouse Itpa gene and its related sequences in the mouse genome
    • Behmanesh M., Sakumi K., Tsuchimoto D., Torisu K., Ohnishi-Honda Y., Rancourt D.E., and Nakabeppu Y. Characterization of the structure and expression of mouse Itpa gene and its related sequences in the mouse genome. DNA Res. 12 (2005) 39-51
    • (2005) DNA Res. , vol.12 , pp. 39-51
    • Behmanesh, M.1    Sakumi, K.2    Tsuchimoto, D.3    Torisu, K.4    Ohnishi-Honda, Y.5    Rancourt, D.E.6    Nakabeppu, Y.7
  • 27
    • 26444502629 scopus 로고    scopus 로고
    • Identification of an ITPase/XTPase in Escherichia coli by structural and biochemical analysis
    • Zheng J., Singh V.K., and Jia Z. Identification of an ITPase/XTPase in Escherichia coli by structural and biochemical analysis. Structure 13 (2005) 1511-1520
    • (2005) Structure , vol.13 , pp. 1511-1520
    • Zheng, J.1    Singh, V.K.2    Jia, Z.3
  • 28
    • 33947518805 scopus 로고    scopus 로고
    • Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase
    • Burgis N.E., and Cunningham R.P. Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase. J. Biol. Chem. 282 (2007) 3531-3538
    • (2007) J. Biol. Chem. , vol.282 , pp. 3531-3538
    • Burgis, N.E.1    Cunningham, R.P.2
  • 29
    • 8644227618 scopus 로고    scopus 로고
    • Distribution of ITPA P32T alleles in multiple world populations
    • Marsh S., King C.R., Ahluwalia R., and McLeod H.L. Distribution of ITPA P32T alleles in multiple world populations. J. Hum. Genet. 49 (2004) 579-581
    • (2004) J. Hum. Genet. , vol.49 , pp. 579-581
    • Marsh, S.1    King, C.R.2    Ahluwalia, R.3    McLeod, H.L.4
  • 31
    • 0036952564 scopus 로고    scopus 로고
    • DNA polymorphisms in ITPA including basis of inosine triphosphatase deficiency
    • Cao H., and Hegele R.A. DNA polymorphisms in ITPA including basis of inosine triphosphatase deficiency. J. Hum. Genet. 47 (2002) 620-622
    • (2002) J. Hum. Genet. , vol.47 , pp. 620-622
    • Cao, H.1    Hegele, R.A.2
  • 33
    • 31844455940 scopus 로고    scopus 로고
    • Measurement of erythrocyte inosine triphosphate pyrophosphohydrolase (ITPA) activity by HPLC and correlation of ITPA genotype-phenotype in a Caucasian population
    • Shipkova M., Lorenz K., Oellerich M., Wieland E., and von Ahsen N. Measurement of erythrocyte inosine triphosphate pyrophosphohydrolase (ITPA) activity by HPLC and correlation of ITPA genotype-phenotype in a Caucasian population. Clin. Chem. 52 (2006) 240-247
    • (2006) Clin. Chem. , vol.52 , pp. 240-247
    • Shipkova, M.1    Lorenz, K.2    Oellerich, M.3    Wieland, E.4    von Ahsen, N.5
  • 34
    • 33845666273 scopus 로고    scopus 로고
    • The ITPA c.94C>A and g.IVS2+21A>C sequence variants contribute to missplicing of the ITPA gene
    • Arenas M., Duley J., Sumi S., Sanderson J., and Marinaki A. The ITPA c.94C>A and g.IVS2+21A>C sequence variants contribute to missplicing of the ITPA gene. Biochim. Biophys. Acta 1772 (2007) 96-102
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 96-102
    • Arenas, M.1    Duley, J.2    Sumi, S.3    Sanderson, J.4    Marinaki, A.5
  • 35
    • 38549151340 scopus 로고    scopus 로고
    • Characterization of the inosine triphosphatase (ITPA) gene: haplotype structure, haplotype-phenotype correlation and promoter function
    • von Ahsen N., Oellerich M., and Armstrong V.W. Characterization of the inosine triphosphatase (ITPA) gene: haplotype structure, haplotype-phenotype correlation and promoter function. Ther. Drug Monit. 30 (2008) 16-22
    • (2008) Ther. Drug Monit. , vol.30 , pp. 16-22
    • von Ahsen, N.1    Oellerich, M.2    Armstrong, V.W.3
  • 36
    • 12144285961 scopus 로고    scopus 로고
    • Adverse drug reactions to azathioprine therapy are associated with polymorphism in the gene encoding inosine triphosphate pyrophosphatase (ITPase)
    • Marinaki A.M., Ansari A., Duley J.A., Arenas M., Sumi S., Lewis C.M., et al. Adverse drug reactions to azathioprine therapy are associated with polymorphism in the gene encoding inosine triphosphate pyrophosphatase (ITPase). Pharmacogenetics 14 (2004) 181-187
    • (2004) Pharmacogenetics , vol.14 , pp. 181-187
    • Marinaki, A.M.1    Ansari, A.2    Duley, J.A.3    Arenas, M.4    Sumi, S.5    Lewis, C.M.6
  • 38
    • 28044446081 scopus 로고    scopus 로고
    • Association of inosine triphosphatase 94C>A and thiopurine S-methyltransferase deficiency with adverse events and study drop-outs under azathioprine therapy in a prospective Crohn disease study
    • von Ahsen N., Armstrong V.W., Behrens C., von Tirpitz C., Stallmach A., Herfarth H., et al. Association of inosine triphosphatase 94C>A and thiopurine S-methyltransferase deficiency with adverse events and study drop-outs under azathioprine therapy in a prospective Crohn disease study. Clin. Chem. 51 (2005) 2282-2288
    • (2005) Clin. Chem. , vol.51 , pp. 2282-2288
    • von Ahsen, N.1    Armstrong, V.W.2    Behrens, C.3    von Tirpitz, C.4    Stallmach, A.5    Herfarth, H.6
  • 39
    • 31144446293 scopus 로고    scopus 로고
    • Inosine triphosphate pyrophosphatase and thiopurine S-methyltransferase genotypes relationship to azathioprine-induced myelosuppression
    • Zelinkova Z., Derijks L.J., Stokkers P.C., Vogels E.W., van Kampen A.H., Curvers W., et al. Inosine triphosphate pyrophosphatase and thiopurine S-methyltransferase genotypes relationship to azathioprine-induced myelosuppression. Clin. Gastroenterol. Hepatol. 4 (2006) 44-49
    • (2006) Clin. Gastroenterol. Hepatol. , vol.4 , pp. 44-49
    • Zelinkova, Z.1    Derijks, L.J.2    Stokkers, P.C.3    Vogels, E.W.4    van Kampen, A.H.5    Curvers, W.6
  • 40
    • 58449117037 scopus 로고    scopus 로고
    • Genetic polymorphism of inosine triphosphate pyrophosphatase is a determinant of mercaptopurine metabolism and toxicity during treatment for acute lymphoblastic leukemia
    • Stocco G., Cheok M.H., Crews K.R., Dervieux T., French D., Pei D., et al. Genetic polymorphism of inosine triphosphate pyrophosphatase is a determinant of mercaptopurine metabolism and toxicity during treatment for acute lymphoblastic leukemia. Clin. Pharmacol. Ther. 85 (2009) 164-172
    • (2009) Clin. Pharmacol. Ther. , vol.85 , pp. 164-172
    • Stocco, G.1    Cheok, M.H.2    Crews, K.R.3    Dervieux, T.4    French, D.5    Pei, D.6
  • 41
    • 27444437058 scopus 로고    scopus 로고
    • ITPA genotyping is not predictive for the development of side effects in AZA treated inflammatory bowel disease patients
    • van Dieren J.M., van Vuuren A.J., Kusters J.G., Nieuwenhuis E.E., Kuipers E.J., and van der Woude C.J. ITPA genotyping is not predictive for the development of side effects in AZA treated inflammatory bowel disease patients. Gut 54 (2005) 1664
    • (2005) Gut , vol.54 , pp. 1664
    • van Dieren, J.M.1    van Vuuren, A.J.2    Kusters, J.G.3    Nieuwenhuis, E.E.4    Kuipers, E.J.5    van der Woude, C.J.6
  • 42
    • 33745489615 scopus 로고    scopus 로고
    • Do ITPA and TPMT genotypes predict the development of side effects to AZA?
    • Duley J.A., Marinaki A.M., Arenas M., and Florin T.H. Do ITPA and TPMT genotypes predict the development of side effects to AZA?. Gut 55 (2006) 1048-1049
    • (2006) Gut , vol.55 , pp. 1048-1049
    • Duley, J.A.1    Marinaki, A.M.2    Arenas, M.3    Florin, T.H.4
  • 43
    • 70349174735 scopus 로고    scopus 로고
    • ITPase-deficient mice show growth retardation and die before weaning
    • in press. Epub June 5, doi:10.1038/cdd.2009.53
    • Behmanesh, M., Sakumi, K., Abolhassani, N., Toyokuni, S., Oka, S., Ohnishi, Y. N. et al. (2009). ITPase-deficient mice show growth retardation and die before weaning. Cell Death Differ., in press. Epub June 5, 2009. doi:10.1038/cdd.2009.53.
    • (2009) Cell Death Differ
    • Behmanesh, M.1    Sakumi, K.2    Abolhassani, N.3    Toyokuni, S.4    Oka, S.5    Ohnishi, Y.N.6
  • 45
    • 0032248193 scopus 로고    scopus 로고
    • Overexpression of the yeast HAM1 gene prevents 6-N-hydroxylaminopurine mutagenesis in Escherichia coli
    • Kozmin S.G., Leroy P., and Pavlov Y.I. Overexpression of the yeast HAM1 gene prevents 6-N-hydroxylaminopurine mutagenesis in Escherichia coli. Acta Biochim. Pol. 45 (1998) 645-652
    • (1998) Acta Biochim. Pol. , vol.45 , pp. 645-652
    • Kozmin, S.G.1    Leroy, P.2    Pavlov, Y.I.3
  • 46
    • 34247091997 scopus 로고    scopus 로고
    • Molybdenum cofactor-dependent resistance to N-hydroxylated base analogs in Escherichia coli is independent of MobA function
    • Kozmin S.G., and Schaaper R.M. Molybdenum cofactor-dependent resistance to N-hydroxylated base analogs in Escherichia coli is independent of MobA function. Mutat. Res. 619 (2007) 9-15
    • (2007) Mutat. Res. , vol.619 , pp. 9-15
    • Kozmin, S.G.1    Schaaper, R.M.2
  • 47
    • 0025902273 scopus 로고
    • Endogenous mutagens and the causes of aging and cancer
    • Ames B.N., and Gold L.S. Endogenous mutagens and the causes of aging and cancer. Mutat. Res. 250 (1991) 3-16
    • (1991) Mutat. Res. , vol.250 , pp. 3-16
    • Ames, B.N.1    Gold, L.S.2
  • 48
    • 0027324378 scopus 로고
    • Mutagenesis by 8-oxoguanine: an enemy within
    • Grollman A.P., and Moriya M. Mutagenesis by 8-oxoguanine: an enemy within. Trends Genet. 9 (1993) 246-249
    • (1993) Trends Genet. , vol.9 , pp. 246-249
    • Grollman, A.P.1    Moriya, M.2
  • 49
    • 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., and 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
  • 50
    • 0016176530 scopus 로고
    • Errors in DNA replication as a basis of malignant changes
    • Loeb L.A., Springgate C.F., and Battula N. Errors in DNA replication as a basis of malignant changes. Cancer Res. 34 (1974) 2311-2321
    • (1974) Cancer Res. , vol.34 , pp. 2311-2321
    • Loeb, L.A.1    Springgate, C.F.2    Battula, N.3
  • 51
    • 0031953260 scopus 로고    scopus 로고
    • The mutation rate and cancer
    • Jackson A.L., and Loeb L.A. The mutation rate and cancer. Genetics 148 (1998) 1483-1490
    • (1998) Genetics , vol.148 , pp. 1483-1490
    • Jackson, A.L.1    Loeb, L.A.2
  • 52
    • 0035796023 scopus 로고    scopus 로고
    • The contribution of endogenous sources of DNA damage to the multiple mutations in cancer
    • Jackson A.L., and Loeb L.A. The contribution of endogenous sources of DNA damage to the multiple mutations in cancer. Mutat. Res. 477 (2001) 7-21
    • (2001) Mutat. Res. , vol.477 , pp. 7-21
    • Jackson, A.L.1    Loeb, L.A.2
  • 53
    • 0037018846 scopus 로고    scopus 로고
    • The mammalian mismatch repair pathway removes DNA 8-oxodGMP incorporated from the oxidized dNTP pool
    • Colussi C., Parlanti E., Degan P., Aquilina G., Barnes D., Macpherson P., et al. The mammalian mismatch repair pathway removes DNA 8-oxodGMP incorporated from the oxidized dNTP pool. Curr. Biol. 12 (2002) 912-918
    • (2002) Curr. Biol. , vol.12 , pp. 912-918
    • Colussi, C.1    Parlanti, E.2    Degan, P.3    Aquilina, G.4    Barnes, D.5    Macpherson, P.6
  • 54
    • 1042298162 scopus 로고    scopus 로고
    • Reactive nitrogen species in the chemical biology of inflammation
    • Dedon P.C., and Tannenbaum S.R. Reactive nitrogen species in the chemical biology of inflammation. Arch. Biochem. Biophys. 423 (2004) 12-22
    • (2004) Arch. Biochem. Biophys. , vol.423 , pp. 12-22
    • Dedon, P.C.1    Tannenbaum, S.R.2
  • 55
    • 0141639848 scopus 로고    scopus 로고
    • Effect of increased tea consumption on oxidative DNA damage among smokers: a randomized controlled study
    • Hakim I.A., Harris R.B., Brown S., Chow H.H., Wiseman S., Agarwal S., and Talbot W. Effect of increased tea consumption on oxidative DNA damage among smokers: a randomized controlled study. J. Nutr. 133 (2003) 3303S-3309S
    • (2003) J. Nutr. , vol.133
    • Hakim, I.A.1    Harris, R.B.2    Brown, S.3    Chow, H.H.4    Wiseman, S.5    Agarwal, S.6    Talbot, W.7
  • 56
    • 0041368543 scopus 로고    scopus 로고
    • Cigarette smoking cessation increases plasma levels of several antioxidant micronutrients and improves resistance towards oxidative challenge
    • Polidori M.C., Mecocci P., Stahl W., and Sies H. Cigarette smoking cessation increases plasma levels of several antioxidant micronutrients and improves resistance towards oxidative challenge. Br. J. Nutr. 90 (2003) 147-150
    • (2003) Br. J. Nutr. , vol.90 , pp. 147-150
    • Polidori, M.C.1    Mecocci, P.2    Stahl, W.3    Sies, H.4
  • 57
    • 0032532285 scopus 로고    scopus 로고
    • Oxidation of DNA bases, deoxyribonucleosides and homopolymers by peroxyl radicals
    • Simandan T., Sun J., and 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
  • 58
    • 0037115963 scopus 로고    scopus 로고
    • Oxidative nucleotide damage: consequences and prevention
    • Sekiguchi M., and Tsuzuki T. Oxidative nucleotide damage: consequences and prevention. Oncogene 21 (2002) 8895-8904
    • (2002) Oncogene , vol.21 , pp. 8895-8904
    • Sekiguchi, M.1    Tsuzuki, T.2
  • 60
    • 33847255546 scopus 로고    scopus 로고
    • How to use dynamic light scattering to improve the likelihood of growing macromolecular crystals
    • Borgstahl G.E. How to use dynamic light scattering to improve the likelihood of growing macromolecular crystals. Methods Mol. Biol. 363 (2007) 109-129
    • (2007) Methods Mol. Biol. , vol.363 , pp. 109-129
    • Borgstahl, G.E.1
  • 61
    • 69349096327 scopus 로고    scopus 로고
    • Characterization of high-molecular-weight nonnative aggregates and aggregation kinetics by size exclusion chromatography with inline multi-angle laser light scattering
    • Li Y., Weiss W.F.t., and Roberts C.J. Characterization of high-molecular-weight nonnative aggregates and aggregation kinetics by size exclusion chromatography with inline multi-angle laser light scattering. J. Pharm. Sci. 12 (2009) 12
    • (2009) J. Pharm. Sci. , vol.12 , pp. 12
    • Li, Y.1    Weiss, W.F.t.2    Roberts, C.J.3
  • 63
    • 25444478897 scopus 로고    scopus 로고
    • Genome-wide screening for genes whose deletions confer sensitivity to mutagenic purine base analogs in yeast
    • Stepchenkova E.I., Kozmin S.G., Alenin V.V., and Pavlov Y.I. Genome-wide screening for genes whose deletions confer sensitivity to mutagenic purine base analogs in yeast. BMC Genet. 6 (2005) 31
    • (2005) BMC Genet. , vol.6 , pp. 31
    • Stepchenkova, E.I.1    Kozmin, S.G.2    Alenin, V.V.3    Pavlov, Y.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.