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Volumn 22, Issue 11, 2011, Pages 1022-1029

Susceptibility to intestinal tumorigenesis in folate-deficient mice may be influenced by variation in one-carbon metabolism and DNA repair

Author keywords

Cancer; DNA damage; Folate; Metabolism; One carbon donor; Repair

Indexed keywords

5,10 METHYLENETETRAHYDROFOLATE REDUCTASE (FADH2); CARBON; DNA; DNA GLYCOSYLTRANSFERASE; DNA POLYMERASE; FOLIC ACID; METHIONINE; SERINE;

EID: 80054061671     PISSN: 09552863     EISSN: 18734847     Source Type: Journal    
DOI: 10.1016/j.jnutbio.2010.07.015     Document Type: Article
Times cited : (17)

References (48)
  • 1
    • 34250197957 scopus 로고    scopus 로고
    • Folate and colorectal cancer: an evidence-based critical review
    • Kim Y.I. Folate and colorectal cancer: an evidence-based critical review. Mol Nutr Food Res 2007, 51:267-292.
    • (2007) Mol Nutr Food Res , vol.51 , pp. 267-292
    • Kim, Y.I.1
  • 2
    • 0033007272 scopus 로고    scopus 로고
    • Folate and carcinogenesis: evidence, mechanisms, and implications
    • Kim Y.I. Folate and carcinogenesis: evidence, mechanisms, and implications. J Nutr Biochem 1999, 10:66-88.
    • (1999) J Nutr Biochem , vol.10 , pp. 66-88
    • Kim, Y.I.1
  • 3
    • 0036324027 scopus 로고    scopus 로고
    • Epidemiologic studies of folate and colorectal neoplasia: a review
    • Giovannucci E. Epidemiologic studies of folate and colorectal neoplasia: a review. J Nutr 2002, 132:2350S-2355S.
    • (2002) J Nutr , vol.132
    • Giovannucci, E.1
  • 4
    • 0001912321 scopus 로고    scopus 로고
    • Inherited disorders of folate and cobalamin transport and metabolism
    • McGraw-Hill, Montreal, C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.)
    • Rosenblatt D.S., Fenton W.A. Inherited disorders of folate and cobalamin transport and metabolism. The metabolic and molecular bases of inherited disease 2001, vol. 3:3897-3933. McGraw-Hill, Montreal. C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.).
    • (2001) The metabolic and molecular bases of inherited disease , vol.3 , pp. 3897-3933
    • Rosenblatt, D.S.1    Fenton, W.A.2
  • 5
    • 0029049553 scopus 로고
    • A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase
    • Frosst P., Blom H.J., Milos R., Goyette P., Sheppard C.A., Matthews R.G., et al. A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase. Nat Genet 1995, 10:111-113.
    • (1995) Nat Genet , vol.10 , pp. 111-113
    • Frosst, P.1    Blom, H.J.2    Milos, R.3    Goyette, P.4    Sheppard, C.A.5    Matthews, R.G.6
  • 6
    • 0037444389 scopus 로고    scopus 로고
    • A common variant of the methylenetetrahydrofolate reductase gene (1p36) is associated with an increased risk of cancer
    • Heijmans B.T., Boer J.M., Suchiman H.E., Cornelisse C.J., Westendorp R.G., Kromhout D., et al. A common variant of the methylenetetrahydrofolate reductase gene (1p36) is associated with an increased risk of cancer. Cancer Res 2003, 63:1249-1253.
    • (2003) Cancer Res , vol.63 , pp. 1249-1253
    • Heijmans, B.T.1    Boer, J.M.2    Suchiman, H.E.3    Cornelisse, C.J.4    Westendorp, R.G.5    Kromhout, D.6
  • 7
    • 0035827708 scopus 로고    scopus 로고
    • Heavy chain ferritin enhances serine hydroxymethyltransferase expression and de novo thymidine biosynthesis
    • Oppenheim E.W., Adelman C., Liu X., Stover P.J. Heavy chain ferritin enhances serine hydroxymethyltransferase expression and de novo thymidine biosynthesis. J Biol Chem 2001, 276:19855-19861.
    • (2001) J Biol Chem , vol.276 , pp. 19855-19861
    • Oppenheim, E.W.1    Adelman, C.2    Liu, X.3    Stover, P.J.4
  • 8
    • 0027223085 scopus 로고
    • Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal location
    • Garrow T.A., Brenner A.A., Whitehead V.M., Chen X.N., Duncan R.G., Korenberg J.R., et al. Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal location. J Biol Chem 1993, 268:11910-11916.
    • (1993) J Biol Chem , vol.268 , pp. 11910-11916
    • Garrow, T.A.1    Brenner, A.A.2    Whitehead, V.M.3    Chen, X.N.4    Duncan, R.G.5    Korenberg, J.R.6
  • 9
    • 0025761155 scopus 로고
    • Expression of active domains of a human folate-dependent trifunctional enzyme in Escherichia coli
    • Hum D.W., MacKenzie R.E. Expression of active domains of a human folate-dependent trifunctional enzyme in Escherichia coli. Protein Eng 1991, 4:493-500.
    • (1991) Protein Eng , vol.4 , pp. 493-500
    • Hum, D.W.1    MacKenzie, R.E.2
  • 10
    • 0022378021 scopus 로고
    • NAD-dependent methylenetetrahydrofolate dehydrogenase is expressed by immortal cells
    • Mejia N.R., MacKenzie R.E. NAD-dependent methylenetetrahydrofolate dehydrogenase is expressed by immortal cells. J Biol Chem 1985, 260:14616-14620.
    • (1985) J Biol Chem , vol.260 , pp. 14616-14620
    • Mejia, N.R.1    MacKenzie, R.E.2
  • 11
    • 4444261606 scopus 로고    scopus 로고
    • The expression of mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase supports a role in rapid cell growth
    • Di Pietro E., Wang X.L., MacKenzie R.E. The expression of mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase supports a role in rapid cell growth. Biochim Biophys Acta 2004, 1674:78-84.
    • (2004) Biochim Biophys Acta , vol.1674 , pp. 78-84
    • Di Pietro, E.1    Wang, X.L.2    MacKenzie, R.E.3
  • 12
    • 33745095012 scopus 로고    scopus 로고
    • Mitochondrial one-carbon metabolism is adapted to the specific needs of yeast, plants and mammals
    • Christensen K.E., MacKenzie R.E. Mitochondrial one-carbon metabolism is adapted to the specific needs of yeast, plants and mammals. Bioessays 2006, 28:595-605.
    • (2006) Bioessays , vol.28 , pp. 595-605
    • Christensen, K.E.1    MacKenzie, R.E.2
  • 13
    • 0032570311 scopus 로고    scopus 로고
    • Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes
    • Pawelek P.D., MacKenzie R.E. Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes. Biochem 1998, 37:1109-1115.
    • (1998) Biochem , vol.37 , pp. 1109-1115
    • Pawelek, P.D.1    MacKenzie, R.E.2
  • 14
    • 33751289395 scopus 로고    scopus 로고
    • The molecular dynamics of abnormal folate metabolism and DNA methylation: implications for disease susceptibility and progression
    • Landes Bioscience/Eurekah.com, Texas, P.M. Ueland, R. Rozen (Eds.)
    • James S. The molecular dynamics of abnormal folate metabolism and DNA methylation: implications for disease susceptibility and progression. MTHFR polymorphisms and disease 2004, 78-87. Landes Bioscience/Eurekah.com, Texas. P.M. Ueland, R. Rozen (Eds.).
    • (2004) MTHFR polymorphisms and disease , pp. 78-87
    • James, S.1
  • 16
    • 66849141266 scopus 로고    scopus 로고
    • Polymorphisms in uracil-processing genes, but not one-carbon nutrients, are associated with altered DNA uracil concentrations in an urban Puerto Rican population
    • Chanson A., Parnell L.D., Ciappio E.D., Liu Z., Crott J.W., Tucker K.L., et al. Polymorphisms in uracil-processing genes, but not one-carbon nutrients, are associated with altered DNA uracil concentrations in an urban Puerto Rican population. Am J Clin Nutr 2009, 89:1927-1936.
    • (2009) Am J Clin Nutr , vol.89 , pp. 1927-1936
    • Chanson, A.1    Parnell, L.D.2    Ciappio, E.D.3    Liu, Z.4    Crott, J.W.5    Tucker, K.L.6
  • 17
    • 0035421186 scopus 로고    scopus 로고
    • Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase
    • Nilsen H., Haushalter K.A., Robins P., Barnes D.E., Verdine G.L., Lindahl T. Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase. EMBO J 2001, 20:4278-4286.
    • (2001) EMBO J , vol.20 , pp. 4278-4286
    • Nilsen, H.1    Haushalter, K.A.2    Robins, P.3    Barnes, D.E.4    Verdine, G.L.5    Lindahl, T.6
  • 18
    • 0037115911 scopus 로고    scopus 로고
    • Uracil in DNA - occurrence, consequences and repair
    • Krokan H.E., Drablos F., Slupphaug G. Uracil in DNA - occurrence, consequences and repair. Oncogene 2002, 21:8935-8948.
    • (2002) Oncogene , vol.21 , pp. 8935-8948
    • Krokan, H.E.1    Drablos, F.2    Slupphaug, G.3
  • 19
    • 33751260923 scopus 로고    scopus 로고
    • Low dietary folate initiates intestinal tumors in mice, with altered expression of G2-M checkpoint regulators polo-like kinase 1 and cell division cycle 25c
    • Knock E., Deng L., Wu Q., Leclerc D., Wang X.L., Rozen R. Low dietary folate initiates intestinal tumors in mice, with altered expression of G2-M checkpoint regulators polo-like kinase 1 and cell division cycle 25c. Cancer Res 2006, 66:10349-10356.
    • (2006) Cancer Res , vol.66 , pp. 10349-10356
    • Knock, E.1    Deng, L.2    Wu, Q.3    Leclerc, D.4    Wang, X.L.5    Rozen, R.6
  • 20
    • 41549112569 scopus 로고    scopus 로고
    • Strain differences in mice highlight the role of DNA damage in neoplasia induced by low dietary folate
    • Knock E., Deng L., Wu Q., Lawrance A.K., Wang X.L., Rozen R. Strain differences in mice highlight the role of DNA damage in neoplasia induced by low dietary folate. J Nutr 2008, 138:653-658.
    • (2008) J Nutr , vol.138 , pp. 653-658
    • Knock, E.1    Deng, L.2    Wu, Q.3    Lawrance, A.K.4    Wang, X.L.5    Rozen, R.6
  • 21
    • 29744461120 scopus 로고    scopus 로고
    • Strain differences in the susceptibility to azoxymethane and dextran sodium sulfate-induced colon carcinogenesis in mice
    • Suzuki R., Kohno H., Sugie S., Nakagama H., Tanaka T. Strain differences in the susceptibility to azoxymethane and dextran sodium sulfate-induced colon carcinogenesis in mice. Carcinogenesis 2006, 27:162-169.
    • (2006) Carcinogenesis , vol.27 , pp. 162-169
    • Suzuki, R.1    Kohno, H.2    Sugie, S.3    Nakagama, H.4    Tanaka, T.5
  • 22
    • 0035066175 scopus 로고    scopus 로고
    • Differences in susceptibility to colonic stem cell somatic mutation in three strains of mice
    • Kuraguchi M., Cook H., Williams E.D., Thomas G.A. Differences in susceptibility to colonic stem cell somatic mutation in three strains of mice. J Pathol 2001, 193:517-521.
    • (2001) J Pathol , vol.193 , pp. 517-521
    • Kuraguchi, M.1    Cook, H.2    Williams, E.D.3    Thomas, G.A.4
  • 23
    • 0034662649 scopus 로고    scopus 로고
    • A deficiency in DNA repair and DNA-PKcs expression in the radiosensitive BALB/c mouse
    • Okayasu R., Suetomi K., Yu Y., Silver A., Bedford J.S., Cox R., et al. A deficiency in DNA repair and DNA-PKcs expression in the radiosensitive BALB/c mouse. Cancer Res 2000, 60:4342-4345.
    • (2000) Cancer Res , vol.60 , pp. 4342-4345
    • Okayasu, R.1    Suetomi, K.2    Yu, Y.3    Silver, A.4    Bedford, J.S.5    Cox, R.6
  • 24
    • 2642513835 scopus 로고    scopus 로고
    • Modulation of cystathionine beta-synthase level regulates total serum homocysteine in mice
    • Wang L., Jhee K.H., Hua X., DiBello P.M., Jacobsen D.W., Kruger W.D. Modulation of cystathionine beta-synthase level regulates total serum homocysteine in mice. Circ Res 2004, 94:1318-1324.
    • (2004) Circ Res , vol.94 , pp. 1318-1324
    • Wang, L.1    Jhee, K.H.2    Hua, X.3    DiBello, P.M.4    Jacobsen, D.W.5    Kruger, W.D.6
  • 25
    • 0027981516 scopus 로고
    • Impact of dietary folic acid on reduced folates in mouse plasma and tissues. Relationship to dideazatetrahydrofolate sensitivity
    • Schmitz J.C., Grindey G.B., Schultz R.M., Priest D.G. Impact of dietary folic acid on reduced folates in mouse plasma and tissues. Relationship to dideazatetrahydrofolate sensitivity. Biochem Pharmacol 1994, 48:319-325.
    • (1994) Biochem Pharmacol , vol.48 , pp. 319-325
    • Schmitz, J.C.1    Grindey, G.B.2    Schultz, R.M.3    Priest, D.G.4
  • 26
    • 0029847109 scopus 로고    scopus 로고
    • Severe and mild mutations in cis for the methylenetetrahydrofolate reductase (MTHFR) gene, and description of five novel mutations in MTHFR
    • Goyette P., Christensen B., Rosenblatt D.S., Rozen R. Severe and mild mutations in cis for the methylenetetrahydrofolate reductase (MTHFR) gene, and description of five novel mutations in MTHFR. Am J Hum Genet 1996, 59:1268-1275.
    • (1996) Am J Hum Genet , vol.59 , pp. 1268-1275
    • Goyette, P.1    Christensen, B.2    Rosenblatt, D.S.3    Rozen, R.4
  • 27
    • 34047265849 scopus 로고    scopus 로고
    • Metabolic derangement of methionine and folate metabolism in mice deficient in methionine synthase reductase
    • Elmore C.L., Wu X., Leclerc D., Watson E.D., Bottiglieri T., Krupenko N.I., et al. Metabolic derangement of methionine and folate metabolism in mice deficient in methionine synthase reductase. Mol Genet Metab 2007, 91:85-97.
    • (2007) Mol Genet Metab , vol.91 , pp. 85-97
    • Elmore, C.L.1    Wu, X.2    Leclerc, D.3    Watson, E.D.4    Bottiglieri, T.5    Krupenko, N.I.6
  • 28
    • 33845733594 scopus 로고    scopus 로고
    • SUMO-1-dependent allosteric regulation of thymine DNA glycosylase alters subnuclear localization and CBP/p300 recruitment
    • Mohan R.D., Rao A., Gagliardi J., Tini M. SUMO-1-dependent allosteric regulation of thymine DNA glycosylase alters subnuclear localization and CBP/p300 recruitment. Mol Cell Biol 2007, 27:229-243.
    • (2007) Mol Cell Biol , vol.27 , pp. 229-243
    • Mohan, R.D.1    Rao, A.2    Gagliardi, J.3    Tini, M.4
  • 29
    • 33745438017 scopus 로고    scopus 로고
    • Human methionine synthase reductase is a molecular chaperone for human methionine synthase
    • Yamada K., Gravel R.A., Toraya T., Matthews R.G. Human methionine synthase reductase is a molecular chaperone for human methionine synthase. Proc Natl Acad Sci U S A 2006, 103:9476-9481.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 9476-9481
    • Yamada, K.1    Gravel, R.A.2    Toraya, T.3    Matthews, R.G.4
  • 30
    • 0029805081 scopus 로고    scopus 로고
    • A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase
    • Gallinari P., Jiricny J. A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase. Nature 1996, 383:735-738.
    • (1996) Nature , vol.383 , pp. 735-738
    • Gallinari, P.1    Jiricny, J.2
  • 31
    • 0024541790 scopus 로고
    • In vitro correction of G.T mispairs to G.C pairs in nuclear extracts from human cells
    • Wiebauer K., Jiricny J. In vitro correction of G.T mispairs to G.C pairs in nuclear extracts from human cells. Nature 1989, 339:234-236.
    • (1989) Nature , vol.339 , pp. 234-236
    • Wiebauer, K.1    Jiricny, J.2
  • 32
    • 67649225407 scopus 로고    scopus 로고
    • SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
    • Anderson D.D., Stover P.J. SHMT1 and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis. PLoS One 2009, 4:e5839.
    • (2009) PLoS One , vol.4
    • Anderson, D.D.1    Stover, P.J.2
  • 33
    • 0033532680 scopus 로고    scopus 로고
    • Posttranscriptional regulation of mammalian methionine synthase by B12
    • Gulati S., Brody L.C., Banerjee R. Posttranscriptional regulation of mammalian methionine synthase by B12. Biochem Biophys Res Commun 1999, 259:436-442.
    • (1999) Biochem Biophys Res Commun , vol.259 , pp. 436-442
    • Gulati, S.1    Brody, L.C.2    Banerjee, R.3
  • 34
    • 0042672282 scopus 로고    scopus 로고
    • Vitamin B12 is a strong determinant of low methionine synthase activity and DNA hypomethylation in gastrectomized rats
    • Brunaud L., Alberto J.M., Ayav A., Gerard P., Namour F., Antunes L., et al. Vitamin B12 is a strong determinant of low methionine synthase activity and DNA hypomethylation in gastrectomized rats. Digestion 2003, 68:133-140.
    • (2003) Digestion , vol.68 , pp. 133-140
    • Brunaud, L.1    Alberto, J.M.2    Ayav, A.3    Gerard, P.4    Namour, F.5    Antunes, L.6
  • 35
    • 0030592517 scopus 로고    scopus 로고
    • Lessons from hereditary colorectal cancer
    • Kinzler K.W., Vogelstein B. Lessons from hereditary colorectal cancer. Cell 1996, 87:159-170.
    • (1996) Cell , vol.87 , pp. 159-170
    • Kinzler, K.W.1    Vogelstein, B.2
  • 36
    • 14044269479 scopus 로고    scopus 로고
    • The intracellular localization of APE1/Ref-1: more than a passive phenomenon?
    • Tell G., Damante G., Caldwell D., Kelley M.R. The intracellular localization of APE1/Ref-1: more than a passive phenomenon?. Antioxid Redox Signal 2005, 7:367-384.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 367-384
    • Tell, G.1    Damante, G.2    Caldwell, D.3    Kelley, M.R.4
  • 37
    • 34247581131 scopus 로고    scopus 로고
    • Impaired DNA repair via the base-excision repair pathway after focal ischemic brain injury: a protein phosphorylation-dependent mechanism reversed by hypothermic neuroprotection
    • Luo Y., Ji X., Ling F., Li W., Zhang F., Cao G., et al. Impaired DNA repair via the base-excision repair pathway after focal ischemic brain injury: a protein phosphorylation-dependent mechanism reversed by hypothermic neuroprotection. Front Biosci 2007, 12:1852-1862.
    • (2007) Front Biosci , vol.12 , pp. 1852-1862
    • Luo, Y.1    Ji, X.2    Ling, F.3    Li, W.4    Zhang, F.5    Cao, G.6
  • 38
    • 0033636312 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase (UNG)-deficient mice reveal a primary role of the enzyme during DNA replication
    • Nilsen H., Rosewell I., Robins P., Skjelbred C.F., Andersen S., Slupphaug G., et al. Uracil-DNA glycosylase (UNG)-deficient mice reveal a primary role of the enzyme during DNA replication. Mol Cell 2000, 5:1059-1065.
    • (2000) Mol Cell , vol.5 , pp. 1059-1065
    • Nilsen, H.1    Rosewell, I.2    Robins, P.3    Skjelbred, C.F.4    Andersen, S.5    Slupphaug, G.6
  • 40
    • 70349318664 scopus 로고    scopus 로고
    • Polyamine biosynthesis impacts cellular folate requirements necessary to maintain S-adenosylmethionine and nucleotide pools
    • Bistulfi G., Diegelman P., Foster B.A., Kramer D.L., Porter C.W., Smiraglia D.J. Polyamine biosynthesis impacts cellular folate requirements necessary to maintain S-adenosylmethionine and nucleotide pools. FASEB J 2009, 23:2888-2897.
    • (2009) FASEB J , vol.23 , pp. 2888-2897
    • Bistulfi, G.1    Diegelman, P.2    Foster, B.A.3    Kramer, D.L.4    Porter, C.W.5    Smiraglia, D.J.6
  • 41
    • 0023925454 scopus 로고
    • Interactions between deoxyribonucleotide and DNA synthesis
    • Reichard P. Interactions between deoxyribonucleotide and DNA synthesis. Annu Rev Biochem 1988, 57:349-374.
    • (1988) Annu Rev Biochem , vol.57 , pp. 349-374
    • Reichard, P.1
  • 42
    • 0025676019 scopus 로고
    • Activity of an NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase in normal tissue, neoplastic cells, and oncogene-transformed cells
    • Smith G.K., Banks S.D., Monaco T.J., Rigual R., Duch D.S., Mullin R.J., et al. Activity of an NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase in normal tissue, neoplastic cells, and oncogene-transformed cells. Arch Biochem Biophys 1990, 283:367-371.
    • (1990) Arch Biochem Biophys , vol.283 , pp. 367-371
    • Smith, G.K.1    Banks, S.D.2    Monaco, T.J.3    Rigual, R.4    Duch, D.S.5    Mullin, R.J.6
  • 43
    • 0027500390 scopus 로고
    • NAD(+)-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase: detection of the mRNA in normal murine tissues and transcriptional regulation of the gene in cell lines
    • Peri K.G., MacKenzie R.E. NAD(+)-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase: detection of the mRNA in normal murine tissues and transcriptional regulation of the gene in cell lines. Biochim Biophys Acta 1993, 1171:281-287.
    • (1993) Biochim Biophys Acta , vol.1171 , pp. 281-287
    • Peri, K.G.1    MacKenzie, R.E.2
  • 44
    • 14844297720 scopus 로고    scopus 로고
    • Disruption of the Mthfd1 gene reveals a monofunctional 10-formyltetrahydrofolate synthetase in mammalian mitochondria
    • Christensen K.E., Patel H., Kuzmanov U., Mejia N.R., MacKenzie R.E. Disruption of the Mthfd1 gene reveals a monofunctional 10-formyltetrahydrofolate synthetase in mammalian mitochondria. J Biol Chem 2005, 280:7597-7602.
    • (2005) J Biol Chem , vol.280 , pp. 7597-7602
    • Christensen, K.E.1    Patel, H.2    Kuzmanov, U.3    Mejia, N.R.4    MacKenzie, R.E.5
  • 45
    • 4344701997 scopus 로고    scopus 로고
    • Imbalanced base excision repair in response to folate deficiency is accelerated by polymerase beta haploinsufficiency
    • Cabelof D.C., Raffoul J.J., Nakamura J., Kapoor D., Abdalla H., Heydari A.R. Imbalanced base excision repair in response to folate deficiency is accelerated by polymerase beta haploinsufficiency. J Biol Chem 2004, 279:36504-36513.
    • (2004) J Biol Chem , vol.279 , pp. 36504-36513
    • Cabelof, D.C.1    Raffoul, J.J.2    Nakamura, J.3    Kapoor, D.4    Abdalla, H.5    Heydari, A.R.6
  • 46
    • 0034659762 scopus 로고    scopus 로고
    • Analysis of uracil-DNA glycosylases from the murine Ung gene reveals differential expression in tissues and in embryonic development and a subcellular sorting pattern that differs from the human homologues
    • Nilsen H., Steinsbekk K.S., Otterlei M., Slupphaug G., Aas P.A., Krokan H.E. Analysis of uracil-DNA glycosylases from the murine Ung gene reveals differential expression in tissues and in embryonic development and a subcellular sorting pattern that differs from the human homologues. Nucleic Acids Res 2000, 28:2277-2285.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2277-2285
    • Nilsen, H.1    Steinsbekk, K.S.2    Otterlei, M.3    Slupphaug, G.4    Aas, P.A.5    Krokan, H.E.6


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