메뉴 건너뛰기




Volumn 6, Issue 4, 2007, Pages 454-460

Co-ordination of DNA single strand break repair

Author keywords

Base excision repair; DNA repair enzymes; Single strand break

Indexed keywords

DNA BASE; PHOSPHATE; REACTIVE OXYGEN METABOLITE; SINGLE STRANDED DNA;

EID: 33847630719     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2006.10.009     Document Type: Article
Times cited : (89)

References (75)
  • 1
    • 0034192265 scopus 로고    scopus 로고
    • The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis
    • Boiteux S., and Radicella J.P. The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis. Arch. Biochem. Biophys. 377 (2000) 1-8
    • (2000) Arch. Biochem. Biophys. , vol.377 , pp. 1-8
    • Boiteux, S.1    Radicella, J.P.2
  • 4
    • 0037115910 scopus 로고    scopus 로고
    • Dynamics and diversions in base excision DNA repair of oxidized abasic lesions
    • Demple B., and DeMott M.S. Dynamics and diversions in base excision DNA repair of oxidized abasic lesions. Oncogene 21 (2002) 8926-8934
    • (2002) Oncogene , vol.21 , pp. 8926-8934
    • Demple, B.1    DeMott, M.S.2
  • 5
    • 0012762626 scopus 로고    scopus 로고
    • Milligan Four mechanisms for the production of complex damage
    • Ward J.F., and Milligan J.R. Milligan Four mechanisms for the production of complex damage. Radiat. Res. 148 (1997) 481-522
    • (1997) Radiat. Res. , vol.148 , pp. 481-522
    • Ward, J.F.1    Milligan, J.R.2
  • 6
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature 362 (1993) 709-715
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 7
    • 0034620584 scopus 로고    scopus 로고
    • 8-OxodGTP incorporation by DNA polymerase beta is modified by active site residue Asn279
    • Miller H., Prasad R., Wilson S.H., Johnson F., and Grollman A.P. 8-OxodGTP incorporation by DNA polymerase beta is modified by active site residue Asn279. Biochemistry 39 (2000) 1029-1033
    • (2000) Biochemistry , vol.39 , pp. 1029-1033
    • Miller, H.1    Prasad, R.2    Wilson, S.H.3    Johnson, F.4    Grollman, A.P.5
  • 8
    • 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
  • 9
    • 22744457037 scopus 로고    scopus 로고
    • Human DNA topoisomerase I: relaxation, roles, and damage control
    • Leppard J.B., and Champoux J.J. Human DNA topoisomerase I: relaxation, roles, and damage control. Chromosoma 114 (2005) 75-85
    • (2005) Chromosoma , vol.114 , pp. 75-85
    • Leppard, J.B.1    Champoux, J.J.2
  • 10
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA epair 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 epair 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
  • 11
    • 0025936119 scopus 로고
    • Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants
    • Robson C.N., and Hickson I.D. Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants. Nucleic Acids Res. 19 (1991) 5519-5523
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5519-5523
    • Robson, C.N.1    Hickson, I.D.2
  • 14
    • 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. U.S.A. 93 (1996) 8919-8923
    • (1996) Proc. Natl. Acad. U.S.A. , vol.93 , pp. 8919-8923
    • Xanthoudakis, S.1    Smeyne, R.J.2    Wallace, J.D.3    Curran, T.4
  • 15
    • 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
  • 17
    • 0035837587 scopus 로고    scopus 로고
    • The major human abasic endonuclease: formation, consequences and repair of abasic lesions in DNA
    • Wilson 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, D.M.1    Barsky, D.2
  • 18
    • 0026004662 scopus 로고
    • Two distinct human diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidised DNA
    • Chen D.S., Herman V.G., and Demple B. Two distinct human diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidised DNA. Nucleic Acids Res. 19 (1991) 5907-5914
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5907-5914
    • Chen, D.S.1    Herman, V.G.2    Demple, B.3
  • 19
    • 0033105112 scopus 로고    scopus 로고
    • Removal by human apurinic/apyrimidinic endonuclease 1 (Ape 1) and Escherichia coli exonuclease III of 3′-phosphoglycolates from DNA treated with neocarzinostatin, calicheamicin, and gamma-radiation
    • Chaudhry M.A., Dedon P.C., Wilson D.M., Demple B., and Weinfeld M. Removal by human apurinic/apyrimidinic endonuclease 1 (Ape 1) and Escherichia coli exonuclease III of 3′-phosphoglycolates from DNA treated with neocarzinostatin, calicheamicin, and gamma-radiation. Biochem. Pharmacol. 57 (1999) 531-538
    • (1999) Biochem. Pharmacol. , vol.57 , pp. 531-538
    • Chaudhry, M.A.1    Dedon, P.C.2    Wilson, D.M.3    Demple, B.4    Weinfeld, M.5
  • 20
    • 0038690166 scopus 로고    scopus 로고
    • Properties of and substrate determinants for the exonuclease activity of human apurinic endonuclease Ape1
    • Wilson D.M. Properties of and substrate determinants for the exonuclease activity of human apurinic endonuclease Ape1. J. Mol. Biol. 330 (2003) 1027-1037
    • (2003) J. Mol. Biol. , vol.330 , pp. 1027-1037
    • Wilson, D.M.1
  • 21
    • 0019876798 scopus 로고
    • Purification and characterization of an apurinic/apyrimidinic endonuclease from HeLa cells
    • Kane C.M., and Linn S. Purification and characterization of an apurinic/apyrimidinic endonuclease from HeLa cells. J. Biol. Chem. 256 (1981) 3405-3414
    • (1981) J. Biol. Chem. , vol.256 , pp. 3405-3414
    • Kane, C.M.1    Linn, S.2
  • 22
    • 14444274333 scopus 로고    scopus 로고
    • Excision of C-4′-oxidized deoxyribose lesions from double-stranded DNA by human apurinic/apyrimidinic endonuclease (Ape1 protein) and DNA polymerase beta
    • Xu Y.J., Kim E.Y., and Demple B. Excision of C-4′-oxidized deoxyribose lesions from double-stranded DNA by human apurinic/apyrimidinic endonuclease (Ape1 protein) and DNA polymerase beta. J. Biol. Chem. 273 (1998) 28837-28844
    • (1998) J. Biol. Chem. , vol.273 , pp. 28837-28844
    • Xu, Y.J.1    Kim, E.Y.2    Demple, B.3
  • 23
    • 0028245076 scopus 로고
    • Removal of 3′-phosphoglycolate from DNA strand-break damage in an oligonucleotide substrate by recombinant human apurinic/apyrimidinic endonuclease 1
    • Winters T.A., Henner W.D., Russell P.S., McCullough A., and Jorgensen T.J. Removal of 3′-phosphoglycolate from DNA strand-break damage in an oligonucleotide substrate by recombinant human apurinic/apyrimidinic endonuclease 1. Nucleic Acids Res. 22 (1994) 1866-1873
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1866-1873
    • Winters, T.A.1    Henner, W.D.2    Russell, P.S.3    McCullough, A.4    Jorgensen, T.J.5
  • 24
    • 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
  • 25
    • 0030788621 scopus 로고    scopus 로고
    • 3′-phosphodiesterase activity of human apurinic/apyrimidinic endonuclease at DNA double-strand break ends
    • Suh D., Wilson III D.M., and Povirk L.F. 3′-phosphodiesterase activity of human apurinic/apyrimidinic endonuclease at DNA double-strand break ends. Nucleic Acids Res. 25 (1997) 2495-2500
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2495-2500
    • Suh, D.1    Wilson III, D.M.2    Povirk, L.F.3
  • 26
    • 3142770341 scopus 로고    scopus 로고
    • APE1 is the major 3′- phosphoglycolate activity in human cell extracts
    • Parsons J.L., Dianova I.I., 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, I.I.2    Dianov, G.L.3
  • 28
    • 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
  • 29
    • 17844365289 scopus 로고    scopus 로고
    • APE1-dependent repair of DNA single-strand breaks containing 3′-end 8-oxoguanine
    • Parsons J.L., Dianova I.I., and Dianov G.L. APE1-dependent repair of DNA single-strand breaks containing 3′-end 8-oxoguanine. Nucleic Acids Res. 33 (2005) 2204-2209
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2204-2209
    • Parsons, J.L.1    Dianova, I.I.2    Dianov, G.L.3
  • 30
    • 0033588161 scopus 로고    scopus 로고
    • Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3′-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage
    • Jilani A., Ramotar D., Slack C., Ong C., Yang X.M., Scherer S.W., and Lasko D.D. Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3′-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage. J. Biol. Chem. 274 (1999) 24176-24186
    • (1999) J. Biol. Chem. , vol.274 , pp. 24176-24186
    • Jilani, A.1    Ramotar, D.2    Slack, C.3    Ong, C.4    Yang, X.M.5    Scherer, S.W.6    Lasko, D.D.7
  • 33
    • 28044453306 scopus 로고    scopus 로고
    • End-damage-specific proteins facilitate recruitment or stability of X-ray cross-complementing protein 1 at the sites of DNA single-strand break repair
    • Parsons J.L., Dianova I.I., Boswell E., Weinfeld M., and Dianov G.L. End-damage-specific proteins facilitate recruitment or stability of X-ray cross-complementing protein 1 at the sites of DNA single-strand break repair. FEBS J. 272 (2005) 5753-5763
    • (2005) FEBS J. , vol.272 , pp. 5753-5763
    • Parsons, J.L.1    Dianova, I.I.2    Boswell, E.3    Weinfeld, M.4    Dianov, G.L.5
  • 34
    • 2342541592 scopus 로고    scopus 로고
    • Stable downregulation of human polynucleotide kinase enhances spontaneous mutation frequency and sensitizes cells to genotoxic agents
    • Rasouli-Nia A., Karimi-Busheri F., and Weinfeld M. Stable downregulation of human polynucleotide kinase enhances spontaneous mutation frequency and sensitizes cells to genotoxic agents. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 6905-6910
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 6905-6910
    • Rasouli-Nia, A.1    Karimi-Busheri, F.2    Weinfeld, M.3
  • 35
    • 0033569666 scopus 로고    scopus 로고
    • Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes
    • Pouliot J.J., Yao K.C., Robertson C.A., and Nash H.A. Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes. Science 286 (1999) 552-555
    • (1999) Science , vol.286 , pp. 552-555
    • Pouliot, J.J.1    Yao, K.C.2    Robertson, C.A.3    Nash, H.A.4
  • 36
    • 0029816199 scopus 로고    scopus 로고
    • A mutation in a Saccharomyces cerevisiae gene (RAD3) required for nucleotide excision repair and transcription increases the efficiency of mismatch correction
    • Yang Y., Johnson A.L., Johnston L.H., Siede W., Friedberg E.C., Ramachandran K., and Kunz B.A. A mutation in a Saccharomyces cerevisiae gene (RAD3) required for nucleotide excision repair and transcription increases the efficiency of mismatch correction. Genetics 144 (1996) 459-466
    • (1996) Genetics , vol.144 , pp. 459-466
    • Yang, Y.1    Johnson, A.L.2    Johnston, L.H.3    Siede, W.4    Friedberg, E.C.5    Ramachandran, K.6    Kunz, B.A.7
  • 37
    • 0036009232 scopus 로고    scopus 로고
    • Resistance of 3′-phosphoglycolate DNA ends to digestion by mammalian DNase III
    • Inamdar K.V., Yu Y., and Povirk L.F. Resistance of 3′-phosphoglycolate DNA ends to digestion by mammalian DNase III. Radiat. Res. 157 (2002) 306-311
    • (2002) Radiat. Res. , vol.157 , pp. 306-311
    • Inamdar, K.V.1    Yu, Y.2    Povirk, L.F.3
  • 39
    • 0037178839 scopus 로고    scopus 로고
    • Conversion of phosphoglycolate to phosphate termini on 3′ overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1
    • Inamdar K.V., Pouliot J.J., Zhou T., Lees-Miller S.P., Rasouli-Nia A., and Povirk L.F. Conversion of phosphoglycolate to phosphate termini on 3′ overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1. J. Biol. Chem. 277 (2002) 27162-27168
    • (2002) J. Biol. Chem. , vol.277 , pp. 27162-27168
    • Inamdar, K.V.1    Pouliot, J.J.2    Zhou, T.3    Lees-Miller, S.P.4    Rasouli-Nia, A.5    Povirk, L.F.6
  • 40
    • 0034871092 scopus 로고    scopus 로고
    • Pathways for repair of topoisomerase I covalent complexes in Saccharomyces cerevisiae
    • Pouliot J.J., Robertson C.A., and Nash H.A. Pathways for repair of topoisomerase I covalent complexes in Saccharomyces cerevisiae. Genes Cells 6 (2001) 677-687
    • (2001) Genes Cells , vol.6 , pp. 677-687
    • Pouliot, J.J.1    Robertson, C.A.2    Nash, H.A.3
  • 42
    • 0037162392 scopus 로고    scopus 로고
    • Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases
    • Brenner C. Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. Biochemistry 41 (2002) 9003-9014
    • (2002) Biochemistry , vol.41 , pp. 9003-9014
    • Brenner, C.1
  • 43
    • 33744937625 scopus 로고    scopus 로고
    • Aprataxin forms a discrete branch in the HIT (histidine triad) superfamily of proteins with both DNA/RNA binding and nucleotide hydrolase activities
    • Kijas A.W., Harris J.L., Harris J.M., and Lavin M.F. Aprataxin forms a discrete branch in the HIT (histidine triad) superfamily of proteins with both DNA/RNA binding and nucleotide hydrolase activities. J. Biol. Chem. 281 (2006) 13939-13948
    • (2006) J. Biol. Chem. , vol.281 , pp. 13939-13948
    • Kijas, A.W.1    Harris, J.L.2    Harris, J.M.3    Lavin, M.F.4
  • 46
    • 0037428228 scopus 로고    scopus 로고
    • DNA single-strand break repair and spinocerebellar ataxia
    • Caldecott K.W. DNA single-strand break repair and spinocerebellar ataxia. Cell 112 (2003) 7-10
    • (2003) Cell , vol.112 , pp. 7-10
    • Caldecott, K.W.1
  • 50
    • 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., and 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
  • 51
    • 0037326709 scopus 로고    scopus 로고
    • Protein-protein interactions during mammalian DNA single-strand break repair
    • Caldecott K.W. Protein-protein interactions during mammalian DNA single-strand break repair. Biochem. Soc. Trans. 31 (2003) 247-251
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 247-251
    • Caldecott, K.W.1
  • 52
  • 54
    • 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
  • 56
    • 23244437030 scopus 로고    scopus 로고
    • DNA polymerase β promotes recruitment of DNA ligase IIIα-XRCC1 to sites of base excision repair
    • Parsons J.L., Dianova I.I., Allinson S.L., and Dianov G.L. DNA polymerase β promotes recruitment of DNA ligase IIIα-XRCC1 to sites of base excision repair. Biochemistry 44 (2005) 10613-10619
    • (2005) Biochemistry , vol.44 , pp. 10613-10619
    • Parsons, J.L.1    Dianova, I.I.2    Allinson, S.L.3    Dianov, G.L.4
  • 57
    • 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
  • 58
    • 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
  • 59
    • 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., and 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
  • 60
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase β 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 β 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
  • 61
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair
    • Matsumoto Y., and 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
  • 63
    • 0030941295 scopus 로고    scopus 로고
    • XRCC1 protein interacts with one of two distinct forms of DNA ligase III
    • Nash R.A., Caldecott K.W., Barnes D.E., and Lindahl T. XRCC1 protein interacts with one of two distinct forms of DNA ligase III. Biochemistry 36 (1997) 5207-5211
    • (1997) Biochemistry , vol.36 , pp. 5207-5211
    • Nash, R.A.1    Caldecott, K.W.2    Barnes, D.E.3    Lindahl, T.4
  • 64
    • 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
  • 65
    • 17444364433 scopus 로고    scopus 로고
    • Poly(ADPribose) polymerase-1 protects excessive DNA strand breaks from deterioration during repair in human cell extracts
    • Parsons J.L., Dianova I.I., Allinson S.L., and Dianov G.L. Poly(ADPribose) polymerase-1 protects excessive DNA strand breaks from deterioration during repair in human cell extracts. FEBS J. 272 (2005) 2012-2021
    • (2005) FEBS J. , vol.272 , pp. 2012-2021
    • Parsons, J.L.1    Dianova, I.I.2    Allinson, S.L.3    Dianov, G.L.4
  • 66
    • 24744447821 scopus 로고    scopus 로고
    • The role of poly(ADP-ribose) in the DNA damage signaling network
    • Malanga M., and Althaus F.R. The role of poly(ADP-ribose) in the DNA damage signaling network. Biochem. Cell. Biol. 83 (2005) 354-364
    • (2005) Biochem. Cell. Biol. , vol.83 , pp. 354-364
    • Malanga, M.1    Althaus, F.R.2
  • 68
    • 0029957245 scopus 로고    scopus 로고
    • XRCC1 polypeptide interacts with DNA polymerase β and possibly poly (ADPribose) polymerase, and DNA ligase III is a novel molecular 'nicksensor' in vitro
    • Caldecott K.W., Aoufouchi S., Johnson P., and Shall S. XRCC1 polypeptide interacts with DNA polymerase β and possibly poly (ADPribose) polymerase, and DNA ligase III is a novel molecular 'nicksensor' 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
  • 70
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase β and the XRCC1 protein
    • Kubota Y., Nash R.A., Klungland A., Schar P., Barnes D., and Lindahl T. Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase β 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.5    Lindahl, T.6
  • 71
    • 0035009313 scopus 로고    scopus 로고
    • Mammalian DNA single-strand break repair: an Xra(y)ted affair
    • Caldecott K.W. Mammalian DNA single-strand break repair: an Xra(y)ted affair. Bioessays 23 (2001) 447-455
    • (2001) Bioessays , vol.23 , pp. 447-455
    • Caldecott, K.W.1
  • 72
    • 0038583869 scopus 로고    scopus 로고
    • Spatial and temporal cellular responses to single-strand breaks in human cells
    • Okano S., Lan L., Caldecott K.W., Mori T., and Yasui A. Spatial and temporal cellular responses to single-strand breaks in human cells. Mol. Cell. Biol. 23 (2003) 3974-3981
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3974-3981
    • Okano, S.1    Lan, L.2    Caldecott, K.W.3    Mori, T.4    Yasui, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.