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Volumn 44, Issue 23, 2005, Pages 8397-8407

DNA-bound redox activity of DNA repair glycosylases containing [4Fe-4S] clusters

Author keywords

[No Author keywords available]

Indexed keywords

DEGRADATION; ELECTRODES; ELECTRON TRANSPORT PROPERTIES; ENZYMES; ESCHERICHIA COLI; GENES; OXIDATION; REDOX REACTIONS; SIGNALING;

EID: 20444411178     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047494n     Document Type: Article
Times cited : (166)

References (98)
  • 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
    • 0042872991 scopus 로고    scopus 로고
    • Chemistry and biology of DNA repair
    • Scharer, O. D. (2003) Chemistry and biology of DNA repair, Angew. Chem., Int. Ed. Engl. 42, 2946-2974.
    • (2003) Angew. Chem., Int. Ed. Engl. , vol.42 , pp. 2946-2974
    • Scharer, O.D.1
  • 4
    • 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, 1221-1262.
    • (1998) Chem. Rev. , vol.98 , pp. 1221-1262
    • David, S.S.1    Williams, S.D.2
  • 5
    • 0031149139 scopus 로고    scopus 로고
    • How do DNA repair proteins locate damaged bases in the genome?
    • Verdine, G. L., and Bruner, S. D. (1997) How do DNA repair proteins locate damaged bases in the genome?, Chem. Biol. 4, 329-334.
    • (1997) Chem. Biol. , vol.4 , pp. 329-334
    • Verdine, G.L.1    Bruner, S.D.2
  • 6
    • 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
  • 7
    • 0024971541 scopus 로고
    • Modulation of the DNA scanning activity of the Micrococcus luteus UV endonuclease
    • Hamilton, R. W., and Lloyd, R. S. (1989) Modulation of the DNA scanning activity of the Micrococcus luteus UV endonuclease, J. Biol. Chem. 264, 17422-17427.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17422-17427
    • Hamilton, R.W.1    Lloyd, R.S.2
  • 8
    • 0029054792 scopus 로고
    • Comparison of recombination in vitro and in E. coli cells: Measure of the effective concentration of DNA in vivo
    • Hildebrandt, E. R., and Cozzarelli, N. R. (1995) Comparison of recombination in vitro and in E. coli cells: measure of the effective concentration of DNA in vivo, Cell 81, 331-340.
    • (1995) Cell , vol.81 , pp. 331-340
    • Hildebrandt, E.R.1    Cozzarelli, N.R.2
  • 9
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • Demple, B., and Harrison, L. (1994) Repair of oxidative damage to DNA: enzymology and biology, Annu. Rev. Biochem. 63, 915-948.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 10
    • 2442590835 scopus 로고    scopus 로고
    • Transcriptional mutagenesis induced by uracil and 8-oxoguanine in Escherichia coli
    • Bregeon, D., Doddridge, Z. A., You, H. J., Weiss, B., and Doetsch, P. W. (2003) Transcriptional mutagenesis induced by uracil and 8-oxoguanine in Escherichia coli, Mol. Cells 12, 959-970.
    • (2003) Mol. Cells , vol.12 , pp. 959-970
    • Bregeon, D.1    Doddridge, Z.A.2    You, H.J.3    Weiss, B.4    Doetsch, P.W.5
  • 11
    • 0037192812 scopus 로고    scopus 로고
    • Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6
    • Gu, Y., Parker, A., Wilson, T. M., Bai, H., Chang, D. Y., and Lu, A. L. (2002) Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6, J. Biol. Chem. 277, 11135-11142.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11135-11142
    • Gu, Y.1    Parker, A.2    Wilson, T.M.3    Bai, H.4    Chang, D.Y.5    Lu, A.L.6
  • 12
    • 0035253515 scopus 로고    scopus 로고
    • Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) 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 (Ape1) 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
  • 13
    • 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
  • 14
    • 0035877851 scopus 로고    scopus 로고
    • Stimulation of human endonuclease III by Y box-binding protein 1 (DNA-binding protein B). Interaction between a base excision repair enzyme and a transcription factor
    • Marenstein, D. R., Ocampo, M. T., Chan, M. K., Altamirano, A., Basu, A. K., Boorstein, R. J., Cunningham, R. P., and Teebor, G. W. (2001) Stimulation of human endonuclease III by Y box-binding protein 1 (DNA-binding protein B). Interaction between a base excision repair enzyme and a transcription factor, J. Biol. Chem. 276, 21242-21249.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21242-21249
    • Marenstein, D.R.1    Ocampo, M.T.2    Chan, M.K.3    Altamirano, A.4    Basu, A.K.5    Boorstein, R.J.6    Cunningham, R.P.7    Teebor, G.W.8
  • 16
    • 0348010372 scopus 로고    scopus 로고
    • In vitro and in vivo dimerization of human endonuclease III stimulates its activity
    • Liu, X., Choudhury, S., and Roy, R. (2003) In vitro and in vivo dimerization of human endonuclease III stimulates its activity, J. Biol. Chem. 278, 50061-50069.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50061-50069
    • Liu, X.1    Choudhury, S.2    Roy, R.3
  • 17
    • 0037462768 scopus 로고    scopus 로고
    • A dimeric mechanism for contextual target recognition by MutY glycosylase
    • Wong, I., Bernards, A. S., Miller, J. K., and Wirz, J. A. (2003) A dimeric mechanism for contextual target recognition by MutY glycosylase, J. Biol. Chem. 278, 2411-2418.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2411-2418
    • Wong, I.1    Bernards, A.S.2    Miller, J.K.3    Wirz, J.A.4
  • 18
    • 0033079847 scopus 로고    scopus 로고
    • Long-range oxidative damage to DNA: Effects of distance and sequence
    • Nunez, M. E., Hall, D. B., and Barton, J. K. (1999) Long-range oxidative damage to DNA: effects of distance and sequence, Chem. Biol. 6, 85-97.
    • (1999) Chem. Biol. , vol.6 , pp. 85-97
    • Nunez, M.E.1    Hall, D.B.2    Barton, J.K.3
  • 19
    • 0033555454 scopus 로고    scopus 로고
    • Electron transfer between bases in double helical DNA
    • Kelley, S. O., and Barton, J. K. (1999) Electron transfer between bases in double helical DNA, Science 283, 375-381.
    • (1999) Science , vol.283 , pp. 375-381
    • Kelley, S.O.1    Barton, J.K.2
  • 20
    • 0030665685 scopus 로고    scopus 로고
    • Photoinduced electron transfer in ethidium-modified DNA duplexes: Dependence on distance and base stacking
    • Kelley, S. O., Holmlin, R. E., Stemp, E. D. A., and Barton, J. K. (1997) Photoinduced electron transfer in ethidium-modified DNA duplexes: dependence on distance and base stacking, J. Am. Chem. Soc. 119, 9861-9870.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 9861-9870
    • Kelley, S.O.1    Holmlin, R.E.2    Stemp, E.D.A.3    Barton, J.K.4
  • 22
    • 0034058321 scopus 로고    scopus 로고
    • Long-range charge transfer in DNA: Transient structural distortions control the distance dependence
    • Schuster, G. B. (2000) Long-range charge transfer in DNA: transient structural distortions control the distance dependence, Acc. Chem. Res. 33, 253-260.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 253-260
    • Schuster, G.B.1
  • 23
    • 0035997345 scopus 로고    scopus 로고
    • Long-distance electron transfer through DNA
    • Giese, B. (2002) Long-distance electron transfer through DNA, Annu. Rev. Biochem. 71, 51-70.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 51-70
    • Giese, B.1
  • 24
    • 0035850541 scopus 로고    scopus 로고
    • Influence of intervening mismatches on long-range guanine oxidation in DNA duplexes
    • Bhattacharya, P. K., and Barton, J. K. (2001) Influence of intervening mismatches on long-range guanine oxidation in DNA duplexes, J. Am. Chem. Soc. 123, 8649-8656.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8649-8656
    • Bhattacharya, P.K.1    Barton, J.K.2
  • 25
    • 0031005140 scopus 로고    scopus 로고
    • Sensitivity of DNA-mediated electron transfer to the intervening π-stack: A probe for the integrity of the DNA base stack
    • Hall, D. B., and Barton, J. K. (1997) Sensitivity of DNA-mediated electron transfer to the intervening π-stack: a probe for the integrity of the DNA base stack, J. Am. Chem. Soc. 119, 5045-5046.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5045-5046
    • Hall, D.B.1    Barton, J.K.2
  • 26
    • 0035826678 scopus 로고    scopus 로고
    • How different DNA-binding proteins affect long-range oxidative damage to DNA
    • Rajski, S. R., and Barton, J. K. (2001) How different DNA-binding proteins affect long-range oxidative damage to DNA, Biochemistry 40, 5556-5564.
    • (2001) Biochemistry , vol.40 , pp. 5556-5564
    • Rajski, S.R.1    Barton, J.K.2
  • 27
    • 0036197920 scopus 로고    scopus 로고
    • An electrical probe of protein-DNA interactions on DNA-modified surfaces
    • Boon, E. M., Salas, J. E., and Barton, J. K. (2002) An electrical probe of protein-DNA interactions on DNA-modified surfaces, Nat. Biotechnol. 20, 282-286.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 282-286
    • Boon, E.M.1    Salas, J.E.2    Barton, J.K.3
  • 28
    • 0033772184 scopus 로고    scopus 로고
    • Mutation detection by electrocatalysis at DNA-modified electrodes
    • Boon, E. M., Ceres, D. M., Drummond, T. G., Hill, M. G., and Barton, J. K. (2000) Mutation detection by electrocatalysis at DNA-modified electrodes, Nat. Biotechnol. 18, 1096-1100.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1096-1100
    • Boon, E.M.1    Ceres, D.M.2    Drummond, T.G.3    Hill, M.G.4    Barton, J.K.5
  • 29
    • 0036238830 scopus 로고    scopus 로고
    • Oxidative charge transport through DNA in nucleosome core particles
    • Nunez, M. E., Noyes, K. T., and Barton, J. K. (2002) Oxidative charge transport through DNA in nucleosome core particles, Chem. Biol. 9, 403-415.
    • (2002) Chem. Biol. , vol.9 , pp. 403-415
    • Nunez, M.E.1    Noyes, K.T.2    Barton, J.K.3
  • 30
    • 0035940432 scopus 로고    scopus 로고
    • Evidence for charge transport in the nucleus
    • Nunez, M. E., Holmquist, G. P., and Barton, J. K. (2001) Evidence for charge transport in the nucleus, Biochemistry 40, 12465-12471.
    • (2001) Biochemistry , vol.40 , pp. 12465-12471
    • Nunez, M.E.1    Holmquist, G.P.2    Barton, J.K.3
  • 31
    • 0035969706 scopus 로고    scopus 로고
    • On the non-uniform distribution of guanine in introns of human genes: Possible protection of exons against oxidation by proximal intron poly-G sequences
    • Friedman, K. A., and Heller, A. (2001) On the non-uniform distribution of guanine in introns of human genes: possible protection of exons against oxidation by proximal intron poly-G sequences, J. Phys. Chem. B 105, 11859-11865.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 11859-11865
    • Friedman, K.A.1    Heller, A.2
  • 32
    • 0033953141 scopus 로고    scopus 로고
    • DNA repair: Models for damage and mismatch recognition
    • Rajski, S. R., Jackson, B. A., and Barton, J. K. (2000) DNA repair: models for damage and mismatch recognition, Mutat. Res. 447, 49-72.
    • (2000) Mutat. Res. , vol.447 , pp. 49-72
    • Rajski, S.R.1    Jackson, B.A.2    Barton, J.K.3
  • 37
    • 0031679414 scopus 로고    scopus 로고
    • Spore photoproduct lyase from Bacillus subtilis spores is a novel iron-sulfur DNA repair enzyme which shares features with proteins such as class III anaerobic ribonucleotide reductases and pyruvate-formate lyases
    • Rebeil, R., Sun, Y., Chooback, L., Pedraza-Reyes, M., Kinsland, C., Begley, T. P., and Nicholson, W. L. (1998) Spore photoproduct lyase from Bacillus subtilis spores is a novel iron-sulfur DNA repair enzyme which shares features with proteins such as class III anaerobic ribonucleotide reductases and pyruvate-formate lyases, J. Bacteriol. 180, 4879-4885.
    • (1998) J. Bacteriol. , vol.180 , pp. 4879-4885
    • Rebeil, R.1    Sun, Y.2    Chooback, L.3    Pedraza-Reyes, M.4    Kinsland, C.5    Begley, T.P.6    Nicholson, W.L.7
  • 38
    • 0037187074 scopus 로고    scopus 로고
    • Electron paramagnetic resonance study reveals a putative iron-sulfur cluster in human rpS3 protein
    • Lee, C. H., Kim, S. H., Choi, J. I., Choi, J. Y., Lee, C. E., and Kim, J. (2002) Electron paramagnetic resonance study reveals a putative iron-sulfur cluster in human rpS3 protein, Mol. Cells 13, 154-156.
    • (2002) Mol. Cells , vol.13 , pp. 154-156
    • Lee, C.H.1    Kim, S.H.2    Choi, J.I.3    Choi, J.Y.4    Lee, C.E.5    Kim, J.6
  • 39
    • 0023992806 scopus 로고
    • The MutY gene: A mutator locus in Eshcherichia coli that generates G:C to T:A transversions
    • Nghiem, Y., Cabrera, M., Cupples, C. G., and Miller, J. H. (1988) The MutY gene: a mutator locus in Eshcherichia coli that generates G:C to T:A transversions, Proc. Natl. Acad. Sci. U.S.A. 85, 2709-2713.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 2709-2713
    • Nghiem, Y.1    Cabrera, M.2    Cupples, C.G.3    Miller, J.H.4
  • 40
    • 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
  • 41
    • 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
  • 42
    • 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 17, 10964-10968.
    • (1992) Biochemistry , vol.17 , pp. 10964-10968
    • Michaels, M.L.1    Tchou, J.2    Grollman, A.P.3    Miller, J.H.4
  • 43
    • 0030475264 scopus 로고    scopus 로고
    • Specific recognition of A/G and A/7,8-dihydro-8-oxoguanine (8-oxoG) mismatches by Escherichia coli MutY: Removal of the C-terminal domain preferentially affects A/8-oxoG recognition
    • Gogos, A., Cillo, J., Clarke, N. D., and Lu, A. L. (1996) Specific recognition of A/G and A/7,8-dihydro-8-oxoguanine (8-oxoG) mismatches by Escherichia coli MutY: removal of the C-terminal domain preferentially affects A/8-oxoG recognition, Biochemistry 35, 16665-16671.
    • (1996) Biochemistry , vol.35 , pp. 16665-16671
    • Gogos, A.1    Cillo, J.2    Clarke, N.D.3    Lu, A.L.4
  • 44
    • 0028825742 scopus 로고
    • DNA determinants and substrate specificities of Escherichia coli MutY
    • Lu, A. L., Tsai-Wu, J. J., and Cillo, J. (1995) DNA determinants and substrate specificities of Escherichia coli MutY, J. Biol. Chem. 270, 23582-23588.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23582-23588
    • Lu, A.L.1    Tsai-Wu, J.J.2    Cillo, J.3
  • 45
    • 0030018681 scopus 로고    scopus 로고
    • Identification of the structural and functional domains of MutY, an Escherichia coli DNA mismatch repair enzyme
    • Manuel, R. C., Czerwinski, E. W., and Lloyd, R. S. (1996) Identification of the structural and functional domains of MutY, an Escherichia coli DNA mismatch repair enzyme, J. Biol. Chem. 271, 16218-16226.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16218-16226
    • Manuel, R.C.1    Czerwinski, E.W.2    Lloyd, R.S.3
  • 46
    • 0030987556 scopus 로고    scopus 로고
    • Cloning, overexpression, and biochemical characterization of the catalytic domain of MutY
    • Manuel, R. C., and Lloyd, R. S. (1997) Cloning, overexpression, and biochemical characterization of the catalytic domain of MutY, Biochemistry 36, 11140-11152.
    • (1997) Biochemistry , vol.36 , pp. 11140-11152
    • Manuel, R.C.1    Lloyd, R.S.2
  • 47
    • 0346434114 scopus 로고    scopus 로고
    • Probing the requirements for recognition and catalysis in Fpg and MutY with nonpolar adenine isosteres
    • Francis, A. W., Helquist, S. A., Kool, E. T., and David, S. S. (2003) Probing the requirements for recognition and catalysis in Fpg and MutY with nonpolar adenine isosteres, J. Am. Chem. Soc. 125, 16235-16242.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16235-16242
    • Francis, A.W.1    Helquist, S.A.2    Kool, E.T.3    David, S.S.4
  • 49
    • 0027428503 scopus 로고
    • MutY repair is mutagenic in MutT-strains of Escherichia coli
    • Vidmar, J. J., and Cupples, C. G. (1993) MutY repair is mutagenic in MutT-strains of Escherichia coli, Can. J. Microbiol. 39, 892-894.
    • (1993) Can. J. Microbiol. , vol.39 , pp. 892-894
    • Vidmar, J.J.1    Cupples, C.G.2
  • 51
    • 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
  • 53
    • 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, 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, S.7    Tainer, J.A.8
  • 54
    • 0025301064 scopus 로고
    • MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III
    • Michaels, M. L., Pham, L., Nghiem, Y., Cruz, C., and Miller, J. H. (1990) MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III, Nucleic Acids Res. 18, 3841-3845.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3841-3845
    • Michaels, M.L.1    Pham, L.2    Nghiem, Y.3    Cruz, C.4    Miller, J.H.5
  • 55
    • 0018926091 scopus 로고
    • DNA N-glycosylases and UV repair
    • Demple, B., and Linn, S. (1980) DNA N-glycosylases and UV repair, Nature 287, 203-208.
    • (1980) Nature , vol.287 , pp. 203-208
    • Demple, B.1    Linn, S.2
  • 56
    • 0021106244 scopus 로고
    • Characterization of the Escherichia coli X-ray endonuclease, endonuclease III
    • Katcher, H. L., and Wallace, S. S. (1983) Characterization of the Escherichia coli X-ray endonuclease, endonuclease III, Biochemistry 22, 4071-4081.
    • (1983) Biochemistry , vol.22 , pp. 4071-4081
    • Katcher, H.L.1    Wallace, S.S.2
  • 57
    • 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., and Lindahl, T. (1984) 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. 259, 5543-5548.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5543-5548
    • Breimer, L.H.1    Lindahl, T.2
  • 58
    • 0023057569 scopus 로고
    • Photoalkylated DNA and ultraviolet-irradiated DNA are incised at cytosines by endonuclease III
    • Duker, N. J., and Weiss, R. B. (1986) Photoalkylated DNA and ultraviolet-irradiated DNA are incised at cytosines by endonuclease III, Nucleic Acids Res. 26, 6621-6631.
    • (1986) Nucleic Acids Res. , vol.26 , pp. 6621-6631
    • Duker, N.J.1    Weiss, R.B.2
  • 59
    • 0024328839 scopus 로고
    • UV-induced pyrimidine hydrates in DNA are repaired by bacterial and mammalian DNA glycosylase activities
    • Boorstein, R. J., Hilbert, T. P., Cadet, J., Cunningham, R. P., and Teebor, G. W. (1989) UV-induced pyrimidine hydrates in DNA are repaired by bacterial and mammalian DNA glycosylase activities, Biochemistry 28, 6164-6170.
    • (1989) Biochemistry , vol.28 , pp. 6164-6170
    • Boorstein, R.J.1    Hilbert, T.P.2    Cadet, J.3    Cunningham, R.P.4    Teebor, G.W.5
  • 60
    • 0030061005 scopus 로고    scopus 로고
    • Excision of oxidative cytosine modifications from gamma-irradiated DNA by Escherichia coli endonuclease III and human whole-cell extracts
    • Wagner, J. R., Blount, B. C., and Weinfeld, M. (1996) Excision of oxidative cytosine modifications from gamma-irradiated DNA by Escherichia coli endonuclease III and human whole-cell extracts, Anal. Biochem. 233, 76-86.
    • (1996) Anal. Biochem. , vol.233 , pp. 76-86
    • Wagner, J.R.1    Blount, B.C.2    Weinfeld, M.3
  • 61
    • 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., and Boiteux, S. (1993) Substrate specificity of the Escherichia coli endonuclease III: excision of thymine- and cytosine-derived lesions in DNA produced by radiation-generated free radicals, Biochemistry 32, 12105-12111.
    • (1993) Biochemistry , vol.32 , pp. 12105-12111
    • Dizdaroglu, M.1    Laval, J.2    Boiteux, S.3
  • 63
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer, M. M., Ahern, H., Xing, D., Cunningham, R. P., and Tainer, J. A. (1995) Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure, EMBO J. 14, 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
  • 64
    • 0001580531 scopus 로고    scopus 로고
    • Structure-function correlations in high-potential iron proteins
    • Cowan, J. A., and Lui, S. M. (1998) Structure-function correlations in high-potential iron proteins, Adv. Inorg. Chem. 45, 313-350.
    • (1998) Adv. Inorg. Chem. , vol.45 , pp. 313-350
    • Cowan, J.A.1    Lui, S.M.2
  • 65
    • 0026707674 scopus 로고
    • The role of the iron-sulfur cluster in Escherichia coli endonuclease III. A resonance Raman study
    • Fu, W., O'Handley, S., Cunningham, R. P., and Johnson, M. K. (1992) The role of the iron-sulfur cluster in Escherichia coli endonuclease III. A resonance Raman study, J. Biol. Chem. 267. 16135-16137.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16135-16137
    • Fu, W.1    O'Handley, S.2    Cunningham, R.P.3    Johnson, M.K.4
  • 67
    • 0032566764 scopus 로고    scopus 로고
    • Characterization of the recombinant MutY homolog, an adenine DNA glycosylase, from yeast Schizosaccharomyces pombe
    • Lu, A. L., and Fawcett, W. P. (1998) Characterization of the recombinant MutY homolog, an adenine DNA glycosylase, from yeast Schizosaccharomyces pombe, J. Biol. Chem. 273, 25098-25105.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25098-25105
    • Lu, A.L.1    Fawcett, W.P.2
  • 68
    • 0028831129 scopus 로고
    • Characterization of a mammalian homolog of the Escherichia coli MutY mismatch repair protein
    • McGoldrick, J. P., Yeh, Y. C., Solomon, M., Essigmann, J. M., and Lu, A. L. (1995) Characterization of a mammalian homolog of the Escherichia coli MutY mismatch repair protein, Mol. Cell. Biol. 15, 989-996.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 989-996
    • McGoldrick, J.P.1    Yeh, Y.C.2    Solomon, M.3    Essigmann, J.M.4    Lu, A.L.5
  • 69
    • 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
    • Ikeda, S., Biswas, T., Roy, R., Izumi, T., Boldogh, I., Kurosky, A., Sarker, A. H., Seki, S., and Mitra, S. (1998) 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, 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
  • 70
    • 0034734383 scopus 로고    scopus 로고
    • Structure and function in the uracil-DNA glycosylase superfamily
    • Pearl, L. H. (2000) Structure and function in the uracil-DNA glycosylase superfamily, Mutat. Res. 460, 165-181.
    • (2000) Mutat. Res. , vol.460 , pp. 165-181
    • Pearl, L.H.1
  • 72
    • 0035915398 scopus 로고    scopus 로고
    • Excision of uracil from DNA by the hyperthermophilic Afung protein is dependent on the opposite base and stimulated by heat-induced transition of a more open structure
    • Knaevlsrud, I., Ruoff, P., Anensen, H., Klungland, A., Bjelland, S., and Birkeland, N. K. (2001) Excision of uracil from DNA by the hyperthermophilic Afung protein is dependent on the opposite base and stimulated by heat-induced transition of a more open structure, Mutat. Res. 487, 173-190.
    • (2001) Mutat. Res. , vol.487 , pp. 173-190
    • Knaevlsrud, I.1    Ruoff, P.2    Anensen, H.3    Klungland, A.4    Bjelland, S.5    Birkeland, N.K.6
  • 73
    • 0035839610 scopus 로고    scopus 로고
    • Biochemical characterization of uracil processing activities in the hyperthermophilic archaeon Pyrobaculum aerophilum
    • Sartori, A. A., Schar, P., Fitz-Gibbon, S., Miller, J. H., and Jiricny, J. (2001) Biochemical characterization of uracil processing activities in the hyperthermophilic archaeon Pyrobaculum aerophilum, J. Biol. Chem. 276, 29979-29986.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29979-29986
    • Sartori, A.A.1    Schar, P.2    Fitz-Gibbon, S.3    Miller, J.H.4    Jiricny, J.5
  • 74
    • 0035804794 scopus 로고    scopus 로고
    • Characterization of the full length uracil-DNA glycosylase in the extreme thermophile Thermotoga maritima
    • Sandigursky, M., Faje, A., and Franklin, W. A. (2001) Characterization of the full length uracil-DNA glycosylase in the extreme thermophile Thermotoga maritima, Mutat. Res. 485, 187-195.
    • (2001) Mutat. Res. , vol.485 , pp. 187-195
    • Sandigursky, M.1    Faje, A.2    Franklin, W.A.3
  • 75
    • 0034705405 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase in the extreme thermophile Archaeoglobus fulgidus
    • Sandigursky, M., and Franklin, W. A. (2000) Uracil-DNA glycosylase in the extreme thermophile Archaeoglobus fulgidus, J. Biol. Chem. 275, 19146-19149.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19146-19149
    • Sandigursky, M.1    Franklin, W.A.2
  • 76
    • 0016257644 scopus 로고
    • Heat-induced deamination of cytosine residues in deoxyribonucleic acid
    • Lindahl, T., and Nyberg, B. (1974) Heat-induced deamination of cytosine residues in deoxyribonucleic acid, Biochemistry 13, 3405-3410.
    • (1974) Biochemistry , vol.13 , pp. 3405-3410
    • Lindahl, T.1    Nyberg, B.2
  • 77
    • 0030985997 scopus 로고    scopus 로고
    • Rates of spontaneous mutation in an archaeon from geothermal environments
    • Jacobs, K. L., and Grogan, D. W. (1997) Rates of spontaneous mutation in an archaeon from geothermal environments, J. Bacteriol. 179, 3298-3303.
    • (1997) J. Bacteriol. , vol.179 , pp. 3298-3303
    • Jacobs, K.L.1    Grogan, D.W.2
  • 78
    • 0006717746 scopus 로고
    • Cobalt(II) and cobalt(III) coordination compounds
    • Thomas, N. C., Pringle, K., and Deacon, G. B. (1989) Cobalt(II) and cobalt(III) coordination compounds, J. Chem. Educ. 66, 516-517.
    • (1989) J. Chem. Educ. , vol.66 , pp. 516-517
    • Thomas, N.C.1    Pringle, K.2    Deacon, G.B.3
  • 79
    • 0024393445 scopus 로고
    • Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene
    • Asahara, H., Wistort, P. M., Bank, J. F., Bakerian, R. H., and Cunningham, R. P. (1989) Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene, Biochemistry 28, 4444-4449.
    • (1989) Biochemistry , vol.28 , pp. 4444-4449
    • Asahara, H.1    Wistort, P.M.2    Bank, J.F.3    Bakerian, R.H.4    Cunningham, R.P.5
  • 80
    • 49149135789 scopus 로고
    • Dexoynucleoside phosphoramidites-a new class of key intermediates for deoxypolynucleotide synthesis
    • Beaucage, S. L., and Caruthers, M. H. (1981) Dexoynucleoside phosphoramidites-a new class of key intermediates for deoxypolynucleotide synthesis, Tetrahedron Lett. 22, 1859-1862.
    • (1981) Tetrahedron Lett. , vol.22 , pp. 1859-1862
    • Beaucage, S.L.1    Caruthers, M.H.2
  • 81
    • 0033572711 scopus 로고    scopus 로고
    • Single-base mismatch detection based on charge transduction through DNA
    • Kelley, S. O., Boon, E. M., Barton, J. K., Jackson, N. M., and Hill, M. G. (1999) Single-base mismatch detection based on charge transduction through DNA, Nucleic Acids Res. 27, 4830-4837.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4830-4837
    • Kelley, S.O.1    Boon, E.M.2    Barton, J.K.3    Jackson, N.M.4    Hill, M.G.5
  • 82
    • 0000486126 scopus 로고
    • Cyclic voltammetric analysis of ferrocene alkanethiol monolayer electrode kinetics based on Marcus theory
    • Tender, L., Carter, M. T., and Murray, R. W. (1994) Cyclic voltammetric analysis of ferrocene alkanethiol monolayer electrode kinetics based on Marcus theory, Anal. Chem. 66, 3173-3181.
    • (1994) Anal. Chem. , vol.66 , pp. 3173-3181
    • Tender, L.1    Carter, M.T.2    Murray, R.W.3
  • 83
    • 33846281497 scopus 로고    scopus 로고
    • Reactions of complex metalloproteins studied by protein-film voltammetry
    • Armstrong, F. A., Heering, H. A., and Hirst, J. (1997) Reactions of complex metalloproteins studied by protein-film voltammetry, Chem. Soc. Rev. 26, 169-188.
    • (1997) Chem. Soc. Rev. , vol.26 , pp. 169-188
    • Armstrong, F.A.1    Heering, H.A.2    Hirst, J.3
  • 84
    • 77956752465 scopus 로고
    • Direct electrochemistry of proteins and enzymes
    • Guo, L. H., and Hill, H. A. O. (1991) Direct electrochemistry of proteins and enzymes, Adv. Inorg. Chem. 36, 341-375.
    • (1991) Adv. Inorg. Chem. , vol.36 , pp. 341-375
    • Guo, L.H.1    Hill, H.A.O.2
  • 85
    • 16344377473 scopus 로고    scopus 로고
    • A role for iron-sulfur clusters in DNA repair
    • Lukianova, O. A., and David, S. S. (2005) A role for iron-sulfur clusters in DNA repair, Curr. Opin. Chem. Biol. 9, 145-151.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 145-151
    • Lukianova, O.A.1    David, S.S.2
  • 86
    • 0034730073 scopus 로고    scopus 로고
    • Investigations of the oxidative disassembly of Fe-S clusters in Clostridium pasteurianum 8Fe ferredoxin using pulsed-protein-film voltammetry
    • Camba, R., and Armstrong, F. A. (2000) Investigations of the oxidative disassembly of Fe-S clusters in Clostridium pasteurianum 8Fe ferredoxin using pulsed-protein-film voltammetry, Biochemistry 39, 10587-10598.
    • (2000) Biochemistry , vol.39 , pp. 10587-10598
    • Camba, R.1    Armstrong, F.A.2
  • 91
    • 0017804089 scopus 로고
    • The soluble "high potential" type iron-sulfur protein from mitochondria is aconitase
    • Ruzicka, F. J., and Beinert, J. (1978) The soluble "high potential" type iron-sulfur protein from mitochondria is aconitase, J. Biol. Chem. 253, 2514-2517.
    • (1978) J. Biol. Chem. , vol.253 , pp. 2514-2517
    • Ruzicka, F.J.1    Beinert, J.2
  • 92
    • 0024804717 scopus 로고
    • Voltammetric studies of the interaction of metal chelates with DNA. 2. Trischelated complexes of cobalt(III) and iron(II) with 1, 10-phenanthroline and 2,2′-bipyridine
    • Carter, M. T., Rodriguez, M., and Bard, A. J. (1989) Voltammetric studies of the interaction of metal chelates with DNA. 2. Trischelated complexes of cobalt(III) and iron(II) with 1, 10-phenanthroline and 2,2′-bipyridine, J. Am. Chem. Soc. 111, 8901-8911.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8901-8911
    • Carter, M.T.1    Rodriguez, M.2    Bard, A.J.3
  • 93
    • 0025195298 scopus 로고
    • 1H NMR studies of tris(phenanthroline) metal complexes bound to oligonucleotides: Characterization of binding modes
    • 1H NMR studies of tris(phenanthroline) metal complexes bound to oligonucleotides: characterization of binding modes, Biochemistry 29, 1701-1709.
    • (1990) Biochemistry , vol.29 , pp. 1701-1709
    • Rehmann, J.P.1    Barton, J.K.2
  • 94
    • 0345627986 scopus 로고    scopus 로고
    • The structure of iron-sulfur proteins
    • Sticht, H. and Rosch, P. (1998) The structure of iron-sulfur proteins, Prog. Biophys. Mol. Biol. 70, 95-136.
    • (1998) Prog. Biophys. Mol. Biol. , vol.70 , pp. 95-136
    • Sticht, H.1    Rosch, P.2
  • 95
    • 1342304229 scopus 로고    scopus 로고
    • Structural basis for removal of 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 removal of 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
  • 96
    • 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


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