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Volumn 76, Issue 6, 2002, Pages 640-648

Ultraviolet-B-induced inactivation of human OGG1, the repair enzyme for removal of 8-oxoguanine in DNA

Author keywords

[No Author keywords available]

Indexed keywords

2,6 DIAMINO 4 HYDROXY 5N METHYLFORMAMIDOPYRIMIDINE; 8 HYDROXYGUANINE; ARGON; DNA; OLIGONUCLEOTIDE; PROTEIN; PROTEIN OGG1; PYRIMIDINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0036985884     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2002)076<0640:UBIIOH>2.0.CO;2     Document Type: Article
Times cited : (15)

References (35)
  • 1
    • 0030049032 scopus 로고    scopus 로고
    • Damage to DNA by reactive oxygen and nitrogen species: Role in inflammatory disease and progression to cancer
    • Wiseman, H. and B. Halliwell (1996) Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer. Biochem. J. 313, 17-29.
    • (1996) Biochem. J. , vol.313 , pp. 17-29
    • Wiseman, H.1    Halliwell, B.2
  • 2
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel, T. and N. J. Holbrook (2000) Oxidants, oxidative stress and the biology of ageing. Nature 408, 239-247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 4
    • 0002625659 scopus 로고
    • UV-A (320-380) radiation as an oxidative stress
    • Edited by H. Sies. Academic Press, London
    • Tyrrell, R. M. (1991) UV-A (320-380) radiation as an oxidative stress. In Oxidative Stress: Oxidant and Antioxidants (Edited by H. Sies), pp. 57-83. Academic Press, London.
    • (1991) Oxidative Stress: Oxidant and Antioxidants , pp. 57-83
    • Tyrrell, R.M.1
  • 5
    • 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
  • 6
    • 0025973703 scopus 로고
    • Chemical determination of free radical-induced damage to DNA
    • Dizdaroglu, M. (1991) Chemical determination of free radical-induced damage to DNA. Free Radic. Biol. Med. 10, 225-242.
    • (1991) Free Radic. Biol. Med. , vol.10 , pp. 225-242
    • Dizdaroglu, M.1
  • 7
  • 8
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers, J. H. J. (2001) Genome maintenance mechanisms for preventing cancer. Nature 411, 366-374.
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.J.1
  • 9
    • 0034192265 scopus 로고    scopus 로고
    • The human OGG1 gene: Structure, functions and its implication in the process of carcinogenesis
    • Boiteux, S. and J. P. Radicella (2000) The human OGG1 gene: structure, functions and its implication in the process of carcinogenesis. Arch. Biochem. Biophys. 377, 1-8.
    • (2000) Arch. Biochem. Biophys. , vol.377 , pp. 1-8
    • Boiteux, S.1    Radicella, J.P.2
  • 10
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homologue of the OGG1 gene of Saccharomyces cerevisiae
    • Radicella, J. P., C. Dherin, C. Desmaze, M. S. Fox and S. Boiteux (1997) Cloning and characterization of hOGG1, a human homologue of the OGG1 gene of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 94, 8010-8015.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8010-8015
    • Radicella, J.P.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.4    Boiteux, S.5
  • 11
    • 0343353893 scopus 로고    scopus 로고
    • Characterization of the hOGG1 promoter and its expression during cell cycle
    • Dhénaut, A. and J. P. Radicella (2000) Characterization of the hOGG1 promoter and its expression during cell cycle. Mutat. Res. 461, 109-118.
    • (2000) Mutat. Res. , vol.461 , pp. 109-118
    • Dhénaut, A.1    Radicella, J.P.2
  • 12
    • 0001343498 scopus 로고
    • Nature, identification and properties of intermediates produced by UV excitation of indole derivatives at low and room temperatures
    • Santus, R., M. Bazin and M. Aubailly (1980) Nature, identification and properties of intermediates produced by UV excitation of indole derivatives at low and room temperatures. Rev. Chem. lntermed. 3, 231-283.
    • (1980) Rev. Chem. lntermed. , vol.3 , pp. 231-283
    • Santus, R.1    Bazin, M.2    Aubailly, M.3
  • 13
    • 0014771842 scopus 로고
    • Photochemical reactions in amino acid residues and inactivation of enzymes during UV irradiation
    • Vladimirov, Y. A., D. I. Roshchupkin and E. E. Fesenko (1970) Photochemical reactions in amino acid residues and inactivation of enzymes during UV irradiation. Photochem. Photobiol. 11, 227-246.
    • (1970) Photochem. Photobiol. , vol.11 , pp. 227-246
    • Vladimirov, Y.A.1    Roshchupkin, D.I.2    Fesenko, E.E.3
  • 14
    • 0001937522 scopus 로고
    • Photosensitization
    • Edited by K. C. Smith. Plenum Press, New York
    • Spikes, J. D. (1989) Photosensitization. In The Science of Photobiology (Edited by K. C. Smith), pp. 79-110. Plenum Press, New York.
    • (1989) The Science of Photobiology , pp. 79-110
    • Spikes, J.D.1
  • 15
    • 0034661689 scopus 로고    scopus 로고
    • Effect of single mutations in the OGG1 gene found in human tumors on the substrate specificity of the Ogg1 protein
    • Audebert, M., J. P. Radicella and M. Dizdaroglu (2000) Effect of single mutations in the OGG1 gene found in human tumors on the substrate specificity of the Ogg1 protein. Nucleic Acids Res. 28, 2672-2678.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2672-2678
    • Audebert, M.1    Radicella, J.P.2    Dizdaroglu, M.3
  • 16
    • 0025493932 scopus 로고
    • UVB-induced photoperoxidation of lipids of human low and high density lipoproteins: A possible role tryptophan residues
    • Salmon, S., J. C. Mazière, R. Santus, P. Morliëre and N. Bouchemal (1990) UVB-induced photoperoxidation of lipids of human low and high density lipoproteins: a possible role tryptophan residues. Photochem. Photobiol. 52, 541-545.
    • (1990) Photochem. Photobiol. , vol.52 , pp. 541-545
    • Salmon, S.1    Mazière, J.C.2    Santus, R.3    Morliëre, P.4    Bouchemal, N.5
  • 18
    • 0021760535 scopus 로고
    • Two rotameric forms of open ring 7-methylguanine are present in alkylated polynucleotides
    • Boiteux, S., J. Belleney, B. P. Roques and J. Laval (1984) Two rotameric forms of open ring 7-methylguanine are present in alkylated polynucleotides. Nucleic Acids Res. 12, 5429-5439.
    • (1984) Nucleic Acids Res , vol.12 , pp. 5429-5439
    • Boiteux, S.1    Belleney, J.2    Roques, B.P.3    Laval, J.4
  • 20
    • 0014479075 scopus 로고
    • Fluorescence quenching and isostope effects in tryptophan
    • Eisinger, J. and G. Navon (1969) Fluorescence quenching and isostope effects in tryptophan. J. Chem. Phys. 50, 2069-2071.
    • (1969) J. Chem. Phys. , vol.50 , pp. 2069-2071
    • Eisinger, J.1    Navon, G.2
  • 21
    • 0017519662 scopus 로고
    • Ultraviolet action spectrum for tryptophan destruction in aqueous solution
    • Borkman, R. F. (1977) Ultraviolet action spectrum for tryptophan destruction in aqueous solution. Photochem. Photobiol. 26, 163-166.
    • (1977) Photochem. Photobiol. , vol.26 , pp. 163-166
    • Borkman, R.F.1
  • 22
    • 0001596835 scopus 로고
    • Direct observation of monophotonic photoionization in tryptophan excited by 300-nm radiation. A laser photolysis study
    • Bazin, M., L. K. Patterson and R. Santus (1983) Direct observation of monophotonic photoionization in tryptophan excited by 300-nm radiation. A laser photolysis study. J. Phys. Chem. 87, 189-190.
    • (1983) J. Phys. Chem. , vol.87 , pp. 189-190
    • Bazin, M.1    Patterson, L.K.2    Santus, R.3
  • 23
    • 0013431655 scopus 로고
    • UV laser matrix desorption/ionization mass spectrometry of proteins in the 100000 Dalton range
    • Karas, M., U. Bahr and F. Hillenkamp (1989) UV laser matrix desorption/ionization mass spectrometry of proteins in the 100000 Dalton range. Int. J. Mass Spectrom. Ion Processes 92, 231-242.
    • (1989) Int. J. Mass Spectrom. Ion Processes , vol.92 , pp. 231-242
    • Karas, M.1    Bahr, U.2    Hillenkamp, F.3
  • 25
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • Brunet, S. D., D. P. G. Norman and G. L. Verdine (2000) Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature 403, 859-866.
    • (2000) Nature , vol.403 , pp. 859-866
    • Brunet, S.D.1    Norman, D.P.G.2    Verdine, G.L.3
  • 26
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein, E. A., N. S. Vedenkina and M. N. Ivkova (1973) Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 18, 263-279.
    • (1973) Photochem. Photobiol. , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 27
    • 0021485819 scopus 로고
    • Influence of the location of tryptophanyl residues in proteins on their photosensitivity
    • Pigault, C. and D. Gerard (1984) Influence of the location of tryptophanyl residues in proteins on their photosensitivity. Photochem. Photobiol. 40, 291-296.
    • (1984) Photochem. Photobiol. , vol.40 , pp. 291-296
    • Pigault, C.1    Gerard, D.2
  • 28
    • 0016927359 scopus 로고
    • Photochemical inactivation of enzymes
    • Edited by M. Ebert and A. Howard. North-Holland, Amsterdam
    • Grossweiner, L. I. (1976) Photochemical inactivation of enzymes. In Current Topics in Radiation Research Quarterly, Vol. II (Edited by M. Ebert and A. Howard), pp. 141-199. North-Holland, Amsterdam.
    • (1976) Current Topics in Radiation Research Quarterly , vol.2 , pp. 141-199
    • Grossweiner, L.I.1
  • 29
    • 0025394074 scopus 로고
    • The rates of photolysis of the four individual tryptophan residues in UV exposed calfy-II crystallin
    • Tallmadge, D. H. and R. F. Borkman (1990) The rates of photolysis of the four individual tryptophan residues in UV exposed calfy-II crystallin. Photochem. Photobiol. 51, 363-368.
    • (1990) Photochem. Photobiol. , vol.51 , pp. 363-368
    • Tallmadge, D.H.1    Borkman, R.F.2
  • 30
    • 0022105409 scopus 로고
    • The effect of pH on the aerobic and anaerobic photolysis of tryptophan and some tryptophan-containing dipeptides
    • Hibbard, L. B., N. J. Kirk and R. F. Borkman (1985) The effect of pH on the aerobic and anaerobic photolysis of tryptophan and some tryptophan-containing dipeptides. Photochem. Photobiol. 42, 99-106.
    • (1985) Photochem. Photobiol. , vol.42 , pp. 99-106
    • Hibbard, L.B.1    Kirk, N.J.2    Borkman, R.F.3
  • 31
    • 84985493646 scopus 로고
    • The anaerobic photolysis of tryptophan containing peptides
    • Dillon, J. (1980) The anaerobic photolysis of tryptophan containing peptides. Photochem. Photobiol. 32, 37-39.
    • (1980) Photochem. Photobiol. , vol.32 , pp. 37-39
    • Dillon, J.1
  • 32
    • 0016219849 scopus 로고
    • N-formlyl-kynurenine, a tryptophan photooxidation product as a photodynamic photosensitizer
    • Walrant, P. and R. Santus (1974) N-formlyl-kynurenine, a tryptophan photooxidation product as a photodynamic photosensitizer. Photochem. Photobiol. 19, 411-417.
    • (1974) Photochem. Photobiol. , vol.19 , pp. 411-417
    • Walrant, P.1    Santus, R.2
  • 33
    • 0016157085 scopus 로고
    • Ultraviolet and N-formyl-kynurenine-sensitized photoinactivation of bovine carbonic anhydrase: An intemal photodynamic effect
    • Walrant, P. and R. Santus (1974) Ultraviolet and N-formyl-kynurenine-sensitized photoinactivation of bovine carbonic anhydrase: an intemal photodynamic effect. Photochem. Photobiol. 20, 455-460.
    • (1974) Photochem. Photobiol. , vol.20 , pp. 455-460
    • Walrant, P.1    Santus, R.2
  • 34
    • 0017600319 scopus 로고
    • Specific recognition of single-stranded nucleic acids. Interaction of tryptophan-containing peptides with native, denatured and ultraviolet-irradiated DNA
    • Toulmé, J. J. and C. Hélène (1977) Specific recognition of single-stranded nucleic acids. Interaction of tryptophan-containing peptides with native, denatured and ultraviolet-irradiated DNA. J. Biol. Chem. 252, 244-249.
    • (1977) J. Biol. Chem. , vol.252 , pp. 244-249
    • Toulmé, J.J.1    Hélène, C.2
  • 35
    • 84918833988 scopus 로고
    • Critical review of rate constants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals
    • Buxton, G. V., C. L. Greenstock, W. P. Helman and A. B. Ross (1988) Critical review of rate constants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals. J. Phys. Chem. Ref. Data 17, 513-886.
    • (1988) J. Phys. Chem. Ref. Data , vol.17 , pp. 513-886
    • Buxton, G.V.1    Greenstock, C.L.2    Helman, W.P.3    Ross, A.B.4


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