메뉴 건너뛰기




Volumn 577, Issue 1-2 SPEC. ISS., 2005, Pages 55-76

DNA base damage recognition and removal: New twists and grooves

Author keywords

Base excision repair; DNA damage recognition; DNA glycosylase structure

Indexed keywords

8 HYDROXYGUANINE; BACTERIAL ENZYME; DNA BASE; DNA FORMAMIDOPYRIMIDINE GLYCOSYLASE; DNA GLYCOSYLASE MUTT; DNA GLYCOSYLASE MUTY; DNA GLYCOSYLTRANSFERASE; DOUBLE STRANDED DNA; ENZYME; ENZYME HOGG1; FLUOROURACIL; NUCLEOTIDE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; SINGLE STRANDED DNA; TATA BINDING PROTEIN; TOXIN; UNCLASSIFIED DRUG; URACIL; URACIL DNA GLYCOSYLTRANSFERASE;

EID: 24044460415     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2005.03.012     Document Type: Review
Times cited : (190)

References (136)
  • 1
    • 0004146634 scopus 로고
    • Cambridge University Press Cambridge, UK
    • E. Schroedinger What is Life? 1944 Cambridge University Press Cambridge, UK
    • (1944) What Is Life?
    • Schroedinger, E.1
  • 2
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • T. Lindahl Instability and decay of the primary structure of DNA Nature 362 1993 709 715
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 3
    • 0142150241 scopus 로고    scopus 로고
    • Harmful health effects of cigarette smoking
    • S.K. Das Harmful health effects of cigarette smoking Mol. Cell. Biochem. 253 2003 159 165
    • (2003) Mol. Cell. Biochem. , vol.253 , pp. 159-165
    • Das, S.K.1
  • 5
    • 0242268065 scopus 로고    scopus 로고
    • Mammalian DNA base excision repair proteins: Their interactions and role in repair of oxidative DNA damage
    • T. Izumi, L.R. Wiederhold, G. Roy, R. Roy, A. Jaiswal, K.K. Bhakat, S. Mitra, and T.K. Hazra Mammalian DNA base excision repair proteins: their interactions and role in repair of oxidative DNA damage Toxicology 193 2003 43 65
    • (2003) Toxicology , vol.193 , pp. 43-65
    • Izumi, T.1    Wiederhold, L.R.2    Roy, G.3    Roy, R.4    Jaiswal, A.5    Bhakat, K.K.6    Mitra, S.7    Hazra, T.K.8
  • 6
    • 0348140585 scopus 로고    scopus 로고
    • Abasic sites in DNA: Repair and biological consequences in Saccharomyces cerevisiae
    • S. Boiteux, and M. Guillet Abasic sites in DNA: repair and biological consequences in Saccharomyces cerevisiae DNA Repair (Amsterdam) 3 2004 1 12
    • (2004) DNA Repair (Amsterdam) , vol.3 , pp. 1-12
    • Boiteux, S.1    Guillet, M.2
  • 9
    • 2942532239 scopus 로고    scopus 로고
    • Modulation of the 5′-deoxyribose-5-phosphate lyase and DNA synthesis activities of mammalian DNA polymerase beta by apurinic/apyrimidinic endonuclease 1
    • D. Wong, and B. Demple Modulation of the 5′-deoxyribose-5-phosphate lyase and DNA synthesis activities of mammalian DNA polymerase beta by apurinic/apyrimidinic endonuclease 1 J. Biol. Chem. 279 2004 25268 25275
    • (2004) J. Biol. Chem. , vol.279 , pp. 25268-25275
    • Wong, D.1    Demple, B.2
  • 10
    • 0347510577 scopus 로고    scopus 로고
    • Orchestration of base excision repair by controlling the rates of enzymatic activities
    • S.L. Allinson, K.M. Sleeth, G.E. Matthewman, and G.L. Dianov Orchestration of base excision repair by controlling the rates of enzymatic activities DNA Repair (Amsterdam) 3 2004 23 31
    • (2004) DNA Repair (Amsterdam) , vol.3 , pp. 23-31
    • Allinson, S.L.1    Sleeth, K.M.2    Matthewman, G.E.3    Dianov, G.L.4
  • 11
    • 0035940441 scopus 로고    scopus 로고
    • Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair
    • I.I. Dianova, V.A. Bohr, and G.L. Dianov Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair Biochemistry 40 2001 12639 12644
    • (2001) Biochemistry , vol.40 , pp. 12639-12644
    • Dianova, I.I.1    Bohr, V.A.2    Dianov, G.L.3
  • 12
    • 0342350255 scopus 로고    scopus 로고
    • Interaction between PCNA and DNA ligase I is critical for joining of Okazaki fragments and long-patch base-excision repair
    • D.S. Levin, A.E. McKenna, T.A. Motycka, Y. Matsumoto, and A.E. Tomkinson Interaction between PCNA and DNA ligase I is critical for joining of Okazaki fragments and long-patch base-excision repair Curr. Biol. 10 2000 919 922
    • (2000) Curr. Biol. , vol.10 , pp. 919-922
    • Levin, D.S.1    McKenna, A.E.2    Motycka, T.A.3    Matsumoto, Y.4    Tomkinson, A.E.5
  • 13
    • 0034733694 scopus 로고    scopus 로고
    • Base excision repair in yeast and mammals
    • A. Memisoglu, and L. Samson Base excision repair in yeast and mammals Mutat. Res. 451 2000 39 51
    • (2000) Mutat. Res. , vol.451 , pp. 39-51
    • Memisoglu, A.1    Samson, L.2
  • 16
    • 0028604549 scopus 로고
    • Unified catalytic mechanism for DNA glycosylases
    • M.L. Dodson, M.L. Michaels, and R.S. Lloyd Unified catalytic mechanism for DNA glycosylases J. Biol. Chem. 269 1994 32709 32712
    • (1994) J. Biol. Chem. , vol.269 , pp. 32709-32712
    • Dodson, M.L.1    Michaels, M.L.2    Lloyd, R.S.3
  • 17
    • 0029013243 scopus 로고
    • The catalytic mechanism of Fpg protein. Evidence for a Schiff base intermediate and amino terminus localization of the catalytic site
    • J. Tchou, and A.P. Grollman The catalytic mechanism of Fpg protein. Evidence for a Schiff base intermediate and amino terminus localization of the catalytic site J. Biol. Chem. 270 1995 11671 11677
    • (1995) J. Biol. Chem. , vol.270 , pp. 11671-11677
    • Tchou, J.1    Grollman, A.P.2
  • 18
    • 0036294464 scopus 로고    scopus 로고
    • Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM
    • J.C. Fromme, and G.L. Verdine Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM Nat. Struct. Biol. 9 2002 544 552
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 544-552
    • Fromme, J.C.1    Verdine, G.L.2
  • 19
    • 0037925462 scopus 로고    scopus 로고
    • Structure of a trapped endonuclease III-DNA covalent intermediate
    • J.C. Fromme, and G.L. Verdine Structure of a trapped endonuclease III-DNA covalent intermediate EMBO J. 22 2003 3461 3471
    • (2003) EMBO J. , vol.22 , pp. 3461-3471
    • Fromme, J.C.1    Verdine, G.L.2
  • 23
    • 0032534053 scopus 로고    scopus 로고
    • Evidence that MutY is a monofunctional glycosylase capable of forming a covalent Schiff base intermediate with substrate DNA
    • S.D. Williams, and S.S. David Evidence that MutY is a monofunctional glycosylase capable of forming a covalent Schiff base intermediate with substrate DNA Nucl. Acids Res. 26 1998 5123 5133
    • (1998) Nucl. Acids Res. , vol.26 , pp. 5123-5133
    • Williams, S.D.1    David, S.S.2
  • 25
    • 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
    • T. Hollis, Y. Ichikawa, and T. Ellenberger DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA EMBO J. 19 2000 758 766
    • (2000) EMBO J. , vol.19 , pp. 758-766
    • Hollis, T.1    Ichikawa, Y.2    Ellenberger, T.3
  • 26
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • S.D. Bruner, D.P. Norman, and G.L. Verdine Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA Nature 403 2000 859 866
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.2    Verdine, G.L.3
  • 27
    • 0032498302 scopus 로고    scopus 로고
    • Crystal structure of a G:T/U mismatch-specific DNA glycosylase: Mismatch recognition by complementary-strand interactions
    • T.E. Barrett, R. Savva, G. Panayotou, T. Barlow, T. Brown, J. Jiricny, and L.H. Pearl Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions Cell 92 1998 117 129
    • (1998) Cell , vol.92 , pp. 117-129
    • Barrett, T.E.1    Savva, R.2    Panayotou, G.3    Barlow, T.4    Brown, T.5    Jiricny, J.6    Pearl, L.H.7
  • 28
    • 0032167424 scopus 로고    scopus 로고
    • Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
    • S.S. Parikh, C.D. Mol, G. Slupphaug, S. Bharati, H.E. Krokan, and J.A. Tainer Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA EMBO J. 17 1998 5214 5226
    • (1998) EMBO J. , vol.17 , pp. 5214-5226
    • Parikh, S.S.1    Mol, C.D.2    Slupphaug, G.3    Bharati, S.4    Krokan, H.E.5    Tainer, J.A.6
  • 29
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination
    • C.D. Mol, T. Izumi, S. Mitra, and J.A. Tainer DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination Nature 403 2000 451 456
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 30
    • 0033529716 scopus 로고    scopus 로고
    • Structure of the DNA repair enzyme endonuclease IV and its DNA complex: Double-nucleotide flipping at abasic sites and three-metal-ion catalysis
    • D.J. Hosfield, Y. Guan, B.J. Haas, R.P. Cunningham, and J.A. Tainer Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis Cell 98 1999 397 408
    • (1999) Cell , vol.98 , pp. 397-408
    • Hosfield, D.J.1    Guan, Y.2    Haas, B.J.3    Cunningham, R.P.4    Tainer, J.A.5
  • 31
    • 0034625082 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase-DNA substrate and product structures: Conformational strain promotes catalytic efficiency by coupled stereoelectronic effects
    • S.S. Parikh, G. Walcher, G.D. Jones, G. Slupphaug, H.E. Krokan, G.M. Blackburn, and J.A. Tainer Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects Proc. Natl. Acad. Sci. U.S.A. 97 2000 5083 5088
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5083-5088
    • Parikh, S.S.1    Walcher, G.2    Jones, G.D.3    Slupphaug, G.4    Krokan, H.E.5    Blackburn, G.M.6    Tainer, J.A.7
  • 32
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • M.M. Thayer, H. Ahern, D. Xing, R.P. Cunningham, and J.A. Tainer Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure EMBO J. 14 1995 4108 4120
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 35
    • 0141754009 scopus 로고    scopus 로고
    • Crystal structures of 3-methyladenine DNA glycosylase MagIII and the recognition of alkylated bases
    • B.F. Eichman, E.J. O'Rourke, J.P. Radicella, and T. Ellenberger Crystal structures of 3-methyladenine DNA glycosylase MagIII and the recognition of alkylated bases EMBO J. 22 2003 4898 4909
    • (2003) EMBO J. , vol.22 , pp. 4898-4909
    • Eichman, B.F.1    O'Rourke, E.J.2    Radicella, J.P.3    Ellenberger, T.4
  • 36
    • 0028863468 scopus 로고
    • Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: Structural basis for damaged DNA recognition
    • D.G. Vassylyev, T. Kashiwagi, Y. Mikami, M. Ariyoshi, S. Iwai, E. Ohtsuka, and K. Morikawa Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition Cell 83 1995 773 782
    • (1995) Cell , vol.83 , pp. 773-782
    • Vassylyev, D.G.1    Kashiwagi, T.2    Mikami, Y.3    Ariyoshi, M.4    Iwai, S.5    Ohtsuka, E.6    Morikawa, K.7
  • 37
    • 0036305835 scopus 로고    scopus 로고
    • Structure and activity of a thermostable thymine-DNA glycosylase: Evidence for base twisting to remove mismatched normal DNA bases
    • C.D. Mol, A.S. Arvai, T.J. Begley, R.P. Cunningham, and J.A. Tainer Structure and activity of a thermostable thymine-DNA glycosylase: evidence for base twisting to remove mismatched normal DNA bases J. Mol. Biol. 315 2002 373 384
    • (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
  • 40
    • 0036730599 scopus 로고    scopus 로고
    • 3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member
    • A.C. Drohat, K. Kwon, D.J. Krosky, and J.T. Stivers 3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member Nat. Struct. Biol. 9 2002 659 664
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 659-664
    • Drohat, A.C.1    Kwon, K.2    Krosky, D.J.3    Stivers, J.T.4
  • 41
    • 1342304229 scopus 로고    scopus 로고
    • Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase
    • J.C. Fromme, A. Banerjee, S.J. Huang, and G.L. Verdine Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase Nature 427 2004 652 656
    • (2004) Nature , vol.427 , pp. 652-656
    • Fromme, J.C.1    Banerjee, A.2    Huang, S.J.3    Verdine, G.L.4
  • 42
    • 11844306632 scopus 로고    scopus 로고
    • A DNA glycosylase from Pyrobaculum aerophilum with an 8-oxoguanine binding mode and a noncanonical helix-hairpin-helix structure
    • G.M. Lingaraju, A.A. Sartori, D. Kostrewa, A.E. Prota, J. Jiricny, and F.K. Winkler A DNA glycosylase from Pyrobaculum aerophilum with an 8-oxoguanine binding mode and a noncanonical helix-hairpin-helix structure Structure (Cambridge) 13 2005 87 98
    • (2005) Structure (Cambridge) , vol.13 , pp. 87-98
    • Lingaraju, G.M.1    Sartori, A.A.2    Kostrewa, D.3    Prota, A.E.4    Jiricny, J.5    Winkler, F.K.6
  • 43
    • 0032538337 scopus 로고    scopus 로고
    • Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: Mechanisms for nucleotide flipping and base excision
    • A.Y. Lau, O.D. Scharer, L. Samson, G.L. Verdine, and T. Ellenberger Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision Cell 95 1998 249 258
    • (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
  • 44
    • 0029929070 scopus 로고    scopus 로고
    • The helix-hairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA
    • A.J. Doherty, L.C. Serpell, and C.P. Ponting The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA Nucl. Acids Res. 24 1996 2488 2497
    • (1996) Nucl. Acids Res. , vol.24 , pp. 2488-2497
    • Doherty, A.J.1    Serpell, L.C.2    Ponting, C.P.3
  • 45
    • 0032475933 scopus 로고    scopus 로고
    • Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: Coupling DNA and PCNA binding to FEN-1 activity
    • D.J. Hosfield, C.D. Mol, B. Shen, and J.A. Tainer Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity Cell 95 1998 135 146
    • (1998) Cell , vol.95 , pp. 135-146
    • Hosfield, D.J.1    Mol, C.D.2    Shen, B.3    Tainer, J.A.4
  • 46
    • 0034254724 scopus 로고    scopus 로고
    • Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8
    • M. Sugahara, T. Mikawa, T. Kumasaka, M. Yamamoto, R. Kato, K. Fukuyama, Y. Inoue, and S. Kuramitsu Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8 EMBO J. 19 2000 3857 3869
    • (2000) EMBO J. , vol.19 , pp. 3857-3869
    • Sugahara, M.1    Mikawa, T.2    Kumasaka, T.3    Yamamoto, M.4    Kato, R.5    Fukuyama, K.6    Inoue, Y.7    Kuramitsu, S.8
  • 47
    • 0037124320 scopus 로고    scopus 로고
    • Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA
    • L. Serre, K. Pereira de Jesus, S. Boiteux, C. Zelwer, and B. Castaing Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA EMBO J. 21 2002 2854 2865
    • (2002) EMBO J. , vol.21 , pp. 2854-2865
    • Serre, L.1    Pereira De Jesus, K.2    Boiteux, S.3    Zelwer, C.4    Castaing, B.5
  • 48
    • 0346435086 scopus 로고    scopus 로고
    • DNA lesion recognition by the bacterial repair enzyme MutM
    • J.C. Fromme, and G.L. Verdine DNA lesion recognition by the bacterial repair enzyme MutM J. Biol. Chem. 278 2003 51543 51548
    • (2003) J. Biol. Chem. , vol.278 , pp. 51543-51548
    • Fromme, J.C.1    Verdine, G.L.2
  • 49
    • 3142702720 scopus 로고    scopus 로고
    • The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity
    • S. Doublie, V. Bandaru, J.P. Bond, and S.S. Wallace The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity Proc. Natl. Acad. Sci. U.S.A. 101 2004 10284 10289
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 10284-10289
    • Doublie, S.1    Bandaru, V.2    Bond, J.P.3    Wallace, S.S.4
  • 50
    • 8744262953 scopus 로고    scopus 로고
    • Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein
    • A. Das, L. Rajagopalan, V.S. Mathura, S.J. Rigby, S. Mitra, and T.K. Hazra Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein J. Biol. Chem. 279 2004 47132 47138
    • (2004) J. Biol. Chem. , vol.279 , pp. 47132-47138
    • Das, A.1    Rajagopalan, L.2    Mathura, V.S.3    Rigby, S.J.4    Mitra, S.5    Hazra, T.K.6
  • 51
    • 0347379928 scopus 로고    scopus 로고
    • Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2
    • H. Dou, S. Mitra, and T.K. Hazra Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2 J. Biol. Chem. 278 2003 49679 49684
    • (2003) J. Biol. Chem. , vol.278 , pp. 49679-49684
    • Dou, H.1    Mitra, S.2    Hazra, T.K.3
  • 53
    • 0037509930 scopus 로고    scopus 로고
    • Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions
    • A. Masaoka, M. Matsubara, R. Hasegawa, T. Tanaka, S. Kurisu, H. Terato, Y. Ohyama, N. Karino, A. Matsuda, and H. Ide Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions Biochemistry 42 2003 5003 5012
    • (2003) Biochemistry , vol.42 , pp. 5003-5012
    • Masaoka, A.1    Matsubara, M.2    Hasegawa, R.3    Tanaka, T.4    Kurisu, S.5    Terato, H.6    Ohyama, Y.7    Karino, N.8    Matsuda, A.9    Ide, H.10
  • 54
    • 0038771139 scopus 로고    scopus 로고
    • Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1
    • J.E. Wibley, T.R. Waters, K. Haushalter, G.L. Verdine, and L.H. Pearl Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1 Mol. Cell 11 2003 1647 1659
    • (2003) Mol. Cell , vol.11 , pp. 1647-1659
    • Wibley, J.E.1    Waters, T.R.2    Haushalter, K.3    Verdine, G.L.4    Pearl, L.H.5
  • 55
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
    • C.D. Mol, A.S. Arvai, G. Slupphaug, B. Kavli, I. Alseth, H.E. Krokan, and J.A. Tainer Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis Cell 80 1995 869 878
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 57
    • 0037449138 scopus 로고    scopus 로고
    • Energetics of lesion recognition by a DNA repair protein: Thermodynamic characterization of formamidopyrimidine-glycosylase (Fpg) interactions with damaged DNA duplexes
    • C.A. Minetti, D.P. Remeta, D.O. Zharkov, G.E. Plum, F. Johnson, A.P. Grollman, and K.J. Breslauer Energetics of lesion recognition by a DNA repair protein: thermodynamic characterization of formamidopyrimidine-glycosylase (Fpg) interactions with damaged DNA duplexes J. Mol. Biol. 328 2003 1047 1060
    • (2003) J. Mol. Biol. , vol.328 , pp. 1047-1060
    • Minetti, C.A.1    Remeta, D.P.2    Zharkov, D.O.3    Plum, G.E.4    Johnson, F.5    Grollman, A.P.6    Breslauer, K.J.7
  • 58
    • 0042342532 scopus 로고    scopus 로고
    • A mechanistic perspective on the chemistry of DNA repair glycosylases
    • J.T. Stivers, and Y.L. Jiang A mechanistic perspective on the chemistry of DNA repair glycosylases Chem. Rev. 103 2003 2729 2759
    • (2003) Chem. Rev. , vol.103 , pp. 2729-2759
    • Stivers, J.T.1    Jiang, Y.L.2
  • 60
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae
    • J.P. Radicella, C. Dherin, C. Desmaze, M.S. Fox, and S. Boiteux Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae Proc. Natl. Acad. Sci. U.S.A. 94 1997 8010 8015
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8010-8015
    • Radicella, J.P.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.4    Boiteux, S.5
  • 61
    • 0032555571 scopus 로고    scopus 로고
    • Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease. III. Direct identification of Lys-212 as the active nucleophilic residue
    • S. Ikeda, T. Biswas, R. Roy, T. Izumi, I. Boldogh, A. Kurosky, A.H. Sarker, S. Seki, and S. Mitra Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease. III. Direct identification of Lys-212 as the active nucleophilic residue J. Biol. Chem. 273 1998 21585 21593
    • (1998) J. Biol. Chem. , vol.273 , pp. 21585-21593
    • Ikeda, S.1    Biswas, T.2    Roy, R.3    Izumi, T.4    Boldogh, I.5    Kurosky, A.6    Sarker, A.H.7    Seki, S.8    Mitra, S.9
  • 62
    • 0037162995 scopus 로고    scopus 로고
    • Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions
    • T.K. Hazra, Y.W. Kow, Z. Hatahet, B. Imhoff, I. Boldogh, S.K. Mokkapati, S. Mitra, and T. Izumi Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions J. Biol. Chem. 277 2002 30417 30420
    • (2002) J. Biol. Chem. , vol.277 , pp. 30417-30420
    • Hazra, T.K.1    Kow, Y.W.2    Hatahet, Z.3    Imhoff, B.4    Boldogh, I.5    Mokkapati, S.K.6    Mitra, S.7    Izumi, T.8
  • 64
    • 0030703177 scopus 로고    scopus 로고
    • Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites
    • M. Bjoras, L. Luna, B. Johnsen, E. Hoff, T. Haug, T. Rognes, and E. Seeberg Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites EMBO J. 16 1997 6314 6322
    • (1997) EMBO J. , vol.16 , pp. 6314-6322
    • Bjoras, M.1    Luna, L.2    Johnsen, B.3    Hoff, E.4    Haug, T.5    Rognes, T.6    Seeberg, E.7
  • 65
    • 0036290411 scopus 로고    scopus 로고
    • Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase
    • M. Bjoras, E. Seeberg, L. Luna, L.H. Pearl, and T.E. Barrett Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase J. Mol. Biol. 317 2002 171 177
    • (2002) J. Mol. Biol. , vol.317 , pp. 171-177
    • Bjoras, M.1    Seeberg, E.2    Luna, L.3    Pearl, L.H.4    Barrett, T.E.5
  • 66
    • 1342266756 scopus 로고    scopus 로고
    • The human 8-oxoguanine DNA N-glycosylase 1 (hOGG1) DNA repair enzyme and its association with lung cancer risk
    • J. Park, L. Chen, M.S. Tockman, A. Elahi, and P. Lazarus The human 8-oxoguanine DNA N-glycosylase 1 (hOGG1) DNA repair enzyme and its association with lung cancer risk Pharmacogenetics 14 2004 103 109
    • (2004) Pharmacogenetics , vol.14 , pp. 103-109
    • Park, J.1    Chen, L.2    Tockman, M.S.3    Elahi, A.4    Lazarus, P.5
  • 68
    • 12344307152 scopus 로고    scopus 로고
    • Product inhibition and magnesium modulate the dual reaction mode of hOgg1
    • I. Morland, L. Luna, E. Gustad, E. Seeberg, and M. Bjoras Product inhibition and magnesium modulate the dual reaction mode of hOgg1 DNA Repair (Amsterdam) 4 2005 381 387
    • (2005) DNA Repair (Amsterdam) , vol.4 , pp. 381-387
    • Morland, I.1    Luna, L.2    Gustad, E.3    Seeberg, E.4    Bjoras, M.5
  • 69
    • 0026701365 scopus 로고
    • The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)
    • M.L. Michaels, and J.H. Miller 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
  • 70
    • 0037459233 scopus 로고    scopus 로고
    • Insight into the functional consequences of inherited variants of the hMYH adenine glycosylase associated with colorectal cancer: Complementation assays with hMYH variants and pre-steady-state kinetics of the corresponding mutated E. coli enzymes
    • N.H. Chmiel, A.L. Livingston, and S.S. David Insight into the functional consequences of inherited variants of the hMYH adenine glycosylase associated with colorectal cancer: complementation assays with hMYH variants and pre-steady-state kinetics of the corresponding mutated E. coli enzymes J. Mol. Biol. 327 2003 431 443
    • (2003) J. Mol. Biol. , vol.327 , pp. 431-443
    • Chmiel, N.H.1    Livingston, A.L.2    David, S.S.3
  • 73
    • 0034610354 scopus 로고    scopus 로고
    • Role for lysine 142 in the excision of adenine from A:G mispairs by MutY DNA glycosylase of Escherichia coli
    • D.O. Zharkov, R. Gilboa, I. Yagil, J.H. Kycia, S.E. Gerchman, G. Shoham, and A.P. Grollman Role for lysine 142 in the excision of adenine from A:G mispairs by MutY DNA glycosylase of Escherichia coli Biochemistry 39 2000 14768 14778
    • (2000) Biochemistry , vol.39 , pp. 14768-14778
    • Zharkov, D.O.1    Gilboa, R.2    Yagil, I.3    Kycia, J.H.4    Gerchman, S.E.5    Shoham, G.6    Grollman, A.P.7
  • 74
    • 0042324507 scopus 로고    scopus 로고
    • Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product
    • M.A. Massiah, V. Saraswat, H.F. Azurmendi, and A.S. Mildvan Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product Biochemistry 42 2003 10140 10154
    • (2003) Biochemistry , vol.42 , pp. 10140-10154
    • Massiah, M.A.1    Saraswat, V.2    Azurmendi, H.F.3    Mildvan, A.S.4
  • 76
    • 0030818650 scopus 로고    scopus 로고
    • Kinetics of excision of purine lesions from DNA by Escherichia coli Fpg protein
    • A. Karakaya, P. Jaruga, V.A. Bohr, A.P. Grollman, and M. Dizdaroglu Kinetics of excision of purine lesions from DNA by Escherichia coli Fpg protein Nucl. Acids Res. 25 1997 474 479
    • (1997) Nucl. Acids Res. , vol.25 , pp. 474-479
    • Karakaya, A.1    Jaruga, P.2    Bohr, V.A.3    Grollman, A.P.4    Dizdaroglu, M.5
  • 77
    • 0025871264 scopus 로고
    • MutM, a protein that prevents G.C → T.A transversions, is formamidopyrimidine-DNA glycosylase
    • M.L. Michaels, L. Pham, C. Cruz, and J.H. Miller MutM, a protein that prevents G.C → T.A transversions, is formamidopyrimidine-DNA glycosylase Nucl. Acids Res. 19 1991 3629 3632
    • (1991) Nucl. Acids Res. , vol.19 , pp. 3629-3632
    • Michaels, M.L.1    Pham, L.2    Cruz, C.3    Miller, J.H.4
  • 78
    • 0142187125 scopus 로고    scopus 로고
    • Structural characterization of the Fpg family of DNA glycosylases
    • D.O. Zharkov, G. Shoham, and A.P. Grollman Structural characterization of the Fpg family of DNA glycosylases DNA Repair (Amsterdam) 2 2003 839 862
    • (2003) DNA Repair (Amsterdam) , vol.2 , pp. 839-862
    • Zharkov, D.O.1    Shoham, G.2    Grollman, A.P.3
  • 79
    • 6344223490 scopus 로고    scopus 로고
    • Structural basis for the recognition of the FapydG lesion (2,6-diamino-4-hydroxy-5-formamidopyrimidine) by formamidopyrimidine-DNA glycosylase
    • F. Coste, M. Ober, T. Carell, S. Boiteux, C. Zelwer, and B. Castaing Structural basis for the recognition of the FapydG lesion (2,6-diamino-4- hydroxy-5-formamidopyrimidine) by formamidopyrimidine-DNA glycosylase J. Biol. Chem. 279 2004 44074 44083
    • (2004) J. Biol. Chem. , vol.279 , pp. 44074-44083
    • Coste, F.1    Ober, M.2    Carell, T.3    Boiteux, S.4    Zelwer, C.5    Castaing, B.6
  • 80
    • 0018166688 scopus 로고
    • Accumulation of small fragments of DNA in isolated HeLa cell nuclei due to transient incorporation of dUMP
    • E. Wist, O. Unhjem, and H. Krokan Accumulation of small fragments of DNA in isolated HeLa cell nuclei due to transient incorporation of dUMP Biochim. Biophys. Acta 520 1978 253 270
    • (1978) Biochim. Biophys. Acta , vol.520 , pp. 253-270
    • Wist, E.1    Unhjem, O.2    Krokan, H.3
  • 81
    • 0013608322 scopus 로고
    • Transient accumulation of Okazaki fragments as a result of uracil incorporation into nascent DNA
    • B.K. Tye, P.O. Nyman, I.R. Lehman, S. Hochhauser, and B. Weiss Transient accumulation of Okazaki fragments as a result of uracil incorporation into nascent DNA Proc. Natl. Acad. Sci. U.S.A. 74 1977 154 157
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 154-157
    • Tye, B.K.1    Nyman, P.O.2    Lehman, I.R.3    Hochhauser, S.4    Weiss, B.5
  • 82
    • 0037019315 scopus 로고    scopus 로고
    • AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification
    • S.K. Petersen-Mahrt, R.S. Harris, and M.S. Neuberger AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification Nature 418 2002 99 103
    • (2002) Nature , vol.418 , pp. 99-103
    • Petersen-Mahrt, S.K.1    Harris, R.S.2    Neuberger, M.S.3
  • 83
    • 0037076208 scopus 로고    scopus 로고
    • AID-GFP chimeric protein increases hypermutation of Ig genes with no evidence of nuclear localization
    • C. Rada, J.M. Jarvis, and C. Milstein AID-GFP chimeric protein increases hypermutation of Ig genes with no evidence of nuclear localization Proc. Natl. Acad. Sci. U.S.A. 99 2002 7003 7008
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 7003-7008
    • Rada, C.1    Jarvis, J.M.2    Milstein, C.3
  • 86
    • 18644363009 scopus 로고    scopus 로고
    • HUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup
    • B. Kavli, O. Sundheim, M. Akbari, M. Otterlei, H. Nilsen, F. Skorpen, P.A. Aas, L. Hagen, H.E. Krokan, and G. Slupphaug hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup J. Biol. Chem. 277 2002 39926 39936
    • (2002) J. Biol. Chem. , vol.277 , pp. 39926-39936
    • Kavli, B.1    Sundheim, O.2    Akbari, M.3    Otterlei, M.4    Nilsen, H.5    Skorpen, F.6    Aas, P.A.7    Hagen, L.8    Krokan, H.E.9    Slupphaug, G.10
  • 87
    • 0019306430 scopus 로고
    • Uracil DNA-glycosylase. Purification and properties of this enzyme isolated from blast cells of acute myelocytic leukemia patients
    • S.J. Caradonna, and Y.C. Cheng Uracil DNA-glycosylase. Purification and properties of this enzyme isolated from blast cells of acute myelocytic leukemia patients J. Biol. Chem. 255 1980 2293 2300
    • (1980) J. Biol. Chem. , vol.255 , pp. 2293-2300
    • Caradonna, S.J.1    Cheng, Y.C.2
  • 88
    • 0020478598 scopus 로고
    • Properties of purified uracil-DNA glycosylase from calf thymus. An in vitro study using synthetic DNA-like substrates
    • M. Talpaert-Borle, F. Campagnari, and D.M. Creissen Properties of purified uracil-DNA glycosylase from calf thymus. An in vitro study using synthetic DNA-like substrates J. Biol. Chem. 257 1982 1208 1214
    • (1982) J. Biol. Chem. , vol.257 , pp. 1208-1214
    • Talpaert-Borle, M.1    Campagnari, F.2    Creissen, D.M.3
  • 89
    • 0030841051 scopus 로고    scopus 로고
    • Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene
    • H. Nilsen, M. Otterlei, T. Haug, K. Solum, T.A. Nagelhus, F. Skorpen, and H.E. Krokan Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene Nucl. Acids Res. 25 1997 750 755
    • (1997) Nucl. Acids Res. , vol.25 , pp. 750-755
    • Nilsen, H.1    Otterlei, M.2    Haug, T.3    Solum, K.4    Nagelhus, T.A.5    Skorpen, F.6    Krokan, H.E.7
  • 90
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase
    • R. Savva, K. McAuley-Hecht, T. Brown, and L. Pearl The structural basis of specific base-excision repair by uracil-DNA glycosylase Nature 373 1995 487 493
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 91
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • G. Slupphaug, C.D. Mol, B. Kavli, A.S. Arvai, H.E. Krokan, and J.A. Tainer A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA Nature 384 1996 87 92
    • (1996) Nature , vol.384 , 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
  • 92
    • 0033120232 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: Structure and glycosylase mechanism revisited
    • G. Xiao, M. Tordova, J. Jagadeesh, A.C. Drohat, J.T. Stivers, and G.L. Gilliland Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited Proteins 35 1999 13 24
    • (1999) Proteins , vol.35 , pp. 13-24
    • Xiao, G.1    Tordova, M.2    Jagadeesh, J.3    Drohat, A.C.4    Stivers, J.T.5    Gilliland, G.L.6
  • 93
    • 0042568932 scopus 로고    scopus 로고
    • The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features
    • I. Leiros, E. Moe, O. Lanes, A.O. Smalas, and N.P. Willassen The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features Acta Crystallogr. D: Biol. Crystallogr. 59 2003 1357 1365
    • (2003) Acta Crystallogr. D: Biol. Crystallogr. , vol.59 , pp. 1357-1365
    • Leiros, I.1    Moe, E.2    Lanes, O.3    Smalas, A.O.4    Willassen, N.P.5
  • 94
    • 0037205473 scopus 로고    scopus 로고
    • Presteady-state analysis of a single catalytic turnover by Escherichia coli uracil-DNA glycosylase reveals a "pinch-pull-push" mechanism
    • I. Wong, A.J. Lundquist, A.S. Bernards, and D.W. Mosbaugh Presteady-state analysis of a single catalytic turnover by Escherichia coli uracil-DNA glycosylase reveals a "pinch-pull-push" mechanism J. Biol. Chem. 277 2002 19424 19432
    • (2002) J. Biol. Chem. , vol.277 , pp. 19424-19432
    • Wong, I.1    Lundquist, A.J.2    Bernards, A.S.3    Mosbaugh, D.W.4
  • 95
    • 0034734383 scopus 로고    scopus 로고
    • Structure and function in the uracil-DNA glycosylase superfamily
    • L.H. Pearl Structure and function in the uracil-DNA glycosylase superfamily Mutat. Res. 460 2000 165 181
    • (2000) Mutat. Res. , vol.460 , pp. 165-181
    • Pearl, L.H.1
  • 96
    • 0023651289 scopus 로고
    • A specific mismatch repair event protects mammalian cells from loss of 5-methylcytosine
    • T.C. Brown, and J. Jiricny A specific mismatch repair event protects mammalian cells from loss of 5-methylcytosine Cell 50 1987 945 950
    • (1987) Cell , vol.50 , pp. 945-950
    • Brown, T.C.1    Jiricny, J.2
  • 98
    • 0029805081 scopus 로고    scopus 로고
    • A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase
    • P. Gallinari, and J. Jiricny A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase Nature 383 1996 735 738
    • (1996) Nature , vol.383 , pp. 735-738
    • Gallinari, P.1    Jiricny, J.2
  • 99
    • 0032506037 scopus 로고    scopus 로고
    • A 55-kDa protein isolated from human cells shows DNA glycosylase activity toward 3,N4-ethenocytosine and the G/T mismatch
    • B. Hang, M. Medina, H. Fraenkel-Conrat, and B. Singer A 55-kDa protein isolated from human cells shows DNA glycosylase activity toward 3,N4-ethenocytosine and the G/T mismatch Proc. Natl. Acad. Sci. U.S.A. 95 1998 13561 13566
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13561-13566
    • Hang, B.1    Medina, M.2    Fraenkel-Conrat, H.3    Singer, B.4
  • 101
    • 0033602148 scopus 로고    scopus 로고
    • Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors
    • K.A. Haushalter, M.W. Todd Stukenberg, M.W. Kirschner, and G.L. Verdine Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors Curr. Biol. 9 1999 174 185
    • (1999) Curr. Biol. , vol.9 , pp. 174-185
    • Haushalter, K.A.1    Todd Stukenberg, M.W.2    Kirschner, M.W.3    Verdine, G.L.4
  • 102
    • 0038185257 scopus 로고    scopus 로고
    • Mammalian 5-formyluracil-DNA glycosylase. 1. Identification and characterization of a novel activity that releases 5-formyluracil from DNA
    • M. Matsubara, A. Masaoka, T. Tanaka, T. Miyano, N. Kato, H. Terato, Y. Ohyama, S. Iwai, and H. Ide Mammalian 5-formyluracil-DNA glycosylase. 1. Identification and characterization of a novel activity that releases 5-formyluracil from DNA Biochemistry 42 2003 4993 5002
    • (2003) Biochemistry , vol.42 , pp. 4993-5002
    • Matsubara, M.1    Masaoka, A.2    Tanaka, T.3    Miyano, T.4    Kato, N.5    Terato, H.6    Ohyama, Y.7    Iwai, S.8    Ide, H.9
  • 106
    • 0033486062 scopus 로고    scopus 로고
    • Solution structure of the methyl-CpG-binding domain of the methylation-dependent transcriptional repressor MBD1
    • I. Ohki, N. Shimotake, N. Fujita, M. Nakao, and M. Shirakawa Solution structure of the methyl-CpG-binding domain of the methylation-dependent transcriptional repressor MBD1 EMBO J. 18 1999 6653 6661
    • (1999) EMBO J. , vol.18 , pp. 6653-6661
    • Ohki, I.1    Shimotake, N.2    Fujita, N.3    Nakao, M.4    Shirakawa, M.5
  • 107
    • 0035906936 scopus 로고    scopus 로고
    • Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA
    • I. Ohki, N. Shimotake, N. Fujita, J. Jee, T. Ikegami, M. Nakao, and M. Shirakawa Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA Cell 105 2001 487 497
    • (2001) Cell , vol.105 , pp. 487-497
    • Ohki, I.1    Shimotake, N.2    Fujita, N.3    Jee, J.4    Ikegami, T.5    Nakao, M.6    Shirakawa, M.7
  • 109
    • 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
    • P. Wu, C. Qiu, A. Sohail, X. Zhang, A.S. Bhagwat, and X. Cheng 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 2003 5285 5291
    • (2003) J. Biol. Chem. , vol.278 , pp. 5285-5291
    • Wu, P.1    Qiu, C.2    Sohail, A.3    Zhang, X.4    Bhagwat, A.S.5    Cheng, X.6
  • 110
    • 0030587564 scopus 로고    scopus 로고
    • Human dUTP pyrophosphatase: Uracil recognition by a beta hairpin and active sites formed by three separate subunits
    • C.D. Mol, J.M. Harris, E.M. McIntosh, and J.A. Tainer Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits Structure 4 1996 1077 1092
    • (1996) Structure , vol.4 , pp. 1077-1092
    • Mol, C.D.1    Harris, J.M.2    McIntosh, E.M.3    Tainer, J.A.4
  • 111
    • 0033555756 scopus 로고    scopus 로고
    • Crystal structure of dUTPase from equine infectious anaemia virus; Active site metal binding in a substrate analogue complex
    • Z. Dauter, R. Persson, A.M. Rosengren, P.O. Nyman, K.S. Wilson, and E.S. Cedergren-Zeppezauer Crystal structure of dUTPase from equine infectious anaemia virus; active site metal binding in a substrate analogue complex J. Mol. Biol. 285 1999 655 673
    • (1999) J. Mol. Biol. , vol.285 , pp. 655-673
    • Dauter, Z.1    Persson, R.2    Rosengren, A.M.3    Nyman, P.O.4    Wilson, K.S.5    Cedergren-Zeppezauer, E.S.6
  • 114
    • 0041665086 scopus 로고    scopus 로고
    • Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii
    • J.L. Huffman, H. Li, R.H. White, and J.A. Tainer Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii J. Mol. Biol. 331 2003 885 896
    • (2003) J. Mol. Biol. , vol.331 , pp. 885-896
    • Huffman, J.L.1    Li, H.2    White, R.H.3    Tainer, J.A.4
  • 115
    • 17744410903 scopus 로고    scopus 로고
    • A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the hyperthermophilic archaeon Methanocaldococcus jannaschii
    • O. Bjornberg, J. Neuhard, and P.O. Nyman A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the hyperthermophilic archaeon Methanocaldococcus jannaschii J. Biol. Chem. 278 2003 20667 20672
    • (2003) J. Biol. Chem. , vol.278 , pp. 20667-20672
    • Bjornberg, O.1    Neuhard, J.2    Nyman, P.O.3
  • 118
    • 4444321494 scopus 로고    scopus 로고
    • The crystal structure of a complex of Campylobacter jejuni dUTPase with substrate analogue sheds light on the mechanism and suggests the "basic module" for dimeric d(C/U)TPases
    • O.V. Moroz, M. Harkiolaki, M.Y. Galperin, A.A. Vagin, D. Gonzalez-Pacanowska, and K.S. Wilson The crystal structure of a complex of Campylobacter jejuni dUTPase with substrate analogue sheds light on the mechanism and suggests the "basic module" for dimeric d(C/U)TPases J. Mol. Biol. 342 2004 1583 1597
    • (2004) J. Mol. Biol. , vol.342 , pp. 1583-1597
    • Moroz, O.V.1    Harkiolaki, M.2    Galperin, M.Y.3    Vagin, A.A.4    Gonzalez-Pacanowska, D.5    Wilson, K.S.6
  • 119
    • 0027215935 scopus 로고
    • Excision of 3-methylguanine from alkylated DNA by 3-methyladenine DNA glycosylase I of Escherichia coli
    • S. Bjelland, M. Bjoras, and E. Seeberg Excision of 3-methylguanine from alkylated DNA by 3-methyladenine DNA glycosylase I of Escherichia coli Nucl. Acids Res. 21 1993 2045 2049
    • (1993) Nucl. Acids Res. , vol.21 , pp. 2045-2049
    • Bjelland, S.1    Bjoras, M.2    Seeberg, E.3
  • 120
    • 0034733623 scopus 로고    scopus 로고
    • A novel 3-methyladenine DNA glycosylase from helicobacter pylori defines a new class within the endonuclease III family of base excision repair glycosylases
    • E.J. O'Rourke, C. Chevalier, S. Boiteux, A. Labigne, L. Ielpi, and J.P. Radicella A novel 3-methyladenine DNA glycosylase from helicobacter pylori defines a new class within the endonuclease III family of base excision repair glycosylases J. Biol. Chem. 275 2000 20077 20083
    • (2000) J. Biol. Chem. , vol.275 , pp. 20077-20083
    • O'Rourke, E.J.1    Chevalier, C.2    Boiteux, S.3    Labigne, A.4    Ielpi, L.5    Radicella, J.P.6
  • 121
    • 0034599723 scopus 로고    scopus 로고
    • Active and alkylated human AGT structures: A novel zinc site, inhibitor and extrahelical base binding
    • D.S. Daniels, C.D. Mol, A.S. Arvai, S. Kanugula, A.E. Pegg, and J.A. Tainer Active and alkylated human AGT structures: a novel zinc site, inhibitor and extrahelical base binding EMBO J. 19 2000 1719 1730
    • (2000) EMBO J. , vol.19 , pp. 1719-1730
    • Daniels, D.S.1    Mol, C.D.2    Arvai, A.S.3    Kanugula, S.4    Pegg, A.E.5    Tainer, J.A.6
  • 122
    • 0033600847 scopus 로고    scopus 로고
    • Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase
    • H. Hashimoto, T. Inoue, M. Nishioka, S. Fujiwara, M. Takagi, T. Imanaka, and Y. Kai Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase J. Mol. Biol. 292 1999 707 716
    • (1999) J. Mol. Biol. , vol.292 , pp. 707-716
    • Hashimoto, H.1    Inoue, T.2    Nishioka, M.3    Fujiwara, S.4    Takagi, M.5    Imanaka, T.6    Kai, Y.7
  • 124
    • 0028354364 scopus 로고
    • Crystal structure of a suicidal DNA repair protein: The Ada O6-methylguanine-DNA methyltransferase from E. coli
    • M.H. Moore, J.M. Gulbis, E.J. Dodson, B. Demple, and P.C. Moody Crystal structure of a suicidal DNA repair protein: the Ada O6-methylguanine-DNA methyltransferase from E. coli EMBO J. 13 1994 1495 1501
    • (1994) EMBO J. , vol.13 , pp. 1495-1501
    • Moore, M.H.1    Gulbis, J.M.2    Dodson, E.J.3    Demple, B.4    Moody, P.C.5
  • 125
    • 0037068446 scopus 로고    scopus 로고
    • Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
    • S.C. Trewick, T.F. Henshaw, R.P. Hausinger, T. Lindahl, and B. Sedgwick Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage Nature 419 2002 174 178
    • (2002) Nature , vol.419 , pp. 174-178
    • Trewick, S.C.1    Henshaw, T.F.2    Hausinger, R.P.3    Lindahl, T.4    Sedgwick, B.5
  • 126
    • 0037068433 scopus 로고    scopus 로고
    • AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
    • P.O. Falnes, R.F. Johansen, and E. Seeberg AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli Nature 419 2002 178 182
    • (2002) Nature , vol.419 , pp. 178-182
    • Falnes, P.O.1    Johansen, R.F.2    Seeberg, E.3
  • 127
    • 0035221419 scopus 로고    scopus 로고
    • The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases
    • L. Aravind, and E.V. Koonin The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases Genome Biol. 2 2001 (RESEARCH0007)
    • (2001) Genome Biol. , vol.2
    • Aravind, L.1    Koonin, E.V.2
  • 130
    • 3042686671 scopus 로고    scopus 로고
    • The Escherichia coli 3-methyladenine DNA glycosylase AlkA has a remarkably versatile active site
    • P.J. O'Brien, and T. Ellenberger The Escherichia coli 3-methyladenine DNA glycosylase AlkA has a remarkably versatile active site J. Biol. Chem. 279 2004 26876 26884
    • (2004) J. Biol. Chem. , vol.279 , pp. 26876-26884
    • O'Brien, P.J.1    Ellenberger, T.2
  • 131
    • 0032518911 scopus 로고    scopus 로고
    • Release of normal bases from intact DNA by a native DNA repair enzyme
    • K.G. Berdal, R.F. Johansen, and E. Seeberg Release of normal bases from intact DNA by a native DNA repair enzyme EMBO J. 17 1998 363 367
    • (1998) EMBO J. , vol.17 , pp. 363-367
    • Berdal, K.G.1    Johansen, R.F.2    Seeberg, E.3
  • 132
    • 0034610336 scopus 로고    scopus 로고
    • Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG
    • A.Y. Lau, M.D. Wyatt, B.J. Glassner, L.D. Samson, and T. Ellenberger Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG Proc. Natl. Acad. Sci. U.S.A. 97 2000 13573 13578
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13573-13578
    • Lau, A.Y.1    Wyatt, M.D.2    Glassner, B.J.3    Samson, L.D.4    Ellenberger, T.5
  • 133
    • 0030595337 scopus 로고    scopus 로고
    • Structural classification of HTH DNA-binding domains and protein-DNA interaction modes
    • R. Wintjens, and M. Rooman Structural classification of HTH DNA-binding domains and protein-DNA interaction modes J. Mol. Biol. 262 1996 294 313
    • (1996) J. Mol. Biol. , vol.262 , pp. 294-313
    • Wintjens, R.1    Rooman, M.2
  • 134
    • 14844346741 scopus 로고    scopus 로고
    • A bifunctional DNA repair protein from Ferroplasma acidarmanus exhibits O6-alkylguanine-DNA alkyltransferase and endonuclease V activities
    • S. Kanugula, G.T. Pauly, R.C. Moschel, and A.E. Pegg A bifunctional DNA repair protein from Ferroplasma acidarmanus exhibits O6-alkylguanine-DNA alkyltransferase and endonuclease V activities Proc. Natl. Acad. Sci U.S.A. 2005
    • (2005) Proc. Natl. Acad. Sci U.S.A.
    • Kanugula, S.1    Pauly, G.T.2    Moschel, R.C.3    Pegg, A.E.4
  • 135
    • 0742321956 scopus 로고    scopus 로고
    • Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair
    • B.R. Chapados, D.J. Hosfield, S. Han, J. Qiu, B. Yelent, B. Shen, and J.A. Tainer Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair Cell 116 2004 39 50
    • (2004) Cell , vol.116 , pp. 39-50
    • Chapados, B.R.1    Hosfield, D.J.2    Han, S.3    Qiu, J.4    Yelent, B.5    Shen, B.6    Tainer, J.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.