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Volumn 85, Issue 11, 2003, Pages 1073-1082

Transcription-coupled repair of 8-oxoguanine in human cells and its deficiency in some DNA repair diseases

Author keywords

8 Oxoguanine; Ageing; Cockayne syndrome; Neurological disorders; RNA polymerase II; Transcription coupled repair

Indexed keywords

8 HYDROXYGUANINE; ADENOSINE TRIPHOSPHATASE; BRCA1 PROTEIN; BRCA2 PROTEIN; DNA; GENOMIC DNA; PROTEIN; PROTEIN MSH2; PROTEIN XPB; PROTEIN XPG; REACTIVE OXYGEN METABOLITE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; XERODERMA PIGMENTOSUM GROUP D PROTEIN;

EID: 0942268172     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2003.11.005     Document Type: Article
Times cited : (27)

References (81)
  • 2
    • 0036363646 scopus 로고    scopus 로고
    • Mechanisms of transcription-coupled DNA repair
    • Svejstrup J.Q. Mechanisms of transcription-coupled DNA repair. Nat. Rev. Mol. Cell Biol. 3:2002;21-29.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 21-29
    • Svejstrup, J.Q.1
  • 3
    • 0030822591 scopus 로고    scopus 로고
    • Cockayne syndrome group B protein enhances elongation by RNA polymerase II
    • Selby C.P., Sancar A. Cockayne syndrome group B protein enhances elongation by RNA polymerase II. Proc. Natl. Acad. Sci. USA. 94:1997;11205-11209.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11205-11209
    • Selby, C.P.1    Sancar, A.2
  • 4
    • 0035201056 scopus 로고    scopus 로고
    • Requirement for yeast RAD26, a homolog of the human CSB gene, in elongation by RNA polymerase II
    • Lee S.K., Yu S.L., Prakash L., Prakash S. Requirement for yeast RAD26, a homolog of the human CSB gene, in elongation by RNA polymerase II. Mol. Cell Biol. 21:2001;8651-8656.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 8651-8656
    • Lee, S.K.1    Yu, S.L.2    Prakash, L.3    Prakash, S.4
  • 7
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell. 113:2003;357-367.
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3    Sawada, J.4    Saijo, M.5    Drapkin, R.6    Kisselev, A.F.7    Tanaka, K.8    Nakatani, Y.9
  • 8
    • 0037039443 scopus 로고    scopus 로고
    • Translocation of Cockayne syndrome group a protein to the nuclear matrix: Possible relevance to transcription-coupled DNA repair
    • Kamiuchi S., Saijo M., Citterio E., de Jager M., Hoeijmakers J.H., Tanaka K. Translocation of Cockayne syndrome group A protein to the nuclear matrix: possible relevance to transcription-coupled DNA repair. Proc. Natl. Acad. Sci. USA. 99:2002;201-206.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 201-206
    • Kamiuchi, S.1    Saijo, M.2    Citterio, E.3    De Jager, M.4    Hoeijmakers, J.H.5    Tanaka, K.6
  • 9
    • 0037996882 scopus 로고    scopus 로고
    • 8-Oxoguanine lesioned B-DNA molecule complexed with repair enzyme hOGG1: A molecular dynamics study
    • Pinak M. 8-Oxoguanine lesioned B-DNA molecule complexed with repair enzyme hOGG1: a molecular dynamics study. J. Comput. Chem. 24:2003;898-907.
    • (2003) J. Comput. Chem. , vol.24 , pp. 898-907
    • Pinak, M.1
  • 10
    • 0043231319 scopus 로고    scopus 로고
    • Electrostatic energy analysis of 8-oxoguanine DNA lesion-molecular dynamics study
    • Pinak M. Electrostatic energy analysis of 8-oxoguanine DNA lesion-molecular dynamics study. Comput. Biol. Chem. 27:2003;431-441.
    • (2003) Comput. Biol. Chem. , vol.27 , pp. 431-441
    • Pinak, M.1
  • 11
    • 0035830851 scopus 로고    scopus 로고
    • Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase delta. Steady-state and pre-steady-state kinetic analysis
    • Einolf H.J., Guengerich F.P. Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase delta. Steady-state and pre-steady-state kinetic analysis. J. Biol. Chem. 276:2001;3764-3771.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3764-3771
    • Einolf, H.J.1    Guengerich, F.P.2
  • 13
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae
    • Radicella J.P., Dherin C., Desmaze C., Fox M.S., Boiteux S. Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 94:1997;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
  • 14
    • 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., Miller J.H. 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. 178:1996;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
  • 15
    • 0028566359 scopus 로고
    • Genomic structure and chromosome location of the human mutT homologue gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G transversion
    • Furuichi M., Yoshida M.C., Oda H., Tajiri T., Nakabeppu Y., Tsuzuki T., Sekiguchi M. Genomic structure and chromosome location of the human mutT homologue gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G transversion. Genomics. 24:1994;485-490.
    • (1994) Genomics , vol.24 , pp. 485-490
    • Furuichi, M.1    Yoshida, M.C.2    Oda, H.3    Tajiri, T.4    Nakabeppu, Y.5    Tsuzuki, T.6    Sekiguchi, M.7
  • 16
    • 0034623063 scopus 로고    scopus 로고
    • Characterization of a novel 8-oxoguanine-DNA glycosylase activity in Escherichia coli and identification of the enzyme as endonuclease VIII
    • Hazra T.K., Izumi T., Venkataraman R., Kow Y.W., Dizdaroglu M., Mitra S. Characterization of a novel 8-oxoguanine-DNA glycosylase activity in Escherichia coli and identification of the enzyme as endonuclease VIII. J. Biol. Chem. 275:2000;27762-27767.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27762-27767
    • Hazra, T.K.1    Izumi, T.2    Venkataraman, R.3    Kow, Y.W.4    Dizdaroglu, M.5    Mitra, S.6
  • 17
    • 0032533794 scopus 로고    scopus 로고
    • The presence of two distinct 8-oxoguanine repair enzymes in human cells: Their potential complementary roles in preventing mutation
    • Hazra T.K., Izumi T., Maidt L., Floyd R.A., Mitra S. The presence of two distinct 8-oxoguanine repair enzymes in human cells: their potential complementary roles in preventing mutation. Nucleic Acids Res. 26:1998;5116-5122.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5116-5122
    • Hazra, T.K.1    Izumi, T.2    Maidt, L.3    Floyd, R.A.4    Mitra, S.5
  • 19
    • 0034682518 scopus 로고    scopus 로고
    • Transcription coupled repair of 8-oxoguanine in murine cells: The ogg1 protein is required for repair in nontranscribed sequences but not in transcribed sequences
    • Le Page F., Klungland A., Barnes D.E., Sarasin A., Boiteux S. Transcription coupled repair of 8-oxoguanine in murine cells: the ogg1 protein is required for repair in nontranscribed sequences but not in transcribed sequences. Proc. Natl. Acad. Sci. USA. 97:2000;8397-8402.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8397-8402
    • Le Page, F.1    Klungland, A.2    Barnes, D.E.3    Sarasin, A.4    Boiteux, S.5
  • 20
    • 0942297398 scopus 로고    scopus 로고
    • Repair of oxidized bases from DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2
    • Dou H., Mitra S., Hazra T.K. Repair of oxidized bases from DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2. J. Biol. Chem. 30:2003;30.
    • (2003) J. Biol. Chem. , vol.30 , pp. 30
    • Dou, H.1    Mitra, S.2    Hazra, T.K.3
  • 21
    • 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., Doetsch P.W. Transcriptional mutagenesis induced by uracil and 8-oxoguanine in Escherichia coli. Mol. Cell. 12:2003;959-970.
    • (2003) Mol. Cell , vol.12 , pp. 959-970
    • Bregeon, D.1    Doddridge, Z.A.2    You, H.J.3    Weiss, B.4    Doetsch, P.W.5
  • 22
    • 0026533905 scopus 로고
    • Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): Excision of purine lesions in DNA produced by ionizing radiation or photosensitization
    • Boiteux S., Gajewski E., Laval J., Dizdaroglu M. Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): excision of purine lesions in DNA produced by ionizing radiation or photosensitization. Biochemistry. 31:1992;106-110.
    • (1992) Biochemistry , vol.31 , pp. 106-110
    • Boiteux, S.1    Gajewski, E.2    Laval, J.3    Dizdaroglu, M.4
  • 23
    • 0027469856 scopus 로고
    • Effects of DNA lesions on transcription elongation by T7 RNA polymerase
    • Chen Y.H., Bogenhagen D.F. Effects of DNA lesions on transcription elongation by T7 RNA polymerase. J. Biol. Chem. 268:1993;5849-5855.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5849-5855
    • Chen, Y.H.1    Bogenhagen, D.F.2
  • 24
    • 0032516880 scopus 로고    scopus 로고
    • Effects of nonbulky DNA base damages on Escherichia coli RNA polymerase-mediated elongation and promoter clearance
    • Viswanathan A., Doetsch P.W. Effects of nonbulky DNA base damages on Escherichia coli RNA polymerase-mediated elongation and promoter clearance. J. Biol. Chem. 273:1998;21276-21281.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21276-21281
    • Viswanathan, A.1    Doetsch, P.W.2
  • 25
    • 0037470158 scopus 로고    scopus 로고
    • Effects of endogenous DNA base lesions on transcription elongation by mammalian RNA polymerase II. Implications for transcription-coupled DNA repair and transcriptional mutagenesis
    • Kuraoka I., Endou M., Yamaguchi Y., Wada T., Handa H., Tanaka K. Effects of endogenous DNA base lesions on transcription elongation by mammalian RNA polymerase II. Implications for transcription-coupled DNA repair and transcriptional mutagenesis. J. Biol. Chem. 278:2003;7294-7299.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7294-7299
    • Kuraoka, I.1    Endou, M.2    Yamaguchi, Y.3    Wada, T.4    Handa, H.5    Tanaka, K.6
  • 26
    • 0034646516 scopus 로고    scopus 로고
    • Transcription-coupled repair of 8-oxoguanine: Requirement for XPG, TFIIH, and CSB and implications for Cockayne syndrome
    • Le Page F., Kwoh E.E., Avrutskaya A., Gentil A., Leadon S.A., Sarasin A., Cooper P.K. Transcription-coupled repair of 8-oxoguanine: requirement for XPG, TFIIH, and CSB and implications for Cockayne syndrome. Cell. 101:2000;159-171.
    • (2000) Cell , vol.101 , pp. 159-171
    • Le Page, F.1    Kwoh, E.E.2    Avrutskaya, A.3    Gentil, A.4    Leadon, S.A.5    Sarasin, A.6    Cooper, P.K.7
  • 27
    • 0034307185 scopus 로고    scopus 로고
    • BRCA1 and BRCA2 are necessary for the transcription-coupled repair of the oxidative 8-oxoguanine lesion in human cells
    • Le Page F., Randrianarison V., Marot D., Cabannes J., Perricaudet M., Feunteun J., Sarasin A. BRCA1 and BRCA2 are necessary for the transcription-coupled repair of the oxidative 8-oxoguanine lesion in human cells. Cancer Res. 60:2000;5548-5552.
    • (2000) Cancer Res. , vol.60 , pp. 5548-5552
    • Le Page, F.1    Randrianarison, V.2    Marot, D.3    Cabannes, J.4    Perricaudet, M.5    Feunteun, J.6    Sarasin, A.7
  • 28
    • 0031025997 scopus 로고    scopus 로고
    • Defective transcription-coupled repair of oxidative base damage in Cockayne syndrome patients from XP group G
    • Cooper P.K., Nouspikel T., Clarkson S.G., Leadon S.A. Defective transcription-coupled repair of oxidative base damage in Cockayne syndrome patients from XP group G. Science. 275:1997;990-993.
    • (1997) Science , vol.275 , pp. 990-993
    • Cooper, P.K.1    Nouspikel, T.2    Clarkson, S.G.3    Leadon, S.A.4
  • 29
    • 0033603440 scopus 로고    scopus 로고
    • BRCA1 expression restores radiation resistance in BRCA1-defective cancer cells through enhancement of transcription-coupled DNA repair
    • Abbott D.W., Thompson M.E., Robinson-Benion C., Tomlinson G., Jensen R.A., Holt J.T. BRCA1 expression restores radiation resistance in BRCA1-defective cancer cells through enhancement of transcription-coupled DNA repair. J. Biol. Chem. 274:1999;18808-18812.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18808-18812
    • Abbott, D.W.1    Thompson, M.E.2    Robinson-Benion, C.3    Tomlinson, G.4    Jensen, R.A.5    Holt, J.T.6
  • 30
    • 0032029577 scopus 로고    scopus 로고
    • Repair and mutagenic potency of 8-oxoG:A and 8-oxoG:C base pairs in mammalian cells
    • Le Page F., Guy A., Cadet J., Sarasin A., Gentil A. Repair and mutagenic potency of 8-oxoG:A and 8-oxoG:C base pairs in mammalian cells. Nucleic Acids Res. 26:1998;1276-1281.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1276-1281
    • Le Page, F.1    Guy, A.2    Cadet, J.3    Sarasin, A.4    Gentil, A.5
  • 31
    • 0034724274 scopus 로고    scopus 로고
    • BRCA1 interaction with RNA polymerase II reveals a role for hRPB2 and hRPB10alpha in activated transcription
    • Schlegel B.P., Green V.J., Ladias J.A., Parvin J.D. BRCA1 interaction with RNA polymerase II reveals a role for hRPB2 and hRPB10alpha in activated transcription. Proc. Natl. Acad. Sci. USA. 97:2000;3148-3153.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3148-3153
    • Schlegel, B.P.1    Green, V.J.2    Ladias, J.A.3    Parvin, J.D.4
  • 32
    • 0033105926 scopus 로고    scopus 로고
    • Repair of 8-oxoguanine in DNA is deficient in Cockayne syndrome group B cells
    • Dianov G., Bischoff C., Sunesen M., Bohr V.A. Repair of 8-oxoguanine in DNA is deficient in Cockayne syndrome group B cells. Nucleic Acids Res. 27:1999;1365-1368.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1365-1368
    • Dianov, G.1    Bischoff, C.2    Sunesen, M.3    Bohr, V.A.4
  • 33
    • 0037118577 scopus 로고    scopus 로고
    • Global genome repair of 8-oxoG in hamster cells requires a functional CSB gene product
    • Sunesen M., Stevnsner T., Brosh R.M. Jr, Dianov G.L., Bohr V.A. Global genome repair of 8-oxoG in hamster cells requires a functional CSB gene product. Oncogene. 21:2002;3571-3578.
    • (2002) Oncogene , vol.21 , pp. 3571-3578
    • Sunesen, M.1    Stevnsner, T.2    Brosh Jr., R.M.3    Dianov, G.L.4    Bohr, V.A.5
  • 35
    • 18744368449 scopus 로고    scopus 로고
    • A global DNA repair mechanism involving the Cockayne syndrome B (CSB) gene product can prevent the in vivo accumulation of endogenous oxidative DNA base damage
    • Osterod M., Larsen E., Le Page F., Hengstler J.G., Van Der Horst G.T., Boiteux S., Klungland A., Epe B. A global DNA repair mechanism involving the Cockayne syndrome B (CSB) gene product can prevent the in vivo accumulation of endogenous oxidative DNA base damage. Oncogene. 21:2002;8232-8239.
    • (2002) Oncogene , vol.21 , pp. 8232-8239
    • Osterod, M.1    Larsen, E.2    Le Page, F.3    Hengstler, J.G.4    Van Der Horst, G.T.5    Boiteux, S.6    Klungland, A.7    Epe, B.8
  • 36
    • 0036837549 scopus 로고    scopus 로고
    • Functional crosstalk between hOgg1 and the helicase domain of Cockayne syndrome group B protein
    • Tuo J., Chen C., Zeng X., Christiansen M., Bohr V.A. Functional crosstalk between hOgg1 and the helicase domain of Cockayne syndrome group B protein. DNA Repair (Amst.). 1:2002;913-927.
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 913-927
    • Tuo, J.1    Chen, C.2    Zeng, X.3    Christiansen, M.4    Bohr, V.A.5
  • 37
    • 0037468273 scopus 로고    scopus 로고
    • The transcriptional response after oxidative stress is defective in Cockayne syndrome group B cells
    • Kyng K.J., May A., Brosh R.M. Jr, Cheng W.H., Chen C., Becker K.G., Bohr V.A. The transcriptional response after oxidative stress is defective in Cockayne syndrome group B cells. Oncogene. 22:2003;1135-1149.
    • (2003) Oncogene , vol.22 , pp. 1135-1149
    • Kyng, K.J.1    May, A.2    Brosh Jr., R.M.3    Cheng, W.H.4    Chen, C.5    Becker, K.G.6    Bohr, V.A.7
  • 38
    • 0030902253 scopus 로고    scopus 로고
    • Reduced RNA polymerase II transcription in intact and permeabilized Cockayne syndrome group B cells
    • Balajee A.S., May A., Dianov G.L., Friedberg E.C., Bohr V.A. Reduced RNA polymerase II transcription in intact and permeabilized Cockayne syndrome group B cells. Proc. Natl. Acad. Sci. USA. 94:1997;4306-4311.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4306-4311
    • Balajee, A.S.1    May, A.2    Dianov, G.L.3    Friedberg, E.C.4    Bohr, V.A.5
  • 39
    • 0032945268 scopus 로고    scopus 로고
    • Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs
    • Nishioka K., Ohtsubo T., Oda H., Fujiwara T., Kang D., Sugimachi K., Nakabeppu Y. Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs. Mol. Biol. Cell. 10:1999;1637-1652.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1637-1652
    • Nishioka, K.1    Ohtsubo, T.2    Oda, H.3    Fujiwara, T.4    Kang, D.5    Sugimachi, K.6    Nakabeppu, Y.7
  • 40
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace D.C. Mitochondrial diseases in man and mouse. Science. 283:1999;1482-1488.
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 41
    • 0032436502 scopus 로고    scopus 로고
    • Oxidative damage and mutation to mitochondrial DNA and age-dependent decline of mitochondrial respiratory function
    • Wei Y.H., Lu C.Y., Lee H.C., Pang C.Y., Ma Y.S. Oxidative damage and mutation to mitochondrial DNA and age-dependent decline of mitochondrial respiratory function. Ann. N.Y. Acad. Sci. 854:1998;155-170.
    • (1998) Ann. N.Y. Acad. Sci. , vol.854 , pp. 155-170
    • Wei, Y.H.1    Lu, C.Y.2    Lee, H.C.3    Pang, C.Y.4    Ma, Y.S.5
  • 43
    • 0032564458 scopus 로고    scopus 로고
    • Physical interaction between components of DNA mismatch repair and nucleotide excision repair
    • Bertrand P., Tishkoff D.X., Filosi N., Dasgupta R., Kolodner R.D. Physical interaction between components of DNA mismatch repair and nucleotide excision repair. Proc. Natl. Acad. Sci. USA. 95:1998;14278-14283.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14278-14283
    • Bertrand, P.1    Tishkoff, D.X.2    Filosi, N.3    Dasgupta, R.4    Kolodner, R.D.5
  • 44
    • 0029887819 scopus 로고    scopus 로고
    • Transcription-coupled repair deficiency and mutations in human mismatch repair genes
    • Mellon I., Rajpal D.K., Koi M., Boland C.R., Champe G.N. Transcription-coupled repair deficiency and mutations in human mismatch repair genes. Science. 272:1996;557-560.
    • (1996) Science , vol.272 , pp. 557-560
    • Mellon, I.1    Rajpal, D.K.2    Koi, M.3    Boland, C.R.4    Champe, G.N.5
  • 45
    • 0033054250 scopus 로고    scopus 로고
    • Excision repair invades the territory of mismatch repair
    • Sancar A. Excision repair invades the territory of mismatch repair. Nat. Genet. 21:1999;247-249.
    • (1999) Nat. Genet. , vol.21 , pp. 247-249
    • Sancar, A.1
  • 46
    • 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., Lu A.L. 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. 277:2002;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
  • 47
    • 0033197818 scopus 로고    scopus 로고
    • MSH2 and MSH6 are required for removal of adenine misincorporated opposite 8-oxo-guanine in S. cerevisiae
    • Ni T.T., Marsischky G.T., Kolodner R.D. MSH2 and MSH6 are required for removal of adenine misincorporated opposite 8-oxo-guanine in S. cerevisiae. Mol. Cell. 4:1999;439-444.
    • (1999) Mol. Cell , vol.4 , pp. 439-444
    • Ni, T.T.1    Marsischky, G.T.2    Kolodner, R.D.3
  • 48
    • 0041928171 scopus 로고    scopus 로고
    • Potential role of MLH1 in the induction of p53 and apoptosis by blocking transcription on damaged DNA templates
    • Yanamadala S., Ljungman M. Potential role of MLH1 in the induction of p53 and apoptosis by blocking transcription on damaged DNA templates. Mol. Cancer Res. 1:2003;747-754.
    • (2003) Mol. Cancer Res. , vol.1 , pp. 747-754
    • Yanamadala, S.1    Ljungman, M.2
  • 49
    • 0035837651 scopus 로고    scopus 로고
    • Somatic mutations and single nucleotide polymorphisms of base excision repair genes involved in the repair of 8-hydroxyguanine in damaged DNA
    • Shinmura K., Yamaguchi S., Saitoh T., Kohno T., Yokota J. Somatic mutations and single nucleotide polymorphisms of base excision repair genes involved in the repair of 8-hydroxyguanine in damaged DNA. Cancer Lett. 166:2001;65-69.
    • (2001) Cancer Lett. , vol.166 , pp. 65-69
    • Shinmura, K.1    Yamaguchi, S.2    Saitoh, T.3    Kohno, T.4    Yokota, J.5
  • 50
    • 0031428463 scopus 로고    scopus 로고
    • Cigarette smoking induces an increase in oxidative DNA damage, 8-hydroxydeoxyguanosine, in a central site of the human lung
    • Asami S., Manabe H., Miyake J., Tsurudome Y., Hirano T., Yamaguchi R., Itoh H., Kasai H. Cigarette smoking induces an increase in oxidative DNA damage, 8-hydroxydeoxyguanosine, in a central site of the human lung. Carcinogenesis. 18:1997;1763-1766.
    • (1997) Carcinogenesis , vol.18 , pp. 1763-1766
    • Asami, S.1    Manabe, H.2    Miyake, J.3    Tsurudome, Y.4    Hirano, T.5    Yamaguchi, R.6    Itoh, H.7    Kasai, H.8
  • 53
    • 0036113829 scopus 로고    scopus 로고
    • A single nucleotide polymorphism at the splice donor site of the human MYH base excision repair genes results in reduced translation efficiency of its transcripts
    • Yamaguchi S., Shinmura K., Saitoh T., Takenoshita S., Kuwano H., Yokota J. A single nucleotide polymorphism at the splice donor site of the human MYH base excision repair genes results in reduced translation efficiency of its transcripts. Genes Cells. 7:2002;461-474.
    • (2002) Genes Cells , vol.7 , pp. 461-474
    • Yamaguchi, S.1    Shinmura, K.2    Saitoh, T.3    Takenoshita, S.4    Kuwano, H.5    Yokota, J.6
  • 56
    • 0141960200 scopus 로고    scopus 로고
    • Exposing the MYtH about base excision repair and human inherited disease
    • Cheadle J.P., Sampson J.R. Exposing the MYtH about base excision repair and human inherited disease. Hum. Mol. Genet. 12:2003;R159-R165.
    • (2003) Hum. Mol. Genet. , vol.12
    • Cheadle, J.P.1    Sampson, J.R.2
  • 60
    • 0037530306 scopus 로고    scopus 로고
    • HOGG1 Ser326Cys polymorphism modifies the significance of the environmental risk factor for colon cancer
    • Kim J.I., Park Y.J., Kim K.H., Song B.J., Lee M.S., Kim C.N., Chang S.H. hOGG1 Ser326Cys polymorphism modifies the significance of the environmental risk factor for colon cancer. World J. Gastroenterol. 9:2003;956-960.
    • (2003) World J. Gastroenterol. , vol.9 , pp. 956-960
    • Kim, J.I.1    Park, Y.J.2    Kim, K.H.3    Song, B.J.4    Lee, M.S.5    Kim, C.N.6    Chang, S.H.7
  • 61
    • 2942571939 scopus 로고    scopus 로고
    • Age-associated decrease of oxidative repair enzymes, human 8-oxoguanine DNA glycosylases (hOgg1), in human aging
    • Chen S.K., Hsieh W.A., Tsai M.H., Chen C.C., Hong A.I., Wei Y.H., Chang W.P. Age-associated decrease of oxidative repair enzymes, human 8-oxoguanine DNA glycosylases (hOgg1), in human aging. J. Radiat. Res. (Tokyo). 44:2003;31-35.
    • (2003) J. Radiat. Res. (Tokyo) , vol.44 , pp. 31-35
    • Chen, S.K.1    Hsieh, W.A.2    Tsai, M.H.3    Chen, C.C.4    Hong, A.I.5    Wei, Y.H.6    Chang, W.P.7
  • 63
    • 0035820074 scopus 로고    scopus 로고
    • UV light-induced degradation of RNA polymerase II is dependent on the Cockayne's syndrome a and B proteins but not p53 or MLH1
    • McKay B.C., Chen F., Clarke S.T., Wiggin H.E., Harley L.M., Ljungman M. UV light-induced degradation of RNA polymerase II is dependent on the Cockayne's syndrome A and B proteins but not p53 or MLH1. Mutat. Res. 485:2001;93-105.
    • (2001) Mutat. Res. , vol.485 , pp. 93-105
    • McKay, B.C.1    Chen, F.2    Clarke, S.T.3    Wiggin, H.E.4    Harley, L.M.5    Ljungman, M.6
  • 64
    • 0035807072 scopus 로고    scopus 로고
    • Ultraviolet radiation alters the phosphorylation of RNA polymerase II large subunit and accelerates its proteasome-dependent degradation
    • Luo Z., Zheng J., Lu Y., Bregman D.B. Ultraviolet radiation alters the phosphorylation of RNA polymerase II large subunit and accelerates its proteasome-dependent degradation. Mutat. Res. 486:2001;259-274.
    • (2001) Mutat. Res. , vol.486 , pp. 259-274
    • Luo, Z.1    Zheng, J.2    Lu, Y.3    Bregman, D.B.4
  • 66
    • 0033634972 scopus 로고    scopus 로고
    • Activation of p53 or loss of the Cockayne syndrome group B repair protein causes metaphase fragility of human U1, U2, and 5S genes
    • Yu A., Fan H.Y., Liao D., Bailey A.D., Weiner A.M. Activation of p53 or loss of the Cockayne syndrome group B repair protein causes metaphase fragility of human U1, U2, and 5S genes. Mol. Cell. 5:2000;801-810.
    • (2000) Mol. Cell , vol.5 , pp. 801-810
    • Yu, A.1    Fan, H.Y.2    Liao, D.3    Bailey, A.D.4    Weiner, A.M.5
  • 67
    • 0344874275 scopus 로고    scopus 로고
    • Effects of genomic context and chromatin structure on transcription-coupled and global genomic repair in mammalian cells
    • Feng Z., Hu W., Chasin L.A., Tang M.S. Effects of genomic context and chromatin structure on transcription-coupled and global genomic repair in mammalian cells. Nucleic Acids Res. 31:2003;5897-5906.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5897-5906
    • Feng, Z.1    Hu, W.2    Chasin, L.A.3    Tang, M.S.4
  • 68
    • 0032472378 scopus 로고    scopus 로고
    • Site-specific repair of cyclobutane pyrimidine dimers in a positioned nucleosome by photolyase and T4 endonuclease V in vitro
    • Schieferstein U., Thoma F. Site-specific repair of cyclobutane pyrimidine dimers in a positioned nucleosome by photolyase and T4 endonuclease V in vitro. EMBO J. 17:1998;306-316.
    • (1998) EMBO J. , vol.17 , pp. 306-316
    • Schieferstein, U.1    Thoma, F.2
  • 69
    • 0033568312 scopus 로고    scopus 로고
    • ATP-dependent remodeling and acetylation as regulators of chromatin fluidity
    • Kingston R.E., Narlikar G.J. ATP-dependent remodeling and acetylation as regulators of chromatin fluidity. Genes Dev. 13:1999;2339-2352.
    • (1999) Genes Dev. , vol.13 , pp. 2339-2352
    • Kingston, R.E.1    Narlikar, G.J.2
  • 70
    • 0030667078 scopus 로고    scopus 로고
    • Recruitment of the putative transcription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes
    • Tantin D., Kansal A., Carey M. Recruitment of the putative transcription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes. Mol. Cell Biol. 17:1997;6803-6814.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6803-6814
    • Tantin, D.1    Kansal, A.2    Carey, M.3
  • 71
    • 0032561475 scopus 로고    scopus 로고
    • RNA polymerase II elongation complexes containing the Cockayne syndrome group B protein interact with a molecular complex containing the transcription factor IIH components xeroderma pigmentosum B and p62
    • Tantin D. RNA polymerase II elongation complexes containing the Cockayne syndrome group B protein interact with a molecular complex containing the transcription factor IIH components xeroderma pigmentosum B and p62. J. Biol. Chem. 273:1998;27794-27799.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27794-27799
    • Tantin, D.1
  • 72
    • 0035313754 scopus 로고    scopus 로고
    • Mechanism of transcription initiation and promoter escape by RNA polymerase II
    • Dvir A., Conaway J.W., Conaway R.C. Mechanism of transcription initiation and promoter escape by RNA polymerase II. Curr. Opin. Genet Dev. 11:2001;209-214.
    • (2001) Curr. Opin. Genet Dev. , vol.11 , pp. 209-214
    • Dvir, A.1    Conaway, J.W.2    Conaway, R.C.3
  • 73
    • 0033032157 scopus 로고    scopus 로고
    • Recovery of RNA synthesis from the DHFR gene following UV-irradiation precedes the removal of photolesions from the transcribed strand
    • Ljungman M. Recovery of RNA synthesis from the DHFR gene following UV-irradiation precedes the removal of photolesions from the transcribed strand. Carcinogenesis. 20:1999;395-399.
    • (1999) Carcinogenesis , vol.20 , pp. 395-399
    • Ljungman, M.1
  • 74
    • 0037193542 scopus 로고    scopus 로고
    • Repair of 8-oxoG is slower in endogenous nuclear genes than in mitochondrial DNA and is without strand bias
    • Thorslund T., Sunesen M., Bohr V.A., Stevnsner T. Repair of 8-oxoG is slower in endogenous nuclear genes than in mitochondrial DNA and is without strand bias. DNA Repair (Amst.). 1:2002;261-273.
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 261-273
    • Thorslund, T.1    Sunesen, M.2    Bohr, V.A.3    Stevnsner, T.4
  • 75
    • 0026508774 scopus 로고
    • Cockayne syndrome: Review of 140 cases
    • Nance M.A., Berry S.A. Cockayne syndrome: review of 140 cases. Am. J. Med. Genet. 42:1992;68-84.
    • (1992) Am. J. Med. Genet. , vol.42 , pp. 68-84
    • Nance, M.A.1    Berry, S.A.2
  • 76
    • 0037196071 scopus 로고    scopus 로고
    • Translesion synthesis by RNA polymerases: Occurrence and biological implications for transcriptional mutagenesis
    • Doetsch P.W. Translesion synthesis by RNA polymerases: occurrence and biological implications for transcriptional mutagenesis. Mutat. Res. 510:2002;131-140.
    • (2002) Mutat. Res. , vol.510 , pp. 131-140
    • Doetsch, P.W.1
  • 77
    • 0028807735 scopus 로고
    • RNA polymerase bypass at sites of dihydrouracil: Implications for transcriptional mutagenesis
    • Liu J., Zhou W., Doetsch P.W. RNA polymerase bypass at sites of dihydrouracil: implications for transcriptional mutagenesis. Mol. Cell Biol. 15:1995;6729-6735.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 6729-6735
    • Liu, J.1    Zhou, W.2    Doetsch, P.W.3
  • 81
    • 0037414341 scopus 로고    scopus 로고
    • Choice between death by senescence or by cancer?
    • Sarasin A. Choice between death by senescence or by cancer? DNA Repair (Amst.). 2:2003;437-439.
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 437-439
    • Sarasin, A.1


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