메뉴 건너뛰기




Volumn 224, Issue 1-2, 2006, Pages 44-55

The human apurinic/apyrimidinic endonuclease-1 suppresses activation of poly(adp-ribose) polymerase-1 induced by DNA single strand breaks

Author keywords

AP endonuclease; DNA base excision repair; Necrosis; Oxidative stress; PARP1

Indexed keywords

ARGININE; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE 1; HYDROGEN PEROXIDE; MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 33745198464     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tox.2006.04.025     Document Type: Article
Times cited : (29)

References (80)
  • 2
    • 0029010778 scopus 로고
    • Site-directed mutagenesis of the human DNA repair enzyme HAP1: identification of residues important for AP endonuclease and RNase H activity
    • Barzilay G., Walker L.J., Robson C.N., and Hickson I.D. Site-directed mutagenesis of the human DNA repair enzyme HAP1: identification of residues important for AP endonuclease and RNase H activity. Nucleic Acids Res. 23 (1995) 1544-1550
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1544-1550
    • Barzilay, G.1    Walker, L.J.2    Robson, C.N.3    Hickson, I.D.4
  • 3
    • 0030839865 scopus 로고    scopus 로고
    • Oxidative decay of DNA
    • Beckman K.B., and 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
  • 4
    • 0032980426 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae ETH1 gene, an inducible homolog of exonuclease III that provides resistance to DNA-damaging agents and limits spontaneous mutagenesis
    • Bennett R.A. The Saccharomyces cerevisiae ETH1 gene, an inducible homolog of exonuclease III that provides resistance to DNA-damaging agents and limits spontaneous mutagenesis. Mol. Cell. Biol. 19 (1999) 1800-1809
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1800-1809
    • Bennett, R.A.1
  • 5
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway
    • Bennett R.A., Wilson III D.M., Wong D., and 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 III, D.M.2    Wong, D.3    Demple, B.4
  • 6
    • 0028927261 scopus 로고
    • Reactions of oxyl radicals with DNA
    • Breen A.P., and Murphy J.A. Reactions of oxyl radicals with DNA. Free Rad. Biol. Med. 18 (1995) 1033-1077
    • (1995) Free Rad. Biol. Med. , vol.18 , pp. 1033-1077
    • Breen, A.P.1    Murphy, J.A.2
  • 7
    • 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., and 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
  • 8
    • 2342507720 scopus 로고    scopus 로고
    • AP endonuclease and poly(ADP-ribose) polymerase-1 interact with the same base excision repair intermediate
    • Cistulli C., Lavrik O.I., Prasad R., Hou E., and Wilson S.H. AP endonuclease and poly(ADP-ribose) polymerase-1 interact with the same base excision repair intermediate. DNA Repair (Amst) 3 (2004) 581-591
    • (2004) DNA Repair (Amst) , vol.3 , pp. 581-591
    • Cistulli, C.1    Lavrik, O.I.2    Prasad, R.3    Hou, E.4    Wilson, S.H.5
  • 9
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours D., Desnoyers S., D'Silva I., and Poirier G.G. Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 342 (1999) 249-268
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 12
    • 0026709243 scopus 로고
    • Free-radical mechanisms involved in the formation of sequence-dependent bistranded DNA lesions by the antitumor antibiotics bleomycin, neocarzinostatin, and calicheamicin
    • Dedon P.C., and Goldberg I.H. Free-radical mechanisms involved in the formation of sequence-dependent bistranded DNA lesions by the antitumor antibiotics bleomycin, neocarzinostatin, and calicheamicin. Chem. Res. Toxicol. 5 (1992) 311-332
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 311-332
    • Dedon, P.C.1    Goldberg, I.H.2
  • 13
    • 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 II, Bohr V.A., and 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 II1    Bohr, V.A.2    Dianov, G.L.3
  • 14
    • 0347379928 scopus 로고    scopus 로고
    • Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2
    • Dou H., Mitra S., and Hazra T.K. Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2. J. Biol. Chem. 278 (2003) 49679-49684
    • (2003) J. Biol. Chem. , vol.278 , pp. 49679-49684
    • Dou, H.1    Mitra, S.2    Hazra, T.K.3
  • 18
    • 0242299711 scopus 로고    scopus 로고
    • APE/Ref-1 and the mammalian response to genotoxic stress
    • Fritz G., Grosch S., Tomicic M., and Kaina B. APE/Ref-1 and the mammalian response to genotoxic stress. Toxicology 193 (2003) 67-78
    • (2003) Toxicology , vol.193 , pp. 67-78
    • Fritz, G.1    Grosch, S.2    Tomicic, M.3    Kaina, B.4
  • 19
    • 0033611583 scopus 로고    scopus 로고
    • Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1
    • Fritz G., and Kaina B. Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1. Oncogene 18 (1999) 1033-1040
    • (1999) Oncogene , vol.18 , pp. 1033-1040
    • Fritz, G.1    Kaina, B.2
  • 20
    • 13244299159 scopus 로고    scopus 로고
    • A vital role for ape1/ref1 protein in repairing spontaneous DNA damage in human cells
    • Fung H., and Demple B. A vital role for ape1/ref1 protein in repairing spontaneous DNA damage in human cells. Mol. Cell. 17 (2005) 463-470
    • (2005) Mol. Cell. , vol.17 , pp. 463-470
    • Fung, H.1    Demple, B.2
  • 21
    • 1242320312 scopus 로고    scopus 로고
    • The major human AP endonuclease (Ape1) is involved in the nucleotide incision repair pathway
    • Gros L., AA I., Ide H., Elder R., and Saparbaev M. The major human AP endonuclease (Ape1) is involved in the nucleotide incision repair pathway. Nucleic Acids Res. 32 (2004) 1-9
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1-9
    • Gros, L.1    AA, I.2    Ide, H.3    Elder, R.4    Saparbaev, M.5
  • 22
    • 0033598713 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion
    • Ha H.C., and 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
  • 25
    • 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.K., Izumi T., Kow Y.W., and 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.K.1    Izumi, T.2    Kow, Y.W.3    Mitra, S.4
  • 26
    • 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., and 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
  • 27
    • 0021111515 scopus 로고
    • gamma Ray induced deoxyribonucleic acid strand breaks. 3′-Glycolate termini
    • Henner W., Rodriguez L., Hech S., and 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
  • 28
    • 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., and 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
  • 29
    • 0037049975 scopus 로고    scopus 로고
    • Alternative nucleotide incision repair pathway for oxidative DNA damage
    • Ischenko A.A., and Saparbaev M.K. Alternative nucleotide incision repair pathway for oxidative DNA damage. Nature 415 (2002) 183-187
    • (2002) Nature , vol.415 , pp. 183-187
    • Ischenko, A.A.1    Saparbaev, M.K.2
  • 31
    • 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., and 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
  • 32
    • 0030478864 scopus 로고    scopus 로고
    • Negative regulation of the major human AP-endonuclease, a multifunctional protein
    • Izumi T., Henner W.D., and Mitra S. Negative regulation of the major human AP-endonuclease, a multifunctional protein. Biochemistry 35 (1996) 14679-14683
    • (1996) Biochemistry , vol.35 , pp. 14679-14683
    • Izumi, T.1    Henner, W.D.2    Mitra, S.3
  • 33
    • 0033583089 scopus 로고    scopus 로고
    • Intragenic suppression of an active site mutation in the human apurinic/apyrimidinic endonuclease
    • Izumi T., Malecki J., Chaudhry M.A., Weinfeld M., Hill J.H., Lee J.C., and Mitra S. Intragenic suppression of an active site mutation in the human apurinic/apyrimidinic endonuclease. J. Mol. Biol. 287 (1999) 47-57
    • (1999) J. Mol. Biol. , vol.287 , pp. 47-57
    • Izumi, T.1    Malecki, J.2    Chaudhry, M.A.3    Weinfeld, M.4    Hill, J.H.5    Lee, J.C.6    Mitra, S.7
  • 34
    • 1642494900 scopus 로고    scopus 로고
    • Effects of backbone contacts 3′ to the abasic site on the cleavage and the product binding by human apurinic/apyrimidinic endonuclease (APE1)
    • Izumi T., Schein C.H., Oezguen N., Feng Y., and Braun W. Effects of backbone contacts 3′ to the abasic site on the cleavage and the product binding by human apurinic/apyrimidinic endonuclease (APE1). Biochemistry 43 (2004) 684-689
    • (2004) Biochemistry , vol.43 , pp. 684-689
    • Izumi, T.1    Schein, C.H.2    Oezguen, N.3    Feng, Y.4    Braun, W.5
  • 35
    • 0242268065 scopus 로고    scopus 로고
    • Mammalian DNA base excision repair proteins: their interactions and role in repair of oxidative DNA damage
    • Izumi T., Wiederhold L.R., Roy G., Roy R., Jaiswal A., Bhakat K.K., Mitra S., and Hazra T.K. Mammalian DNA base excision repair proteins: their interactions and role in repair of oxidative DNA damage. Toxicology 193 (2003) 43-65
    • (2003) Toxicology , vol.193 , pp. 43-65
    • Izumi, T.1    Wiederhold, L.R.2    Roy, G.3    Roy, R.4    Jaiswal, A.5    Bhakat, K.K.6    Mitra, S.7    Hazra, T.K.8
  • 36
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan H.E., Standal R., and 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
  • 37
    • 0036464533 scopus 로고    scopus 로고
    • Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter
    • Kuninger D., Izumi T., Papaconstantinou J., and Mitra S. Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter. Nucleic Acids Res. 30 (2002) 823-829
    • (2002) Nucleic Acids Res. , vol.30 , pp. 823-829
    • Kuninger, D.1    Izumi, T.2    Papaconstantinou, J.3    Mitra, S.4
  • 38
    • 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., and 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
  • 39
    • 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., and 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
  • 40
    • 0033621353 scopus 로고    scopus 로고
    • The RAD2 domain of human exonuclease 1 exhibits 5′ to 3′ exonuclease and flap structure-specific endonuclease activities
    • Lee B.I., and Wilson III D.M. The RAD2 domain of human exonuclease 1 exhibits 5′ to 3′ exonuclease and flap structure-specific endonuclease activities. J. Biol. Chem. 274 (1999) 37763-37769
    • (1999) J. Biol. Chem. , vol.274 , pp. 37763-37769
    • Lee, B.I.1    Wilson III, D.M.2
  • 41
    • 0018620965 scopus 로고
    • DNA glycosylases, endonucleases for apurinic/apyrimidinic sites, and base excision-repair
    • Lindahl T. DNA glycosylases, endonucleases for apurinic/apyrimidinic sites, and base excision-repair. Prog. Nucleic. Acid Res. Mol. Biol. 22 (1979) 135-192
    • (1979) Prog. Nucleic. Acid Res. Mol. Biol. , vol.22 , pp. 135-192
    • Lindahl, T.1
  • 42
    • 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
  • 44
    • 0020645075 scopus 로고
    • In vitro transcription: whole-cell extract
    • Manley J.L., Fire A., Samuels M., and Sharp P.A. In vitro transcription: whole-cell extract. Meth. Enz. 101 (1983) 568-582
    • (1983) Meth. Enz. , vol.101 , pp. 568-582
    • Manley, J.L.1    Fire, A.2    Samuels, M.3    Sharp, P.A.4
  • 46
    • 0031844311 scopus 로고    scopus 로고
    • XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
    • Masson M., Niedergang C., Schreiber V., Muller S., Menissier-de Murcia J., and de Murcia G. XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol. Cell. Biol. 18 (1998) 3563-3571
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3563-3571
    • Masson, M.1    Niedergang, C.2    Schreiber, V.3    Muller, S.4    Menissier-de Murcia, J.5    de Murcia, G.6
  • 47
    • 0032515067 scopus 로고    scopus 로고
    • Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium
    • Masuda Y., Bennett R.A., and Demple B. Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium. J. Biol. Chem. 273 (1998) 30360-30365
    • (1998) J. Biol. Chem. , vol.273 , pp. 30360-30365
    • Masuda, Y.1    Bennett, R.A.2    Demple, B.3
  • 51
    • 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., and 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 (2000) 211-229
    • (2000) Mutat. Res. , vol.460 , pp. 211-229
    • Mol, C.D.1    Hosfield, D.J.2    Tainer, J.A.3
  • 52
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination
    • Mol C.D., Izumi T., Mitra S., and Tainer J.A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination. Nature 403 (2000) 451-456
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 53
    • 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., and 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
  • 54
    • 0021832063 scopus 로고
    • Changes of DNA repair mechanisms during the aging of the rat
    • Niedermuller H., Hofecker G., and Skalicky M. Changes of DNA repair mechanisms during the aging of the rat. Mech. Age. Dev. 29 (1985) 221-238
    • (1985) Mech. Age. Dev. , vol.29 , pp. 221-238
    • Niedermuller, H.1    Hofecker, G.2    Skalicky, M.3
  • 56
    • 0032567807 scopus 로고    scopus 로고
    • Mutant AP endonuclease in patients with amyotrophic lateral sclerosis
    • Olkowski Z.L. Mutant AP endonuclease in patients with amyotrophic lateral sclerosis. Neuroreport 9 (1998) 239-242
    • (1998) Neuroreport , vol.9 , pp. 239-242
    • Olkowski, Z.L.1
  • 57
    • 3142770341 scopus 로고    scopus 로고
    • APE1 is the major 3′-phosphoglycolate activity in human cell extracts
    • Parsons J.L., Dianova II, and Dianov G.L. APE1 is the major 3′-phosphoglycolate activity in human cell extracts. Nucleic Acids Res. 32 (2004) 3531-3536
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3531-3536
    • Parsons, J.L.1    Dianova II2    Dianov, G.L.3
  • 60
    • 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., and 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
  • 61
    • 0032512439 scopus 로고    scopus 로고
    • Specific Interaction of wild type and truncated mouse N-methylpurine-DNA glycosylase with ethenoadenine-containing DNA
    • Roy R., Biswas T., Hazra T.K., Roy G., Grabowski D.T., Izumi T., Srinivasan G., and Mitra S. Specific Interaction of wild type and truncated mouse N-methylpurine-DNA glycosylase with ethenoadenine-containing DNA. Biochemistry 37 (1998) 580-589
    • (1998) Biochemistry , vol.37 , pp. 580-589
    • Roy, R.1    Biswas, T.2    Hazra, T.K.3    Roy, G.4    Grabowski, D.T.5    Izumi, T.6    Srinivasan, G.7    Mitra, S.8
  • 62
    • 0026507413 scopus 로고
    • Role of poly(ADP-ribose) formation in DNA repair
    • Satoh M.S., and 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
  • 63
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells
    • Schreiber E., Matthias P., Muller M.M., and Schaffner W. Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells. Nucleic Acids Res. 17 (1989) 6419
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 65
    • 0034608478 scopus 로고    scopus 로고
    • Screening of AP endonuclease as a candidate gene for amyotrophic lateral sclerosis (ALS)
    • Tomkins J., Dempster S., Banner S.J., Cookson M.R., and Shaw P.J. Screening of AP endonuclease as a candidate gene for amyotrophic lateral sclerosis (ALS). Neuroreport 11 (2000) 1695-1697
    • (2000) Neuroreport , vol.11 , pp. 1695-1697
    • Tomkins, J.1    Dempster, S.2    Banner, S.J.3    Cookson, M.R.4    Shaw, P.J.5
  • 66
    • 0031972353 scopus 로고    scopus 로고
    • Structure and function of mammalian DNA ligases
    • Tomkinson A., and 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
  • 67
    • 0034437623 scopus 로고    scopus 로고
    • Tsutakawa, S., Cooper, P., 2000. Transcriptioncoupled repair of oxidative dna damage in human cells: mechanisms and consequences. Cold Spring Harbor Laboratory Press, p. 201.
  • 68
    • 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., and 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
  • 69
    • 0028922462 scopus 로고
    • Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease
    • Wang Z.Q., Auer B., Stingl L., Berghammer H., Haidacher D., Schweiger M., and Wagner E.F. Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease. Genes Dev. 9 (1995) 509-520
    • (1995) Genes Dev. , vol.9 , pp. 509-520
    • Wang, Z.Q.1    Auer, B.2    Stingl, L.3    Berghammer, H.4    Haidacher, D.5    Schweiger, M.6    Wagner, E.F.7
  • 71
    • 0027973491 scopus 로고
    • The complexity of DNA damage: relevance to biological consequences
    • Ward J.F. The complexity of DNA damage: relevance to biological consequences. Int. J. Rad. Biol. 66 (1994) 427-432
    • (1994) Int. J. Rad. Biol. , vol.66 , pp. 427-432
    • Ward, J.F.1
  • 72
    • 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., and 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
  • 74
    • 0030839750 scopus 로고    scopus 로고
    • Abasic site binding by the human apurinic endonuclease, Ape, and determination of the DNA contact sites
    • Wilson III D.M., Takeshita M., and Demple B. Abasic site binding by the human apurinic endonuclease, Ape, and determination of the DNA contact sites. Nucleic Acids Res. 25 (1997) 933-939
    • (1997) Nucleic Acids Res. , vol.25 , pp. 933-939
    • Wilson III, D.M.1    Takeshita, M.2    Demple, B.3
  • 75
    • 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
  • 76
    • 0034093291 scopus 로고    scopus 로고
    • Passing the baton in base excision repair
    • Wilson S.H., and 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
  • 77
    • 0029829265 scopus 로고    scopus 로고
    • The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice
    • Xanthoudakis S., Smeyne R.J., Wallace J.D., and Curran T. The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 8919-8923
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8919-8923
    • Xanthoudakis, S.1    Smeyne, R.J.2    Wallace, J.D.3    Curran, T.4
  • 78
    • 0035253515 scopus 로고    scopus 로고
    • Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatch
    • Yang H., Clendenin W.M., Wong D., Demple B., Slupska M.M., Chiang J.-H., and Miller J.H. 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
  • 79
    • 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., and 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
  • 80
    • 2642536197 scopus 로고    scopus 로고
    • Alkylating DNA damage stimulates a regulated form of necrotic cell death
    • Zong W.X., Ditsworth D., Bauer D.E., Wang Z.Q., and Thompson C.B. Alkylating DNA damage stimulates a regulated form of necrotic cell death. Genes Dev. 18 (2004) 1272-1282
    • (2004) Genes Dev. , vol.18 , pp. 1272-1282
    • Zong, W.X.1    Ditsworth, D.2    Bauer, D.E.3    Wang, Z.Q.4    Thompson, C.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.