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Volumn 39, Issue 4, 2011, Pages 1473-1484

A discontinuous DNA glycosylase domain in a family of enzymes that excise 5-methylcytosine

Author keywords

[No Author keywords available]

Indexed keywords

5 METHYLCYTOSINE; ARABIDOPSIS PROTEIN; ASPARAGINE; ASPARTIC ACID; DNA GLYCOSYLTRANSFERASE; GLUTAMINE; PHENYLALANINE; REPRESSOR OF SILENCING 1 PROTEIN; THREONINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 79952322214     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq982     Document Type: Article
Times cited : (24)

References (61)
  • 1
    • 77952355762 scopus 로고    scopus 로고
    • Genome-wide evolutionary analysis of eukaryotic DNA methylation
    • Zemach, A., McDaniel, I.E., Silva, P. and Zilberman, D. (2010) Genome-wide evolutionary analysis of eukaryotic DNA methylation. Science, 328, 916-919.
    • (2010) Science , vol.328 , pp. 916-919
    • Zemach, A.1    McDaniel, I.E.2    Silva, P.3    Zilberman, D.4
  • 4
    • 73349104113 scopus 로고    scopus 로고
    • Active DNA demethylation mediated by DNA glycosylases
    • Zhu, J.K. (2009) Active DNA demethylation mediated by DNA glycosylases. Annu. Rev. Genet., 43, 143-166.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 143-166
    • Zhu, J.K.1
  • 5
    • 22844457491 scopus 로고    scopus 로고
    • DNA methylation and human disease
    • DOI 10.1038/nrg1655
    • Robertson, K.D. (2005) DNA methylation and human disease. Nat. Rev. Genet., 6, 597-610. (Pubitemid 41044297)
    • (2005) Nature Reviews Genetics , vol.6 , Issue.8 , pp. 597-610
    • Robertson, K.D.1
  • 6
    • 33947315736 scopus 로고    scopus 로고
    • Cancer epigenomics: DNA methylomes and histone-modification maps
    • DOI 10.1038/nrg2005, PII NRG2005
    • Esteller, M. (2007) Cancer epigenomics: DNA methylomes and histone-modification maps. Nat. Rev. Genet., 8, 286-298. (Pubitemid 46439286)
    • (2007) Nature Reviews Genetics , vol.8 , Issue.4 , pp. 286-298
    • Esteller, M.1
  • 7
    • 34249279527 scopus 로고    scopus 로고
    • Stability and flexibility of epigenetic gene regulation in mammalian development
    • DOI 10.1038/nature05918, PII NATURE05918
    • Reik, W. (2007) Stability and flexibility of epigenetic gene regulation in mammalian development. Nature, 447, 425-432. (Pubitemid 46816749)
    • (2007) Nature , vol.447 , Issue.7143 , pp. 425-432
    • Reik, W.1
  • 8
    • 0037074009 scopus 로고    scopus 로고
    • ROS1, a repressor of transcriptional gene silencing in Arabidopsis, encodes a DNA glycosylase/lyase
    • DOI 10.1016/S0092-8674(02)01133-9
    • Gong, Z., Morales-Ruiz, T., Ariza, R.R., Roldan-Arjona, T., David, L. and Zhu, J.K. (2002) ROS1, a repressor of transcriptional gene silencing in Arabidopsis, encodes a DNA glycosylase/lyase. Cell, 111, 803-814. (Pubitemid 36106402)
    • (2002) Cell , vol.111 , Issue.6 , pp. 803-814
    • Gong, Z.1    Morales-Ruiz, T.2    Ariza, R.R.3    Roldan-Arjona, T.4    David, L.5    Zhu, J.-K.6
  • 9
    • 0037067658 scopus 로고    scopus 로고
    • DEMETER, a DNA glycosylase domain protein, is required for endosperm gene imprinting and seed viability in Arabidopsis
    • DOI 10.1016/S0092-8674(02)00807-3
    • Choi, Y., Gehring, M., Johnson, L., Hannon, M., Harada, J.J., Goldberg, R.B., Jacobsen, S.E. and Fischer, R.L. (2002) DEMETER, a DNA glycosylase domain protein, is required for endosperm gene imprinting and seed viability in Arabidopsis. Cell, 110, 33-42. (Pubitemid 34874604)
    • (2002) Cell , vol.110 , Issue.1 , pp. 33-42
    • Choi, Y.1    Gehring, M.2    Johnson, L.3    Hannon, M.4    Harada, J.J.5    Goldberg, R.B.6    Jacobsen, S.E.7    Fischer, R.L.8
  • 11
    • 32044470027 scopus 로고    scopus 로고
    • DEMETER DNA glycosylase establishes MEDEA polycomb gene self-imprinting by allele-specific demethylation
    • DOI 10.1016/j.cell.2005.12.034, PII S0092867406000687
    • Gehring, M., Huh, J.H., Hsieh, T.F., Penterman, J., Choi, Y., Harada, J.J., Goldberg, R.B. and Fischer, R.L. (2006) DEMETER DNA glycosylase establishes MEDEA polycomb gene self-imprinting by allele-specific demethylation. Cell, 124, 495-506. (Pubitemid 43199436)
    • (2006) Cell , vol.124 , Issue.3 , pp. 495-506
    • Gehring, M.1    Huh, J.H.2    Hsieh, T.-F.3    Penterman, J.4    Choi, Y.5    Harada, J.J.6    Goldberg, R.B.7    Fischer, R.L.8
  • 14
    • 46249125864 scopus 로고    scopus 로고
    • Arabidopsis DEMETER-LIKE proteins DML2 and DML3 are required for appropriate distribution of DNA methylation marks
    • Ortega-Galisteo, A.P., Morales-Ruiz, T., Ariza, R.R. and Roldan-Arjona, T. (2008) Arabidopsis DEMETER-LIKE proteins DML2 and DML3 are required for appropriate distribution of DNA methylation marks. Plant Mol. Biol., 67, 671-681.
    • (2008) Plant Mol. Biol. , vol.67 , pp. 671-681
    • Ortega-Galisteo, A.P.1    Morales-Ruiz, T.2    Ariza, R.R.3    Roldan-Arjona, T.4
  • 15
    • 33845866061 scopus 로고    scopus 로고
    • The DNA Glycosylase/Lyase ROS1 Functions in Pruning DNA Methylation Patterns in Arabidopsis
    • DOI 10.1016/j.cub.2006.10.059, PII S0960982206024341
    • Zhu, J., Kapoor, A., Sridhar, V.V., Agius, F. and Zhu, J.K. (2007) The DNA glycosylase/lyase ROS1 functions in pruning DNA methylation patterns in Arabidopsis. Curr. Biol., 17, 54-59. (Pubitemid 46027567)
    • (2007) Current Biology , vol.17 , Issue.1 , pp. 54-59
    • Zhu, J.1    Kapoor, A.2    Sridhar, V.V.3    Agius, F.4    Zhu, J.-K.5
  • 17
    • 67149086996 scopus 로고    scopus 로고
    • Extensive demethylation of repetitive elements during seed development underlies gene imprinting
    • Gehring, M., Bubb, K.L. and Henikoff, S. (2009) Extensive demethylation of repetitive elements during seed development underlies gene imprinting. Science, 324, 1447-1451.
    • (2009) Science , vol.324 , pp. 1447-1451
    • Gehring, M.1    Bubb, K.L.2    Henikoff, S.3
  • 18
    • 1642515876 scopus 로고    scopus 로고
    • One-Way Control of FWA Imprinting in Arabidopsis Endosperm by DNA Methylation
    • DOI 10.1126/science.1089835
    • Kinoshita, T., Miura, A., Choi, Y., Kinoshita, Y., Cao, X., Jacobsen, S.E., Fischer, R.L. and Kakutani, T. (2004) One-way control of FWA imprinting in Arabidopsis endosperm by DNA methylation. Science, 303, 521-523. (Pubitemid 38120849)
    • (2004) Science , vol.303 , Issue.5657 , pp. 521-523
    • Kinoshita, T.1    Miura, A.2    Choi, Y.3    Kinoshita, Y.4    Cao, X.5    Jacobsen, S.E.6    Fischer, R.L.7    Kakutani, T.8
  • 19
    • 0030220956 scopus 로고    scopus 로고
    • Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily
    • DOI 10.1016/S0960-9822(02)00641-3
    • Nash, H.M., Bruner, S.D., Scharer, O.D., Kawate, T., Addona, T.A., Spooner, E., Lane, W.S. and Verdine, G.L. (1996) Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily. Curr. Biol., 6, 968-980. (Pubitemid 26350717)
    • (1996) Current Biology , vol.6 , Issue.8 , pp. 968-980
    • Nash, H.M.1    Bruner, S.D.2    Scharer, O.D.3    Kawate, T.4    Addona, T.A.5    Spooner, E.6    Lane, W.S.7    Verdine, G.L.8
  • 20
    • 77954938544 scopus 로고    scopus 로고
    • Methylation-independent DNA binding modulates specificity of repressor of silencing 1 (ROS1) and facilitates demethylation in long substrates
    • Ponferrada-Marin, M.I., Martinez-Macias, M.I., Morales-Ruiz, T., Roldan-Arjona, T. and Ariza, R.R. (2010) Methylation-independent DNA binding modulates specificity of repressor of silencing 1 (ROS1) and facilitates demethylation in long substrates. J. Biol. Chem., 285, 23032-23039.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23032-23039
    • Ponferrada-Marin, M.I.1    Martinez-Macias, M.I.2    Morales-Ruiz, T.3    Roldan-Arjona, T.4    Ariza, R.R.5
  • 21
    • 67949118893 scopus 로고    scopus 로고
    • ROS1 5-methylcytosine DNA glycosylase is a slow-turnover catalyst that initiates DNA demethylation in a distributive fashion
    • Ponferrada-Marin, M.I., Roldan-Arjona, T. and Ariza, R.R. (2009) ROS1 5-methylcytosine DNA glycosylase is a slow-turnover catalyst that initiates DNA demethylation in a distributive fashion. Nucleic Acids Res., 37, 4264-4274.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 4264-4274
    • Ponferrada-Marin, M.I.1    Roldan-Arjona, T.2    Ariza, R.R.3
  • 23
  • 24
    • 0043123123 scopus 로고    scopus 로고
    • Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments
    • DOI 10.1093/nar/gkg522
    • Poirot, O., O'Toole, E. and Notredame, C. (2003) Tcoffee@igs: a web server for computing, evaluating and combining multiple sequence alignments. Nucleic Acids Res., 31, 3503-3506. (Pubitemid 37442186)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3503-3506
    • Poirot, O.1    O'Toole, E.2    Notredame, C.3
  • 25
    • 1342288004 scopus 로고    scopus 로고
    • The Jalview Java alignment editor
    • DOI 10.1093/bioinformatics/btg430
    • Clamp, M., Cuff, J., Searle, S.M. and Barton, G.J. (2004) The Jalview Java alignment editor. Bioinformatics, 20, 426-427. (Pubitemid 38262778)
    • (2004) Bioinformatics , vol.20 , Issue.3 , pp. 426-427
    • Clamp, M.1    Cuff, J.2    Searle, S.M.3    Barton, G.J.4
  • 26
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • DOI 10.1093/nar/gkg520
    • Schwede, T., Kopp, J., Guex, N. and Peitsch, M.C. (2003) SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res., 31, 3381-3385. (Pubitemid 37442164)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 27
    • 0037925462 scopus 로고    scopus 로고
    • Structure of a trapped endonuclease III-DNA covalent intermediate
    • DOI 10.1093/emboj/cdg311
    • Fromme, J.C. and Verdine, G.L. (2003) Structure of a trapped endonuclease III-DNA covalent intermediate. EMBO J., 22, 3461-3471. (Pubitemid 36834876)
    • (2003) EMBO Journal , vol.22 , Issue.13 , pp. 3461-3471
    • Fromme, J.C.1    Verdine, G.L.2
  • 29
    • 18744391410 scopus 로고    scopus 로고
    • Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding
    • DOI 10.1038/nmeth740
    • Park, C. and Marqusee, S. (2005) Pulse proteolysis: a simple method for quantitative determination of protein stability and ligand binding. Nat. Methods, 2, 207-212. (Pubitemid 41122128)
    • (2005) Nature Methods , vol.2 , Issue.3 , pp. 207-212
    • Park, C.1    Marqusee, S.2
  • 30
    • 0034721829 scopus 로고    scopus 로고
    • Separating substrate recognition from base hydrolysis in human thymine DNA glycosylase by mutational analysis
    • Hardeland, U., Bentele, M., Jiricny, J. and Schar, P. (2000) Separating substrate recognition from base hydrolysis in human thymine DNA glycosylase by mutational analysis. J. Biol. Chem., 275, 33449-33456.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33449-33456
    • Hardeland, U.1    Bentele, M.2    Jiricny, J.3    Schar, P.4
  • 31
    • 0038074420 scopus 로고    scopus 로고
    • The versatile thymine DNA-glycosylase: A comparative characterization of the human, Drosophila and fission yeast orthologs
    • DOI 10.1093/nar/gkg344
    • Hardeland, U., Bentele, M., Jiricny, J. and Schar, P. (2003) The versatile thymine DNA-glycosylase: a comparative characterization of the human, Drosophila and fission yeast orthologs. Nucleic Acids Res., 31, 2261-2271. (Pubitemid 37442093)
    • (2003) Nucleic Acids Research , vol.31 , Issue.9 , pp. 2261-2271
    • Hardeland, U.1    Bentele, M.2    Jiricny, J.3    Schar, P.4
  • 32
    • 0036305835 scopus 로고    scopus 로고
    • Structure and activity of a thermostable thymine-DNA glycosylase: Evidence for base twisting to remove mismatched normal DNA bases
    • DOI 10.1006/jmbi.2001.5264
    • Mol, C.D., Arvai, A.S., Begley, T.J., Cunningham, R.P. and Tainer, J.A. (2002) Structure and activity of a thermostable thymine-DNA glycosylase: evidence for base twisting to remove mismatched normal DNA bases. J. Mol. Biol., 315, 373-384. (Pubitemid 34729346)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.3 , pp. 373-384
    • Mol, C.D.1    Arvai, A.S.2    Begley, T.J.3    Cunningham, R.P.4    Tainer, J.A.5
  • 33
    • 0037096192 scopus 로고    scopus 로고
    • Combining structural and bioinformatics methods for the analysis of functionally important residues in DNA glycosylases
    • DOI 10.1016/S0891-5849(02)00828-6, PII S0891584902008286
    • Zharkov, D.O. and Grollman, A.P. (2002) Combining structural and bioinformatics methods for the analysis of functionally important residues in DNA glycosylases. Free Radic. Biol. Med., 32, 1254-1263. (Pubitemid 34607629)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.12 , pp. 1254-1263
    • Zharkov, D.O.1    Grollman, A.P.2
  • 34
    • 26644474797 scopus 로고    scopus 로고
    • Engineering functional changes in Escherichia coli endonuclease III based on phylogenetic and structural analyses
    • DOI 10.1074/jbc.M504916200
    • Watanabe, T., Blaisdell, J.O., Wallace, S.S. and Bond, J.P. (2005) Engineering functional changes in Escherichia coli endonuclease III based on phylogenetic and structural analyses. J. Biol. Chem., 280, 34378-34384. (Pubitemid 41443164)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.40 , pp. 34378-34384
    • Watanabe, T.1    Blaisdell, J.O.2    Wallace, S.S.3    Bond, J.P.4
  • 35
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan, H.E., Standal, R. and Slupphaug, G. (1997) DNA glycosylases in the base excision repair of DNA. Biochem. J., 325, 1-16. (Pubitemid 27322679)
    • (1997) Biochemical Journal , vol.325 , Issue.1 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 36
    • 0037079688 scopus 로고    scopus 로고
    • Two amino acid replacements change the substrate preference of DNA mismatch glycosylase Mig.Mthl from T/G to A/G
    • Fondufe-Mittendorf, Y.N., Harer, C., Kramer, W. and Fritz, H.J. (2002) Two amino acid replacements change the substrate preference of DNA mismatch glycosylase Mig.MthI from T/G to A/G. Nucleic Acids Res., 30, 614-621. (Pubitemid 34679625)
    • (2002) Nucleic Acids Research , vol.30 , Issue.2 , pp. 614-621
    • Fondufe-Mittendorf, Y.N.1    Harer, C.2    Kramer, W.3    Fritz, H.-J.4
  • 37
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • DOI 10.1038/35002510
    • Bruner, S.D., Norman, D.P. and Verdine, G.L. (2000) Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature, 403, 859-866. (Pubitemid 30130980)
    • (2000) Nature , vol.403 , Issue.6772 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.G.2    Verdine, G.L.3
  • 38
    • 0034651873 scopus 로고    scopus 로고
    • DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA
    • Hollis, T., Ichikawa, Y. and Ellenberger, T. (2000) DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA. EMBO J., 19, 758-766. (Pubitemid 30093749)
    • (2000) EMBO Journal , vol.19 , Issue.4 , pp. 758-766
    • Hollis, T.1    Ichikawa, Y.2    Ellenberger, T.3
  • 39
    • 0037199967 scopus 로고    scopus 로고
    • Effects of hydrogen bonding within a damaged base pair on the activity of wild type and DNA-intercalating mutants of human alkyladenine DNA glycosylase
    • DOI 10.1074/jbc.M204475200
    • Vallur, A.C., Feller, J.A., Abner, C.W., Tran, R.K. and Bloom, L.B. (2002) Effects of hydrogen bonding within a damaged base pair on the activity of wild type and DNA-intercalating mutants of human alkyladenine DNA glycosylase. J. Biol. Chem., 277, 31673-31678. (Pubitemid 34968971)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.35 , pp. 31673-31678
    • Vallur, A.C.1    Feller, J.A.2    Abner, C.W.3    Tran, R.K.4    Bloom, L.B.5
  • 40
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • DOI 10.1038/384087a0
    • Slupphaug, G., Mol, C.D., Kavli, B., Arvai, A.S., Krokan, H.E. and Tainer, J.A. (1996) A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature, 384, 87-92. (Pubitemid 26374594)
    • (1996) Nature , vol.384 , Issue.6604 , pp. 87-92
    • Slupphaug, G.1    Mol, C.D.2    Kavli, B.3    Arvai, A.S.4    Krokan, H.E.5    Tainer, J.A.6
  • 41
    • 73649103725 scopus 로고    scopus 로고
    • Role of two strictly conserved residues in nucleotide flipping and N-glycosylic bond cleavage by human thymine DNA glycosylase
    • Maiti, A., Morgan, M.T. and Drohat, A.C. (2009) Role of two strictly conserved residues in nucleotide flipping and N-glycosylic bond cleavage by human thymine DNA glycosylase. J. Biol. Chem., 284, 36680-36688.
    • (2009) J. Biol. Chem. , vol.284 , pp. 36680-36688
    • Maiti, A.1    Morgan, M.T.2    Drohat, A.C.3
  • 43
    • 0038475941 scopus 로고    scopus 로고
    • Mismatch repair in methylated DNA: Structure and activity of the mismatch-specific thymine glycosylase domain of methyl-CpG-binding protein MBD4
    • DOI 10.1074/jbc.M210884200
    • Wu, P., Qiu, C., Sohail, A., Zhang, X., Bhagwat, A.S. and Cheng, X. (2003) Mismatch repair in methylated DNA. Structure and activity of the mismatch-specific thymine glycosylase domain of methyl-CpG-binding protein MBD4. J. Biol. Chem., 278, 5285-5291. (Pubitemid 36801043)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.7 , pp. 5285-5291
    • Wu, P.1    Qiu, C.2    Sohail, A.3    Zhang, X.4    Bhagwat, A.S.5    Cheng, X.6
  • 44
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson, H.J. and Wright, P.E. (2005) Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell. Biol., 6, 197-208. (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 46
    • 0023127167 scopus 로고
    • Escherichia coli endonuclease III is not an endonuclease but a β-elimination catalyst
    • Bailly, V. and Verly, W.G. (1987) Escherichia coli endonuclease III is not an endonuclease but a beta-elimination catalyst. Biochem. J., 242, 565-572. (Pubitemid 17026608)
    • (1987) Biochemical Journal , vol.242 , Issue.2 , pp. 565-572
    • Bailly, V.1    Verly, W.G.2
  • 47
    • 0141754009 scopus 로고    scopus 로고
    • Crystal structures of 3-methyladenine DNA glycosylase MagIII and the recognition of alkylated bases
    • DOI 10.1093/emboj/cdg505
    • Eichman, B.F., O'Rourke, E.J., Radicella, J.P. and Ellenberger, T. (2003) Crystal structures of 3-methyladenine DNA glycosylase MagIII and the recognition of alkylated bases. EMBO J., 22, 4898-4909. (Pubitemid 37222012)
    • (2003) EMBO Journal , vol.22 , Issue.19 , pp. 4898-4909
    • Eichman, B.F.1    O'Rourke, E.J.2    Radicella, J.P.3    Ellenberger, T.4
  • 48
    • 53649089723 scopus 로고    scopus 로고
    • The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix
    • Hashimoto, H., Horton, J.R., Zhang, X., Bostick, M., Jacobsen, S.E. and Cheng, X. (2008) The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix. Nature, 455, 826-829.
    • (2008) Nature , vol.455 , pp. 826-829
    • Hashimoto, H.1    Horton, J.R.2    Zhang, X.3    Bostick, M.4    Jacobsen, S.E.5    Cheng, X.6
  • 49
    • 53649097070 scopus 로고    scopus 로고
    • Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism
    • Arita, K., Ariyoshi, M., Tochio, H., Nakamura, Y. and Shirakawa, M. (2008) Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism. Nature, 455, 818-821.
    • (2008) Nature , vol.455 , pp. 818-821
    • Arita, K.1    Ariyoshi, M.2    Tochio, H.3    Nakamura, Y.4    Shirakawa, M.5
  • 51
    • 33847663262 scopus 로고    scopus 로고
    • The enigmatic thymine DNA glycosylase
    • DOI 10.1016/j.dnarep.2006.10.013, PII S1568786406003223, Repair of small base lesions in DNA-from molecular biology to phenotype
    • Cortazar, D., Kunz, C., Saito, Y., Steinacher, R. and Schar, P. (2006) The enigmatic thymine DNA glycosylase. DNA Repair, 6, 489-504. (Pubitemid 46357052)
    • (2007) DNA Repair , vol.6 , Issue.4 , pp. 489-504
    • Cortazar, D.1    Kunz, C.2    Saito, Y.3    Steinacher, R.4    Schar, P.5
  • 52
    • 48249147403 scopus 로고    scopus 로고
    • Crystal structure of human thymine DNA glycosylase bound to DNA elucidates sequence-specific mismatch recognition
    • Maiti, A., Morgan, M.T., Pozharski, E. and Drohat, A.C. (2008) Crystal structure of human thymine DNA glycosylase bound to DNA elucidates sequence-specific mismatch recognition. Proc. Natl Acad. Sci. USA, 105, 8890-8895.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 8890-8895
    • Maiti, A.1    Morgan, M.T.2    Pozharski, E.3    Drohat, A.C.4
  • 54
    • 3843090592 scopus 로고    scopus 로고
    • The coupling of tight DNA binding and base flipping. Identification of a conserved structural motif in base flipping enzymes
    • DOI 10.1074/jbc.M402950200
    • Estabrook, R.A., Lipson, R., Hopkins, B. and Reich, N. (2004) The coupling of tight DNA binding and base flipping: identification of a conserved structural motif in base flipping enzymes. J. Biol. Chem., 279, 31419-31428. (Pubitemid 39037809)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.30 , pp. 31419-31428
    • Estabrook, R.A.1    Lipson, R.2    Hopkins, B.3    Reich, N.4
  • 55
    • 77953699733 scopus 로고    scopus 로고
    • Helix unwinding and base flipping enable human MTERF1 to terminate mitochondrial transcription
    • Yakubovskaya, E., Mejia, E., Byrnes, J., Hambardjieva, E. and Garcia-Diaz, M. (2010) Helix unwinding and base flipping enable human MTERF1 to terminate mitochondrial transcription. Cell, 141, 982-993.
    • (2010) Cell , vol.141 , pp. 982-993
    • Yakubovskaya, E.1    Mejia, E.2    Byrnes, J.3    Hambardjieva, E.4    Garcia-Diaz, M.5
  • 56
    • 0031149139 scopus 로고    scopus 로고
    • How do DNA repair proteins locate damaged bases in the genome?
    • Verdine, G.L. and Bruner, S.D. (1997) How do DNA repair proteins locate damaged bases in the genome? Chem. Biol., 4, 329-334. (Pubitemid 27276850)
    • (1997) Chemistry and Biology , vol.4 , Issue.5 , pp. 329-334
    • Verdine, G.L.1    Bruner, S.D.2
  • 57
    • 34848899274 scopus 로고    scopus 로고
    • Enzymatic capture of an extrahelical thymine in the search for uracil in DNA
    • DOI 10.1038/nature06131, PII NATURE06131
    • Parker, J.B., Bianchet, M.A., Krosky, D.J., Friedman, J.I., Amzel, L.M. and Stivers, J.T. (2007) Enzymatic capture of an extrahelical thymine in the search for uracil in DNA. Nature, 449, 433-437. (Pubitemid 47509542)
    • (2007) Nature , vol.449 , Issue.7161 , pp. 433-437
    • Parker, J.B.1    Bianchet, M.A.2    Krosky, D.J.3    Friedman, J.I.4    Amzel, L.M.5    Stivers, J.T.6
  • 58
    • 15844379169 scopus 로고    scopus 로고
    • Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA
    • DOI 10.1038/nature03458
    • Banerjee, A., Yang, W., Karplus, M. and Verdine, G.L. (2005) Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA. Nature, 434, 612-618. (Pubitemid 40488548)
    • (2005) Nature , vol.434 , Issue.7033 , pp. 612-618
    • Banerjee, A.1    Yang, W.2    Karplus, M.3    Verdine, G.L.4
  • 59
    • 33644511436 scopus 로고    scopus 로고
    • Structure of a DNA glycosylase searching for lesions
    • Banerjee, A., Santos, W.L. and Verdine, G.L. (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
  • 60
    • 77953654163 scopus 로고    scopus 로고
    • Detection of damaged DNA bases by DNA glycosylase enzymes
    • Friedman, J.I. and Stivers, J.T. (2010) Detection of damaged DNA bases by DNA glycosylase enzymes. Biochemistry, 49, 4957-4967.
    • (2010) Biochemistry , vol.49 , pp. 4957-4967
    • Friedman, J.I.1    Stivers, J.T.2
  • 61
    • 0032951710 scopus 로고    scopus 로고
    • Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1
    • DOI 10.1074/jbc.274.1.67
    • Waters, T.R., Gallinari, P., Jiricny, J. and Swann, P.F. (1999) Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1. J. Biol. Chem., 274, 67-74. (Pubitemid 29035031)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.1 , pp. 67-74
    • Waters, T.R.1    Gallinari, P.2    Jiricnyl, J.3    Swann, P.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.