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Volumn 468, Issue 7322, 2010, Pages 406-413

An unprecedented nucleic acid capture mechanism for excision of DNA damage

Author keywords

[No Author keywords available]

Indexed keywords

ALKD GLYCOSYLASE; BACTERIAL ENZYME; DNA; NUCLEIC ACID; UNCLASSIFIED DRUG;

EID: 78549243696     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09428     Document Type: Article
Times cited : (63)

References (65)
  • 1
    • 33746488809 scopus 로고    scopus 로고
    • DNA repair: From molecular mechanism to human disease
    • Friedberg, E. C. et al. DNA repair: from molecular mechanism to human disease. DNA Repair (Amst.) 5, 986-996 (2006).
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 986-996
    • Friedberg, E.C.1
  • 4
    • 0023189690 scopus 로고
    • The determination of urinary 3-methyladenine in humans as a potential monitor of exposure to methylating agents
    • Shuker, D. E., Bailey, E., Parry, A., Lamb, J. & Farmer, P. B. The determination of urinary 3-methyladenine in humans as a potential monitor of exposure to methylating agents. Carcinogenesis 8, 959-962 (1987).
    • (1987) Carcinogenesis , vol.8 , pp. 959-962
    • Shuker, D.E.1    Bailey, E.2    Parry, A.3    Lamb, J.4    Farmer, P.B.5
  • 5
    • 0026673948 scopus 로고
    • Relevance of urinary DNA adducts as markers of carcinogen exposure
    • Shuker, D. E. & Farmer, P. B. Relevance of urinary DNA adducts as markers of carcinogen exposure. Chem. Res. Toxicol. 5, 450-460 (1992).
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 450-460
    • Shuker, D.E.1    Farmer, P.B.2
  • 6
    • 0022363977 scopus 로고
    • Methylation-induced blockstoin vitro DNA replication
    • Larson, K., Sahm, J., Shenkar, R. & Strauss, B.Methylation-induced blockstoin vitro DNA replication. Mutat. Res. 150, 77-84 (1985).
    • (1985) Mutat. Res. , vol.150 , pp. 77-84
    • Larson, K.1    Sahm, J.2    Shenkar, R.3    Strauss, B.4
  • 7
    • 42449091527 scopus 로고    scopus 로고
    • Eukaryotic Y-family polymerases bypass a 3-methyl-2'-deoxyadenosine analog in vitro and methyl methanesulfonate-induced DNA damage in vivo
    • Plosky, B. S. et al. Eukaryotic Y-family polymerases bypass a 3-methyl-2'-deoxyadenosine analog in vitro and methyl methanesulfonate-induced DNA damage in vivo. Nucleic Acids Res. 36, 2152-2162 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2152-2162
    • Plosky, B.S.1
  • 8
    • 3242727654 scopus 로고    scopus 로고
    • Biologically relevant chemical reactions of N7-alkylguanine residues in DNA
    • Gates, K. S., Nooner, T. & Dutta, S. Biologically relevant chemical reactions of N7-alkylguanine residues in DNA. Chem. Res. Toxicol. 17, 839-856 (2004).
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 839-856
    • Gates, K.S.1    Nooner, T.2    Dutta, S.3
  • 9
    • 4143149415 scopus 로고    scopus 로고
    • Site-specific DNA damage recognition by enzyme-induced base flipping
    • Stivers, J. T. Site-specific DNA damage recognition by enzyme-induced base flipping. Prog. Nucleic Acid Res. Mol. Biol. 77, 37-65 (2004).
    • (2004) Prog. Nucleic Acid Res. Mol. Biol. , vol.77 , pp. 37-65
    • Stivers, J.T.1
  • 10
    • 38849207616 scopus 로고    scopus 로고
    • Extrahelical damaged base recognitionby DNA glycosylase enzymes
    • Stivers, J. T.Extrahelical damaged base recognitionby DNA glycosylase enzymes. Chemistry 14, 786-793 (2008).
    • (2008) Chemistry , vol.14 , pp. 786-793
    • Stivers, J.T.1
  • 11
    • 0042342532 scopus 로고    scopus 로고
    • A mechanistic perspectiveonthe chemistryofDNA repair glycosylases
    • Stivers, J.T. & Jiang, Y. L.A mechanistic perspectiveonthe chemistryofDNA repair glycosylases. Chem. Rev. 103, 2729-2760 (2003).
    • (2003) Chem. Rev. , vol.103 , pp. 2729-2760
    • Stivers, J.T.1    Jiang, Y.L.2
  • 12
    • 0034625082 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase-DNA substrate and product structures: Conformational strain promotes catalytic efficiency by coupled stereoelectronic effects
    • Parikh, S. S. et al. Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects. Proc. Natl Acad. Sci. USA 97, 5083-5088 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5083-5088
    • Parikh, S.S.1
  • 13
    • 0036305835 scopus 로고    scopus 로고
    • Structure and activity of a thermostable thymine-DNA glycosylase: Evidence for base twisting to remove mismatched normal DNA bases
    • Mol, C. D., Arvai, A. S., Begley, T. J., Cunningham, R. P. & Tainer, J. A. 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 (2002).
    • (2002) J. Mol. Biol. , vol.315 , pp. 373-384
    • Mol, C.D.1    Arvai, A.S.2    Begley, T.J.3    Cunningham, R.P.4    Tainer, J.A.5
  • 14
    • 0036730599 scopus 로고    scopus 로고
    • 3-Methyladenine DNA glycosylase i is an unexpected helix-hairpin-helix superfamily member
    • Drohat, A. C., Kwon, K., Krosky, D. J. & Stivers, J. T. 3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member. Nature Struct. Biol. 9, 659-664 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 659-664
    • Drohat, A.C.1    Kwon, K.2    Krosky, D.J.3    Stivers, J.T.4
  • 15
    • 0141754009 scopus 로고    scopus 로고
    • Crystal structures of 3-methyladenine DNA glycosylase MagIII and the recognition of alkylated bases
    • Eichman, B. F., O'Rourke, E. J., Radicella, J. P. & Ellenberger, T. Crystal structures of 3-methyladenine DNA glycosylase MagIII and the recognition of alkylated bases. EMBO J. 22, 4898-4909 (2003).
    • (2003) EMBO J. , vol.22 , pp. 4898-4909
    • Eichman, B.F.1    O'Rourke, E.J.2    Radicella, J.P.3    Ellenberger, T.4
  • 16
    • 34247555529 scopus 로고    scopus 로고
    • DNA damage recognition and repair by 3-methyladenine DNA glycosylase i (TAG)
    • Metz, A. H., Hollis, T. & Eichman, B. F. DNA damage recognition and repair by 3-methyladenine DNA glycosylase I (TAG). EMBO J. 26, 2411-2420 (2007).
    • (2007) EMBO J. , vol.26 , pp. 2411-2420
    • Metz, A.H.1    Hollis, T.2    Eichman, B.F.3
  • 17
    • 33645057457 scopus 로고    scopus 로고
    • Anew protein superfamily includestwo novel 3-methyladenineDNA glycosylases from Bacillus cereus
    • Alseth, I.et al.Anew protein superfamily includestwo novel 3-methyladenineDNA glycosylases from Bacillus cereus, AlkC and AlkD. Mol. Microbiol. 59, 1602-1609 (2006).
    • (2006) AlkC and AlkD. Mol. Microbiol. , vol.59 , pp. 1602-1609
    • Alseth, I.1
  • 18
    • 34249862768 scopus 로고    scopus 로고
    • Structural insight into repairofalkylated DNAbya new superfamily of DNA glycosylases comprising HEAT-like repeats
    • Dalhus, B.et al. Structural insight into repairofalkylated DNAbya new superfamily of DNA glycosylases comprising HEAT-like repeats. Nucleic Acids Res. 35, 2451-2459 (2007).
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2451-2459
    • Dalhus, B.1
  • 19
    • 46649086715 scopus 로고    scopus 로고
    • A new protein architecture for processing alkylation damaged DNA: The crystal structure of DNA glycosylase AlkD
    • Rubinson, E. H., Metz, A. H., O'Quin, J. & Eichman, B. F. A new protein architecture for processing alkylation damaged DNA: the crystal structure of DNA glycosylase AlkD. J. Mol. Biol. 381, 13-23 (2008).
    • (2008) J. Mol. Biol. , vol.381 , pp. 13-23
    • Rubinson, E.H.1    Metz, A.H.2    O'Quin, J.3    Eichman, B.F.4
  • 20
    • 0029392854 scopus 로고
    • HEAT repeatsinthe Huntington's disease protein
    • Andrade, M.A.& Bork, P. HEAT repeatsinthe Huntington's disease protein. Nature Genet. 11, 115-116 (1995).
    • (1995) Nature Genet. , vol.11 , pp. 115-116
    • Andrade, M.A.1    Bork, P.2
  • 21
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-b bound to the IBB domain of importin-a
    • Cingolani, G., Petosa, C., Weis, K. & Muller, C. W. Structure of importin-b bound to the IBB domain of importin-a. Nature 399, 221-229 (1999).
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 22
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the ? Ran-Importin b interaction at 2.3A resolution
    • Vetter, I. R., Arndt, A., Kutay, U., Gorlich, D. & Wittinghofer, A. Structural view of the ? Ran-Importin b interaction at 2.3A resolution. Cell 97, 635-646 (1999).
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Gorlich, D.4    Wittinghofer, A.5
  • 23
    • 77953168644 scopus 로고    scopus 로고
    • Thermodynamic characterization of DNA with 3-deazaadenine and 3-methyl-3-deazaadenine substitutions
    • Ganguly, M., Wang, R.-W., Marky, L. A. & Gold, B.Thermodynamic characterization of DNA with 3-deazaadenine and 3-methyl-3-deazaadenine substitutions. J.Phys. Chem. B 114, 7656-7661 (2010).
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7656-7661
    • Ganguly, M.1    Wang, R.-W.2    Markyl., A.3    Gold, B.4
  • 24
    • 1642411206 scopus 로고    scopus 로고
    • Dissecting the broad substrate specificity of human 3-methyladenine-DNA glycosylase
    • O'Brien, P. J. & Ellenberger, T. Dissecting the broad substrate specificity of human 3-methyladenine-DNA glycosylase. J. Biol. Chem. 279, 9750-9757 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 9750-9757
    • O'Brien, P.J.1    Ellenberger, T.2
  • 25
    • 3042686671 scopus 로고    scopus 로고
    • The Escherichia coli 3-methyladenine DNA glycosylase AlkA has a remarkably versatile active site
    • O'Brien, P. J. & Ellenberger, T. The Escherichia coli 3-methyladenine DNA glycosylase AlkA has a remarkably versatile active site. J. Biol. Chem. 279, 26876-26884 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 26876-26884
    • O'Brien, P.J.1    Ellenberger, T.2
  • 26
    • 0035834751 scopus 로고    scopus 로고
    • Turning on uracil-DNA glycosylase using a pyrene nucleotide switch
    • Jiang, Y. L., Kwon, K. & Stivers, J. T. Turning on uracil-DNA glycosylase using a pyrene nucleotide switch. J. Biol. Chem. 276, 42347-42354 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 42347-42354
    • Jiang, Y.L.1    Kwon, K.2    Stivers, J.T.3
  • 27
    • 0033535375 scopus 로고    scopus 로고
    • DNA adduct formation from tobacco-specific N-nitrosamines
    • Hecht, S. S. DNA adduct formation from tobacco-specific N-nitrosamines. Mutat. Res. 424, 127-142 (1999).
    • (1999) Mutat. Res. , vol.424 , pp. 127-142
    • Hecht, S.S.1
  • 28
    • 0032538337 scopus 로고    scopus 로고
    • Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: Mechanisms for nucleotide flipping and base excision
    • Lau, A.Y., Scharer, O.D., Samson, L., Verdine, G.L.& Ellenberger, T.Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision. Cell 95, 249-258 (1998).
    • (1998) Cell , vol.95 , pp. 249-258
    • Lau, A.Y.1    Scharer, O.D.2    Samson, L.3    Verdine, G.L.4    Ellenberger, T.5
  • 29
    • 33644511436 scopus 로고    scopus 로고
    • Structureof aDNA glycosylase searching for lesions
    • Banerjee, A., Santos, W.L.& Verdine, G. L.Structureof aDNA glycosylase searching for lesions. Science 311, 1153-1157 (2006).
    • (2006) Science , vol.311 , pp. 1153-1157
    • Banerjee, A.1    Santos, W.L.2    Verdine, G.L.3
  • 30
    • 15844379169 scopus 로고    scopus 로고
    • Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA
    • Banerjee, A., Yang, W., Karplus, M. & Verdine, G. L. Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA. Nature 434, 612-618 (2005).
    • (2005) Nature , vol.434 , pp. 612-618
    • Banerjee, A.1    Yang, W.2    Karplus, M.3    Verdine, G.L.4
  • 31
    • 60349094184 scopus 로고    scopus 로고
    • Damage detection and base flipping in direct DNA alkylation repair
    • Yang, C. G., Garcia, K. & He, C. Damage detection and base flipping in direct DNA alkylation repair. ChemBioChem 10, 417-423 (2009).
    • (2009) Chem Bio Chem , vol.10 , pp. 417-423
    • Yang, C.G.1    Garcia, K.2    He, C.3
  • 32
    • 42549128712 scopus 로고    scopus 로고
    • Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA
    • Yang, C. G. et al. Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA. Nature 452, 961-965 (2008).
    • (2008) Nature , vol.452 , pp. 961-965
    • Yang, C.G.1
  • 33
    • 0022423486 scopus 로고
    • Base-base mismatches. Thermodynamics of double helix formation for dCA3XA3G 1 dCT3YT3G (X, y 5 A, C, G, T)
    • Aboul-ela, F., Koh, D., Tinoco, I. Jr & Martin, F. H. Base-base mismatches. Thermodynamics of double helix formation for dCA3XA3G 1 dCT3YT3G (X, Y 5 A, C, G, T). Nucleic Acids Res. 13, 4811-4824 (1985).
    • (1985) Nucleic Acids Res. , vol.13 , pp. 4811-4824
    • Aboul-Ela, F.1    Koh, D.2    Tinoco Jr., I.3    Martin, F.H.4
  • 34
    • 0003976684 scopus 로고
    • Aberrantly methylated DNA: Site-specific introduction of N-7-methyl-29-deoxyguanosine into the Dickerson/Drew dodecamer
    • Ezaz-Nikpay, K. & Verdine, G. L. Aberrantly methylated DNA: site-specific introduction of N-7-methyl-29-deoxyguanosine into the Dickerson/Drew dodecamer. J. Am. Chem. Soc. 114, 6562-6563 (1992).
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6562-6563
    • Ezaz-Nikpay, K.1    Verdine, G.L.2
  • 35
    • 0028675029 scopus 로고
    • The effects of N7-methylguanine on duplex DNA structure
    • Ezaz-Nikpay, K. & Verdine, G. L. The effects of N7-methylguanine on duplex DNA structure. Chem. Biol. 1, 235-240 (1994).
    • (1994) Chem. Biol. , vol.1 , pp. 235-240
    • Ezaz-Nikpay, K.1    Verdine, G.L.2
  • 36
    • 51349152032 scopus 로고    scopus 로고
    • Synthesis and structure of duplexDNAcontainingthe genotoxic nucleobase lesionN7-methylguanine
    • Lee, S., Bowman, B.R., Ueno, Y., Wang, S.& Verdine, G.L.Synthesis and structure of duplexDNAcontainingthe genotoxic nucleobase lesionN7- methylguanine.J.Am. Chem. Soc. 130, 11570-11571 (2008).
    • (2008) J.Am. Chem. Soc. , vol.130 , pp. 11570-11571
    • Lee, S.1    Bowman, B.R.2    Ueno, Y.3    Wang, S.4    Verdine, G.L.5
  • 37
    • 0023664744 scopus 로고
    • The structureofguanosine-thymidine mismatchesinB-DNA at 2.5-A resolution
    • Hunter, W.N.et al. The structureofguanosine-thymidine mismatchesinB-DNA at 2.5-A resolution. J. Biol. Chem. 262, 9962-9970 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 9962-9970
    • Hunter, W.N.1
  • 38
    • 0035909316 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase acts by substrate autocatalysis
    • Dinner, A. R., Blackburn, G. M. & Karplus, M. Uracil-DNA glycosylase acts by substrate autocatalysis. Nature 413, 752-755 (2001).
    • (2001) Nature , vol.413 , pp. 752-755
    • Dinner, A.R.1    Blackburn, G.M.2    Karplus, M.3
  • 39
    • 0345270445 scopus 로고    scopus 로고
    • Powering DNA repair through substrate electrostatic interactions
    • Jiang, Y. L., Ichikawa, Y., Song, F. & Stivers, J. T. Powering DNA repair through substrate electrostatic interactions. Biochemistry 42, 1922-1929 (2003).
    • (2003) Biochemistry , vol.42 , pp. 1922-1929
    • Jiang, Y.L.1    Ichikawa, Y.2    Song, F.3    Stivers, J.T.4
  • 40
    • 38149049320 scopus 로고    scopus 로고
    • Repair of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone-induced DNA pyridyloxobutylation by nucleotide excision repair
    • Brown, P. J., Bedard, L. L. & Massey, T. E. Repair of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone-induced DNA pyridyloxobutylation by nucleotide excision repair. Cancer Lett. 260, 48-55 (2008).
    • (2008) Cancer Lett. , vol.260 , pp. 48-55
    • Brown, P.J.1    Bedard, L.L.2    Massey, T.E.3
  • 41
    • 68949107651 scopus 로고    scopus 로고
    • The influence of repair pathways on the cytotoxicity and mutagenicity induced by the pyridyloxobutylation pathway of tobacco-specific nitrosamines
    • Li, L. et al. The influence of repair pathways on the cytotoxicity and mutagenicity induced by the pyridyloxobutylation pathway of tobacco-specific nitrosamines. Chem. Res. Toxicol. 22, 1464-1472 (2009).
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 1464-1472
    • Li, L.1
  • 42
    • 34948892722 scopus 로고    scopus 로고
    • Recognition of DNA damage by the Rad4 nucleotide excision repair protein
    • Min, J. H. & Pavletich, N. P. Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature 449, 570-575 (2007).
    • (2007) Nature , vol.449 , pp. 570-575
    • Min, J.H.1    Pavletich, N.P.2
  • 43
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination
    • Mol, C. D., Izumi, T., Mitra, S. & Tainer, J. A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination. Nature 403, 451-456 (2000).
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 44
    • 67249113070 scopus 로고    scopus 로고
    • Flipping of alkylated DNA damage bridges base and nucleotide excision repair
    • Tubbs, J. L. et al. Flipping of alkylated DNA damage bridges base and nucleotide excision repair. Nature 459, 808-813 (2009).
    • (2009) Nature , vol.459 , pp. 808-813
    • Tubbs, J.L.1
  • 45
    • 0033782987 scopus 로고    scopus 로고
    • HEAT repeats associated with condensins, Cohesins, Andother complexes involvedinchromosome-related functions
    • Neuwald, A. F. & Hirano, T. HEAT repeats associated with condensins, Cohesins, Andother complexes involvedinchromosome-related functions. Genome Res. 10, 1445-1452 (2000).
    • (2000) Genome Res. , vol.10 , pp. 1445-1452
    • Neuwald, A.F.1    Hirano, T.2
  • 46
    • 0037462453 scopus 로고    scopus 로고
    • The ATRs ATMs, and TORs are giant HEAT repeat proteins
    • Perry, J. & Kleckner, N.The ATRs, ATMs, And TORs are giant HEAT repeat proteins. Cell 112, 151-155 (2003).
    • (2003) Cell , vol.112 , pp. 151-155
    • Perry, J.1    Kleckner, N.2
  • 47
    • 40049096125 scopus 로고    scopus 로고
    • Cryo-EM structure of the DNA-dependent protein kinase catalytic subunit at subnanometer resolution reveals a helices and insight into DNA binding
    • Williams, D. R., Lee, K. J., Shi, J., Chen, D. J. & Stewart, P. L. Cryo-EM structure of the DNA-dependent protein kinase catalytic subunit at subnanometer resolution reveals a helices and insight into DNA binding. Structure 16, 468-477 (2008).
    • (2008) Structure , vol.16 , pp. 468-477
    • Williams, D.R.1    Lee, K.J.2    Shi, J.3    Chen, D.J.4    Stewart, P.L.5
  • 48
    • 73849140503 scopus 로고    scopus 로고
    • Crystal structure of DNA-PKcs revealsalargeopen- ringcradle comprised of HEAT repeats
    • Sibanda, B. L., Chirgadze, D. Y. & Blundell, T. L. Crystal structure of DNA-PKcs revealsalargeopen- ringcradle comprised of HEAT repeats. Nature 463, 118-121 (2010).
    • (2010) Nature , vol.463 , pp. 118-121
    • Sibanda, B.L.1    Chirgadze, D.Y.2    Blundell, T.L.3
  • 49
    • 0036909326 scopus 로고    scopus 로고
    • The synthesis of anti-fixed 3-methyl-3-deaza-29-deoxyadenosine and other 3H-imidazo[4, 5-c]pyridine analogs
    • Irani, R. J. & SantaLucia, J. Jr. The synthesis of anti-fixed 3-methyl-3-deaza-29-deoxyadenosine and other 3H-imidazo[4, 5-c]pyridine analogs. Nucleosides Nucleotides Nucleic Acids 21, 737-751 (2002).
    • (2002) Nucleosides Nucleotides Nucleic Acids , vol.21 , pp. 737-751
    • Irani, R.J.1    Santa Lucia Jr., J.2
  • 50
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 52
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr.D54, 905-921 (1998).
    • (1998) Acta Crystallogr. , vol.D54 , pp. 905-921
    • Brünger, A.T.1
  • 53
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125, 156-165 (1999).
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 55
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 56
    • 0000243829 scopus 로고
    • Procheck - A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S. & Thornton, J. M. Procheck - a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291 (1993).
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 57
    • 0024058085 scopus 로고
    • The definition of generalized helicoidal parameters and of axis curvature for irregular nucleic acids
    • Lavery, R. & Sklenar, H. The definition of generalized helicoidal parameters and of axis curvature for irregular nucleic acids. J. Biomol. Struct. Dyn. 6, 63-91 (1988).
    • (1988) J. Biomol. Struct. Dyn. , vol.6 , pp. 63-91
    • Lavery, R.1    Sklenar, H.2
  • 58
    • 0034728369 scopus 로고    scopus 로고
    • Substrate specificity of human methylpurine DNA N-glycosylase
    • Asaeda, A. et al. Substrate specificity of human methylpurine DNA N-glycosylase. Biochemistry 39, 1959-1965 (2000).
    • (2000) Biochemistry , vol.39 , pp. 1959-1965
    • Asaeda, A.1
  • 59
    • 57749170001 scopus 로고    scopus 로고
    • Akinetic assaytomonitor RNA decapping under single-turnover conditions
    • Jones, B.N., Quang-Dang, D.U., Oku, Y. & Gross, J.D. Akinetic assaytomonitor RNA decapping under single-turnover conditions. Methods Enzymol.448, 23-40 (2008).
    • (2008) Methods Enzymol , vol.448 , pp. 23-40
    • Jones, B.N.1    Quang-Dang, D.U.2    Oku, Y.3    Gross, J.D.4
  • 60
    • 67649592232 scopus 로고    scopus 로고
    • Human AP endonuclease 1 stimulates multiple-turnover base excision by alkyladenine DNA glycosylase
    • Baldwin, M. R. & O'Brien, P. J. Human AP endonuclease 1 stimulates multiple-turnover base excision by alkyladenine DNA glycosylase. Biochemistry 48, 6022-6033 (2009).
    • (2009) Biochemistry , vol.48 , pp. 6022-6033
    • Baldwin, M.R.1    O'Brien, P.J.2
  • 61
    • 71749091666 scopus 로고    scopus 로고
    • Efficient recognition of an unpaired lesion by a DNA repair glycosylase
    • Lyons, D. M. & O'Brien, P. J. Efficient recognition of an unpaired lesion by a DNA repair glycosylase. J. Am. Chem. Soc. 131, 17742-17743 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17742-17743
    • Lyons, D.M.1    O'Brien, P.J.2
  • 62
    • 35648950472 scopus 로고    scopus 로고
    • Pre-steady-state kinetic characterization of the AP endonuclease activity of human AP endonuclease 1
    • Maher, R. L. & Bloom, L. B. Pre-steady-state kinetic characterization of the AP endonuclease activity of human AP endonuclease 1. J. Biol. Chem. 282, 30577-30585 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 30577-30585
    • Maher, R.L.1    Bloom, L.B.2
  • 63
    • 33845755964 scopus 로고    scopus 로고
    • Slow base excision by human alkyladenine DNA glycosylase limits the rate of formation of AP sites and AP endonuclease 1 does not stimulate base excision
    • Maher, R. L., Vallur, A. C., Feller, J. A. & Bloom, L. B. Slow base excision by human alkyladenine DNA glycosylase limits the rate of formation of AP sites and AP endonuclease 1 does not stimulate base excision. DNA Repair (Amst.) 6, 71-81 (2007).
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 71-81
    • Maher, R.L.1    Vallur, A.C.2    Feller, J.A.3    Bloom, L.B.4
  • 64
    • 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. & Drohat, A. C. 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).
    • (2009) J. Biol. Chem. , vol.284 , pp. 36680-36688
    • Maiti, A.1    Morgan, M.T.2    Drohat, A.C.3
  • 65
    • 33749171576 scopus 로고    scopus 로고
    • Specificity of human thymine DNA glycosylase depends on N-glycosidic bond stability
    • Bennett, M. T. et al. Specificity of human thymine DNA glycosylase depends on N-glycosidic bond stability. J. Am. Chem. Soc. 128, 12510-12519 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12510-12519
    • Bennett, M.T.1


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