메뉴 건너뛰기




Volumn 44, Issue 43, 2005, Pages 14179-14190

Insight into the roles of tyrosine 82 and glycine 253 in the Escherichia coli adenine glycosylase MutY

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DNA; ENZYMES; MODIFICATION; SUBSTITUTION REACTIONS; TUMORS;

EID: 27444434257     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050976u     Document Type: Article
Times cited : (37)

References (77)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl, T. (1993) Instability and decay of the primary structure of DNA, Nature 362, 709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 3
    • 0033520969 scopus 로고    scopus 로고
    • Quality control by DNA repair
    • Lindahl, T., and Wood, R. D. (1999) Quality control by DNA repair, Science 286, 1897-1905.
    • (1999) Science , vol.286 , pp. 1897-1905
    • Lindahl, T.1    Wood, R.D.2
  • 4
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan, H. E., Standal, R., and Slupphaug, G. (1997) DNA glycosylases in the base excision repair of DNA, Biochem. J. 325, 1-16.
    • (1997) Biochem. J. , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 5
    • 0031574192 scopus 로고    scopus 로고
    • Base excision repair enzyme family portrait: Integrating the structure and chemistry of an entire DNA repair pathway
    • Parikh, S. S., Mol, C. D., and Tainer, J. A. (1997) Base excision repair enzyme family portrait: integrating the structure and chemistry of an entire DNA repair pathway, Structure 5, 1543-1550.
    • (1997) Structure , vol.5 , pp. 1543-1550
    • Parikh, S.S.1    Mol, C.D.2    Tainer, J.A.3
  • 6
    • 0001473891 scopus 로고    scopus 로고
    • Chemistry of glycosylases and endonucleases involved in base-excision repair
    • David, S. S., and Williams, S. D. (1998) Chemistry of glycosylases and endonucleases involved in base-excision repair, Chem. Rev. 98, 1221-1261.
    • (1998) Chem. Rev. , vol.98 , pp. 1221-1261
    • David, S.S.1    Williams, S.D.2
  • 7
    • 0027324378 scopus 로고
    • Mutagenesis by 8-oxoguanine: An enemy within
    • Grollman, A. P., and Moriya, M. (1993) Mutagenesis by 8-oxoguanine: an enemy within, Trends Genet. 9, 246-249.
    • (1993) Trends Genet. , vol.9 , pp. 246-249
    • Grollman, A.P.1    Moriya, M.2
  • 8
    • 4243545125 scopus 로고    scopus 로고
    • Oxidative nucleobase modifications leading to strand scission
    • Burrows, C. J., and Muller, J. G. (1998) Oxidative nucleobase modifications leading to strand scission, Chem. Rev. 98, 1109-1151.
    • (1998) Chem. Rev. , vol.98 , pp. 1109-1151
    • Burrows, C.J.1    Muller, J.G.2
  • 9
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani, S., Takeshita, M., and Grollman, A. P. (1991) Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG, Nature 349, 431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 10
    • 0026452281 scopus 로고
    • Genetic effects of oxidative DNA damage: Comparative mutagenesis of 7,8-dihydro-8-oxo-guanine and 7,8-dihydro-8-oxoadenine in Escherichia coli
    • Wood, M. L., Esteve, A., Morningstar, M. L., Kuziemo, G. M., and Essigman, J. M. (1992) Genetic effects of oxidative DNA damage: comparative mutagenesis of 7,8-dihydro-8-oxo-guanine and 7,8-dihydro-8-oxoadenine in Escherichia coli, Nucleic Acids Res. 20, 6023-6032.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6023-6032
    • Wood, M.L.1    Esteve, A.2    Morningstar, M.L.3    Kuziemo, G.M.4    Essigman, J.M.5
  • 11
    • 0026701365 scopus 로고
    • The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)
    • Michaels, M. L., and Miller, J. H. (1992) The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine), J. Bacteriol. 174, 6321-6325.
    • (1992) J. Bacteriol. , vol.174 , pp. 6321-6325
    • Michaels, M.L.1    Miller, J.H.2
  • 12
    • 0026447255 scopus 로고
    • A repair system for 8-oxo-7,8-dihydrodeoxyguanine
    • Michaels, M. L., Tchou, J., Grollman, A. P., and Miller, J. H. (1992) A repair system for 8-oxo-7,8-dihydrodeoxyguanine, Biochemistry 31, 10964-10968.
    • (1992) Biochemistry , vol.31 , pp. 10964-10968
    • Michaels, M.L.1    Tchou, J.2    Grollman, A.P.3    Miller, J.H.4
  • 13
    • 0028933674 scopus 로고
    • Functional cooperation of MutT, MutM, and MutY proteins in preventing caused by spontaneous oxidation of guanine nucleotides in Escherichia coli
    • Tajiri, T., Maki, H., and Sekiguchi, M. (1995) Functional cooperation of MutT, MutM, and MutY proteins in preventing caused by spontaneous oxidation of guanine nucleotides in Escherichia coli, Mutat. Res. 366, 257-267.
    • (1995) Mutat. Res. , vol.366 , pp. 257-267
    • Tajiri, T.1    Maki, H.2    Sekiguchi, M.3
  • 14
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyzes a potent mutagenic substrate for DNA synthesis
    • Maki, H., and Sekiguchi, M. (1992) MutT protein specifically hydrolyzes a potent mutagenic substrate for DNA synthesis, Nature 355, 273-275.
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 15
    • 0032840464 scopus 로고    scopus 로고
    • Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein
    • Slupska, M. M., Luther, W. M., Chiang, J.-H., Yang, H., and Miller, J. H. (1999) Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein, J. Bacteriol. 181, 6210-6213.
    • (1999) J. Bacteriol. , vol.181 , pp. 6210-6213
    • Slupska, M.M.1    Luther, W.M.2    Chiang, J.-H.3    Yang, H.4    Miller, J.H.5
  • 16
    • 0030738194 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase
    • Rosenquist, T. A., Zharkov, D. O., and Grollman, A. P. (1997) Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase, Proc. Natl. Acad. Sci. U.S.A. 94, 7429-7434.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7429-7434
    • Rosenquist, T.A.1    Zharkov, D.O.2    Grollman, A.P.3
  • 17
    • 0036312376 scopus 로고    scopus 로고
    • Hypoxia induces mitochondrial DNA damage and stimulates expression of a DNA repair enzyme, the Escherichia coli MutY DNA glycosylase homolog (MYH), in vivo, in the rat brain
    • Lee, H.-M., Wang, C., Hu, Z., Greeley, G. H., Makalowski, W., Hellmich, H. L., and Englander, E. W. (2002) Hypoxia induces mitochondrial DNA damage and stimulates expression of a DNA repair enzyme, the Escherichia coli MutY DNA glycosylase homolog (MYH), in vivo, in the rat brain, J. Neurochem. 80, 928-937.
    • (2002) J. Neurochem. , vol.80 , pp. 928-937
    • Lee, H.-M.1    Wang, C.2    Hu, Z.3    Greeley, G.H.4    Makalowski, W.5    Hellmich, H.L.6    Englander, E.W.7
  • 18
    • 0035253515 scopus 로고    scopus 로고
    • Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Apel) in mammalian base excision repair of an A/GO mismatch
    • Yang, H., Clendenin, W. M., Wong, D., Demple, B., Slupska, M. M., Chiang, J.-H., and Miller, J. H. (2001) Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Apel) in mammalian base excision repair of an A/GO mismatch, Nucleic Acids Res. 29, 743-752.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 743-752
    • Yang, H.1    Clendenin, W.M.2    Wong, D.3    Demple, B.4    Slupska, M.M.5    Chiang, J.-H.6    Miller, J.H.7
  • 19
    • 0026703168 scopus 로고
    • Escherichia coli MutY protein has both N-glycosylase and apurinic/apyrimidinic endonuclease activities on A·C and A·G mispairs
    • Tsai-Wu, J.-J., Liu, H.-F., and Lu, A.-L. (1992) Escherichia coli MutY protein has both N-glycosylase and apurinic/apyrimidinic endonuclease activities on A·C and A·G mispairs, Proc. Natl. Acad. Sci. U.S.A. 89, 8779-8783.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8779-8783
    • Tsai-Wu, J.-J.1    Liu, H.-F.2    Lu, A.-L.3
  • 20
    • 0032553004 scopus 로고    scopus 로고
    • Single-turnover and pre-steady-state kinetics of the reaction of the adenine glycosylase MutY with mismatch-containing DNA substrates
    • Porello, S. L., Leyes, A. E., and David, S. S. (1998) Single-turnover and pre-steady-state kinetics of the reaction of the adenine glycosylase MutY with mismatch-containing DNA substrates, Biochemistry 37, 14756-14764.
    • (1998) Biochemistry , vol.37 , pp. 14756-14764
    • Porello, S.L.1    Leyes, A.E.2    David, S.S.3
  • 21
    • 0035863770 scopus 로고    scopus 로고
    • Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain
    • Chmiel, N. H., Golinelli, M. P., Francis, A. W., and David, S. S. (2001) Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain, Nucleic Acids Res. 29, 553-564.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 553-564
    • Chmiel, N.H.1    Golinelli, M.P.2    Francis, A.W.3    David, S.S.4
  • 22
    • 0043032741 scopus 로고    scopus 로고
    • Adenine release is fast in MutY-catalyzed hydrolysis of G:A and 8-oxo-G:A DNA mismatches
    • McCann, J. A. B., and Berti, P. J. (2003) Adenine release is fast in MutY-catalyzed hydrolysis of G:A and 8-oxo-G:A DNA mismatches, J. Biol. Chem. 278, 29587-29592.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29587-29592
    • McCann, J.A.B.1    Berti, P.J.2
  • 23
    • 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
    • Wong, I., Lundquist, A. J., Bernards, A. S., and Mosbaugh, D. W. (2002) Presteady-state analysis of a single catalytic turnover by Escherichia coli uracil-DNA glycosylase reveals a "pinch-pull-push" mechanism, J. Biol. Chem. 277, 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
  • 24
    • 0037199967 scopus 로고    scopus 로고
    • Effects of hydrogen bonding within a damaged base pair on the activity of wild-type and DNA-intercalating mutants of human alkyladenine DNA glycosylase
    • Vallur, A. C., Feller, J. A., Abner, C. W., Tran, R. K., and Bloom, L. B. (2002) Effects of hydrogen bonding within a damaged base pair on the activity of wild-type and DNA-intercalating mutants of human alkyladenine DNA glycosylase, J. Biol. Chem. 277, 31673-31678.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31673-31678
    • Vallur, A.C.1    Feller, J.A.2    Abner, C.W.3    Tran, R.K.4    Bloom, L.B.5
  • 25
    • 0141790433 scopus 로고    scopus 로고
    • Recognition and removal of oxidized guanines in duplex DNA by the base excision repair enzymes hOGG1, yOGG1, and yOGG2
    • Leipold, M. D., Workman, H., Muller, J. G., Burrows, C. J., and David, S. S. (2003) Recognition and removal of oxidized guanines in duplex DNA by the base excision repair enzymes hOGG1, yOGG1, and yOGG2, Biochemistry 38, 11373-11381.
    • (2003) Biochemistry , vol.38 , pp. 11373-11381
    • Leipold, M.D.1    Workman, H.2    Muller, J.G.3    Burrows, C.J.4    David, S.S.5
  • 28
    • 0026684849 scopus 로고
    • Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA
    • Michaels, M. L., Cruz, C., Grollman, A. P., and Miller, J. H. (1992) Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA, Proc. Natl. Acad. Sci. U.S.A. 89, 7022-7025.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7022-7025
    • Michaels, M.L.1    Cruz, C.2    Grollman, A.P.3    Miller, J.H.4
  • 30
    • 0030004207 scopus 로고    scopus 로고
    • Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage
    • Slupska, M. M., Baikalov, C., Luther, W. M., Chiang, J.-H., Wei, Y.-F., and Miller, J. H. (1996) Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage, J. Bacteriol. 178, 3885-3892.
    • (1996) J. Bacteriol. , vol.178 , pp. 3885-3892
    • Slupska, M.M.1    Baikalov, C.2    Luther, W.M.3    Chiang, J.-H.4    Wei, Y.-F.5    Miller, J.H.6
  • 31
    • 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
    • Chmiel, N. H., Livingston, A. L., and David, S. S. (2003) 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, 431-443.
    • (2003) J. Mol. Biol. , vol.327 , pp. 431-443
    • Chmiel, N.H.1    Livingston, A.L.2    David, S.S.3
  • 32
  • 34
    • 0141960200 scopus 로고    scopus 로고
    • Exposing the MYtH about base excision repair and human genetic disease
    • Cheadle, J. P., and Sampson, J. R. (2003) Exposing the MYtH about base excision repair and human genetic disease, Hum. Mol. Genet. 12, R159-R165.
    • (2003) Hum. Mol. Genet. , vol.12
    • Cheadle, J.P.1    Sampson, J.R.2
  • 36
    • 13244261067 scopus 로고    scopus 로고
    • The potential for increased clinical sensitivity in genetic testing for polyposis colorectal cancer through the analysis of MYH mutations in North American patients
    • Eliason, K., Hendrickson, B. C., Judkins, T., Norton, M., Leclair, B., Lyon, E., Ward, B., Noll, W., and Scholl, T. (2005) The potential for increased clinical sensitivity in genetic testing for polyposis colorectal cancer through the analysis of MYH mutations in North American patients, J. Med. Genet. 42, 95-96.
    • (2005) J. Med. Genet. , vol.42 , pp. 95-96
    • Eliason, K.1    Hendrickson, B.C.2    Judkins, T.3    Norton, M.4    Leclair, B.5    Lyon, E.6    Ward, B.7    Noll, W.8    Scholl, T.9
  • 37
    • 0042670003 scopus 로고    scopus 로고
    • Inherited defects in the DNA glycosylase MYH cause multiple colorectal adenoma and carcinoma
    • Cheadle, J. P., Dolwani, S., and Sampson, J. R. (2003) Inherited defects in the DNA glycosylase MYH cause multiple colorectal adenoma and carcinoma, Carcinogenesis 24, 1281-1282.
    • (2003) Carcinogenesis , vol.24 , pp. 1281-1282
    • Cheadle, J.P.1    Dolwani, S.2    Sampson, J.R.3
  • 38
    • 4644335014 scopus 로고    scopus 로고
    • Colorectal cancer and inherited mutations in base-excision repair
    • Chow, E., Thirlwell, C., Macrae, F., and Lipton, L. (2004) Colorectal cancer and inherited mutations in base-excision repair, Lancet Oncol. 5, 600-606.
    • (2004) Lancet Oncol. , vol.5 , pp. 600-606
    • Chow, E.1    Thirlwell, C.2    Macrae, F.3    Lipton, L.4
  • 40
    • 3543020359 scopus 로고    scopus 로고
    • The multiple colorectal adenoma phenotype and MYH, a excision repair gene
    • Lipton, L., and Tomlinson, I. P. M. (2004) The multiple colorectal adenoma phenotype and MYH, a excision repair gene, Clin. Gastroenterol. Hepatol. 2, 633-638.
    • (2004) Clin. Gastroenterol. Hepatol. , vol.2 , pp. 633-638
    • Lipton, L.1    Tomlinson, I.P.M.2
  • 41
    • 0031763884 scopus 로고    scopus 로고
    • MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily
    • Guan, Y., Manuel, R. C., Arvai, A. S., Parikh, S. S., Mol, C. D., Miller, J. H., Lloyd, R. S., and Tainer, J. A. (1998) MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily, Nat. Struct. Biol. 5, 1058-1064.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1058-1064
    • Guan, Y.1    Manuel, R.C.2    Arvai, A.S.3    Parikh, S.S.4    Mol, C.D.5    Miller, J.H.6    Lloyd, R.S.7    Tainer, J.A.8
  • 42
    • 0042342532 scopus 로고    scopus 로고
    • A mechanistic perspective on the chemistry of DNA repair glycosylases
    • Stivers, J. T., and Jiang, Y. L. (2003) A mechanistic perspective on the chemistry of DNA repair glycosylases, Chem. Rev. 103, 2729-2759.
    • (2003) Chem. Rev. , vol.103 , pp. 2729-2759
    • Stivers, J.T.1    Jiang, Y.L.2
  • 44
    • 0036290411 scopus 로고    scopus 로고
    • Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase
    • Bjoras, M., Seeberg, E., Luna, L., Pearl, L. H., and Barrett, T. E. (2002) Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase, J. Mol. Biol. 317, 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
  • 45
    • 0036431531 scopus 로고    scopus 로고
    • Role of base flipping in specific recognition of damaged DNA by repair enzymes
    • Fuxreiter, M., Luo, N., Jedlovszky, P., Simon, L, and Osman, R. (2002) Role of base flipping in specific recognition of damaged DNA by repair enzymes, J. Mol. Biol. 323, 823-834.
    • (2002) J. Mol. Biol. , vol.323 , pp. 823-834
    • Fuxreiter, M.1    Luo, N.2    Jedlovszky, P.3    Simon, L.4    Osman, R.5
  • 46
    • 0142126715 scopus 로고    scopus 로고
    • Human alkyladenine DNA glycosylase uses acid-base catalysis for selective excision of damaged purines
    • O'Brien, P. J., and Ellenberger, T. (2003) Human alkyladenine DNA glycosylase uses acid-base catalysis for selective excision of damaged purines, Biochemistry 42, 12418-12429.
    • (2003) Biochemistry , vol.42 , pp. 12418-12429
    • O'Brien, P.J.1    Ellenberger, T.2
  • 47
    • 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., and Seeberg, E. (2002) 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, 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
  • 48
    • 1342304229 scopus 로고    scopus 로고
    • Structural basis for removing adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase
    • Fromme, J. C., Banerjee, A., Huang, S. J., and Verdine, G. L. (2004) Structural basis for removing adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase, Nature 427, 652-656.
    • (2004) Nature , vol.427 , pp. 652-656
    • Fromme, J.C.1    Banerjee, A.2    Huang, S.J.3    Verdine, G.L.4
  • 49
    • 0033580647 scopus 로고    scopus 로고
    • The C-terminal domain of the adenine-DNA glycosylase MutY confers specificity for 8-oxoguanine-adenine mispairs and may have evolved from MutT, an 8-oxo-dGTPase
    • Noll, D. M., Gogos, A., Granek, J. A., and Clarke, N. D. (1999) The C-terminal domain of the adenine-DNA glycosylase MutY confers specificity for 8-oxoguanine-adenine mispairs and may have evolved from MutT, an 8-oxo-dGTPase, Biochemistry 38, 6374-6379.
    • (1999) Biochemistry , vol.38 , pp. 6374-6379
    • Noll, D.M.1    Gogos, A.2    Granek, J.A.3    Clarke, N.D.4
  • 51
    • 0037925462 scopus 로고    scopus 로고
    • Structure of a trapped endonuclease III-DNA covalent intermediate
    • Fromme, J. C., and Verdine, G. L. (2003) Structure of a trapped endonuclease III-DNA covalent intermediate, EMBO J. 22, 3461-3471.
    • (2003) EMBO J. , vol.22 , pp. 3461-3471
    • Fromme, J.C.1    Verdine, G.L.2
  • 54
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 55
    • 0029836886 scopus 로고    scopus 로고
    • Specific recognition of substrate analogs by the DNA mismatch repair enzyme MutY
    • Porello, S. L., Williams, S. D., Kuhn, H., Michaels, M. L., and David, S. S. (1996) Specific recognition of substrate analogs by the DNA mismatch repair enzyme MutY, J. Am. Chem. Soc. 118, 10684-10692.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10684-10692
    • Porello, S.L.1    Williams, S.D.2    Kuhn, H.3    Michaels, M.L.4    David, S.S.5
  • 56
    • 0034254745 scopus 로고    scopus 로고
    • Positively charged residues within the iron-sulfur cluster loop of E. coli MutY participate in damage recognition and removal
    • Chepanoske, C. L., Golinelli, M. P., Williams, S. D., and David, S. S. (2000) Positively charged residues within the iron-sulfur cluster loop of E. coli MutY participate in damage recognition and removal, Arch. Biochem. Biophys. 380, 11-19.
    • (2000) Arch. Biochem. Biophys. , vol.380 , pp. 11-19
    • Chepanoske, C.L.1    Golinelli, M.P.2    Williams, S.D.3    David, S.S.4
  • 57
    • 0037151055 scopus 로고    scopus 로고
    • Escherichia coli apurinic-apyrimidinic endonucleases enhance the turnover of the adenine glycosylase MutY with G:A substrates
    • Pope, M. A., Porello, S. L., and David, S. S. (2002) Escherichia coli apurinic-apyrimidinic endonucleases enhance the turnover of the adenine glycosylase MutY with G:A substrates, J. Biol. Chem. 277, 22605-22615.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22605-22615
    • Pope, M.A.1    Porello, S.L.2    David, S.S.3
  • 59
    • 1642494901 scopus 로고    scopus 로고
    • A residue in MutY important for catalysis indentified by photocross-linking and mass spectrometry
    • Chepanoske, C. L., Lukianova, O. L., Lombard, M., Golinelli-Cohen, M.-P., and David, S. S. (2004) A residue in MutY important for catalysis indentified by photocross-linking and mass spectrometry, Biochemistry 43, 651-662.
    • (2004) Biochemistry , vol.43 , pp. 651-662
    • Chepanoske, C.L.1    Lukianova, O.L.2    Lombard, M.3    Golinelli-Cohen, M.-P.4    David, S.S.5
  • 60
    • 0028933306 scopus 로고
    • Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase
    • Slupphaug, G., Eftedal, I., Bharati, S., Helle, N. M., Haug, T., Levine, D. W., and Krokan, H. E. (1995) Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase, Biochemistry 34, 128-138.
    • (1995) Biochemistry , vol.34 , pp. 128-138
    • Slupphaug, G.1    Eftedal, I.2    Bharati, S.3    Helle, N.M.4    Haug, T.5    Levine, D.W.6    Krokan, H.E.7
  • 61
    • 0026323912 scopus 로고
    • Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA
    • Record, M. T., Ha, J.-H., and Fisher, M. A. (1991) Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA, Methods Enzymol. 208, 291-343.
    • (1991) Methods Enzymol. , vol.208 , pp. 291-343
    • Record, M.T.1    Ha, J.-H.2    Fisher, M.A.3
  • 62
    • 0034610336 scopus 로고    scopus 로고
    • Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG
    • Lau, A. Y., Wyatt, M. D., Glassner, B. J., Samson, L. D., and Ellenberger, T. (2000) Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG, Proc. Natl. Acad. Sci. U.S.A. 97, 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
  • 63
    • 0032538337 scopus 로고    scopus 로고
    • Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: Mechanisms for nucleotide flipping and base excision
    • Lau, A. Y., Scharer, O. D., Samson, L. D., Verdine, G. L., and Ellenberger, T. (1998) Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision, Cell 95, 249-258.
    • (1998) Cell , vol.95 , pp. 249-258
    • Lau, A.Y.1    Scharer, O.D.2    Samson, L.D.3    Verdine, G.L.4    Ellenberger, T.5
  • 64
    • 0032167424 scopus 로고    scopus 로고
    • Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
    • Parikh, S. S., Mol, C. D., Slupphaug, G., Bharati, S., Krokan, H. E., and Tainer, J. A. (1998) Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA, EMBO J. 17, 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
  • 65
    • 4444286415 scopus 로고    scopus 로고
    • Contribution of a conserved phenylalanine residue to the activity of Escherichia coli uracil DNA glycosylase
    • Shaw, R. W., Feller, J. A., and Bloom, L. B. (2004) Contribution of a conserved phenylalanine residue to the activity of Escherichia coli uracil DNA glycosylase, DNA Repair 3, 1273-1283.
    • (2004) DNA Repair , vol.3 , pp. 1273-1283
    • Shaw, R.W.1    Feller, J.A.2    Bloom, L.B.3
  • 66
    • 0034651873 scopus 로고    scopus 로고
    • DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA
    • Hollis, T., Ichikawa, Y., and Ellenberger, T. (2000) DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA, EMBO J. 19, 758-766.
    • (2000) EMBO J. , vol.19 , pp. 758-766
    • Hollis, T.1    Ichikawa, Y.2    Ellenberger, T.3
  • 68
    • 0037100702 scopus 로고    scopus 로고
    • Effects of mutations at tyrosine 66 and asparagine 123 in the active site pocket of Escherichia coli uracil DNA glycosylase on uracil excision from synthetic DNA oligomers: Evidence for the occurrence of long-range interactions between enzyme and substrate
    • Handa, P., Acharya, N., and Varshney, U. (2002) Effects of mutations at tyrosine 66 and asparagine 123 in the active site pocket of Escherichia coli uracil DNA glycosylase on uracil excision from synthetic DNA oligomers: evidence for the occurrence of long-range interactions between enzyme and substrate, Nucleic Acids Res. 30, 3086-3095.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3086-3095
    • Handa, P.1    Acharya, N.2    Varshney, U.3
  • 69
    • 0035907352 scopus 로고    scopus 로고
    • The role of leucine 191 of Escherichia coli uracil DNA glycosylase in the formation of a highly stable complex with the substrate mimic, ugi, and in uracil excision from the synthetic substrate
    • Handa, P., Roy, S., and Varshney, U. (2001) The role of leucine 191 of Escherichia coli uracil DNA glycosylase in the formation of a highly stable complex with the substrate mimic, ugi, and in uracil excision from the synthetic substrate, J. Biol. Chem. 276, 17324-17331.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17324-17331
    • Handa, P.1    Roy, S.2    Varshney, U.3
  • 71
    • 15844379169 scopus 로고    scopus 로고
    • Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA
    • Banerjee, A., Yang, W., Karplus, M., and Verdine, G. L. (2005) Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA, Nature 434, 612-618.
    • (2005) Nature , vol.434 , pp. 612-618
    • Banerjee, A.1    Yang, W.2    Karplus, M.3    Verdine, G.L.4
  • 72
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxo-guanine in DNA
    • Brimer, S. D., Norman, D. P. G., and Verdine, G. L. (2000) Structural basis for recognition and repair of the endogenous mutagen 8-oxo-guanine in DNA, Nature 403, 859-866.
    • (2000) Nature , vol.403 , pp. 859-866
    • Brimer, S.D.1    Norman, D.P.G.2    Verdine, G.L.3
  • 73
    • 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., and Castaing, B. (2004) Structural basis for the recognition of the FapydG lesion (2,6-diamino-4-hydroxy-5-formamidopyrimidine) by formamidopyrimidine-DNA glycosylase, J. Biol. Chem. 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
  • 74
    • 4143149415 scopus 로고    scopus 로고
    • Site-specific DNA damage recognition by enzyme-induced base flipping
    • Stivers, J. T. (2004) Site-specific DNA damage recognition by enzyme-induced base flipping, Prog. Nucleic Acid Res. 77, 37-65.
    • (2004) Prog. Nucleic Acid Res. , vol.77 , pp. 37-65
    • Stivers, J.T.1
  • 76
    • 0034093291 scopus 로고    scopus 로고
    • Passing the baton in base excision repair
    • Wilson, S. H., and Kunkel, T. A. (2000) Passing the baton in base excision repair, Nat. Struct. Biol. 7, 176-178.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 176-178
    • Wilson, S.H.1    Kunkel, T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.