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Volumn 685, Issue 1-2, 2010, Pages 80-89

Poly(ADP-ribose) polymerase 1 regulates activity of DNA polymerase β in long patch base excision repair

Author keywords

Base excision repair; DNA synthesis; Poly(ADP ribose) polymerase 1

Indexed keywords

DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA DIRECTED DNA POLYMERASE BETA; FLAP ENDONUCLEASE; FLAP ENDONUCLEASE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; UNCLASSIFIED DRUG;

EID: 75749125340     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2009.08.009     Document Type: Article
Times cited : (63)

References (60)
  • 1
    • 0034113805 scopus 로고    scopus 로고
    • Suppression of spontaneous mutagenesis in human cells by DNA base excision-repair
    • Lindahl T. Suppression of spontaneous mutagenesis in human cells by DNA base excision-repair. Mutat. Res. 462 (2000) 129-135
    • (2000) Mutat. Res. , vol.462 , pp. 129-135
    • Lindahl, T.1
  • 3
    • 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
  • 4
    • 0035837587 scopus 로고    scopus 로고
    • The major human abasic endonuclease: formation, consequences and repair of abasic lesions in DNA
    • Wilson III D.M., and Barsky D. The major human abasic endonuclease: formation, consequences and repair of abasic lesions in DNA. Mutat. Res. 485 (2001) 283-307
    • (2001) Mutat. Res. , vol.485 , pp. 283-307
    • Wilson III, D.M.1    Barsky, D.2
  • 5
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair
    • Matsumoto Y., and Kim K. Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair. Science 269 (1995) 699-702
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 8
    • 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., and 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
  • 9
    • 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., and 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
  • 10
    • 0033553510 scopus 로고    scopus 로고
    • Role of DNA polymerase β in the excision step of long patch mammalian base excision repair
    • Dianov G.L., Prasad R., Wilson S.H., and Bohr V.A. Role of DNA polymerase β in the excision step of long patch mammalian base excision repair. J. Biol. Chem. 274 (1999) 13741-13743
    • (1999) J. Biol. Chem. , vol.274 , pp. 13741-13743
    • Dianov, G.L.1    Prasad, R.2    Wilson, S.H.3    Bohr, V.A.4
  • 11
    • 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.S., McKenna A.E., Motycka T.A., Matsumoto Y., and Tomkinson A.E. Interaction between PCNA and DNA ligase I is critical for joining of Okazaki fragments and long patch base-excision repair. Curr. Biol. 15 (2000) 919-922
    • (2000) Curr. Biol. , vol.15 , pp. 919-922
    • Levin, D.S.1    McKenna, A.E.2    Motycka, T.A.3    Matsumoto, Y.4    Tomkinson, A.E.5
  • 12
    • 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
  • 13
    • 33644634986 scopus 로고    scopus 로고
    • Structure and mechanism of DNA polymerase β
    • Beard W.A., and Wilson S.H. Structure and mechanism of DNA polymerase β. Chem. Rev. 106 (2006) 361-382
    • (2006) Chem. Rev. , vol.106 , pp. 361-382
    • Beard, W.A.1    Wilson, S.H.2
  • 14
    • 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., and 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
  • 16
    • 34250379523 scopus 로고    scopus 로고
    • The checkpoint clamp, Rad9-Rad1-Hus1 complex, preferentially stimulates the activity of apurinic/apyrimidinic endonuclease 1 and DNA polymerase β in long patch base excision repair
    • Gembka A., Toueille M., Smirnova E., Poltz R., Ferrari E., Villani G., and Hübscher U. The checkpoint clamp, Rad9-Rad1-Hus1 complex, preferentially stimulates the activity of apurinic/apyrimidinic endonuclease 1 and DNA polymerase β in long patch base excision repair. Nucleic Acids Res. 35 (2007) 2596-2608
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2596-2608
    • Gembka, A.1    Toueille, M.2    Smirnova, E.3    Poltz, R.4    Ferrari, E.5    Villani, G.6    Hübscher, U.7
  • 17
    • 0034635403 scopus 로고    scopus 로고
    • FEN1 stimulation of DNA polymerase beta mediates an excision step in mammalian long patch base excision repair
    • Prasad R., Dianov G.L., Bohr V.A., and Wilson S.H. FEN1 stimulation of DNA polymerase beta mediates an excision step in mammalian long patch base excision repair. J. Biol. Chem. 275 (2000) 4460-4466
    • (2000) J. Biol. Chem. , vol.275 , pp. 4460-4466
    • Prasad, R.1    Dianov, G.L.2    Bohr, V.A.3    Wilson, S.H.4
  • 18
    • 13544261768 scopus 로고    scopus 로고
    • DNA polymerase beta and flap endonuclease 1 enzymatic specificities sustain DNA synthesis for long patch base excision repair
    • Liu Y., Beard W.A., Shock D.D., Prasad R., Hou E.W., and Wilson S.H. DNA polymerase beta and flap endonuclease 1 enzymatic specificities sustain DNA synthesis for long patch base excision repair. J. Biol. Chem. 280 (2005) 3665-3674
    • (2005) J. Biol. Chem. , vol.280 , pp. 3665-3674
    • Liu, Y.1    Beard, W.A.2    Shock, D.D.3    Prasad, R.4    Hou, E.W.5    Wilson, S.H.6
  • 19
    • 0035980003 scopus 로고    scopus 로고
    • DNA polymerase β-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 β-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
  • 20
    • 14844338678 scopus 로고    scopus 로고
    • Human base excision repair enzymes apurinic/apyrimidinic endonuclease1 (APE1), DNA polymerase β and poly(ADP-ribose) polymerase 1: Interplay between strand-displacement DNA synthesis and proofreading exonuclease activity
    • Sukhanova M.V., Khodyreva S.N., Lebedeva N.A., Prasad R., Wilson S.H., and Lavrik O.I. Human base excision repair enzymes apurinic/apyrimidinic endonuclease1 (APE1), DNA polymerase β and poly(ADP-ribose) polymerase 1: Interplay between strand-displacement DNA synthesis and proofreading exonuclease activity. Nucleic Acids Res. 33 (2005) 1222-1229
    • (2005) Nucleic Acids Res. , vol.33 , pp. 1222-1229
    • Sukhanova, M.V.1    Khodyreva, S.N.2    Lebedeva, N.A.3    Prasad, R.4    Wilson, S.H.5    Lavrik, O.I.6
  • 21
    • 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
  • 22
    • 34250349580 scopus 로고    scopus 로고
    • Coordination of steps in single-nucleotide base excision repair mediated by apurinic/apyrimidinic endonuclease 1 and DNA polymerase β
    • Liu Y., Prasad R., Beard W.A., Kedar P.S., Hou E.W., Shock D.D., and Wilson S.H. Coordination of steps in single-nucleotide base excision repair mediated by apurinic/apyrimidinic endonuclease 1 and DNA polymerase β. J. Biol. Chem. 282 (2007) 13532-13541
    • (2007) J. Biol. Chem. , vol.282 , pp. 13532-13541
    • Liu, Y.1    Prasad, R.2    Beard, W.A.3    Kedar, P.S.4    Hou, E.W.5    Shock, D.D.6    Wilson, S.H.7
  • 23
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes
    • Demple B., Herman T., and Chen D.S. Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 11450-11454
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 24
    • 0037034035 scopus 로고    scopus 로고
    • An exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3′ mispaired DNA
    • Chou K.M., and Cheng Y.C. An exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3′ mispaired DNA. Nature 415 (2002) 655-659
    • (2002) Nature , vol.415 , pp. 655-659
    • Chou, K.M.1    Cheng, Y.C.2
  • 25
    • 0037034306 scopus 로고    scopus 로고
    • An APE that proofreads
    • Jiricny J. An APE that proofreads. Nature 415 (2002) 593-594
    • (2002) Nature , vol.415 , pp. 593-594
    • Jiricny, J.1
  • 26
    • 15944381621 scopus 로고    scopus 로고
    • Protein-protein interactions and posttranslational modifications in mammalian base excision repair
    • Fan J., and Wilson III D.M. Protein-protein interactions and posttranslational modifications in mammalian base excision repair. Free Radic. Biol. Med. 38 (2005) 1121-1138
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1121-1138
    • Fan, J.1    Wilson III, D.M.2
  • 27
    • 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
  • 28
    • 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
  • 29
    • 0028865245 scopus 로고
    • Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks
    • Lindahl T., Satoh M.S., Poirier G.G., and Klungland A. Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks. Trends Biochem. Sci. 20 (1995) 405-411
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 405-411
    • Lindahl, T.1    Satoh, M.S.2    Poirier, G.G.3    Klungland, A.4
  • 30
    • 0000102949 scopus 로고
    • Poly(ADP-ribose) polymerase: a molecular nick sensor
    • de Murcia G., and de Murcia J.M. Poly(ADP-ribose) polymerase: a molecular nick sensor. Trends Biochem. Sci. 19 (1994) 172-176
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 172-176
    • de Murcia, G.1    de Murcia, J.M.2
  • 32
    • 44949253890 scopus 로고    scopus 로고
    • Poly ADP-ribose polymerase-1: an international molecule of mystery
    • Woodhouse B.C., and Dianov G.L. Poly ADP-ribose polymerase-1: an international molecule of mystery. DNA Repair 7 (2008) 1077-1086
    • (2008) DNA Repair , vol.7 , pp. 1077-1086
    • Woodhouse, B.C.1    Dianov, G.L.2
  • 33
    • 59349083787 scopus 로고    scopus 로고
    • Delocalization of nucleolar poly(ADP-ribose) polymerase-1 to the nucleoplasm and its novel link to cellular sensitivity to DNA damage
    • Rancourt A., and Satoh M.S. Delocalization of nucleolar poly(ADP-ribose) polymerase-1 to the nucleoplasm and its novel link to cellular sensitivity to DNA damage. DNA Repair 8 (2009) 286-297
    • (2009) DNA Repair , vol.8 , pp. 286-297
    • Rancourt, A.1    Satoh, M.S.2
  • 34
    • 10644246796 scopus 로고    scopus 로고
    • Monitoring base excision repair proteins on damaged DNA using human cell extracts
    • Parsons J.L., and Dianov G.L. Monitoring base excision repair proteins on damaged DNA using human cell extracts. Biochem. Soc. Trans. 32 (2004) 962-963
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 962-963
    • Parsons, J.L.1    Dianov, G.L.2
  • 35
    • 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., de Murcia J.M., 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    de Murcia, J.M.5    de Murcia, G.6
  • 36
    • 0029957245 scopus 로고    scopus 로고
    • XRCC1 polypeptide interacts with DNA polymerase β and possibly poly(ADP-ribose) polymerase, and DNA ligase III is novel molecular 'nick-sensor' in vitro
    • Caldecott K.W., Aoufouchi S., Johnson P., and Shall S. XRCC1 polypeptide interacts with DNA polymerase β and possibly poly(ADP-ribose) polymerase, and DNA ligase III is novel molecular 'nick-sensor' in vitro. Nucleic Acids Res. 24 (1996) 4387-4394
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4387-4394
    • Caldecott, K.W.1    Aoufouchi, S.2    Johnson, P.3    Shall, S.4
  • 37
    • 0035816708 scopus 로고    scopus 로고
    • Photoaffinity labeling of mouse fibroblast enzymes by a base excision repair intermediate
    • 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. 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
  • 38
    • 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 3 (2004) 581-591
    • (2004) DNA Repair , vol.3 , pp. 581-591
    • Cistulli, C.1    Lavrik, O.I.2    Prasad, R.3    Hou, E.4    Wilson, S.H.5
  • 39
    • 3042842128 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerise-1 inhibits strand-displacement DNA synthesis catalysed by DNA polymerase β
    • Sukhanova M.V., Khodyreva S.N., and Lavrik O.I. Poly(ADP-ribose) polymerise-1 inhibits strand-displacement DNA synthesis catalysed by DNA polymerase β. Biochemistry (Mosc.) 69 (2004) 558-568
    • (2004) Biochemistry (Mosc.) , vol.69 , pp. 558-568
    • Sukhanova, M.V.1    Khodyreva, S.N.2    Lavrik, O.I.3
  • 40
    • 85044705667 scopus 로고    scopus 로고
    • New photoreactive N(4)-substituted dCTP analogues:synthesis, photochemical characteristics, and substrate properties in HIV-1 reverse transcriptase catalyzed DNA synthesis
    • Safronov I.V., Shcherbik N.V., Khodyreva S.N., Vlasov V.A., Dobrikov M.I., Shishkin G.V., and Lavrik O.I. New photoreactive N(4)-substituted dCTP analogues:synthesis, photochemical characteristics, and substrate properties in HIV-1 reverse transcriptase catalyzed DNA synthesis. Bioorg. Khim. (Mosc.) 23 (1997) 576-585
    • (1997) Bioorg. Khim. (Mosc.) , vol.23 , pp. 576-585
    • Safronov, I.V.1    Shcherbik, N.V.2    Khodyreva, S.N.3    Vlasov, V.A.4    Dobrikov, M.I.5    Shishkin, G.V.6    Lavrik, O.I.7
  • 41
    • 0242366605 scopus 로고    scopus 로고
    • Interaction of flap endonuclease-1 and replication protein A with photoreactive intermediates of DNA repair
    • Nazarkina J.K., Petrousseva I.O., Safronov I.V., Lavrik O.I., and Khodyreva S.N. Interaction of flap endonuclease-1 and replication protein A with photoreactive intermediates of DNA repair. Biochemistry (Mosc.) 68 (2003) 934-942
    • (2003) Biochemistry (Mosc.) , vol.68 , pp. 934-942
    • Nazarkina, J.K.1    Petrousseva, I.O.2    Safronov, I.V.3    Lavrik, O.I.4    Khodyreva, S.N.5
  • 42
    • 0037228625 scopus 로고    scopus 로고
    • AP endonuclease 1 has no biologically significant 3′ → 5′ exonuclease activity
    • Lebedeva N.A., Khodyreva S.N., Favre A., and Lavrik O.I. AP endonuclease 1 has no biologically significant 3′ → 5′ exonuclease activity. Biochem. Biophys. Res. Commun. 300 (2003) 182-187
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 182-187
    • Lebedeva, N.A.1    Khodyreva, S.N.2    Favre, A.3    Lavrik, O.I.4
  • 43
    • 84937552571 scopus 로고    scopus 로고
    • Reagents for modification of protein-nucleic acids complexes. II. Site-specific photomodification of DNA-polymerase beta complexes with primers elongated by the dCTP exo-N-substituted arylazido derivatives
    • Drachkova I.A., Petruseva I.O., Safronov I.V., Zakharenko A.L., Shishkin G.V., Lavrik O.I., and Khodyreva S.N. Reagents for modification of protein-nucleic acids complexes. II. Site-specific photomodification of DNA-polymerase beta complexes with primers elongated by the dCTP exo-N-substituted arylazido derivatives. Bioorg. Khim. (Mosc.) 27 (2001) 197-204
    • (2001) Bioorg. Khim. (Mosc.) , vol.27 , pp. 197-204
    • Drachkova, I.A.1    Petruseva, I.O.2    Safronov, I.V.3    Zakharenko, A.L.4    Shishkin, G.V.5    Lavrik, O.I.6    Khodyreva, S.N.7
  • 44
    • 0030018848 scopus 로고    scopus 로고
    • Specific interaction of DNA polymerase β and DNA ligase I in multiprotein base excision repair complex from bovine testis
    • Prasad R., Singhal R.K., Srivastava R.K., Molina J.T., Tomkinson A.E., and Wilson S.H. Specific interaction of DNA polymerase β and DNA ligase I in 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, R.K.3    Molina, J.T.4    Tomkinson, A.E.5    Wilson, S.H.6
  • 46
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 47
  • 48
    • 0041386129 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase in base excision repair: always engaged, but not essential for DNA damage processing
    • Allinson S.L., Dianova I.I., and Dianov G.L. Poly(ADP-ribose) polymerase in base excision repair: always engaged, but not essential for DNA damage processing. Acta Biochim. Pol. 50 (2003) 169-179
    • (2003) Acta Biochim. Pol. , vol.50 , pp. 169-179
    • Allinson, S.L.1    Dianova, I.I.2    Dianov, G.L.3
  • 49
    • 0037125135 scopus 로고    scopus 로고
    • Down-regulation of DNA repair synthesis at DNA single-strand interruptions in poly (ADP-ribose) polymerase-1 deficient murine cell extracts
    • Sanderson R.J., and Lindahl T. Down-regulation of DNA repair synthesis at DNA single-strand interruptions in poly (ADP-ribose) polymerase-1 deficient murine cell extracts. DNA Repair 1 (2002) 547-558
    • (2002) DNA Repair , vol.1 , pp. 547-558
    • Sanderson, R.J.1    Lindahl, T.2
  • 50
    • 33746260470 scopus 로고    scopus 로고
    • Influence of poly(ADP-ribose) polymerase and its apoptotic 24-kDa fragment on repair of DNA duplexes in bovine testis nuclear extract
    • Sukhanova M.V., Khodyreva S.N., and Lavrik O.I. Influence of poly(ADP-ribose) polymerase and its apoptotic 24-kDa fragment on repair of DNA duplexes in bovine testis nuclear extract. Biochemistry (Mosc.) 71 (2006) 736-748
    • (2006) Biochemistry (Mosc.) , vol.71 , pp. 736-748
    • Sukhanova, M.V.1    Khodyreva, S.N.2    Lavrik, O.I.3
  • 52
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
    • Pleschke J.M., Kleczkowska H.E., Strohm M., and Althaus F.R. Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275 (2000) 40974-40980
    • (2000) J. Biol. Chem. , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 53
    • 0042632806 scopus 로고    scopus 로고
    • Physical and functional interaction between DNA ligase III alpha and poly(ADP-ribose) polymerase 1 in DNA single-strand break repair
    • Leppard J.B., Dong Z., Mackey Z.B., and Tomkinson A.E. Physical and functional interaction between DNA ligase III alpha and poly(ADP-ribose) polymerase 1 in DNA single-strand break repair. Mol. Cell. Biol. 23 (2003) 5919-5927
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5919-5927
    • Leppard, J.B.1    Dong, Z.2    Mackey, Z.B.3    Tomkinson, A.E.4
  • 54
    • 34047135111 scopus 로고    scopus 로고
    • Suppression of base excision repair reactions by apoptotic 24 kDa-fragment of poly(ADP-ribose) polymerase-1 in bovine testis nuclear extract
    • Sukhanova M., Khodyreva S., and Lavrik O. Suppression of base excision repair reactions by apoptotic 24 kDa-fragment of poly(ADP-ribose) polymerase-1 in bovine testis nuclear extract. DNA Repair 6 (2007) 615-625
    • (2007) DNA Repair , vol.6 , pp. 615-625
    • Sukhanova, M.1    Khodyreva, S.2    Lavrik, O.3
  • 56
    • 0034695632 scopus 로고    scopus 로고
    • Protection against methylation-induced cytotoxicity by DNA polymerase beta-dependent long patch base excision repair
    • Horton J.K., Prasad R., Hou E., and Wilson S.H. Protection against methylation-induced cytotoxicity by DNA polymerase beta-dependent long patch base excision repair. J. Biol. Chem. 275 (2000) 2211-2218
    • (2000) J. Biol. Chem. , vol.275 , pp. 2211-2218
    • Horton, J.K.1    Prasad, R.2    Hou, E.3    Wilson, S.H.4
  • 57
    • 0034659935 scopus 로고    scopus 로고
    • The lyase activity of the DNA repair protein beta-polymerase protects from DNA-damage-induced cytotoxicity
    • Sobol R.W., Prasad R., Evenski A., Baker A., Yang X.P., Horton J.K., and Wilson S.H. The lyase activity of the DNA repair protein beta-polymerase protects from DNA-damage-induced cytotoxicity. Nature 405 (2000) 807-810
    • (2000) Nature , vol.405 , pp. 807-810
    • Sobol, R.W.1    Prasad, R.2    Evenski, A.3    Baker, A.4    Yang, X.P.5    Horton, J.K.6    Wilson, S.H.7
  • 58
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • Hegde M.L., Hazra T.K., and Mitra S. Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells. Cell Res. 18 (2008) 27-47
    • (2008) Cell Res. , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 59
    • 62349120246 scopus 로고    scopus 로고
    • DNA repair in mammalian cells: Base excision repair: the long and short of it
    • Robertson A.B., Klungland A., Rognes T., and Leiros I. DNA repair in mammalian cells: Base excision repair: the long and short of it. Cell. Mol. Life Sci. 66 (2009) 981-993
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 981-993
    • Robertson, A.B.1    Klungland, A.2    Rognes, T.3    Leiros, I.4
  • 60
    • 41849092328 scopus 로고    scopus 로고
    • DNA tandem lesion repair by strand displacement synthesis and nucleotide excision repair
    • Imoto S., Bransfield L.A., Croteau D.L., Van Houten B., and Greenberg M.M. DNA tandem lesion repair by strand displacement synthesis and nucleotide excision repair. Biochemistry 47 (2008) 4306-4316
    • (2008) Biochemistry , vol.47 , pp. 4306-4316
    • Imoto, S.1    Bransfield, L.A.2    Croteau, D.L.3    Van Houten, B.4    Greenberg, M.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.