메뉴 건너뛰기




Volumn 21, Issue 2, 2013, Pages 247-256

Structural Characterization of a Mouse Ortholog of Human NEIL3 with a Marked Preference for Single-Stranded DNA

Author keywords

[No Author keywords available]

Indexed keywords

8 OXOGUANOSINE; DNA FORMAMIDOPYRIMIDINE GLYCOSYLASE; DNA GLYCOSYLTRANSFERASE; GUANOSINE DERIVATIVE; NEIL3 PROTEIN; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 84873405906     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.12.008     Document Type: Article
Times cited : (51)

References (76)
  • 1
    • 77949527495 scopus 로고    scopus 로고
    • Crystal structure of a replicative DNA polymerase bound to the oxidized guanine lesion guanidinohydantoin
    • P. Aller, Y. Ye, S.S. Wallace, C.J. Burrows, and S. Doublié Crystal structure of a replicative DNA polymerase bound to the oxidized guanine lesion guanidinohydantoin Biochemistry 49 2010 2502 2509
    • (2010) Biochemistry , vol.49 , pp. 2502-2509
    • Aller, P.1    Ye, Y.2    Wallace, S.S.3    Burrows, C.J.4    Doublié, S.5
  • 2
    • 0037125133 scopus 로고    scopus 로고
    • A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII
    • V. Bandaru, S. Sunkara, S.S. Wallace, and J.P. Bond A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII DNA Repair (Amst.) 1 2002 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
  • 4
    • 33644511436 scopus 로고    scopus 로고
    • Structure of a DNA glycosylase searching for lesions
    • A. Banerjee, W.L. Santos, and G.L. Verdine Structure of a DNA glycosylase searching for lesions Science 311 2006 1153 1157
    • (2006) Science , vol.311 , pp. 1153-1157
    • Banerjee, A.1    Santos, W.L.2    Verdine, G.L.3
  • 5
    • 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
  • 6
    • 77952407219 scopus 로고    scopus 로고
    • Substitution of Ala for Tyr567 in RB69 DNA polymerase allows dAMP to be inserted opposite 7,8-dihydro-8-oxoguanine
    • J. Beckman, M. Wang, G. Blaha, J. Wang, and W.H. Konigsberg Substitution of Ala for Tyr567 in RB69 DNA polymerase allows dAMP to be inserted opposite 7,8-dihydro-8-oxoguanine Biochemistry 49 2010 4116 4125
    • (2010) Biochemistry , vol.49 , pp. 4116-4125
    • Beckman, J.1    Wang, M.2    Blaha, G.3    Wang, J.4    Konigsberg, W.H.5
  • 7
    • 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
  • 8
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • A.T. Brunger Version 1.2 of the Crystallography and NMR system Nat. Protoc. 2 2007 2728 2733
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 9
    • 0026515277 scopus 로고
    • DNA containing a chemically reduced apurinic site is a high affinity ligand for the E. coli formamidopyrimidine-DNA glycosylase
    • B. Castaing, S. Boiteux, and C. Zelwer DNA containing a chemically reduced apurinic site is a high affinity ligand for the E. coli formamidopyrimidine-DNA glycosylase Nucleic Acids Res. 20 1992 389 394
    • (1992) Nucleic Acids Res. , vol.20 , pp. 389-394
    • Castaing, B.1    Boiteux, S.2    Zelwer, C.3
  • 10
    • 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
  • 11
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • S.S. David, V.L. O'Shea, and S. Kundu Base-excision repair of oxidative DNA damage Nature 447 2007 941 950
    • (2007) Nature , vol.447 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 12
    • 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
  • 13
    • 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. Doublié, 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. USA 101 2004 10284 10289
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10284-10289
    • Doublié, S.1    Bandaru, V.2    Bond, J.P.3    Wallace, S.S.4
  • 15
    • 84865099174 scopus 로고    scopus 로고
    • Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine
    • S. Duclos, P. Aller, P. Jaruga, M. Dizdaroglu, S.S. Wallace, and S. Doublié Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine DNA Repair (Amst.) 11 2012 714 725
    • (2012) DNA Repair (Amst.) , vol.11 , pp. 714-725
    • Duclos, S.1    Aller, P.2    Jaruga, P.3    Dizdaroglu, M.4    Wallace, S.S.5    Doublié, S.6
  • 16
    • 80053206516 scopus 로고    scopus 로고
    • Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA
    • A.R. Dunn, N.M. Kad, S.R. Nelson, D.M. Warshaw, and S.S. Wallace Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA Nucleic Acids Res. 39 2011 7487 7498
    • (2011) Nucleic Acids Res. , vol.39 , pp. 7487-7498
    • Dunn, A.R.1    Kad, N.M.2    Nelson, S.R.3    Warshaw, D.M.4    Wallace, S.S.5
  • 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
    • 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
  • 20
    • 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
  • 21
    • 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
  • 24
    • 84866887356 scopus 로고    scopus 로고
    • Excision of thymine and 5-hydroxymethyluracil by the MBD4 DNA glycosylase domain: Structural basis and implications for active DNA demethylation
    • H. Hashimoto, X. Zhang, and X. Cheng Excision of thymine and 5-hydroxymethyluracil by the MBD4 DNA glycosylase domain: structural basis and implications for active DNA demethylation Nucleic Acids Res. 40 2012 8276 8284
    • (2012) Nucleic Acids Res. , vol.40 , pp. 8276-8284
    • Hashimoto, H.1    Zhang, X.2    Cheng, X.3
  • 25
    • 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
  • 27
    • 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
  • 28
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • M.L. Hegde, T.K. Hazra, and S. Mitra Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells Cell Res. 18 2008 27 47
    • (2008) Cell Res. , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 30
    • 70350028650 scopus 로고    scopus 로고
    • Structural characterization of a viral NEIL1 ortholog unliganded and bound to abasic site-containing DNA
    • K. Imamura, S.S. Wallace, and S. Doublié Structural characterization of a viral NEIL1 ortholog unliganded and bound to abasic site-containing DNA J. Biol. Chem. 284 2009 26174 26183
    • (2009) J. Biol. Chem. , vol.284 , pp. 26174-26183
    • Imamura, K.1    Wallace, S.S.2    Doublié, S.3
  • 31
    • 84856695671 scopus 로고    scopus 로고
    • Structural characterization of viral ortholog of human DNA glycosylase NEIL1 bound to thymine glycol or 5-hydroxyuracil-containing DNA
    • K. Imamura, A. Averill, S.S. Wallace, and S. Doublié Structural characterization of viral ortholog of human DNA glycosylase NEIL1 bound to thymine glycol or 5-hydroxyuracil-containing DNA J. Biol. Chem. 287 2012 4288 4298
    • (2012) J. Biol. Chem. , vol.287 , pp. 4288-4298
    • Imamura, K.1    Averill, A.2    Wallace, S.S.3    Doublié, S.4
  • 32
    • 0033399115 scopus 로고    scopus 로고
    • Single-stranded oligodeoxyribonucleotides are substrates of Fpg protein from Escherichia coli
    • A.A. Ishchenko, N.V. Bulychev, G.A. Maksakova, F. Johnson, and G.A. Nevinsky Single-stranded oligodeoxyribonucleotides are substrates of Fpg protein from Escherichia coli IUBMB Life 48 1999 613 618
    • (1999) IUBMB Life , vol.48 , pp. 613-618
    • Ishchenko, A.A.1    Bulychev, N.V.2    Maksakova, G.A.3    Johnson, F.4    Nevinsky, G.A.5
  • 33
    • 26444571743 scopus 로고    scopus 로고
    • Structural and thermodynamic features of spiroiminodihydantoin damaged DNA duplexes
    • L. Jia, V. Shafirovich, R. Shapiro, N.E. Geacintov, and S. Broyde Structural and thermodynamic features of spiroiminodihydantoin damaged DNA duplexes Biochemistry 44 2005 13342 13353
    • (2005) Biochemistry , vol.44 , pp. 13342-13353
    • Jia, L.1    Shafirovich, V.2    Shapiro, R.3    Geacintov, N.E.4    Broyde, S.5
  • 35
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 38
    • 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
  • 39
    • 0037168491 scopus 로고    scopus 로고
    • In vitro nucleotide misinsertion opposite the oxidized guanosine lesions spiroiminodihydantoin and guanidinohydantoin and DNA synthesis past the lesions using Escherichia coli DNA polymerase i (Klenow fragment)
    • O. Kornyushyna, A.M. Berges, J.G. Muller, and C.J. Burrows In vitro nucleotide misinsertion opposite the oxidized guanosine lesions spiroiminodihydantoin and guanidinohydantoin and DNA synthesis past the lesions using Escherichia coli DNA polymerase I (Klenow fragment) Biochemistry 41 2002 15304 15314
    • (2002) Biochemistry , vol.41 , pp. 15304-15314
    • Kornyushyna, O.1    Berges, A.M.2    Muller, J.G.3    Burrows, C.J.4
  • 40
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. D Biol. Crystallogr. 60 2004 2256 2268
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 42
    • 33749318279 scopus 로고    scopus 로고
    • Catalytic mechanism of Escherichia coli endonuclease VIII: Roles of the intercalation loop and the zinc finger
    • K.Y. Kropachev, D.O. Zharkov, and A.P. Grollman Catalytic mechanism of Escherichia coli endonuclease VIII: roles of the intercalation loop and the zinc finger Biochemistry 45 2006 12039 12049
    • (2006) Biochemistry , vol.45 , pp. 12039-12049
    • Kropachev, K.Y.1    Zharkov, D.O.2    Grollman, A.P.3
  • 43
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Cryst. 26 1993 283 291
    • (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
  • 44
    • 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. Schärer, 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    Schärer, O.D.2    Samson, L.3    Verdine, G.L.4    Ellenberger, T.5
  • 47
    • 48249147403 scopus 로고    scopus 로고
    • Crystal structure of human thymine DNA glycosylase bound to DNA elucidates sequence-specific mismatch recognition
    • A. Maiti, M.T. Morgan, E. Pozharski, and A.C. Drohat Crystal structure of human thymine DNA glycosylase bound to DNA elucidates sequence-specific mismatch recognition Proc. Natl. Acad. Sci. USA 105 2008 8890 8895
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8890-8895
    • Maiti, A.1    Morgan, M.T.2    Pozharski, E.3    Drohat, A.C.4
  • 48
    • 84862014281 scopus 로고    scopus 로고
    • Crystal structure of human methyl-binding domain IV glycosylase bound to abasic DNA
    • B.A. Manvilla, A. Maiti, M.C. Begley, E.A. Toth, and A.C. Drohat Crystal structure of human methyl-binding domain IV glycosylase bound to abasic DNA J. Mol. Biol. 420 2012 164 175
    • (2012) J. Mol. Biol. , vol.420 , pp. 164-175
    • Manvilla, B.A.1    Maiti, A.2    Begley, M.C.3    Toth, E.A.4    Drohat, A.C.5
  • 49
    • 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
  • 50
    • 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
    • I. Morland, V. Rolseth, L. Luna, T. Rognes, M. Bjørås, and E. Seeberg 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. 30 2002 4926 4936
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4926-4936
    • Morland, I.1    Rolseth, V.2    Luna, L.3    Rognes, T.4    Bjørås, M.5    Seeberg, E.6
  • 51
    • 84859005421 scopus 로고    scopus 로고
    • Release from quiescence stimulates the expression of human NEIL3 under the control of the Ras dependent ERK-MAP kinase pathway
    • C.G. Neurauter, L. Luna, and M. Bjørås Release from quiescence stimulates the expression of human NEIL3 under the control of the Ras dependent ERK-MAP kinase pathway DNA Repair (Amst.) 11 2012 401 409
    • (2012) DNA Repair (Amst.) , vol.11 , pp. 401-409
    • Neurauter, C.G.1    Luna, L.2    Bjørås, M.3
  • 52
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp, and B. Honig Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins 11 1991 281 296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 54
    • 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
  • 55
    • 84863008841 scopus 로고    scopus 로고
    • The Fpg/Nei family of DNA glycosylases: Substrates, structures, and search for damage
    • A. Prakash, S. Doublié, and S.S. Wallace The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage Prog. Mol. Biol. Transl. Sci. 110 2012 71 91
    • (2012) Prog. Mol. Biol. Transl. Sci. , vol.110 , pp. 71-91
    • Prakash, A.1    Doublié, S.2    Wallace, S.S.3
  • 58
    • 48149114323 scopus 로고    scopus 로고
    • Widespread distribution of DNA glycosylases removing oxidative DNA lesions in human and rodent brains
    • V. Rolseth, E. Rundén-Pran, L. Luna, C. McMurray, M. Bjørås, and O.P. Ottersen Widespread distribution of DNA glycosylases removing oxidative DNA lesions in human and rodent brains DNA Repair (Amst.) 7 2008 1578 1588
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 1578-1588
    • Rolseth, V.1    Rundén-Pran, E.2    Luna, L.3    McMurray, C.4    Bjørås, M.5    Ottersen, O.P.6
  • 59
    • 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
  • 61
    • 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 Jésus, 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 Jésus, K.2    Boiteux, S.3    Zelwer, C.4    Castaing, B.5
  • 62
    • 50149091510 scopus 로고    scopus 로고
    • Correlated cleavage of damaged DNA by bacterial and human 8-oxoguanine-DNA glycosylases
    • V.S. Sidorenko, and D.O. Zharkov Correlated cleavage of damaged DNA by bacterial and human 8-oxoguanine-DNA glycosylases Biochemistry 47 2008 8970 8976
    • (2008) Biochemistry , vol.47 , pp. 8970-8976
    • Sidorenko, V.S.1    Zharkov, D.O.2
  • 63
    • 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
  • 64
    • 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
  • 66
    • 60849115568 scopus 로고    scopus 로고
    • Human Nei-like protein NEIL3 has AP lyase activity specific for single-stranded DNA and confers oxidative stress resistance in Escherichia coli mutant
    • M. Takao, Y. Oohata, K. Kitadokoro, K. Kobayashi, S. Iwai, A. Yasui, S. Yonei, and Q.M. Zhang Human Nei-like protein NEIL3 has AP lyase activity specific for single-stranded DNA and confers oxidative stress resistance in Escherichia coli mutant Genes Cells 14 2009 261 270
    • (2009) Genes Cells , vol.14 , pp. 261-270
    • Takao, M.1    Oohata, Y.2    Kitadokoro, K.3    Kobayashi, K.4    Iwai, S.5    Yasui, A.6    Yonei, S.7    Zhang, Q.M.8
  • 67
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution, density modification and model building
    • T. Terwilliger SOLVE and RESOLVE: automated structure solution, density modification and model building J. Synchrotron Radiat. 11 2004 49 52
    • (2004) J. Synchrotron Radiat. , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 69
    • 32944471308 scopus 로고    scopus 로고
    • Hematopoietic tissue-specific expression of mouse Neil3 for endonuclease VIII-like protein
    • K. Torisu, D. Tsuchimoto, Y. Ohnishi, and Y. Nakabeppu Hematopoietic tissue-specific expression of mouse Neil3 for endonuclease VIII-like protein J. Biochem. 138 2005 763 772
    • (2005) J. Biochem. , vol.138 , pp. 763-772
    • Torisu, K.1    Tsuchimoto, D.2    Ohnishi, Y.3    Nakabeppu, Y.4
  • 70
    • 0036628726 scopus 로고    scopus 로고
    • Biological consequences of free radical-damaged DNA bases
    • S.S. Wallace Biological consequences of free radical-damaged DNA bases Free Radic. Biol. Med. 33 2002 1 14
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1-14
    • Wallace, S.S.1
  • 72
    • 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
  • 73
    • 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
  • 74
    • 77749252749 scopus 로고    scopus 로고
    • Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts
    • X. Zhao, N. Krishnamurthy, C.J. Burrows, and S.S. David Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts Biochemistry 49 2010 1658 1666
    • (2010) Biochemistry , vol.49 , pp. 1658-1666
    • Zhao, X.1    Krishnamurthy, N.2    Burrows, C.J.3    David, S.S.4
  • 75
    • 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 (Amst.) 2 2003 839 862
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 839-862
    • Zharkov, D.O.1    Shoham, G.2    Grollman, A.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.