메뉴 건너뛰기




Volumn 193, Issue 1-2, 2003, Pages 43-65

Mammalian DNA base excision repair proteins: Their interactions and role in repair of oxidative DNA damage

Author keywords

Base excision repair; DNA; Reactive oxygen species

Indexed keywords

BRCA1 PROTEIN; BRCA2 PROTEIN; DNA; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA DIRECTED DNA POLYMERASE BETA; DNA GLYCOSYLTRANSFERASE; ENDONUCLEASE; ENDONUCLEASE VIII; FLAP ENDONUCLEASE 1 PROTEIN; MYH PROTEIN; NEI LIKE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NUCLEAR PROTEIN; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; POLYNUCLEOTIDE 5' HYDROXYL KINASE; PROTEIN P53; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; XERODERMA PIGMENTOSUM COMPLEMENTATION GROUP G PROTEIN; XRCC1 PROTEIN;

EID: 0242268065     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-483X(03)00289-0     Document Type: Review
Times cited : (185)

References (173)
  • 2
    • 0037039348 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) polymerase in rapid intracellular acidification induced by alkylating DNA damage
    • Affar el B., Shah R., Dallaire A., Castonguay V., Shah G. Role of poly(ADP-ribose) polymerase in rapid intracellular acidification induced by alkylating DNA damage. Proc. Natl. Acad. Sci. U.S.A. 99:2002;245-250.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 245-250
    • Affar El, B.1    Shah, R.2    Dallaire, A.3    Castonguay, V.4    Shah, G.5
  • 4
    • 0031830844 scopus 로고    scopus 로고
    • BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A
    • Anderson S., Schlegel B., Nakajima T., Wolpin E., Parvin J. BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A. Nat. Genet. 19:1998;254-256.
    • (1998) Nat. Genet. , vol.19 , pp. 254-256
    • Anderson, S.1    Schlegel, B.2    Nakajima, T.3    Wolpin, E.4    Parvin, J.5
  • 5
    • 0030760240 scopus 로고    scopus 로고
    • Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage
    • Arai K., Morishita K., Shinmura K., Kohno T., Kim S., Nohmi T., Taniwaki M., Ohwada S.J.Y. Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage. Oncogene. 14:1997;2857-2861.
    • (1997) Oncogene , vol.14 , pp. 2857-2861
    • Arai, K.1    Morishita, K.2    Shinmura, K.3    Kohno, T.4    Kim, S.5    Nohmi, T.6    Taniwaki, M.7    Ohwada, S.J.Y.8
  • 6
    • 0036955119 scopus 로고    scopus 로고
    • High accumulation of oxidative DNA damage, 8-hydroxyguanine, in Mmh/Ogg1 deficient mice by chronic oxidative stress
    • Arai T., Kelly V., Minowa O., Noda T., Nishimura S. High accumulation of oxidative DNA damage, 8-hydroxyguanine, in Mmh/Ogg1 deficient mice by chronic oxidative stress. Carcinogenesis. 23:2002;2005-2010.
    • (2002) Carcinogenesis , vol.23 , pp. 2005-2010
    • Arai, T.1    Kelly, V.2    Minowa, O.3    Noda, T.4    Nishimura, S.5
  • 8
    • 0024521430 scopus 로고
    • Bacteriophage-T4 and Micrococcus luteus UV endonucleases are not endonucleases but beta-elimination and sometimes beta delta-elimination catalysts
    • Bailly V., Sente B., Verly W. Bacteriophage-T4 and Micrococcus luteus UV endonucleases are not endonucleases but beta-elimination and sometimes beta delta-elimination catalysts. Biochem. J. 259:1989;751-759.
    • (1989) Biochem. J. , vol.259 , pp. 751-759
    • Bailly, V.1    Sente, B.2    Verly, W.3
  • 9
    • 0037125133 scopus 로고    scopus 로고
    • A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII
    • Bandaru V., Sunkara S., Wallace S.J.P.B. A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII. DNA Repair. 1:2002;517-529.
    • (2002) DNA Repair , vol.1 , pp. 517-529
    • Bandaru, V.1    Sunkara, S.2    Wallace, S.J.P.B.3
  • 10
    • 0030839865 scopus 로고    scopus 로고
    • Oxidative decay of DNA
    • Beckman K.B., Ames B.N. Oxidative decay of DNA. J. Biol. Chem. 272:1997;19633-19636.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19633-19636
    • Beckman, K.B.1    Ames, B.N.2
  • 11
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway
    • Bennett R.A., Wilson D.M. III, Wong D., Demple B. Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway. Proc. Natl. Acad. Sci. U.S.A. 94:1997;7166-7169.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7166-7169
    • Bennett, R.A.1    Wilson D.M. III2    Wong, D.3    Demple, B.4
  • 12
    • 0033557139 scopus 로고    scopus 로고
    • Bessho, T., 1999. Nucleotide excision repair 3′ endonuclease XPG stimulates the activity of base excision repair enzyme thymine glycol DNA glycosylase. Nucleic Acids Res. 27, 979-983.
    • Bessho, T., 1999. Nucleotide excision repair 3′ endonuclease XPG stimulates the activity of base excision repair enzyme thymine glycol DNA glycosylase. Nucleic Acids Res. 27, 979-983.
  • 13
    • 85030957371 scopus 로고    scopus 로고
    • Bhakat, K., Izumi, T., Yang, S., Hazra, T., Mitra, S. Acetylation of human AP-endonuclease (APE1/Ref1) and repression of the parathyroid hormone gene, submitted for publication.
    • Bhakat, K., Izumi, T., Yang, S., Hazra, T., Mitra, S. Acetylation of human AP-endonuclease (APE1/Ref1) and repression of the parathyroid hormone gene, submitted for publication.
  • 14
    • 0030703177 scopus 로고    scopus 로고
    • Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites
    • Bjoras M., Luna L., Johnsen B., Hoff E., Haug T., Rognes T., Seeberg E. Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites. EMBO J. 16:1997;6314-6322.
    • (1997) EMBO J. , vol.16 , pp. 6314-6322
    • Bjoras, M.1    Luna, L.2    Johnsen, B.3    Hoff, E.4    Haug, T.5    Rognes, T.6    Seeberg, E.7
  • 15
    • 0032742730 scopus 로고    scopus 로고
    • A novel role for Escherichia coli endonuclease VIII in prevention of spontaneous G → T transversions
    • Blaisdell J., Hatahet Z., Wallace S. A novel role for Escherichia coli endonuclease VIII in prevention of spontaneous G → T transversions. J. Bacteriol. 181:1999;6396-6402.
    • (1999) J. Bacteriol. , vol.181 , pp. 6396-6402
    • Blaisdell, J.1    Hatahet, Z.2    Wallace, S.3
  • 16
    • 0033011114 scopus 로고    scopus 로고
    • Mice lacking the poly(ADP-ribose) polymerase gene are resistant to pancreatic beta-cell destruction and diabetes development induced by streptozocin
    • Burkart V., Wang Z.Q., Radons J., Heller B., Herceg Z., Stingl L., Wagner E.F., Kolb H. Mice lacking the poly(ADP-ribose) polymerase gene are resistant to pancreatic beta-cell destruction and diabetes development induced by streptozocin. Nat. Med. 5:1999;314-319.
    • (1999) Nat. Med. , vol.5 , pp. 314-319
    • Burkart, V.1    Wang, Z.Q.2    Radons, J.3    Heller, B.4    Herceg, Z.5    Stingl, L.6    Wagner, E.F.7    Kolb, H.8
  • 17
    • 0028862933 scopus 로고
    • Characterization of the XRCC1-DNA ligase III complex in vitro and its absence from mutant hamster cells
    • Caldecott K., Tucker J., Stanker L., Thompson L. Characterization of the XRCC1-DNA ligase III complex in vitro and its absence from mutant hamster cells. Nucleic Acids Res. 23:1995;4836-4843.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4836-4843
    • Caldecott, K.1    Tucker, J.2    Stanker, L.3    Thompson, L.4
  • 18
    • 0029957245 scopus 로고    scopus 로고
    • XRCC1 polypeptide interacts with DNA polymerase beta and possibly poly(ADP-ribose) polymerase, and DNA ligase III is a novel molecular 'nick-sensor' in vitro
    • Caldecott K., Aoufouchi S., Johnson P., Sharll S. XRCC1 polypeptide interacts with DNA polymerase beta and possibly poly(ADP-ribose) polymerase, and DNA ligase III is a novel molecular 'nick-sensor' in vitro. Nucleic Acids Res. 24:1996;4387-4394.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4387-4394
    • Caldecott, K.1    Aoufouchi, S.2    Johnson, P.3    Sharll, S.4
  • 19
    • 0035098395 scopus 로고    scopus 로고
    • Rates of base excision repair are not solely dependent on levels of initiating enzymes
    • Cappelli E., Hazra T., Hill J., Slupphaug G., Bogliolo M., Frosina G. Rates of base excision repair are not solely dependent on levels of initiating enzymes. Carcinogenesis. 22:2001;387-393.
    • (2001) Carcinogenesis , vol.22 , pp. 387-393
    • Cappelli, E.1    Hazra, T.2    Hill, J.3    Slupphaug, G.4    Bogliolo, M.5    Frosina, G.6
  • 20
    • 0033531271 scopus 로고    scopus 로고
    • The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter
    • Chai Y., Cui J., Shao N., Shyam E., Reddy P., Rao V. The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter. Oncogene. 18:1999;263-268.
    • (1999) Oncogene , vol.18 , pp. 263-268
    • Chai, Y.1    Cui, J.2    Shao, N.3    Shyam, E.4    Reddy, P.5    Rao, V.6
  • 21
    • 0026004662 scopus 로고
    • Two distinct human DNA diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidized DNA
    • Chen D., Herman T., Demple B. Two distinct human DNA diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidized DNA. Nucleic Acids Res. 19:1991;5907-5914.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5907-5914
    • Chen, D.1    Herman, T.2    Demple, B.3
  • 22
    • 0034711275 scopus 로고    scopus 로고
    • Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes
    • Clark A., Valle F., Drotschmann K., Gary R., Kunkel T. Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes. J. Biol. Chem. 275:2000;36498-36501.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36498-36501
    • Clark, A.1    Valle, F.2    Drotschmann, K.3    Gary, R.4    Kunkel, T.5
  • 23
    • 0033605159 scopus 로고    scopus 로고
    • Conserved residues of human XPG protein important for nuclease activity and function in nucleotide excision repair
    • Constantinou A., Gunz D., Evans E., Lalle P., Bates P., Wood R., Clarkson S. Conserved residues of human XPG protein important for nuclease activity and function in nucleotide excision repair. J. Biol. Chem. 274:1999;5637-5648.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5637-5648
    • Constantinou, A.1    Gunz, D.2    Evans, E.3    Lalle, P.4    Bates, P.5    Wood, R.6    Clarkson, S.7
  • 24
    • 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
  • 25
    • 0019976340 scopus 로고
    • Regulation of DNA ligase activity by poly(ADP-ribose)
    • Creissen D., Shall S. Regulation of DNA ligase activity by poly(ADP-ribose). Nature. 296:1982;271-272.
    • (1982) Nature , vol.296 , pp. 271-272
    • Creissen, D.1    Shall, S.2
  • 26
  • 27
    • 85030966634 scopus 로고    scopus 로고
    • DeVita, V.T., Hellman, S., Rosenberg, S.A., 1997. Cancer : Principles & Practice of Oncology. Lippincott-Raven, Philadelphia.
    • DeVita, V.T., Hellman, S., Rosenberg, S.A., 1997. Cancer : Principles & Practice of Oncology. Lippincott-Raven, Philadelphia.
  • 28
    • 0035940441 scopus 로고    scopus 로고
    • Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair
    • Dianova I.I., Bohr V.A., Dianov G.L. Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair. Biochemistry. 40:2001;12639-12644.
    • (2001) Biochemistry , vol.40 , pp. 12639-12644
    • Dianova, I.I.1    Bohr, V.A.2    Dianov, G.L.3
  • 31
    • 0034663530 scopus 로고    scopus 로고
    • DNA polymerase beta is required for efficient DNA strand repair induced by methyl methanesulfonate but not by hydrogen peroxide
    • Fortini P., Pascucci B., Belisario F., Dogliotti E. DNA polymerase beta is required for efficient DNA strand repair induced by methyl methanesulfonate but not by hydrogen peroxide. Nucleic Acids Res. 28:2000;3040-3046.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3040-3046
    • Fortini, P.1    Pascucci, B.2    Belisario, F.3    Dogliotti, E.4
  • 32
    • 85030965154 scopus 로고    scopus 로고
    • Friedberg, E.C., Walker, G.C., Siede, W., 1995. DNA Repair and Mutagenesis. ASM Press, Washington, DC.
    • Friedberg, E.C., Walker, G.C., Siede, W., 1995. DNA Repair and Mutagenesis. ASM Press, Washington, DC.
  • 33
    • 0032512067 scopus 로고    scopus 로고
    • BRCA2 associates with acetyltransferase activity when bound to P/CAF
    • Fuks F., Milner J., Kouzarides T. BRCA2 associates with acetyltransferase activity when bound to P/CAF. Oncogene. 17:1998;2531-2534.
    • (1998) Oncogene , vol.17 , pp. 2531-2534
    • Fuks, F.1    Milner, J.2    Kouzarides, T.3
  • 34
    • 0033570048 scopus 로고    scopus 로고
    • Ref-1 regulates the transactivation and pro-apoptotic funtions of p53 in vivo
    • Gaiddon C., Moorthy N., Prives C. Ref-1 regulates the transactivation and pro-apoptotic funtions of p53 in vivo. EMBO J. 18:1999;5609-5621.
    • (1999) EMBO J. , vol.18 , pp. 5609-5621
    • Gaiddon, C.1    Moorthy, N.2    Prives, C.3
  • 35
    • 0030767281 scopus 로고    scopus 로고
    • The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21
    • Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., Park M.S. The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21. J. Biol. Chem. 272:1997;24522-24529.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24522-24529
    • Gary, R.1    Ludwig, D.L.2    Cornelius, H.L.3    MacInnes, M.A.4    Park, M.S.5
  • 37
    • 0032516654 scopus 로고    scopus 로고
    • BRCA1 required for transcription-coupled repair of oxidative DNA damage
    • Gowen L.C., Avrutskaya A.V., Latour A.M., Koller B.H., Leadon S.A. BRCA1 required for transcription-coupled repair of oxidative DNA damage. Science. 281:1998;1009-1012.
    • (1998) Science , vol.281 , pp. 1009-1012
    • Gowen, L.C.1    Avrutskaya, A.V.2    Latour, A.M.3    Koller, B.H.4    Leadon, S.A.5
  • 38
    • 0033598713 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion
    • Ha H.C., Snyder S.H. Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion. Proc. Natl. Acad. Sci. U.S.A. 96:1999;13978-13982.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13978-13982
    • Ha, H.C.1    Snyder, S.H.2
  • 40
    • 0034531986 scopus 로고    scopus 로고
    • Second human protein with homology to the Escherichia coli abasic endonuclease exonuclease III
    • Hadi M., Wilson D.R. Second human protein with homology to the Escherichia coli abasic endonuclease exonuclease III. Environ. Mol. Mutagen. 36:2000;312-324.
    • (2000) Environ. Mol. Mutagen. , vol.36 , pp. 312-324
    • Hadi, M.1    Wilson, D.R.2
  • 41
    • 0032980573 scopus 로고    scopus 로고
    • Postnatal growth failure, short life span, and early onset of cellular senescence and subsequent immortalization in mice lacking the xeroderma pigmentosum group G gene
    • Harada Y., Shiomi N., Koike R., Ikawa M., Okabe M., Hirota S., Kitamura Y., Kitagawa M., Matsunaga T., Nikaido O., Shiomi T. Postnatal growth failure, short life span, and early onset of cellular senescence and subsequent immortalization in mice lacking the xeroderma pigmentosum group G gene. Mol. Cell. Biol. 19:1999;2366-2372.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2366-2372
    • Harada, Y.1    Shiomi, N.2    Koike, R.3    Ikawa, M.4    Okabe, M.5    Hirota, S.6    Kitamura, Y.7    Kitagawa, M.8    Matsunaga, T.9    Nikaido, O.10    Shiomi, T.11
  • 42
    • 0035869074 scopus 로고    scopus 로고
    • Transcription coactivator p300 binds PCNA and may have a role in DNA repair synthesis
    • Hasan S., Hassa P.O., Imhof R., Hottiger M.O. Transcription coactivator p300 binds PCNA and may have a role in DNA repair synthesis. Nature. 410:2001a;387-391.
    • (2001) Nature , vol.410 , pp. 387-391
    • Hasan, S.1    Hassa, P.O.2    Imhof, R.3    Hottiger, M.O.4
  • 43
    • 0034969453 scopus 로고    scopus 로고
    • Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300
    • Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P., Hubscher U., Hottiger M.O. Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300. Mol. Cell. 7:2001b;1221-1231.
    • (2001) Mol. Cell , vol.7 , pp. 1221-1231
    • Hasan, S.1    Stucki, M.2    Hassa, P.O.3    Imhof, R.4    Gehrig, P.5    Hunziker, P.6    Hubscher, U.7    Hottiger, M.O.8
  • 45
    • 0034830066 scopus 로고    scopus 로고
    • The 2-deoxyribonolactone lesion produced in DNA by neocarzinostatin and other damaging agents forms cross-links with the base-excision repair enzyme endonuclease III
    • Hashimoto M., Greenberg M., Kow Y., Hwang J., Cunningham R. The 2-deoxyribonolactone lesion produced in DNA by neocarzinostatin and other damaging agents forms cross-links with the base-excision repair enzyme endonuclease III. J. Am. Chem. Soc. 123:2001;3161-3162.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3161-3162
    • Hashimoto, M.1    Greenberg, M.2    Kow, Y.3    Hwang, J.4    Cunningham, R.5
  • 47
    • 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
  • 48
    • 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
  • 50
    • 0037162995 scopus 로고    scopus 로고
    • Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions
    • Hazra T., Kow Y., Hatahet Z., Imhoff B., Boldogh I., Mokkapati S., Mitra S., Izumi T. Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions. J. Biol. Chem. 277:2002b;30417-30420.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30417-30420
    • Hazra, T.1    Kow, Y.2    Hatahet, Z.3    Imhoff, B.4    Boldogh, I.5    Mokkapati, S.6    Mitra, S.7    Izumi, T.8
  • 51
    • 0037325763 scopus 로고    scopus 로고
    • The discovery of a new family of mammalian enzymes for repair of oxidatively damaged DNA, and its physiological implications
    • Hazra T., Izumi T., Kow Y.W., Mitra S. The discovery of a new family of mammalian enzymes for repair of oxidatively damaged DNA, and its physiological implications. Carcinogenesis. 24:2003;155-157.
    • (2003) Carcinogenesis , vol.24 , pp. 155-157
    • Hazra, T.1    Izumi, T.2    Kow, Y.W.3    Mitra, S.4
  • 52
    • 0028929611 scopus 로고
    • RPA involvement in the damage-recognition and incision steps of nucleotide excision repair
    • He Z., Henricksen L., Wold M., Ingles C. RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. Nature. 374:1995;566-569.
    • (1995) Nature , vol.374 , pp. 566-569
    • He, Z.1    Henricksen, L.2    Wold, M.3    Ingles, C.4
  • 53
    • 0021111515 scopus 로고
    • Gamma ray induced deoxyribonucleic acid strand breaks. 3′ Glycolate termini
    • Henner W., Rodriguez L., Hech S., Haseltine W. Gamma ray induced deoxyribonucleic acid strand breaks. 3′ Glycolate termini. J. Biol. Chem. 258:1983;711-713.
    • (1983) J. Biol. Chem. , vol.258 , pp. 711-713
    • Henner, W.1    Rodriguez, L.2    Hech, S.3    Haseltine, W.4
  • 54
    • 0030890419 scopus 로고    scopus 로고
    • Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III
    • Hilbert T., Chaung W., Boorstein R., Cunningham R., Teebor G. Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III. J. Biol. Chem. 272:1997;6733-6740.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6733-6740
    • Hilbert, T.1    Chaung, W.2    Boorstein, R.3    Cunningham, R.4    Teebor, G.5
  • 55
    • 0035863739 scopus 로고    scopus 로고
    • Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: Potential coordination of the initial steps in base excision repair
    • Hill J.W., Hazra T.K., Izumi T., Mitra S. Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: potential coordination of the initial steps in base excision repair. Nucleic Acids Res. 29:2001;430-438.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 430-438
    • Hill, J.W.1    Hazra, T.K.2    Izumi, T.3    Mitra, S.4
  • 56
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers J.H. Genome maintenance mechanisms for preventing cancer. Nature. 411:2001;366-374.
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 59
    • 0034981858 scopus 로고    scopus 로고
    • Amino acid substitution variants of APE1 and XRCC1 genes associated with ionizing radiation sensitivity
    • Hu J., Smith T., Miller M., Mohrenweiser H., Golden A., Case L. Amino acid substitution variants of APE1 and XRCC1 genes associated with ionizing radiation sensitivity. Carcinogenesis. 22:2001;917-922.
    • (2001) Carcinogenesis , vol.22 , pp. 917-922
    • Hu, J.1    Smith, T.2    Miller, M.3    Mohrenweiser, H.4    Golden, A.5    Case, L.6
  • 60
    • 0033607196 scopus 로고    scopus 로고
    • Reaction of the hypoxia-selective antitumor agent tirapazamine with a C1′-radical in single-stranded and double-stranded DNA: The drug and its metabolites can serve as surrogates for molecular oxygen in radical-mediated DNA damage reactions
    • Hwang J., Greenberg M., Fuchs T., Gates K. Reaction of the hypoxia-selective antitumor agent tirapazamine with a C1′-radical in single-stranded and double-stranded DNA: the drug and its metabolites can serve as surrogates for molecular oxygen in radical-mediated DNA damage reactions. Biochemistry. 38:1999;14248-14255.
    • (1999) Biochemistry , vol.38 , pp. 14248-14255
    • Hwang, J.1    Greenberg, M.2    Fuchs, T.3    Gates, K.4
  • 61
    • 0037009440 scopus 로고    scopus 로고
    • Interference of papillomavirus E6 protein with single-strand break repair by interaction with XRCC1
    • Iftner T., Elbel M., Schopp B., Hiller T., Loizou J., Caldecott K., Stubenrauch F. Interference of papillomavirus E6 protein with single-strand break repair by interaction with XRCC1. EMBO J. 21:2002;4741-4748.
    • (2002) EMBO J. , vol.21 , pp. 4741-4748
    • Iftner, T.1    Elbel, M.2    Schopp, B.3    Hiller, T.4    Loizou, J.5    Caldecott, K.6    Stubenrauch, F.7
  • 62
    • 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., Mitra S. 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. 273:1998;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
  • 63
    • 0036773066 scopus 로고    scopus 로고
    • Differential intracellular localization of the human and mouse endonuclease III homologs and analysis of the sorting signals
    • Ikeda S., Kohmoto T., Tabata R., Seki Y. Differential intracellular localization of the human and mouse endonuclease III homologs and analysis of the sorting signals. DNA Repair. 1:2002;847-854.
    • (2002) DNA Repair , vol.1 , pp. 847-854
    • Ikeda, S.1    Kohmoto, T.2    Tabata, R.3    Seki, Y.4
  • 64
    • 0030025947 scopus 로고    scopus 로고
    • Interactions involving the human RNA polymerase II transcription/ nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein
    • Iyer N., Reagan M., Wu K., Canagarajah B., Friedberg E. Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein. Biochemistry. 35:1996;2157-2167.
    • (1996) Biochemistry , vol.35 , pp. 2157-2167
    • Iyer, N.1    Reagan, M.2    Wu, K.3    Canagarajah, B.4    Friedberg, E.5
  • 65
    • 0033923815 scopus 로고    scopus 로고
    • Requirement for human AP endonuclease 1 for repair of 3′-blocking damage at DNA single-strand breaks induced by reactive oxygen species
    • Izumi T., Hazra T.K., Boldogh I., Tomkinson A.E., Park M.S., Ikeda S., Mitra S. Requirement for human AP endonuclease 1 for repair of 3′-blocking damage at DNA single-strand breaks induced by reactive oxygen species. Carcinogenesis. 21:2000;1329-1334.
    • (2000) Carcinogenesis , vol.21 , pp. 1329-1334
    • Izumi, T.1    Hazra, T.K.2    Boldogh, I.3    Tomkinson, A.E.4    Park, M.S.5    Ikeda, S.6    Mitra, S.7
  • 70
    • 0037163025 scopus 로고    scopus 로고
    • Direct interaction between mammalian DNA polymerase beta and proliferating cell nuclear antigen
    • Kedar P.S., Kim S.J., Robertson A., Hou E., Prasad R., Horton J.K., Wilson S.H. Direct interaction between mammalian DNA polymerase beta and proliferating cell nuclear antigen. J. Biol. Chem. 277:2002;31115-31123.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31115-31123
    • Kedar, P.S.1    Kim, S.J.2    Robertson, A.3    Hou, E.4    Prasad, R.5    Horton, J.K.6    Wilson, S.H.7
  • 71
    • 0032502675 scopus 로고    scopus 로고
    • Involvement of flap endonuclease 1 in base excision DNA repair
    • Kim K., Biade S., Matsumoto Y. Involvement of flap endonuclease 1 in base excision DNA repair. J. Biol. Chem. 273:1998;8842-8848.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8842-8848
    • Kim, K.1    Biade, S.2    Matsumoto, Y.3
  • 72
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1)
    • Klungland A., Lindahl T. Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). EMBO J. 16:1997;3341-3348.
    • (1997) EMBO J. , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 75
    • 0345701964 scopus 로고    scopus 로고
    • Cross-linking of 2-deoxyribonolactone and its beta-elimination product by base excision repair enzymes
    • Kroeger K., Hashimoto M., Kow Y., Greenberg M. Cross-linking of 2-deoxyribonolactone and its beta-elimination product by base excision repair enzymes. Biochemistry. 42:2003;2449-2455.
    • (2003) Biochemistry , vol.42 , pp. 2449-2455
    • Kroeger, K.1    Hashimoto, M.2    Kow, Y.3    Greenberg, M.4
  • 76
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan H.E., Standal R., Slupphaug G. DNA glycosylases in the base excision repair of DNA. Biochem. J. 325:1997;1-16.
    • (1997) Biochem. J. , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 77
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase beta and the XRCC1 protein
    • Kubota Y., Nash R.A., Klungland A., Schar P., Barnes D.E., Lindahl T. Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein. EMBO J. 15:1996;6662-6670.
    • (1996) EMBO J. , vol.15 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 78
    • 0035816708 scopus 로고    scopus 로고
    • Photoaffinity labeling of mouse fibroblast enzymes by a base excision repair intermediate. Evidence for the role of poly(ADP-ribose) polymerase-1 in DNA repair
    • Lavrik O.I., Prasad R., Sobol R.W., Horton J.K., Ackerman E.J., Wilson S.H. Photoaffinity labeling of mouse fibroblast enzymes by a base excision repair intermediate. Evidence for the role of poly(ADP-ribose) polymerase-1 in DNA repair. J. Biol. Chem. 276:2001;25541-25548.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25541-25548
    • Lavrik, O.I.1    Prasad, R.2    Sobol, R.W.3    Horton, J.K.4    Ackerman, E.J.5    Wilson, S.H.6
  • 79
    • 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. U.S.A. 97:2000a;8397-8402.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8397-8402
    • Le Page, F.1    Klungland, A.2    Barnes, D.E.3    Sarasin, A.4    Boiteux, S.5
  • 80
    • 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. 101:2000b;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
  • 81
    • 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. 60:2000c;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
  • 82
    • 0342350255 scopus 로고    scopus 로고
    • Interaction between PCNA and DNA ligase I is critical for joining of Okazaki fragments and long-patch base-excision repair
    • Levin D., McKenna A., Motycka T., Matsumoto Y., Tomkinson A. Interaction between PCNA and DNA ligase I is critical for joining of Okazaki fragments and long-patch base-excision repair. Curr. Biol. 10:2000;919-922.
    • (2000) Curr. Biol. , vol.10 , pp. 919-922
    • Levin, D.1    McKenna, A.2    Motycka, T.3    Matsumoto, Y.4    Tomkinson, A.5
  • 83
    • 0037036349 scopus 로고    scopus 로고
    • A novel tricomplex of BRCA1, Nmi, and c-Myc inhibits c-Myc-induced human telomerase reverse transcriptase gene (hTERT) promoter activity in breast cancer
    • Li H., Lee T., Avraham H. A novel tricomplex of BRCA1, Nmi, and c-Myc inhibits c-Myc-induced human telomerase reverse transcriptase gene (hTERT) promoter activity in breast cancer. J. Biol. Chem. 277:2002;20965-20973.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20965-20973
    • Li, H.1    Lee, T.2    Avraham, H.3
  • 84
    • 0028799991 scopus 로고
    • Recognition and processing of damaged DNA
    • Lindahl T. Recognition and processing of damaged DNA. J. Cell. Sci. 19(Suppl):1995;73-77.
    • (1995) J. Cell. Sci. , vol.19 , Issue.SUPPL. , pp. 73-77
    • Lindahl, T.1
  • 85
    • 0036386375 scopus 로고    scopus 로고
    • Truncation of amino-terminal tail stimulates activity of human endonuclease III (hNTH1)
    • Liu X., Roy R. Truncation of amino-terminal tail stimulates activity of human endonuclease III (hNTH1). J. Mol. Biol. 321:2002;265-276.
    • (2002) J. Mol. Biol. , vol.321 , pp. 265-276
    • Liu, X.1    Roy, R.2
  • 86
    • 0036146312 scopus 로고    scopus 로고
    • Distinct functions of BRCA1 and BRCA2 in double-strand break repair
    • Liu Y., West S. Distinct functions of BRCA1 and BRCA2 in double-strand break repair. Breast Cancer Res. 4:2002;9-13.
    • (2002) Breast Cancer Res. , vol.4 , pp. 9-13
    • Liu, Y.1    West, S.2
  • 87
    • 0031172802 scopus 로고    scopus 로고
    • A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer
    • Lu R., Nash H.M., Verdine G. A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer. Curr. Biol. 7:1997;397-407.
    • (1997) Curr. Biol. , vol.7 , pp. 397-407
    • Lu, R.1    Nash, H.M.2    Verdine, G.3
  • 88
    • 0031045858 scopus 로고    scopus 로고
    • An alternative splicing event which occurs in mouse pachytene spermatocytes generates a form of DNA ligase III with distinct biochemical properties that may function in meiotic recombination
    • Mackey Z., Ramos W., Levin D., Walter C., McCarrey J., Tomkinson A. An alternative splicing event which occurs in mouse pachytene spermatocytes generates a form of DNA ligase III with distinct biochemical properties that may function in meiotic recombination. Mol. Cell. Biol. 17:1997;989.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 989
    • Mackey, Z.1    Ramos, W.2    Levin, D.3    Walter, C.4    McCarrey, J.5    Tomkinson, A.6
  • 89
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
    • Maki H., Sekiguchi M. MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature. 355:1992;273-275.
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 91
    • 0037984361 scopus 로고    scopus 로고
    • Marenstein, D., Chan, M., Altamirano, A., Basu, A., Boorstein, R., Cunningham, R., Teebor, G., 2003. Substrate specificity of human endonuclease III (hNth1): effect of human AP endonuclease 1 (APE1) on hNth1 activity, J. Biol. Chem. 278, 9005-9012.
    • Marenstein, D., Chan, M., Altamirano, A., Basu, A., Boorstein, R., Cunningham, R., Teebor, G., 2003. Substrate specificity of human endonuclease III (hNth1): effect of human AP endonuclease 1 (APE1) on hNth1 activity, J. Biol. Chem. 278, 9005-9012.
  • 93
    • 0035225868 scopus 로고    scopus 로고
    • Molecular mechanism of PCNA-dependent base excision repair
    • Matsumoto Y. Molecular mechanism of PCNA-dependent base excision repair. Prog. Nucleic Acid Res. Mol. Biol. 68:2001;129-138.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.68 , pp. 129-138
    • Matsumoto, Y.1
  • 94
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair
    • Matsumoto Y., Kim K. Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair. Science. 269:1995;699-702.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 95
    • 0027965229 scopus 로고
    • Proliferating cell nuclear antigen-dependent abasic site repair in Xenopus laevis oocytes: An alternative pathway of base excision DNA repair
    • Matsumoto Y., Kim K., Bogenhagen D.F. Proliferating cell nuclear antigen-dependent abasic site repair in Xenopus laevis oocytes: an alternative pathway of base excision DNA repair. Mol. Cell. Biol. 14:1994;6187-6197.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6187-6197
    • Matsumoto, Y.1    Kim, K.2    Bogenhagen, D.F.3
  • 97
    • 0037036465 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification
    • Milutinovic S., Zhuang Q., Szyf M. Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification. J. Biol. Chem. 277:2002;20974-20978.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20974-20978
    • Milutinovic, S.1    Zhuang, Q.2    Szyf, M.3
  • 100
    • 0035163137 scopus 로고    scopus 로고
    • Complexities of the DNA base excision repair pathway for repair of oxidative DNA damage
    • Mitra S., Boldogh I., Izumi T., Hazra T.K. Complexities of the DNA base excision repair pathway for repair of oxidative DNA damage. Environ. Mol. Mutagen. 38:2001;180-190.
    • (2001) Environ. Mol. Mutagen. , vol.38 , pp. 180-190
    • Mitra, S.1    Boldogh, I.2    Izumi, T.3    Hazra, T.K.4
  • 102
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and its DNA repair coordination
    • Mol C.D., Izumi T., Mitra S., Tainer J.A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and its DNA repair coordination. Nature. 403:2000a;451-456.
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 103
    • 0034734377 scopus 로고    scopus 로고
    • Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: The 3′ ends justify the means
    • Mol C.D., Hosfield D.J., Tainer J.A. Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: the 3′ ends justify the means. Mutat. Res. 460:2000b;211-229.
    • (2000) Mutat. Res. , vol.460 , pp. 211-229
    • Mol, C.D.1    Hosfield, D.J.2    Tainer, J.A.3
  • 104
    • 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., Seeberg E. Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA. Nucleic Acids Res. 30:2002;4926-4936.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4926-4936
    • Morland, I.1    Rolseth, V.2    Luna, L.3    Rognes, T.4    Bjoras, M.5    Seeberg, E.6
  • 106
    • 0030220956 scopus 로고    scopus 로고
    • Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily
    • Nash H.M., Bruner S.D., Scharer O.D., Kawate T., Addona T.A., Spooner E., Lane W.S., Verdine G.L. Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily. Curr. Biol. 6:1996;968-980.
    • (1996) Curr. Biol. , vol.6 , pp. 968-980
    • Nash, H.M.1    Bruner, S.D.2    Scharer, O.D.3    Kawate, T.4    Addona, T.A.5    Spooner, E.6    Lane, W.S.7    Verdine, G.L.8
  • 107
    • 0030990434 scopus 로고    scopus 로고
    • A common mutational pattern in Cockayne syndrome patients from xeroderma pigmentosum group G: Implications for a second XPG function
    • Nouspikel T., Lalle P., Leadon S., Cooper P., Clarkson S. A common mutational pattern in Cockayne syndrome patients from xeroderma pigmentosum group G: implications for a second XPG function. Proc. Natl. Acad. Sci. U.S.A. 94:1997;3116-3121.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 3116-3121
    • Nouspikel, T.1    Lalle, P.2    Leadon, S.3    Cooper, P.4    Clarkson, S.5
  • 109
    • 0032531934 scopus 로고    scopus 로고
    • Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively
    • Otterlei M., Haug T., Nagelhus T.A., Slupphaug G., Lindmo T., Krokan H.E. Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively. Nucleic Acids Res. 26:1998;4611-4617.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4611-4617
    • Otterlei, M.1    Haug, T.2    Nagelhus, T.A.3    Slupphaug, G.4    Lindmo, T.5    Krokan, H.E.6
  • 111
    • 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., Tainer J.A. Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO J. 17:1998;5214-5226.
    • (1998) EMBO J. , vol.17 , pp. 5214-5226
    • Parikh, S.S.1    Mol, C.D.2    Slupphaug, G.3    Bharati, S.4    Krokan, H.E.5    Tainer, J.A.6
  • 112
    • 0035937102 scopus 로고    scopus 로고
    • Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair
    • Parker A., Gu Y., Mahoney W., Lee S., Singh K., Lu A. Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair. J. Biol. Chem. 276:2001;5547-5555.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5547-5555
    • Parker, A.1    Gu, Y.2    Mahoney, W.3    Lee, S.4    Singh, K.5    Lu, A.6
  • 113
    • 0034734383 scopus 로고    scopus 로고
    • Structure and function in the uracil-DNA glycosylase superfamily
    • Pearl L. Structure and function in the uracil-DNA glycosylase superfamily. Mutat. Res. 460:2000;165-181.
    • (2000) Mutat. Res. , vol.460 , pp. 165-181
    • Pearl, L.1
  • 116
    • 0029892846 scopus 로고    scopus 로고
    • Evidence for an imino intermediate in the DNA polymerase beta deoxyribose phosphate excision reaction
    • Piersen C.E., Prasad R., Wilson S.H., Lloyd R.S. Evidence for an imino intermediate in the DNA polymerase beta deoxyribose phosphate excision reaction. J. Biol. Chem. 271:1996;17811-17815.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17811-17815
    • Piersen, C.E.1    Prasad, R.2    Wilson, S.H.3    Lloyd, R.S.4
  • 117
    • 0030018848 scopus 로고    scopus 로고
    • Specific interaction of DNA polymerase beta and DNA ligase I in a multiprotein base excision repair complex from bovine testis
    • Prasad R., Singhal R.K., Srivastava D.K., Molina J.T., Tomkinson A.E., Wilson S.H. Specific interaction of DNA polymerase beta and DNA ligase I in a multiprotein base excision repair complex from bovine testis. J. Biol. Chem. 271:1996;16000-16007.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16000-16007
    • Prasad, R.1    Singhal, R.K.2    Srivastava, D.K.3    Molina, J.T.4    Tomkinson, A.E.5    Wilson, S.H.6
  • 118
    • 0035980003 scopus 로고    scopus 로고
    • DNA polymerase beta-mediated long patch base excision repair. Poly(ADP- ribose)polymerase-1 stimulates strand displacement DNA synthesis
    • Prasad R., Lavrik O.I., Kim S.J., Kedar P., Yang X.P., Vande Berg B.J., Wilson S.H. DNA polymerase beta-mediated long patch base excision repair. Poly(ADP- ribose)polymerase-1 stimulates strand displacement DNA synthesis. J. Biol. Chem. 276:2001;32411-32414.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32411-32414
    • Prasad, R.1    Lavrik, O.I.2    Kim, S.J.3    Kedar, P.4    Yang, X.P.5    Vande Berg, B.J.6    Wilson, S.H.7
  • 119
    • 0035451746 scopus 로고    scopus 로고
    • The HAP1 protein stimulates the turnover of human mismatch-specific thymine-DNA-glycosylase to process 3,N(4)-ethenocytosine residues
    • Privezentzev C., Saparbaev M., Laval J. The HAP1 protein stimulates the turnover of human mismatch-specific thymine-DNA-glycosylase to process 3,N(4)-ethenocytosine residues. Mutat. Res. 480-481:2001;277.
    • (2001) Mutat. Res. , vol.480-481 , pp. 277
    • Privezentzev, C.1    Saparbaev, M.2    Laval, J.3
  • 120
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae
    • Radicella J., Dherin C., Desmaze C., Fox M.S.B. Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 94:1997;8010-8015.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8010-8015
    • Radicella, J.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.B.4
  • 121
    • 0036828697 scopus 로고    scopus 로고
    • AP endonuclease 1 coordinates flap endonuclease 1 and DNA ligase I activity in long patch base excision repair
    • Ranalli T., Tom S., Bambara R. AP endonuclease 1 coordinates flap endonuclease 1 and DNA ligase I activity in long patch base excision repair. J. Biol. Chem. 277:2002;41715-41724.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41715-41724
    • Ranalli, T.1    Tom, S.2    Bambara, R.3
  • 122
    • 0030745912 scopus 로고    scopus 로고
    • In vitro repair of oxidative DNA damage by human nucleotide excision repair system: Possible explanation for neurodegeneration in xeroderma pigmentosum patients
    • Reardon J.T., Bessho T., Kung H.C., Bolton P.H., Sancar A. In vitro repair of oxidative DNA damage by human nucleotide excision repair system: possible explanation for neurodegeneration in xeroderma pigmentosum patients. Proc. Natl. Acad. Sci. U.S.A. 94:1997;9463-9468.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 9463-9468
    • Reardon, J.T.1    Bessho, T.2    Kung, H.C.3    Bolton, P.H.4    Sancar, A.5
  • 123
    • 0034161514 scopus 로고    scopus 로고
    • Essential interaction between the fission yeast DNA polymerase d subunit Cdc27 and Pcn1 (PCNA) mediated through a C-terminal p21cip1-like PCNA binding motif
    • Reynolds N., Warbrick E., Fantes P.A., MacNeill S.A. Essential interaction between the fission yeast DNA polymerase d subunit Cdc27 and Pcn1 (PCNA) mediated through a C-terminal p21cip1-like PCNA binding motif. EMBO J. 19:2000;1108-1118.
    • (2000) EMBO J. , vol.19 , pp. 1108-1118
    • Reynolds, N.1    Warbrick, E.2    Fantes, P.A.3    MacNeill, S.A.4
  • 125
    • 0030738194 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase
    • Rosenquist T., Zharkov D., Grollman A. Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase. Proc. Natl. Acad. Sci. U.S.A. 94:1997;7429-7434.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7429-7434
    • Rosenquist, T.1    Zharkov, D.2    Grollman, A.3
  • 127
    • 0030958623 scopus 로고    scopus 로고
    • Characterization of endonuclease III (nth) and endonuclease VIII (nei) mutants of Escherichia coli K-12
    • Saito Y., Uraki F., Nakajima S., Asaeda A., Onom K., Kubo K., Yamamoto K. Characterization of endonuclease III (nth) and endonuclease VIII (nei) mutants of Escherichia coli K-12. J. Bacteriol. 179:1997;3783-3785.
    • (1997) J. Bacteriol. , vol.179 , pp. 3783-3785
    • Saito, Y.1    Uraki, F.2    Nakajima, S.3    Asaeda, A.4    Onom, K.5    Kubo, K.6    Yamamoto, K.7
  • 129
    • 0026507413 scopus 로고
    • Role of poly(ADP-ribose) formation in DNA repair
    • Satoh M.S., Lindahl T. Role of poly(ADP-ribose) formation in DNA repair. Nature. 356:1992;356-358.
    • (1992) Nature , vol.356 , pp. 356-358
    • Satoh, M.S.1    Lindahl, T.2
  • 130
    • 0042589136 scopus 로고    scopus 로고
    • Total sequence decomposition distinguishes functional modules, "molegos" in apurinic/apyrimidinic endonucleases
    • Schein C.H., Ozgun N., Izumi T., Braun W. Total sequence decomposition distinguishes functional modules, "molegos" in apurinic/apyrimidinic endonucleases. BMC Bioinformatics. 3:2002;37.
    • (2002) BMC Bioinformatics , vol.3 , pp. 37
    • Schein, C.H.1    Ozgun, N.2    Izumi, T.3    Braun, W.4
  • 131
    • 0027255962 scopus 로고
    • Complementation of the DNA repair defect in xeroderma pigmentosum group G cells by a human cDNA related to yeast RAD2
    • Scherly D., Nouspikel T., Corlet J., Ucla C., Bairoch A., Clarkson S. Complementation of the DNA repair defect in xeroderma pigmentosum group G cells by a human cDNA related to yeast RAD2. Nature. 363:1993;182-185.
    • (1993) Nature , vol.363 , pp. 182-185
    • Scherly, D.1    Nouspikel, T.2    Corlet, J.3    Ucla, C.4    Bairoch, A.5    Clarkson, S.6
  • 134
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani S., Takeshita M., Grollman A.P. insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature. 349:1991;431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 135
    • 0035915401 scopus 로고    scopus 로고
    • Disruption of Xpg increases spontaneous mutation frequency, particularly A:T to C:G transversion
    • Shiomi N., Hayashi E., Sasanuma S., Mita K., Shiomi T. Disruption of Xpg increases spontaneous mutation frequency, particularly A:T to C:G transversion. Mutat. Res. 487:2001;127-135.
    • (2001) Mutat. Res. , vol.487 , pp. 127-135
    • Shiomi, N.1    Hayashi, E.2    Sasanuma, S.3    Mita, K.4    Shiomi, T.5
  • 137
    • 0028966181 scopus 로고
    • DNA polymerase beta conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract
    • Singhal R.K., Prasad R., Wilson S.H. DNA polymerase beta conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract. J. Biol. Chem. 270:1995;949-957.
    • (1995) J. Biol. Chem. , vol.270 , pp. 949-957
    • Singhal, R.K.1    Prasad, R.2    Wilson, S.H.3
  • 138
    • 0032516831 scopus 로고    scopus 로고
    • Mammalian abasic site base excision repair. Identification of the reaction sequence and rate-determining steps
    • Srivastava D., Berg B., Prasad R., Molina J., Beard W., Tomkinson A., Wilson S. Mammalian abasic site base excision repair. Identification of the reaction sequence and rate-determining steps. J. Biol. Chem. 273:1998;21203-21209.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21203-21209
    • Srivastava, D.1    Berg, B.2    Prasad, R.3    Molina, J.4    Beard, W.5    Tomkinson, A.6    Wilson, S.7
  • 139
    • 0034254724 scopus 로고    scopus 로고
    • Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8
    • Sugahara M., Mikawa T., Kumasaka T., Yamamoto M., Kato R., Fukuyama K., Inoue Y., Kuramitsu S. Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8. EMBO J. 19:2000;3857-3869.
    • (2000) EMBO J. , vol.19 , pp. 3857-3869
    • Sugahara, M.1    Mikawa, T.2    Kumasaka, T.3    Yamamoto, M.4    Kato, R.5    Fukuyama, K.6    Inoue, Y.7    Kuramitsu, S.8
  • 140
    • 0033954867 scopus 로고    scopus 로고
    • BGP-15, a nicotinic amidoxime derivate protecting heart from ischemia reperfusion injury through modulation of poly(ADP-ribose) polymerase
    • Szabados E., Literati-Nagy P., Farkas B., Sumegi B. BGP-15, a nicotinic amidoxime derivate protecting heart from ischemia reperfusion injury through modulation of poly(ADP-ribose) polymerase. Biochem. Pharmacol. 59:2000;937-945.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 937-945
    • Szabados, E.1    Literati-Nagy, P.2    Farkas, B.3    Sumegi, B.4
  • 142
    • 0028933674 scopus 로고
    • Functional cooperation of MutT, MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotide in Escherichia coli
    • Tajiri T., Maki H., Sekiguchi M. Functional cooperation of MutT, MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotide in Escherichia coli. Mutat. Res. 336:1995;257-267.
    • (1995) Mutat. Res. , vol.336 , pp. 257-267
    • Tajiri, T.1    Maki, H.2    Sekiguchi, M.3
  • 143
    • 0032526616 scopus 로고    scopus 로고
    • Mitochondrial targeting of human DNA glycosylases for repair of oxidative DNA damage
    • Takao M., Aburatani H., Kobayashi K., Yasui A. Mitochondrial targeting of human DNA glycosylases for repair of oxidative DNA damage. Nucleic Acids Res. 26:1998;2917-2922.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2917-2922
    • Takao, M.1    Aburatani, H.2    Kobayashi, K.3    Yasui, A.4
  • 145
    • 0036829538 scopus 로고    scopus 로고
    • A back-up glycosylase in Nth1 knock-out mice is a functional Nei (endonuclease VIII) homologue
    • Takao M., Kanno S., Kobayashi K., Zhang Q., Yonei S., van der Horst G., Yasui A. A back-up glycosylase in Nth1 knock-out mice is a functional Nei (endonuclease VIII) homologue. J. Biol. Chem. 277:2002b;42205-42213.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42205-42213
    • Takao, M.1    Kanno, S.2    Kobayashi, K.3    Zhang, Q.4    Yonei, S.5    Van Der Horst, G.6    Yasui, A.7
  • 146
    • 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., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 14:1995;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
  • 147
    • 0033955346 scopus 로고    scopus 로고
    • XRCC1 keeps DNA from getting stranded
    • Thompson L.H., West M.G. XRCC1 keeps DNA from getting stranded. Mutat. Res. 459:2000;1-18.
    • (2000) Mutat. Res. , vol.459 , pp. 1-18
    • Thompson, L.H.1    West, M.G.2
  • 148
    • 0025202114 scopus 로고
    • Olecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange
    • Thompson L., Brookman K., Jones N., Allen S., Carrano A. Olecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange. Mol. Cell. Biol. 10:1990;6160-6171.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6160-6171
    • Thompson, L.1    Brookman, K.2    Jones, N.3    Allen, S.4    Carrano, A.5
  • 150
    • 0036184090 scopus 로고    scopus 로고
    • Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription
    • Tini M., Benecke A., Um S., Torchia J., Evans R., Chambon P. Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription. Mol. Cell. 9:2002;265-277.
    • (2002) Mol. Cell , vol.9 , pp. 265-277
    • Tini, M.1    Benecke, A.2    Um, S.3    Torchia, J.4    Evans, R.5    Chambon, P.6
  • 151
    • 0031972353 scopus 로고    scopus 로고
    • Structure and function of mammalian DNA ligases
    • Tomkinson A., Mackey Z. Structure and function of mammalian DNA ligases. Mutat. Res. 407:1998;1-9.
    • (1998) Mutat. Res. , vol.407 , pp. 1-9
    • Tomkinson, A.1    Mackey, Z.2
  • 152
    • 0035369734 scopus 로고    scopus 로고
    • Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen
    • Tsuchimoto D., Sakai Y., Sakumi K., Nishioka K., Sasaki M., Fujiwara T., Nakabeppu Y. Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen. Nucleic Acids Res. 29:2001;2349-2360.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2349-2360
    • Tsuchimoto, D.1    Sakai, Y.2    Sakumi, K.3    Nishioka, K.4    Sasaki, M.5    Fujiwara, T.6    Nakabeppu, Y.7
  • 153
    • 0034437623 scopus 로고    scopus 로고
    • Tsutakawa, S., Cooper, P., 2000. Transcription-coupled Repair of Oxidative DNA Damage in Human Cells: Mechanisms and Consequences, vol. 65. Cold Spring Harbor Laboratory Press, pp. 201-215.
    • Tsutakawa, S., Cooper, P., 2000. Transcription-coupled Repair of Oxidative DNA Damage in Human Cells: Mechanisms and Consequences, vol. 65. Cold Spring Harbor Laboratory Press, pp. 201-215.
  • 154
    • 0035890069 scopus 로고    scopus 로고
    • XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions
    • Vidal A.E., Boiteux S., Hickson I.D., Radicella J.P. XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions. EMBO J. 20:2001;6530-6539.
    • (2001) EMBO J. , vol.20 , pp. 6530-6539
    • Vidal, A.E.1    Boiteux, S.2    Hickson, I.D.3    Radicella, J.P.4
  • 155
    • 0033553505 scopus 로고    scopus 로고
    • Murine double minute (MDM2) blocks p53-coactivator interaction, a new mechanism for inhibition of p53-dependent gene expression
    • Wadgaonkar R., Collins T. Murine double minute (MDM2) blocks p53-coactivator interaction, a new mechanism for inhibition of p53-dependent gene expression. J. Biol. Chem. 274:1999;13760-13767.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13760-13767
    • Wadgaonkar, R.1    Collins, T.2
  • 157
    • 0032532543 scopus 로고    scopus 로고
    • BRCA1 binds c-Myc and inhibits its transcriptional and transforming activity in cells
    • Wang Q., Zhang H., Kajino K., Greene M. BRCA1 binds c-Myc and inhibits its transcriptional and transforming activity in cells. Oncogene. 17:1998;1939-1948.
    • (1998) Oncogene , vol.17 , pp. 1939-1948
    • Wang, Q.1    Zhang, H.2    Kajino, K.3    Greene, M.4
  • 158
    • 0034655991 scopus 로고    scopus 로고
    • BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures
    • Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J. BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. Genes Dev. 14:2000;927-939.
    • (2000) Genes Dev. , vol.14 , pp. 927-939
    • Wang, Y.1    Cortez, D.2    Yazdi, P.3    Neff, N.4    Elledge, S.J.5    Qin, J.6
  • 159
    • 0032951710 scopus 로고    scopus 로고
    • Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1
    • Waters T.R., Gallinari P., Jiricny J., Swann P.F. Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1. J. Biol. Chem. 274:1999;67-74.
    • (1999) J. Biol. Chem. , vol.274 , pp. 67-74
    • Waters, T.R.1    Gallinari, P.2    Jiricny, J.3    Swann, P.F.4
  • 160
    • 0034142268 scopus 로고    scopus 로고
    • Insights into the functions of BRCA1 and BRCA2
    • Welcsh P.L., Owens K.N., King M.C. Insights into the functions of BRCA1 and BRCA2. Trends Genet. 16:2000;69-74.
    • (2000) Trends Genet. , vol.16 , pp. 69-74
    • Welcsh, P.L.1    Owens, K.N.2    King, M.C.3
  • 161
    • 0035846899 scopus 로고    scopus 로고
    • XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair
    • Whitehouse C., Taylor R., Thistlethwaite A., Zhang H., Karimi-Busheri F., Lasko D., Weinfeld M., Caldecott K. XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair. Cell. 104:2001;107-117.
    • (2001) Cell , vol.104 , pp. 107-117
    • Whitehouse, C.1    Taylor, R.2    Thistlethwaite, A.3    Zhang, H.4    Karimi-Busheri, F.5    Lasko, D.6    Weinfeld, M.7    Caldecott, K.8
  • 162
    • 0032100860 scopus 로고    scopus 로고
    • Mammalian base excision repair and DNA polymerase beta
    • Wilson S.H. Mammalian base excision repair and DNA polymerase beta. Mutat. Res. 407:1998;203-215.
    • (1998) Mutat. Res. , vol.407 , pp. 203-215
    • Wilson, S.H.1
  • 163
    • 0034093291 scopus 로고    scopus 로고
    • Passing the baton in base excision repair
    • Wilson S.H., Kunkel T.A. Passing the baton in base excision repair. Nat. Struct. Biol. 7:2000;176-178.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 176-178
    • Wilson, S.H.1    Kunkel, T.A.2
  • 166
    • 0037415396 scopus 로고    scopus 로고
    • Action of human apurinic endonuclease (Ape1) on C1′-oxidized deoxyribose damage in DNA
    • Xu Y., DeMott M., Hwang J., Greenberg M., Demple B. Action of human apurinic endonuclease (Ape1) on C1′-oxidized deoxyribose damage in DNA. DNA Repair. 2:2003;175-185.
    • (2003) DNA Repair , vol.2 , pp. 175-185
    • Xu, Y.1    DeMott, M.2    Hwang, J.3    Greenberg, M.4    Demple, B.5
  • 167
    • 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., Miller J.H. 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. 29:2001;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
  • 168
    • 0033609057 scopus 로고    scopus 로고
    • BRCA1 interacts with components of the histone deacetylase complex
    • Yarden R., Brody L. BRCA1 interacts with components of the histone deacetylase complex. Proc. Natl. Acad. Sci. U.S.A. 96:1999;4983-4988.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4983-4988
    • Yarden, R.1    Brody, L.2
  • 170
    • 0034666313 scopus 로고    scopus 로고
    • Substrate specificity and reaction mechanism of murine 8-oxoguanine-DNA glycosylase
    • Zharkov D.O., Rosenquist T.A., Gerchman S.E., Grollman A.P. Substrate specificity and reaction mechanism of murine 8-oxoguanine-DNA glycosylase. J. Biol. Chem. 275:2000;28607-28617.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28607-28617
    • Zharkov, D.O.1    Rosenquist, T.A.2    Gerchman, S.E.3    Grollman, A.P.4
  • 172
    • 0035865399 scopus 로고    scopus 로고
    • A role for p53 in base excision repair
    • Zhou J., Ahn J., Wilson S., Prives C. A role for p53 in base excision repair. EMBO J. 20:2001;914-923.
    • (2001) EMBO J. , vol.20 , pp. 914-923
    • Zhou, J.1    Ahn, J.2    Wilson, S.3    Prives, C.4
  • 173
    • 0032926291 scopus 로고    scopus 로고
    • Blockade of Poly(ADP-ribose) synthetase inhibits neutrophil recruitment, oxidant generation, and mucosal injury in murine colitis
    • Zingarelli B., Szabo C., Salzman A.L. Blockade of Poly(ADP-ribose) synthetase inhibits neutrophil recruitment, oxidant generation, and mucosal injury in murine colitis. Gastroenterology. 116:1999;335-345.
    • (1999) Gastroenterology , vol.116 , pp. 335-345
    • Zingarelli, B.1    Szabo, C.2    Salzman, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.