메뉴 건너뛰기




Volumn 11, Issue 9, 2012, Pages 766-773

Biochemical mapping of human NEIL1 DNA glycosylase and AP lyase activities

Author keywords

Base excision repair; Human NEIL1 DNA glycosylase; Oxidative DNA repair

Indexed keywords

5 HYDROXYCYTOSINE; 5 HYDROXYURACIL; 8 HYDROXYGUANINE; AP LYASE; ARGININE; CYTOSINE DERIVATIVE; DNA GLYCOSYLTRANSFERASE; DOUBLE STRANDED DNA; HISTIDINE; LYASE; METHIONINE; NEIL2 DNA GLYCOSYLASE; PHENYLALANINE; SCHIFF BASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; URACIL DERIVATIVE;

EID: 84865063582     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2012.07.002     Document Type: Article
Times cited : (37)

References (60)
  • 1
    • 33646080824 scopus 로고    scopus 로고
    • Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products
    • Neeley W.L., Essigmann J.M. Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products. Chem. Res. Toxicol. 2006, 19:491-505.
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 491-505
    • Neeley, W.L.1    Essigmann, J.M.2
  • 2
    • 33644635257 scopus 로고    scopus 로고
    • Toward a detailed understanding of base excision repair enzymes: transition state and mechanistic analyses of N-glycoside hydrolysis and N-glycoside transfer
    • Berti P.J., McCann J.A.B. Toward a detailed understanding of base excision repair enzymes: transition state and mechanistic analyses of N-glycoside hydrolysis and N-glycoside transfer. Chem. Rev. 2006, 106:506-555.
    • (2006) Chem. Rev. , vol.106 , pp. 506-555
    • Berti, P.J.1    McCann, J.A.B.2
  • 4
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • David S.S., O'Shea V.L., Kundu S. Base-excision repair of oxidative DNA damage. Nature 2007, 447:941-950.
    • (2007) Nature , vol.447 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 5
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • Hegde M.L., Hazra T.K., Mitra S. Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells. Cell Res. 2008, 18:27-47.
    • (2008) Cell Res. , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 6
    • 0042342532 scopus 로고    scopus 로고
    • A mechanistic perspective on the chemistry of DNA repair glycosylases
    • Stivers J.T., Jiang Y.L. A mechanistic perspective on the chemistry of DNA repair glycosylases. Chem. Rev. 2003, 103:2729-2759.
    • (2003) Chem. Rev. , vol.103 , pp. 2729-2759
    • Stivers, J.T.1    Jiang, Y.L.2
  • 7
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1)
    • Klungland A., Lindahl T. Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). EMBO J. 1997, 16:3341-3348.
    • (1997) EMBO J. , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 8
    • 0027215222 scopus 로고
    • Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerases
    • Lyamichev V., Brow M.A., Dahlberg J.E. Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerases. Science 1993, 260:778-783.
    • (1993) Science , vol.260 , pp. 778-783
    • Lyamichev, V.1    Brow, M.A.2    Dahlberg, J.E.3
  • 9
    • 0025240665 scopus 로고
    • Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites
    • Boiteux S., O'Connor T.R., Lederer F., Gouyette A., Laval J. Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites. J. Biol. Chem. 1990, 265:3916-3922.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3916-3922
    • Boiteux, S.1    O'Connor, T.R.2    Lederer, F.3    Gouyette, A.4    Laval, J.5
  • 10
    • 0026533905 scopus 로고
    • Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): excision of purine lesions in DNA produced by ionizing radiation or photosensitization
    • Boiteux S., Gajewski E., Laval J., Dizdaroglu M. Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): excision of purine lesions in DNA produced by ionizing radiation or photosensitization. Biochemistry 1992, 31:106-110.
    • (1992) Biochemistry , vol.31 , pp. 106-110
    • Boiteux, S.1    Gajewski, E.2    Laval, J.3    Dizdaroglu, M.4
  • 11
    • 0021331957 scopus 로고
    • DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli
    • Breimer L.H., Lindahl T. DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli. J. Biol Chem. 1984, 259:5543-5548.
    • (1984) J. Biol Chem. , vol.259 , pp. 5543-5548
    • Breimer, L.H.1    Lindahl, T.2
  • 12
    • 0026025356 scopus 로고
    • An endonuclease activity of Escherichia coli that specifically removes 8-hydroxyguanine residues from DNA
    • Chung M.H., Kasai H., Jones D.S., Inoue H., Ishikawa H., Ohtsuka E., Nishimura S. An endonuclease activity of Escherichia coli that specifically removes 8-hydroxyguanine residues from DNA. Mutat. Res. 1991, 254:1-12.
    • (1991) Mutat. Res. , vol.254 , pp. 1-12
    • Chung, M.H.1    Kasai, H.2    Jones, D.S.3    Inoue, H.4    Ishikawa, H.5    Ohtsuka, E.6    Nishimura, S.7
  • 13
    • 0027366974 scopus 로고
    • Substrate specificity of the Escherichia coli endonuclease III: excision of thymine- and cytosine-derived lesions in DNA produced by radiation-generated free radicals
    • Dizdaroglu M., Laval J., Boiteux S. Substrate specificity of the Escherichia coli endonuclease III: excision of thymine- and cytosine-derived lesions in DNA produced by radiation-generated free radicals. Biochemistry 1993, 32:12105-12111.
    • (1993) Biochemistry , vol.32 , pp. 12105-12111
    • Dizdaroglu, M.1    Laval, J.2    Boiteux, S.3
  • 14
    • 0028295382 scopus 로고
    • Isolation and characterization of endonuclease VIII from Escherichia coli
    • Melamede R.J., Hatahet Z., Kow Y.W., Ide H., Wallace S.S. Isolation and characterization of endonuclease VIII from Escherichia coli. Biochemistry 1994, 33:1255-1264.
    • (1994) Biochemistry , vol.33 , pp. 1255-1264
    • Melamede, R.J.1    Hatahet, Z.2    Kow, Y.W.3    Ide, H.4    Wallace, S.S.5
  • 17
    • 0030912695 scopus 로고    scopus 로고
    • Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue
    • Aburatani H., Hippo Y., Ishida T., Takashima R., Matsuba C., Kodama T., Takao M., Yasui A., Yamamoto K., Asano M. Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue. Cancer Res. 1997, 57:2151-2156.
    • (1997) Cancer Res. , vol.57 , pp. 2151-2156
    • Aburatani, H.1    Hippo, Y.2    Ishida, T.3    Takashima, R.4    Matsuba, C.5    Kodama, T.6    Takao, M.7    Yasui, A.8    Yamamoto, K.9    Asano, M.10
  • 18
    • 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
    • Bjoras M., Luna L., Johnsen B., Hoff E., Haug T., Rognes T., Seeberg E. Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites. EMBO J. 1997, 16:6314-6322.
    • (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
  • 19
    • 0031172802 scopus 로고    scopus 로고
    • A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer
    • Lu R., Nash H.M., Verdine G.L. A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer. Curr. Biol. 1997, 7:397-407.
    • (1997) Curr. Biol. , vol.7 , pp. 397-407
    • Lu, R.1    Nash, H.M.2    Verdine, G.L.3
  • 20
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae
    • Radicella J.P., Dherin C., Desmaze C., Fox M.S., Boiteux S. Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:8010-8015.
    • (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
  • 24
    • 0037125133 scopus 로고    scopus 로고
    • A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII
    • Bandaru V., Sunkara S., Wallace S.S., Bond J.P. A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII. DNA Repair (Amst) 2002, 1:517-529.
    • (2002) DNA Repair (Amst) , vol.1 , pp. 517-529
    • Bandaru, V.1    Sunkara, S.2    Wallace, S.S.3    Bond, J.P.4
  • 26
    • 0037162995 scopus 로고    scopus 로고
    • Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions
    • Hazra T.K., Kow Y.W., Hatahet Z., Imhoff B., Boldogh I., Mokkapati S.K., Mitra S., Izumi T. Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions. J. Biol. Chem. 2002, 277:30417-30420.
    • (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
  • 28
    • 0037112668 scopus 로고    scopus 로고
    • Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA
    • Morland I., Rolseth V., Luna L., Rognes T., Bjoras M., Seeberg E. Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA. Nucleic Acids Res. 2002, 30:4926-4936.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4926-4936
    • Morland, I.1    Rolseth, V.2    Luna, L.3    Rognes, T.4    Bjoras, M.5    Seeberg, E.6
  • 30
    • 0347379928 scopus 로고    scopus 로고
    • Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2
    • Dou H., Mitra S., Hazra T.K. Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2. J. Biol. Chem. 2003, 278:49679-49684.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49679-49684
    • Dou, H.1    Mitra, S.2    Hazra, T.K.3
  • 31
    • 77951285397 scopus 로고    scopus 로고
    • The role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA
    • Grin I.R., Dianov G.L., Zharkov D.O. The role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA. FEBS Lett. 2010, 584:1553-1557.
    • (2010) FEBS Lett. , vol.584 , pp. 1553-1557
    • Grin, I.R.1    Dianov, G.L.2    Zharkov, D.O.3
  • 32
    • 24044523891 scopus 로고    scopus 로고
    • NEIL1 excises 3' end proximal oxidative DNA lesions resistant to cleavage by NTH1 and OGG1
    • Parsons J.L., Zharkov D.O., Dianov G.L. NEIL1 excises 3' end proximal oxidative DNA lesions resistant to cleavage by NTH1 and OGG1. Nucleic Acids Res. 2005, 33:4849-4856.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4849-4856
    • Parsons, J.L.1    Zharkov, D.O.2    Dianov, G.L.3
  • 33
    • 34047213485 scopus 로고    scopus 로고
    • NEIL1 is the major DNA glycosylase that processes 5-hydroxyuracil in the proximity of a DNA single-strand break
    • Parsons J.L., Kavli B., Slupphaug G., Dianov G.L. NEIL1 is the major DNA glycosylase that processes 5-hydroxyuracil in the proximity of a DNA single-strand break. Biochemistry 2007, 46:4158-4163.
    • (2007) Biochemistry , vol.46 , pp. 4158-4163
    • Parsons, J.L.1    Kavli, B.2    Slupphaug, G.3    Dianov, G.L.4
  • 34
    • 67650302611 scopus 로고    scopus 로고
    • Catalytically impaired hMYH and NEIL1 mutant proteins identified in patients with primary sclerosing cholangitis and cholangiocarcinoma
    • Forsbring M., Vik E.S., Dalhus B., Karlsen T.H., Bergquist A., Schrumpf E., Bjoras M., Boberg K.M., Alseth I. Catalytically impaired hMYH and NEIL1 mutant proteins identified in patients with primary sclerosing cholangitis and cholangiocarcinoma. Carcinogenesis 2009, 30:1147-1154.
    • (2009) Carcinogenesis , vol.30 , pp. 1147-1154
    • Forsbring, M.1    Vik, E.S.2    Dalhus, B.3    Karlsen, T.H.4    Bergquist, A.5    Schrumpf, E.6    Bjoras, M.7    Boberg, K.M.8    Alseth, I.9
  • 35
    • 46849104669 scopus 로고    scopus 로고
    • Superior removal of hydantoin lesions relative to other oxidized bases by the human DNA glycosylase hNEIL1
    • Krishnamurthy N., Zhao X., Burrows C.J., David S.S. Superior removal of hydantoin lesions relative to other oxidized bases by the human DNA glycosylase hNEIL1. Biochemistry 2008, 47:7137-7146.
    • (2008) Biochemistry , vol.47 , pp. 7137-7146
    • Krishnamurthy, N.1    Zhao, X.2    Burrows, C.J.3    David, S.S.4
  • 36
    • 7944222565 scopus 로고    scopus 로고
    • Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2
    • Hailer M.K., Slade P.G., Martin B.D., Rosenquist T.A., Sugden K.D. Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2. DNA Repair (Amst) 2005, 4:41-50.
    • (2005) DNA Repair (Amst) , vol.4 , pp. 41-50
    • Hailer, M.K.1    Slade, P.G.2    Martin, B.D.3    Rosenquist, T.A.4    Sugden, K.D.5
  • 37
    • 77749252749 scopus 로고    scopus 로고
    • Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts
    • Zhao X., Krishnamurthy N., Burrows C.J., David S.S. Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts. Biochemistry 2010, 49:1658-1666.
    • (2010) Biochemistry , vol.49 , pp. 1658-1666
    • Zhao, X.1    Krishnamurthy, N.2    Burrows, C.J.3    David, S.S.4
  • 38
    • 76749136353 scopus 로고    scopus 로고
    • Evidence for the involvement of DNA repair enzyme NEIL1 in nucleotide excision repair of (5'R)- and (5'S)-8,5'-cyclo-2'-deoxyadenosines
    • Jaruga P., Xiao Y., Vartanian V., Lloyd R.S., Dizdaroglu M. Evidence for the involvement of DNA repair enzyme NEIL1 in nucleotide excision repair of (5'R)- and (5'S)-8,5'-cyclo-2'-deoxyadenosines. Biochemistry 2010, 49:1053-1055.
    • (2010) Biochemistry , vol.49 , pp. 1053-1055
    • Jaruga, P.1    Xiao, Y.2    Vartanian, V.3    Lloyd, R.S.4    Dizdaroglu, M.5
  • 39
    • 0030890419 scopus 로고    scopus 로고
    • Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III
    • Hilbert T.P., Chaung W., Boorstein R.J., Cunningham R.P., Teebor G.W. Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III. J. Biol. Chem. 1997, 272:6733-6740.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6733-6740
    • Hilbert, T.P.1    Chaung, W.2    Boorstein, R.J.3    Cunningham, R.P.4    Teebor, G.W.5
  • 41
    • 0037169522 scopus 로고    scopus 로고
    • Determination of active site residues in Escherichia coli endonuclease VIII
    • Burgess S., Jaruga P., Dodson M.L., Dizdaroglu M., Lloyd R.S. Determination of active site residues in Escherichia coli endonuclease VIII. J. Biol. Chem. 2002, 277:2938-2944.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2938-2944
    • Burgess, S.1    Jaruga, P.2    Dodson, M.L.3    Dizdaroglu, M.4    Lloyd, R.S.5
  • 42
    • 0034477635 scopus 로고    scopus 로고
    • Characterization of a cross-linked DNA-endonuclease VIII repair complex by electrospray ionization mass spectrometry
    • Rieger R.A., McTigue M.M., Kycia J.H., Gerchman S.E., Grollman A.P., Iden C.R. Characterization of a cross-linked DNA-endonuclease VIII repair complex by electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 2000, 11:505-515.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 505-515
    • Rieger, R.A.1    McTigue, M.M.2    Kycia, J.H.3    Gerchman, S.E.4    Grollman, A.P.5    Iden, C.R.6
  • 43
    • 0032403120 scopus 로고    scopus 로고
    • Role of lysine-57 in the catalytic activities of Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg protein)
    • Sidorkina O.M., Laval J. Role of lysine-57 in the catalytic activities of Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg protein). Nucleic Acids Res. 1998, 26:5351-5357.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5351-5357
    • Sidorkina, O.M.1    Laval, J.2
  • 44
    • 0030614471 scopus 로고    scopus 로고
    • NH2-terminal proline acts as a nucleophile in the glycosylase/AP-lyase reaction catalyzed by Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg) protein
    • Zharkov D.O., Rieger R.A., Iden C.R., Grollman A.P. NH2-terminal proline acts as a nucleophile in the glycosylase/AP-lyase reaction catalyzed by Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg) protein. J. Biol. Chem. 1997, 272:5335-5341.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5335-5341
    • Zharkov, D.O.1    Rieger, R.A.2    Iden, C.R.3    Grollman, A.P.4
  • 45
    • 0036160405 scopus 로고    scopus 로고
    • Repair of oxidized purines and damaged pyrimidines by E. coli Fpg protein: different roles of proline 2 and lysine 57 residues
    • Saparbaev M., Sidorkina O.M., Jurado J., Privezentzev C.V., Greenberg M.M., Laval J. Repair of oxidized purines and damaged pyrimidines by E. coli Fpg protein: different roles of proline 2 and lysine 57 residues. Environ. Mol. Mutagen. 2002, 39:10-17.
    • (2002) Environ. Mol. Mutagen. , vol.39 , pp. 10-17
    • Saparbaev, M.1    Sidorkina, O.M.2    Jurado, J.3    Privezentzev, C.V.4    Greenberg, M.M.5    Laval, J.6
  • 47
    • 0034642221 scopus 로고    scopus 로고
    • Involvement of phylogenetically conserved acidic amino acid residues in catalysis by an oxidative DNA damage enzyme formamidopyrimidine glycosylase
    • Lavrukhin O.V., Lloyd R.S. Involvement of phylogenetically conserved acidic amino acid residues in catalysis by an oxidative DNA damage enzyme formamidopyrimidine glycosylase. Biochemistry 2000, 39:15266-15271.
    • (2000) Biochemistry , vol.39 , pp. 15266-15271
    • Lavrukhin, O.V.1    Lloyd, R.S.2
  • 49
    • 70350028650 scopus 로고    scopus 로고
    • Structural characterization of a viral NEIL1 ortholog unliganded and bound to abasic site-containing DNA
    • Imamura K., Wallace S.S., Doublie S. Structural characterization of a viral NEIL1 ortholog unliganded and bound to abasic site-containing DNA. J. Biol. Chem. 2009, 284:26174-26183.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26174-26183
    • Imamura, K.1    Wallace, S.S.2    Doublie, S.3
  • 50
    • 84856695671 scopus 로고    scopus 로고
    • Structural characterization of viral ortholog of human DNA glycosylase NEIL1 bound to thymine glycol or 5-hydroxyuracil-containing DNA
    • Imamura K., Averill A., Wallace S.S., Doublie S. Structural characterization of viral ortholog of human DNA glycosylase NEIL1 bound to thymine glycol or 5-hydroxyuracil-containing DNA. J. Biol. Chem. 2012, 287:4288-4298.
    • (2012) J. Biol. Chem. , vol.287 , pp. 4288-4298
    • Imamura, K.1    Averill, A.2    Wallace, S.S.3    Doublie, S.4
  • 51
    • 3142702720 scopus 로고    scopus 로고
    • The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity
    • Doublie S., Bandaru V., Bond J.P., Wallace S.S. 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 2004, 101:10284-10289.
    • (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
  • 52
    • 33644511436 scopus 로고    scopus 로고
    • Structure of a DNA glycosylase searching for lesions
    • Banerjee A., Santos W.L., Verdine G.L. Structure of a DNA glycosylase searching for lesions. Science 2006, 311:1153-1157.
    • (2006) Science , vol.311 , pp. 1153-1157
    • Banerjee, A.1    Santos, W.L.2    Verdine, G.L.3
  • 53
    • 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
    • Coste F., Ober M., Carell T., Boiteux S., Zelwer C., Castaing B. Structural basis for the recognition of the FapydG lesion (2,6-diamino-4-hydroxy-5-formamidopyrimidine) by formamidopyrimidine-DNA glycosylase. J. Biol. Chem. 2004, 279:44074-44083.
    • (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
  • 54
    • 0036294464 scopus 로고    scopus 로고
    • Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM
    • Fromme J.C., Verdine G. Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM. Nat. Struct. Biol. 2002, 9:544-552.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 544-552
    • Fromme, J.C.1    Verdine, G.2
  • 55
    • 0346435086 scopus 로고    scopus 로고
    • DNA lesion recognition by the bacterial repair enzyme MutM
    • Fromme J.C., Verdine G.L. DNA lesion recognition by the bacterial repair enzyme MutM. J. Biol. Chem. 2003, 278:51543-51548.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51543-51548
    • Fromme, J.C.1    Verdine, G.L.2
  • 57
    • 27244433288 scopus 로고    scopus 로고
    • Structural insights into abasic site for Fpg specific binding and catalysis: comparative high-resolution crystallographic studies of Fpg bound to various models of abasic site analogues-containing DNA
    • Pereira de Jesus K., Serre L., Zelwer C., Castaing B. Structural insights into abasic site for Fpg specific binding and catalysis: comparative high-resolution crystallographic studies of Fpg bound to various models of abasic site analogues-containing DNA. Nucleic Acids Res. 2005, 33:5936-5944.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5936-5944
    • Pereira de Jesus, K.1    Serre, L.2    Zelwer, C.3    Castaing, B.4
  • 58
    • 0037124320 scopus 로고    scopus 로고
    • Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA
    • Serre L., Pereira de Jésus K., Boiteux S., Zelwer C., Castaing B. Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA. EMBO J. 2002, 21:2854-2865.
    • (2002) EMBO J. , vol.21 , pp. 2854-2865
    • Serre, L.1    Pereira de Jésus, K.2    Boiteux, S.3    Zelwer, C.4    Castaing, B.5
  • 59
    • 0034254724 scopus 로고    scopus 로고
    • Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8
    • Sugahara M., Mikawa T., Kumasaka T., Yamamoto M., Kato R., Fukuyama K., Inoue Y., Kuramitsu S. Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8. EMBO J. 2000, 19:3857-3869.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.