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Volumn 9, Issue 8, 2008, Pages 619-631

Single-strand break repair and genetic disease

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; SINGLE STRANDED DNA; XRCC1 PROTEIN; APTX PROTEIN, HUMAN; DNA BINDING PROTEIN; NUCLEAR PROTEIN; PHOSPHODIESTERASE; TDP1 PROTEIN, HUMAN;

EID: 48249095920     PISSN: 14710056     EISSN: 14710064     Source Type: Journal    
DOI: 10.1038/nrg2380     Document Type: Review
Times cited : (783)

References (167)
  • 1
    • 0018787368 scopus 로고
    • X-ray induced DNA double strand break production and repair in mammalian cells as measured by neutral filter elution
    • Bradley, M. O. & Kohn, K. W. X-ray induced DNA double strand break production and repair in mammalian cells as measured by neutral filter elution. Nucleic Acids Res. 7, 793-804 (1979).
    • (1979) Nucleic Acids Res , vol.7 , pp. 793-804
    • Bradley, M.O.1    Kohn, K.W.2
  • 2
    • 0037115910 scopus 로고    scopus 로고
    • Dynamics and diversions in base excision DNA repair of oxidized abasic lesions
    • Demple, B. & DeMott, M. S. Dynamics and diversions in base excision DNA repair of oxidized abasic lesions. Oncogene 21, 8926-8934 (2002).
    • (2002) Oncogene , vol.21 , pp. 8926-8934
    • Demple, B.1    DeMott, M.S.2
  • 3
    • 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. & Mitra, S. Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells. Cell Res. 18, 27-47 (2008).
    • (2008) Cell Res , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 4
    • 11544314893 scopus 로고    scopus 로고
    • Oxidative strand scission of nucleic acids: Routes initiated by hydrogen abstraction from the sugar moiety
    • Pogozelski, W. K. & Tullius, T. D. Oxidative strand scission of nucleic acids: routes initiated by hydrogen abstraction from the sugar moiety. Chem. Rev. 98, 1089-1108 (1998).
    • (1998) Chem. Rev , vol.98 , pp. 1089-1108
    • Pogozelski, W.K.1    Tullius, T.D.2
  • 5
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: A molecular perspective
    • Wang, J. C. Cellular roles of DNA topoisomerases: a molecular perspective. Nature Rev. Mol. Cell Biol. 3, 430-440 (2002).
    • (2002) Nature Rev. Mol. Cell Biol , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 6
    • 10744233671 scopus 로고    scopus 로고
    • Repair of and checkpoint response to topoisomerase I-mediated DNA damage
    • Pommier, Y. et al. Repair of and checkpoint response to topoisomerase I-mediated DNA damage. Mutat. Res. 532, 173-203 (2003).
    • (2003) Mutat. Res , vol.532 , pp. 173-203
    • Pommier, Y.1
  • 7
    • 14544268980 scopus 로고    scopus 로고
    • Defective DNA single-strand break repair in spinocerebellar ataxia with axonal neuropathy-1
    • This paper provides the first direct connection between defects in SSBR and neurological disease
    • El-Khamisy, S. F. et al. Defective DNA single-strand break repair in spinocerebellar ataxia with axonal neuropathy-1. Nature 434, 108-113 (2005). This paper provides the first direct connection between defects in SSBR and neurological disease.
    • (2005) Nature , vol.434 , pp. 108-113
    • El-Khamisy, S.F.1
  • 8
    • 28844477965 scopus 로고    scopus 로고
    • Fragmentation of replicating chromosomes triggered by uracil in DNA
    • Kouzminova, E. A. & Kuzminov, A. Fragmentation of replicating chromosomes triggered by uracil in DNA. J. Mol. Biol. 355, 20-33 (2006).
    • (2006) J. Mol. Biol , vol.355 , pp. 20-33
    • Kouzminova, E.A.1    Kuzminov, A.2
  • 9
    • 0035902585 scopus 로고    scopus 로고
    • Kuzminov, A. Single-strand interruptions in replicating chromosomes cause double-strand breaks. Proc. Natl Acad. Sci. USA 98, 8241-8246 (2001). These authors provide supporting evidence for the concept that unrepaired SSBs can lead to DSBs during DNA replication.
    • Kuzminov, A. Single-strand interruptions in replicating chromosomes cause double-strand breaks. Proc. Natl Acad. Sci. USA 98, 8241-8246 (2001). These authors provide supporting evidence for the concept that unrepaired SSBs can lead to DSBs during DNA replication.
  • 10
    • 0025335205 scopus 로고
    • Camptothecin-stabilized topoisomerase I-DNA adducts cause premature termination of transcription
    • Bendixen, C., Thomsen, B., Alsner, J. & Westergaard, O. Camptothecin-stabilized topoisomerase I-DNA adducts cause premature termination of transcription. Biochemistry 29, 5613-5619 (1990).
    • (1990) Biochemistry , vol.29 , pp. 5613-5619
    • Bendixen, C.1    Thomsen, B.2    Alsner, J.3    Westergaard, O.4
  • 11
    • 0027165306 scopus 로고
    • Effects of abasic sites and DNA single-strand breaks on prokaryotic RNA polymerases
    • This paper, together with references 12-13, highlights the seminal concept that SSBs can block transcription
    • Zhou, W. & Doetsch, P. W. Effects of abasic sites and DNA single-strand breaks on prokaryotic RNA polymerases. Proc. Natl Acad. Sci. USA 90, 6601-6605 (1993). This paper, together with references 12-13, highlights the seminal concept that SSBs can block transcription.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6601-6605
    • Zhou, W.1    Doetsch, P.W.2
  • 12
    • 0028604392 scopus 로고
    • Transcription bypass or blockage at single-strand breaks on the DNA template strand: Effect of different 3′ and 5′ flanking groups on the T7 RNA polymerase elongation complex
    • Zhou, W. & Doetsch, P. W. Transcription bypass or blockage at single-strand breaks on the DNA template strand: effect of different 3′ and 5′ flanking groups on the T7 RNA polymerase elongation complex. Biochemistry 33, 14926-14934 (1994).
    • (1994) Biochemistry , vol.33 , pp. 14926-14934
    • Zhou, W.1    Doetsch, P.W.2
  • 13
    • 2442504817 scopus 로고    scopus 로고
    • Single-stranded breaks in DNA but not oxidative DNA base damages block transcriptional elongation by RNA polymerase II in HeLa cell nuclear extracts
    • Kathe, S. D., Shen, G. P. & Wallace, S. S. Single-stranded breaks in DNA but not oxidative DNA base damages block transcriptional elongation by RNA polymerase II in HeLa cell nuclear extracts. J. Biol. Chem. 279, 18511-18520 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 18511-18520
    • Kathe, S.D.1    Shen, G.P.2    Wallace, S.S.3
  • 15
    • 38649092421 scopus 로고    scopus 로고
    • (ADP-ribose) polymerase 1 (PARP-1) and postischemic brain damage
    • Moroni, F. Poly(ADP-ribose) polymerase 1 (PARP-1) and postischemic brain damage. Curr. Opin. Pharmacol. 8, 96-103 (2008).
    • (2008) Curr. Opin. Pharmacol , vol.8 , pp. 96-103
    • Moroni, F.P.1
  • 16
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours, D., Desnoyers, S., D'Silva, I. & Poirier, G. G. Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 342, 249-268 (1999).
    • (1999) Biochem. J , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 19
    • 0035425899 scopus 로고    scopus 로고
    • Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism
    • Davidovic, L., Vodenicharov, M., Affar, E. B. & Poirier, G. G. Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism. Exp. Cell Res. 268, 7-13 (2001).
    • (2001) Exp. Cell Res , vol.268 , pp. 7-13
    • Davidovic, L.1    Vodenicharov, M.2    Affar, E.B.3    Poirier, G.G.4
  • 20
    • 0020636714 scopus 로고
    • Effect of 3-aminobenzamide on the rate of ligation during repair of alkylated DNA in human fibroblasts
    • Morgan, W. F. & Cleaver, J. E. Effect of 3-aminobenzamide on the rate of ligation during repair of alkylated DNA in human fibroblasts. Cancer Res. 43, 3104-3107 (1983).
    • (1983) Cancer Res , vol.43 , pp. 3104-3107
    • Morgan, W.F.1    Cleaver, J.E.2
  • 21
    • 0018906390 scopus 로고
    • (ADP-ribose)n participates in DNA excision repair
    • Durkacz, B. W., Omidiji, O., Gray, D. A. & Shall, S. (ADP-ribose)n participates in DNA excision repair. Nature 283, 593-596 (1980).
    • (1980) Nature , vol.283 , pp. 593-596
    • Durkacz, B.W.1    Omidiji, O.2    Gray, D.A.3    Shall, S.4
  • 22
    • 17444364433 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 protects excessive DNA strand breaks from deterioration during repair in human cell extracts
    • Parsons, J. L., Dianova, II, Allinson, S. L. & Dianov, G. L. Poly(ADP-ribose) polymerase-1 protects excessive DNA strand breaks from deterioration during repair in human cell extracts. Febs J. 272, 2012-2021 (2005).
    • (2005) Febs J , vol.272 , pp. 2012-2021
    • Parsons, J.L.1    Dianova, I.2    Allinson, S.L.3    Dianov, G.L.4
  • 23
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 DNA repair and coordination
    • Mol, C. D., Izumi, T., Mitra, S. & Tainer, J. A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 DNA repair and coordination. Nature 403, 451-456 (2000).
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 24
    • 0032858478 scopus 로고    scopus 로고
    • Rice, P. A. Holding damaged DNA together. Nature Struct. Biol. 6, 805-806 (1999). References 23 and 24 describe a conceptual framework for the organization of BER.
    • Rice, P. A. Holding damaged DNA together. Nature Struct. Biol. 6, 805-806 (1999). References 23 and 24 describe a conceptual framework for the organization of BER.
  • 25
    • 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. Nature Struct. Biol. 7, 176-178 (2000).
    • (2000) Nature Struct. Biol , vol.7 , pp. 176-178
    • Wilson, S.H.1    Kunkel, T.A.2
  • 26
    • 0019810771 scopus 로고
    • The effect of inhibition of (ADP-ribose)n biosynthesis on DNA repair assayed by the nucleoid technique
    • Durkacz, B. W., Shall, S. & Irwin, J. The effect of inhibition of (ADP-ribose)n biosynthesis on DNA repair assayed by the nucleoid technique. Eur. J. Biochem. 121, 65-69 (1981).
    • (1981) Eur. J. Biochem , vol.121 , pp. 65-69
    • Durkacz, B.W.1    Shall, S.2    Irwin, J.3
  • 27
    • 0020400262 scopus 로고
    • Role of poly(adenosine diphosphate ribose) in deoxyribonucleic acid repair in human fibroblasts
    • James, M. R. & Lehmann, A. R. Role of poly(adenosine diphosphate ribose) in deoxyribonucleic acid repair in human fibroblasts. Biochemistry 21, 4007-4013 (1982).
    • (1982) Biochemistry , vol.21 , pp. 4007-4013
    • James, M.R.1    Lehmann, A.R.2
  • 28
    • 0021325425 scopus 로고
    • Poly(ADP-ribosylation) reduces the steady-state level of breaks in DNA following treatment of human cells with alkylating agents
    • Lehmann, A. R. & Broughton, B. C. Poly(ADP-ribosylation) reduces the steady-state level of breaks in DNA following treatment of human cells with alkylating agents. Carcinogenesis 5, 117-119 (1984).
    • (1984) Carcinogenesis , vol.5 , pp. 117-119
    • Lehmann, A.R.1    Broughton, B.C.2
  • 29
    • 0040976524 scopus 로고
    • Hydrogen peroxide-induced injury of cells and its prevention by inhibitors of poly(ADP-ribose) polymerase
    • Schraufstatter, I. U. et al. Hydrogen peroxide-induced injury of cells and its prevention by inhibitors of poly(ADP-ribose) polymerase. Proc. Natl Acad. Sci. USA 83, 4908-4912 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 4908-4912
    • Schraufstatter, I.U.1
  • 30
    • 34547225606 scopus 로고    scopus 로고
    • Poly (ADP-ribose) polymerase-1 accelerates single-strand break repair in concert with poly (ADP-ribose) glycohydrolase
    • Fisher, A., Hochegger, H., Takeda, S. & Caldecott, K. W. Poly (ADP-ribose) polymerase-1 accelerates single-strand break repair in concert with poly (ADP-ribose) glycohydrolase. Mol. Cell Biol. 27, 5597-5605 (2007).
    • (2007) Mol. Cell Biol , vol.27 , pp. 5597-5605
    • Fisher, A.1    Hochegger, H.2    Takeda, S.3    Caldecott, K.W.4
  • 31
    • 0038381446 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 (PARP-1) is required in murine cell lines for base excision repair of oxidative DNA damage in the absence of DNA polymerase beta
    • Le Page, F., Schreiber, V., Dherin, C., De Murcia, G. & Boiteux, S. Poly(ADP-ribose) polymerase-1 (PARP-1) is required in murine cell lines for base excision repair of oxidative DNA damage in the absence of DNA polymerase beta. J. Biol. Chem. 278, 18471-18477 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 18471-18477
    • Le Page, F.1    Schreiber, V.2    Dherin, C.3    De Murcia, G.4    Boiteux, S.5
  • 33
    • 0026642041 scopus 로고
    • Depletion of poly(ADP-ribose) polymerase by antisense RNA expression results in a delay in DNA strand break rejoining
    • Ding, R., Pommier, Y., Kang, V. H. & Smulson, M. Depletion of poly(ADP-ribose) polymerase by antisense RNA expression results in a delay in DNA strand break rejoining. J. Biol. Chem. 267, 12804-12812 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 12804-12812
    • Ding, R.1    Pommier, Y.2    Kang, V.H.3    Smulson, M.4
  • 34
    • 33847096037 scopus 로고    scopus 로고
    • Altered poly(ADP-ribose) metabolism impairs cellular responses to genotoxic stress in a hypomorphic mutant of poly(ADP-ribose) glycohydrolase
    • Gao, H. et al. Altered poly(ADP-ribose) metabolism impairs cellular responses to genotoxic stress in a hypomorphic mutant of poly(ADP-ribose) glycohydrolase. Exp. Cell Res. 313, 984-996 (2007).
    • (2007) Exp. Cell Res , vol.313 , pp. 984-996
    • Gao, H.1
  • 35
    • 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. & Althaus, F. R. Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275, 40974-40980 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 36
    • 0142009654 scopus 로고    scopus 로고
    • A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage
    • El-Khamisy, S. F., Masutani, M., Suzuki, H. & Caldecott, K. W. A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage. Nucleic Acids Res. 31, 5526-5533 (2003).
    • (2003) Nucleic Acids Res , vol.31 , pp. 5526-5533
    • El-Khamisy, S.F.1    Masutani, M.2    Suzuki, H.3    Caldecott, K.W.4
  • 37
    • 4644364562 scopus 로고    scopus 로고
    • In situ analysis of repair processes for oxidative DNA damage in mammalian cells
    • Lan, L. et al. In situ analysis of repair processes for oxidative DNA damage in mammalian cells. Proc. Natl Acad. Sci. USA 101, 13738-13743 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 13738-13743
    • Lan, L.1
  • 38
    • 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. & Yasui, A. Spatial and temporal cellular responses to single-strand breaks in human cells. Mol. Cell Biol. 23, 3974-3981 (2003).
    • (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
  • 39
    • 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. W., Aoufouchi, S., Johnson, P. & Shall, 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, 4387-4394 (1996).
    • (1996) Nucleic Acids Res , vol.24 , pp. 4387-4394
    • Caldecott, K.W.1    Aoufouchi, S.2    Johnson, P.3    Shall, S.4
  • 40
    • 0031844311 scopus 로고    scopus 로고
    • XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
    • Masson, M. et al. XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol. Cell Biol. 18, 3563-3571 (1998).
    • (1998) Mol. Cell Biol , vol.18 , pp. 3563-3571
    • Masson, M.1
  • 41
    • 0041378046 scopus 로고    scopus 로고
    • Caldecott, K. W. XRCC1 and DNA strand break repair. DNA Repair (Amst.) 2, 955-969 (2003).
    • Caldecott, K. W. XRCC1 and DNA strand break repair. DNA Repair (Amst.) 2, 955-969 (2003).
  • 42
    • 33847630719 scopus 로고    scopus 로고
    • Co-ordination of DNA single strand break repair
    • Dianov, G. L. & Parsons, J. L. Co-ordination of DNA single strand break repair. DNA Repair (Amst.) 6, 454-460 (2007).
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 454-460
    • Dianov, G.L.1    Parsons, J.L.2
  • 44
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • Tulin, A. & Spradling, A. Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci. Science 299, 560-562 (2003).
    • (2003) Science , vol.299 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 45
    • 0037102454 scopus 로고    scopus 로고
    • The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development
    • Tulin, A., Stewart, D. & Spradling, A. C. The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development. Genes Dev. 16, 2108-2119 (2002).
    • (2002) Genes Dev , vol.16 , pp. 2108-2119
    • Tulin, A.1    Stewart, D.2    Spradling, A.C.3
  • 46
    • 0023117437 scopus 로고
    • Release of core DNA from nucleosomal core particles following (ADP-ribose)n-modification in vitro
    • Mathis, G. & Althaus, F. R. Release of core DNA from nucleosomal core particles following (ADP-ribose)n-modification in vitro. Biochem. Biophys. Res. Commun. 143, 1049-1054 (1987).
    • (1987) Biochem. Biophys. Res. Commun , vol.143 , pp. 1049-1054
    • Mathis, G.1    Althaus, F.R.2
  • 47
    • 33847618236 scopus 로고    scopus 로고
    • Mammalian single-strand break repair: Mechanisms and links with chromatin
    • Caldecott, K. W. Mammalian single-strand break repair: Mechanisms and links with chromatin. DNA Repair (Amst.) 6, 443-453 (2006).
    • (2006) DNA Repair (Amst.) , vol.6 , pp. 443-453
    • Caldecott, K.W.1
  • 48
    • 0034720734 scopus 로고    scopus 로고
    • Base excision repair is impaired in mammalian cells lacking Poly(ADP- ribose) polymerase-1
    • Dantzer, F. et al. Base excision repair is impaired in mammalian cells lacking Poly(ADP- ribose) polymerase-1. Biochemistry 39, 7559-7569 (2000).
    • (2000) Biochemistry , vol.39 , pp. 7559-7569
    • Dantzer, F.1
  • 49
    • 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. et al. DNA polymerase beta-mediated long patch base excision repair. Poly(ADP-ribose) polymerase-1 stimulates strand displacement DNA synthesis. J. Biol. Chem. 276, 32411-32414 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 32411-32414
    • Prasad, R.1
  • 50
    • 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. & 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 (Amst.) 1, 547-558 (2002).
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 547-558
    • Sanderson, R.J.1    Lindahl, T.2
  • 51
    • 0034725720 scopus 로고    scopus 로고
    • ATP for the DNA ligation step in base excision repair is generated from poly(ADP-ribose)
    • Oei, S. L. & Ziegler, M. ATP for the DNA ligation step in base excision repair is generated from poly(ADP-ribose). J. Biol. Chem. 275, 23234-23239 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 23234-23239
    • Oei, S.L.1    Ziegler, M.2
  • 52
    • 2542457893 scopus 로고    scopus 로고
    • ATP-dependent selection between single nucleotide and long patch base excision repair
    • Petermann, E., Ziegler, M. & Oei, S. L. ATP-dependent selection between single nucleotide and long patch base excision repair. DNA Repair (Amst.) 2, 1101-1114 (2003).
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 1101-1114
    • Petermann, E.1    Ziegler, M.2    Oei, S.L.3
  • 53
    • 0028865245 scopus 로고
    • Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks
    • Lindahl, T., Satoh, M. S., Poirier, G. G. & Klungland, A. Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks. Trends Biochem. Sci. 20, 405-411 (1995).
    • (1995) Trends Biochem. Sci , vol.20 , pp. 405-411
    • Lindahl, T.1    Satoh, M.S.2    Poirier, G.G.3    Klungland, A.4
  • 54
    • 0034659935 scopus 로고    scopus 로고
    • Sobol, R. W. et al. The lyase activity of the DNA repair protein beta-polymerase protects from DNA-damage-induced cytotoxicity. Nature 405, 807-810 (2000). This is an important paper that demonstrated the significance of Pol β in repairing damaged SSB termini.
    • Sobol, R. W. et al. The lyase activity of the DNA repair protein beta-polymerase protects from DNA-damage-induced cytotoxicity. Nature 405, 807-810 (2000). This is an important paper that demonstrated the significance of Pol β in repairing damaged SSB termini.
  • 55
    • 0036468545 scopus 로고    scopus 로고
    • 3-Methyladenine DNA glycosylase-deficient Aag null mice display unexpected bone marrow alkylation resistance
    • Roth, R. B. & Samson, L. D. 3-Methyladenine DNA glycosylase-deficient Aag null mice display unexpected bone marrow alkylation resistance. Cancer Res. 62, 656-660 (2002).
    • (2002) Cancer Res , vol.62 , pp. 656-660
    • Roth, R.B.1    Samson, L.D.2
  • 56
    • 47949120006 scopus 로고    scopus 로고
    • Human methyl purine DNA glycosylase and DNA polymerase beta expression collectively predict sensitivity to temozolomide
    • 13 May, doi:10.1124/mol.108.045112
    • Trivedi, R. N. et al. Human methyl purine DNA glycosylase and DNA polymerase beta expression collectively predict sensitivity to temozolomide. Mol. Pharmacol. 13 May 2008 (doi:10.1124/mol.108.045112).
    • (2008) Mol. Pharmacol
    • Trivedi, R.N.1
  • 57
    • 0141925645 scopus 로고    scopus 로고
    • Base excision repair intermediates induce p53-independent cytotoxic and genotoxic responses
    • Sobol, R. W. et al. Base excision repair intermediates induce p53-independent cytotoxic and genotoxic responses. J. Biol. Chem. 278, 39951-39959 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 39951-39959
    • Sobol, R.W.1
  • 58
    • 0035846899 scopus 로고    scopus 로고
    • Whitehouse, C. J. et al. XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair. Cell 104, 107-117 (2001). These authors describe the first indication of the most important role identified for XRCC1 so far - promoting the processing of damaged DNA termini.
    • Whitehouse, C. J. et al. XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair. Cell 104, 107-117 (2001). These authors describe the first indication of the most important role identified for XRCC1 so far - promoting the processing of damaged DNA termini.
  • 59
    • 0033588301 scopus 로고    scopus 로고
    • Molecular characterization of a human DNA kinase
    • Karimi-Busheri, F. et al. Molecular characterization of a human DNA kinase. J. Biol. Chem. 274, 24187-24194 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 24187-24194
    • Karimi-Busheri, F.1
  • 60
    • 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. et al. 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, 24176-24186 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 24176-24186
    • Jilani, A.1
  • 61
    • 0026554433 scopus 로고
    • Human HeLa cell enzymes that remove phosphoglycolate 3′-end groups from DNA
    • Winters, T. A., Weinfeld, M. & Jorgensen, T. J. Human HeLa cell enzymes that remove phosphoglycolate 3′-end groups from DNA. Nucleic Acids Res. 20, 2573-2580 (1992).
    • (1992) Nucleic Acids Res , vol.20 , pp. 2573-2580
    • Winters, T.A.1    Weinfeld, M.2    Jorgensen, T.J.3
  • 62
    • 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. & 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, 1866-1873 (1994).
    • (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
  • 63
    • 0026004662 scopus 로고
    • Two distinct human DNA diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidized DNA
    • Chen, D. S., Herman, T. & Demple, B. Two distinct human DNA diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidized DNA. Nucleic Acids Res. 19, 5907-5914 (1991).
    • (1991) Nucleic Acids Res , vol.19 , pp. 5907-5914
    • Chen, D.S.1    Herman, T.2    Demple, B.3
  • 64
    • 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. et al. Requirement for human AP endonuclease 1 for repair of 3′-blocking damage at DNA single-strand breaks induced by reactive oxygen species. Carcinogenesis 21, 1329-1334 (2000).
    • (2000) Carcinogenesis , vol.21 , pp. 1329-1334
    • Izumi, T.1
  • 65
    • 3142770341 scopus 로고    scopus 로고
    • APE1 is the major 3′-phosphoglycolate activity in human cell extracts
    • Parsons, J. L., Dianova, I. I. & Dianov, G. L. APE1 is the major 3′-phosphoglycolate activity in human cell extracts. Nucleic Acids Res. 32, 3531-3536 (2004).
    • (2004) Nucleic Acids Res , vol.32 , pp. 3531-3536
    • Parsons, J.L.1    Dianova, I.I.2    Dianov, G.L.3
  • 66
    • 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, 699-702 (1995).
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 67
    • 33646859065 scopus 로고    scopus 로고
    • Roles of base excision repair subpathways in correcting oxidized abasic sites in DNA
    • Sung, J. S. & Demple, B. Roles of base excision repair subpathways in correcting oxidized abasic sites in DNA. Febs J. 273, 1620-1629 (2006).
    • (2006) Febs J , vol.273 , pp. 1620-1629
    • Sung, J.S.1    Demple, B.2
  • 68
    • 3242710517 scopus 로고    scopus 로고
    • AP endonuclease-independent DNA base excision repair in human cells
    • Wiederhold, L. et al. AP endonuclease-independent DNA base excision repair in human cells. Mol. Cell 15, 209-220 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 209-220
    • Wiederhold, L.1
  • 69
    • 0029958378 scopus 로고    scopus 로고
    • A eukaryotic enzyme that can disjoin dead-end covalent complexes between DNA and type I topoisomerases
    • Yang, S. W. et al. A eukaryotic enzyme that can disjoin dead-end covalent complexes between DNA and type I topoisomerases. Proc. Natl. Acad. Sci. USA 93, 11534-11539 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11534-11539
    • Yang, S.W.1
  • 70
    • 0033569666 scopus 로고    scopus 로고
    • Pouliot, J. J., Yao, K. C., Robertson, C. A. & Nash, H. A. Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes. Science 286, 552-555 (1999). This paper contains the seminal finding that TDP1 is an end-processing factor.
    • Pouliot, J. J., Yao, K. C., Robertson, C. A. & Nash, H. A. Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes. Science 286, 552-555 (1999). This paper contains the seminal finding that TDP1 is an end-processing factor.
  • 71
    • 33749821755 scopus 로고    scopus 로고
    • Ahel, I. et al. The neurodegenerative disease protein aprataxin resolves abortive DNA ligation intermediates. Nature 443, 713-716 (2006). These authors describe the seminal finding that 5′-AMP strand breaks are the likely physiological substrate for APTX.
    • Ahel, I. et al. The neurodegenerative disease protein aprataxin resolves abortive DNA ligation intermediates. Nature 443, 713-716 (2006). These authors describe the seminal finding that 5′-AMP strand breaks are the likely physiological substrate for APTX.
  • 72
    • 34248215322 scopus 로고    scopus 로고
    • Actions of aprataxin in multiple DNA repair pathways
    • Rass, U., Ahel, I. & West, S. C. Actions of aprataxin in multiple DNA repair pathways. J. Biol. Chem. 282, 9469-9474 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 9469-9474
    • Rass, U.1    Ahel, I.2    West, S.C.3
  • 73
    • 11144355098 scopus 로고    scopus 로고
    • The protein kinase CK2 facilitates repair of chromosomal DNA single-strand breaks
    • This paper contains the seminal finding that CK2 is a DNA repair protein and is required to assemble XRCC1 end-processing complexes
    • Loizou, J. I. et al. The protein kinase CK2 facilitates repair of chromosomal DNA single-strand breaks. Cell 117, 17-28 (2004). This paper contains the seminal finding that CK2 is a DNA repair protein and is required to assemble XRCC1 end-processing complexes.
    • (2004) Cell , vol.117 , pp. 17-28
    • Loizou, J.I.1
  • 74
    • 4544341920 scopus 로고    scopus 로고
    • The ataxia-oculomotor apraxia 1 gene product has a role distinct from ATM and interacts with the DNA strand break repair proteins XRCC1 and XRCC4
    • This paper and references 75-77 establish APTX as a component of the SSBR machinery
    • Clements, P. M. et al. The ataxia-oculomotor apraxia 1 gene product has a role distinct from ATM and interacts with the DNA strand break repair proteins XRCC1 and XRCC4. DNA Repair (Amst.) 3, 1493-1502 (2004). This paper and references 75-77 establish APTX as a component of the SSBR machinery.
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 1493-1502
    • Clements, P.M.1
  • 75
    • 2542612903 scopus 로고    scopus 로고
    • Aprataxin, a novel protein that protects against genotoxic stress
    • Gueven, N. et al. Aprataxin, a novel protein that protects against genotoxic stress. Hum. Mol. Genet. 13, 1081-1093 (2004).
    • (2004) Hum. Mol. Genet , vol.13 , pp. 1081-1093
    • Gueven, N.1
  • 76
    • 4544314723 scopus 로고    scopus 로고
    • A new XRCC1-containing complex and its role in cellular survival of methyl methanesulfonate treatment
    • Luo, H. et al. A new XRCC1-containing complex and its role in cellular survival of methyl methanesulfonate treatment. Mol. Cell Biol. 24, 8356-8365 (2004).
    • (2004) Mol. Cell Biol , vol.24 , pp. 8356-8365
    • Luo, H.1
  • 77
    • 10744228698 scopus 로고    scopus 로고
    • Aprataxin, the causative protein for EAOH is a nuclear protein with a potential role as a DNA repair protein
    • Sano, Y. et al. Aprataxin, the causative protein for EAOH is a nuclear protein with a potential role as a DNA repair protein. Ann. Neurol. 55, 241-249 (2004).
    • (2004) Ann. Neurol , vol.55 , pp. 241-249
    • Sano, Y.1
  • 78
    • 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. et al. Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein. EMBO J. 15, 6662-6670 (1996).
    • (1996) EMBO J , vol.15 , pp. 6662-6670
    • Kubota, Y.1
  • 79
    • 0345061277 scopus 로고    scopus 로고
    • Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions
    • Plo, I. et al. Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions. DNA Repair (Amst.) 2, 1087-1100 (2003).
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 1087-1100
    • Plo, I.1
  • 80
    • 13744260320 scopus 로고    scopus 로고
    • APE1 overexpression in XRCC1-deficient cells complements the defective repair of oxidative single strand breaks but increases genomic instability
    • Sossou, M. et al. APE1 overexpression in XRCC1-deficient cells complements the defective repair of oxidative single strand breaks but increases genomic instability. Nucleic Acids Res. 33, 298-306 (2005).
    • (2005) Nucleic Acids Res , vol.33 , pp. 298-306
    • Sossou, M.1
  • 81
    • 34948837443 scopus 로고    scopus 로고
    • XRCC1 stimulates polynucleotide kinase by enhancing its damage discrimination and displacement from DNA repair intermediates
    • Mani, R. S. et al. XRCC1 stimulates polynucleotide kinase by enhancing its damage discrimination and displacement from DNA repair intermediates. J. Biol. Chem. 282, 28004-28013 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 28004-28013
    • Mani, R.S.1
  • 82
    • 33847645440 scopus 로고    scopus 로고
    • DNA single-strand break repair is impaired in aprataxin-related ataxia
    • Hirano, M. et al. DNA single-strand break repair is impaired in aprataxin-related ataxia. Ann. Neurol. 61, 162-174 (2007).
    • (2007) Ann. Neurol , vol.61 , pp. 162-174
    • Hirano, M.1
  • 83
    • 0034663530 scopus 로고    scopus 로고
    • DNA polymerase beta is required for efficient DNA strand break 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 break repair induced by methyl methanesulfonate but not by hydrogen peroxide. Nucleic Acids Res. 28, 3040-3046 (2000).
    • (2000) Nucleic Acids Res , vol.28 , pp. 3040-3046
    • Fortini, P.1    Pascucci, B.2    Belisario, F.3    Dogliotti, E.4
  • 84
    • 13744258586 scopus 로고    scopus 로고
    • The accumulation of MMS-induced single strand breaks in G1 phase is recombinogenic in DNA polymerase beta defective mammalian cells
    • Pascucci, B., Russo, M. T., Crescenzi, M., Bignami, M. & Dogliotti, E. The accumulation of MMS-induced single strand breaks in G1 phase is recombinogenic in DNA polymerase beta defective mammalian cells. Nucleic Acids Res. 33, 280-288 (2005).
    • (2005) Nucleic Acids Res , vol.33 , pp. 280-288
    • Pascucci, B.1    Russo, M.T.2    Crescenzi, M.3    Bignami, M.4    Dogliotti, E.5
  • 86
    • 24744472268 scopus 로고    scopus 로고
    • DNA polymerase lambda protects mouse fibroblasts against oxidative DNA damage and is recruited to sites of DNA damage/repair
    • Braithwaite, E. K. et al. DNA polymerase lambda protects mouse fibroblasts against oxidative DNA damage and is recruited to sites of DNA damage/repair. J. Biol. Chem. 280, 31641-31647 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 31641-31647
    • Braithwaite, E.K.1
  • 87
    • 0035860767 scopus 로고    scopus 로고
    • Identification of an intrinsic 5′-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: A possible role in base excision repair
    • Garcia-Diaz, M., Bebenek, K., Kunkel, T. A. & Blanco, L. Identification of an intrinsic 5′-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair. J. Biol. Chem. 276, 34659-34663 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 34659-34663
    • Garcia-Diaz, M.1    Bebenek, K.2    Kunkel, T.A.3    Blanco, L.4
  • 88
    • 0035896008 scopus 로고    scopus 로고
    • 5′-Deoxyribose phosphate lyase activity of human DNA polymerase iota in vitro
    • Bebenek, K. et al. 5′-Deoxyribose phosphate lyase activity of human DNA polymerase iota in vitro. Science 291, 2156-2159 (2001).
    • (2001) Science , vol.291 , pp. 2156-2159
    • Bebenek, K.1
  • 89
    • 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. & Wilson, S. H. FEN1 stimulation of DNA polymerase beta mediates an excision step in mammalian long patch base excision repair. J. Biol. Chem. 275, 4460-4466 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 4460-4466
    • Prasad, R.1    Dianov, G.L.2    Bohr, V.A.3    Wilson, S.H.4
  • 90
    • 34250634072 scopus 로고    scopus 로고
    • Recruitment of DNA repair synthesis machinery to sites of DNA damage/repair in living human cells
    • Hashiguchi, K., Matsumoto, Y. & Yasui, A. Recruitment of DNA repair synthesis machinery to sites of DNA damage/repair in living human cells. Nucleic Acids Res. 35, 2913-2923 (2007).
    • (2007) Nucleic Acids Res , vol.35 , pp. 2913-2923
    • Hashiguchi, K.1    Matsumoto, Y.2    Yasui, A.3
  • 91
    • 0029873178 scopus 로고    scopus 로고
    • Frosina, G. et al. Two pathways for base excision repair in mammalian cells. J. Biol. Chem. 271, 9573-9578 (1996). These data underpin the concept of long-patch and short-patch BER.
    • Frosina, G. et al. Two pathways for base excision repair in mammalian cells. J. Biol. Chem. 271, 9573-9578 (1996). These data underpin the concept of long-patch and short-patch BER.
  • 92
    • 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, 3341-3348 (1997).
    • (1997) Embo J , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 93
    • 2342627913 scopus 로고    scopus 로고
    • Fan, J., Otterlei, M., Wong, H. K., Tomkinson, A. E. & Wilson, D. M. 3rd. XRCC1 co-localizes and physically interacts with PCNA. Nucleic Acids Res. 32, 2193-2201 (2004).
    • Fan, J., Otterlei, M., Wong, H. K., Tomkinson, A. E. & Wilson, D. M. 3rd. XRCC1 co-localizes and physically interacts with PCNA. Nucleic Acids Res. 32, 2193-2201 (2004).
  • 94
    • 42149158852 scopus 로고    scopus 로고
    • Characterization of plant XRCC1 and its interaction with proliferating cell nuclear antigen
    • Uchiyama, Y., Suzuki, Y. & Sakaguchi, K. Characterization of plant XRCC1 and its interaction with proliferating cell nuclear antigen. Planta 227, 1233-1241 (2008).
    • (2008) Planta , vol.227 , pp. 1233-1241
    • Uchiyama, Y.1    Suzuki, Y.2    Sakaguchi, K.3
  • 95
    • 44849118274 scopus 로고    scopus 로고
    • Two DNA binding and nick recognition modules in human DNA ligase III
    • Cotner-Gohara, E., Kim, I. K., Tomkinson, A. E. & Ellenberger, T. Two DNA binding and nick recognition modules in human DNA ligase III. J. Biol. Chem. 283,10764-10772 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 10764-10772
    • Cotner-Gohara, E.1    Kim, I.K.2    Tomkinson, A.E.3    Ellenberger, T.4
  • 96
    • 0035253750 scopus 로고    scopus 로고
    • Antisense-mediated decrease in DNA ligase III expression results in reduced mitochondrial DNA integrity
    • Lakshmipathy, U. & Campbell, C. Antisense-mediated decrease in DNA ligase III expression results in reduced mitochondrial DNA integrity. Nucleic Acids Res. 29, 668-676 (2001).
    • (2001) Nucleic Acids Res , vol.29 , pp. 668-676
    • Lakshmipathy, U.1    Campbell, C.2
  • 97
    • 33846957403 scopus 로고    scopus 로고
    • A novel interaction between DNA ligase III and DNA polymerase gamma plays an essential role in mitochondrial DNA stability
    • De, A. & Campbell, C. A novel interaction between DNA ligase III and DNA polymerase gamma plays an essential role in mitochondrial DNA stability. Biochem. J. 402, 175-186 (2007).
    • (2007) Biochem. J , vol.402 , pp. 175-186
    • De, A.1    Campbell, C.2
  • 98
    • 33746801232 scopus 로고    scopus 로고
    • Differential recruitment of DNA ligase I and III to DNA repair sites
    • Mortusewicz, O., Rothbauer, U., Cardoso, M. C. & Leonhardt, H. Differential recruitment of DNA ligase I and III to DNA repair sites. Nucleic Acids Res. 34, 3523-3532 (2006).
    • (2006) Nucleic Acids Res , vol.34 , pp. 3523-3532
    • Mortusewicz, O.1    Rothbauer, U.2    Cardoso, M.C.3    Leonhardt, H.4
  • 99
    • 0028862933 scopus 로고
    • Characterization of the XRCC1-DNA ligase III complex in vitro and its absence from mutant hamster cells
    • Caldecott, K. W., Tucker, J. D., Stanker, L. H. & Thompson, L. H. Characterization of the XRCC1-DNA ligase III complex in vitro and its absence from mutant hamster cells. Nucleic Acids Res. 23, 4836-4843 (1995).
    • (1995) Nucleic Acids Res , vol.23 , pp. 4836-4843
    • Caldecott, K.W.1    Tucker, J.D.2    Stanker, L.H.3    Thompson, L.H.4
  • 100
    • 0029024927 scopus 로고
    • Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination
    • Wei, Y. F. et al. Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination. Mol. Cell Biol. 15, 3206-3216 (1995).
    • (1995) Mol. Cell Biol , vol.15 , pp. 3206-3216
    • Wei, Y.F.1
  • 101
    • 0034666329 scopus 로고    scopus 로고
    • The DNA ligase III zinc finger stimulates binding to DNA secondary structure and promotes end joining
    • Taylor, R. M., Whitehouse, C. J. & Caldecott, K. W. The DNA ligase III zinc finger stimulates binding to DNA secondary structure and promotes end joining. Nucleic Acids Res. 28, 3558-3563 (2000).
    • (2000) Nucleic Acids Res , vol.28 , pp. 3558-3563
    • Taylor, R.M.1    Whitehouse, C.J.2    Caldecott, K.W.3
  • 102
  • 103
    • 0033618289 scopus 로고    scopus 로고
    • DNA ligase III is recruited to DNA strand breaks by a zinc finger motif homologous to that of poly(ADP-ribose) polymerase. Identification of two functionally distinct DNA binding regions within DNA ligase III
    • Mackey, Z. B. et al. DNA ligase III is recruited to DNA strand breaks by a zinc finger motif homologous to that of poly(ADP-ribose) polymerase. Identification of two functionally distinct DNA binding regions within DNA ligase III. J. Biol. Chem. 274, 21679-21687 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 21679-21687
    • Mackey, Z.B.1
  • 104
    • 20144363082 scopus 로고    scopus 로고
    • DNA ligase III as a candidate component of backup pathways of nonhomologous end joining
    • Wang, H. et al. DNA ligase III as a candidate component of backup pathways of nonhomologous end joining. Cancer Res. 65, 4020-4030 (2005).
    • (2005) Cancer Res , vol.65 , pp. 4020-4030
    • Wang, H.1
  • 105
    • 11244280890 scopus 로고    scopus 로고
    • Involvement of poly(ADP-ribose) polymerase-1 and XRCC1/DNA ligase III in an alternative route for DNA double-strand breaks rejoining
    • Audebert, M., Salles, B. & Calsou, P. Involvement of poly(ADP-ribose) polymerase-1 and XRCC1/DNA ligase III in an alternative route for DNA double-strand breaks rejoining. J. Biol. Chem. 279, 55117-55126 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 55117-55126
    • Audebert, M.1    Salles, B.2    Calsou, P.3
  • 106
    • 27444447893 scopus 로고    scopus 로고
    • Wong, H. K., Kim, D., Hogue, B. A., McNeill, D. R. & Wilson, D. M. 3rd. DNA damage levels and biochemical repair capacities associated with XRCC1 deficiency. Biochemistry 44, 14335-14343 (2005).
    • Wong, H. K., Kim, D., Hogue, B. A., McNeill, D. R. & Wilson, D. M. 3rd. DNA damage levels and biochemical repair capacities associated with XRCC1 deficiency. Biochemistry 44, 14335-14343 (2005).
  • 107
    • 34547116653 scopus 로고    scopus 로고
    • Human Xip1 (C2orf13) is a novel regulator of cellular responses to DNA strand breaks
    • Bekker-Jensen, S. et al. Human Xip1 (C2orf13) is a novel regulator of cellular responses to DNA strand breaks. J. Biol. Chem. 282, 19638-19643 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 19638-19643
    • Bekker-Jensen, S.1
  • 108
    • 34248157719 scopus 로고    scopus 로고
    • Iles, N., Rulten, S., El-Khamisy, S. F. & Caldecott, K. W. APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal dna strand breaks. Mol. Cell Biol. 27, 3793-3803 (2007).
    • Iles, N., Rulten, S., El-Khamisy, S. F. & Caldecott, K. W. APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal dna strand breaks. Mol. Cell Biol. 27, 3793-3803 (2007).
  • 109
    • 0037151051 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1
    • Schreiber, V. et al. Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. J. Biol. Chem. 277, 23028-23036 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 23028-23036
    • Schreiber, V.1
  • 110
    • 33846619711 scopus 로고    scopus 로고
    • Chk2 mediates stabilization of the FoxM1 transcription factor to stimulate expression of DNA repair genes
    • Tan, Y., Raychaudhuri, P. & Costa, R. H. Chk2 mediates stabilization of the FoxM1 transcription factor to stimulate expression of DNA repair genes. Mol. Cell Biol. 27, 1007-1016 (2007).
    • (2007) Mol. Cell Biol , vol.27 , pp. 1007-1016
    • Tan, Y.1    Raychaudhuri, P.2    Costa, R.H.3
  • 111
    • 34547787147 scopus 로고    scopus 로고
    • Ischemic preconditioning induces XRCC1, DNA polymerase-beta, and DNA ligase III and correlates with enhanced base excision repair
    • Li, N., Wu, H., Yang, S. & Chen, D. Ischemic preconditioning induces XRCC1, DNA polymerase-beta, and DNA ligase III and correlates with enhanced base excision repair. DNA Repair (Amst.) 6, 1297-306 (2007).
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 1297-1306
    • Li, N.1    Wu, H.2    Yang, S.3    Chen, D.4
  • 112
    • 0242299711 scopus 로고    scopus 로고
    • APE/Ref-1 and the mammalian response to genotoxic stress
    • Fritz, G., Grosch, S., Tomicic, M. & Kaina, B. APE/Ref-1 and the mammalian response to genotoxic stress. Toxicology 193, 67-78 (2003).
    • (2003) Toxicology , vol.193 , pp. 67-78
    • Fritz, G.1    Grosch, S.2    Tomicic, M.3    Kaina, B.4
  • 113
    • 0036864599 scopus 로고    scopus 로고
    • Acetylation regulates the DNA end-trimming activity of DNA polymerase beta
    • Hasan, S. et al. Acetylation regulates the DNA end-trimming activity of DNA polymerase beta. Mol. Cell 10, 1213-1222 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 1213-1222
    • Hasan, S.1
  • 114
    • 39549106043 scopus 로고    scopus 로고
    • CHIP-mediated degradation and DNA damage-dependent stabilization regulate base excision repair proteins
    • Parsons, J. L. et al. CHIP-mediated degradation and DNA damage-dependent stabilization regulate base excision repair proteins. Mol. Cell 29, 477-487 (2008).
    • (2008) Mol. Cell , vol.29 , pp. 477-487
    • Parsons, J.L.1
  • 115
    • 47249124194 scopus 로고    scopus 로고
    • Chen, D., Yu, Z., Zhu, Z. & Lopez, C. D. E2F1 regulates the base excision repair gene XRCC1 and promotes DNA repair. J. Biol. Chem. 283, 15381-15389 (2008).
    • Chen, D., Yu, Z., Zhu, Z. & Lopez, C. D. E2F1 regulates the base excision repair gene XRCC1 and promotes DNA repair. J. Biol. Chem. 283, 15381-15389 (2008).
  • 116
    • 36749007778 scopus 로고    scopus 로고
    • Terminally differentiated muscle cells are defective in base excision DNA repair and hypersensitive to oxygen injury
    • Narciso, L. et al. Terminally differentiated muscle cells are defective in base excision DNA repair and hypersensitive to oxygen injury. Proc. Natl Acad. Sci. USA 104, 17010-17015 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 17010-17015
    • Narciso, L.1
  • 117
    • 0033168183 scopus 로고    scopus 로고
    • Post-replicative base excision repair in replication foci
    • Otterlei, M. et al. Post-replicative base excision repair in replication foci. EMBO J. 18, 3834-3844 (1999).
    • (1999) EMBO J , vol.18 , pp. 3834-3844
    • Otterlei, M.1
  • 118
    • 34247128593 scopus 로고    scopus 로고
    • Human base excision repair complex is physically associated to DNA replication and cell cycle regulatory proteins
    • Parlanti, E., Locatelli, G., Maga, G. & Dogliotti, E. Human base excision repair complex is physically associated to DNA replication and cell cycle regulatory proteins. Nucleic Acids Res. 35, 1569-1577 (2007).
    • (2007) Nucleic Acids Res , vol.35 , pp. 1569-1577
    • Parlanti, E.1    Locatelli, G.2    Maga, G.3    Dogliotti, E.4
  • 119
    • 0034610276 scopus 로고    scopus 로고
    • Mutation of a BRCT domain selectively disrupts DNA single-strand break repair in noncycling Chinese hamster ovary cells
    • Moore, D. J., Taylor, R. M., Clements, P. & Caldecott, K. W. Mutation of a BRCT domain selectively disrupts DNA single-strand break repair in noncycling Chinese hamster ovary cells. Proc. Natl Acad. Sci. USA 97, 13649-13654 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13649-13654
    • Moore, D.J.1    Taylor, R.M.2    Clements, P.3    Caldecott, K.W.4
  • 120
    • 0033976049 scopus 로고    scopus 로고
    • A cell cycle-specific requirement for the XRCC1 BRCT II domain during mammalian DNA strand break repair
    • Taylor, R. M., Moore, D. J., Whitehouse, J., Johnson, P. & Caldecott, K. W. A cell cycle-specific requirement for the XRCC1 BRCT II domain during mammalian DNA strand break repair. Mol. Cell Biol. 20, 735-740 (2000).
    • (2000) Mol. Cell Biol , vol.20 , pp. 735-740
    • Taylor, R.M.1    Moore, D.J.2    Whitehouse, J.3    Johnson, P.4    Caldecott, K.W.5
  • 121
    • 0035009313 scopus 로고    scopus 로고
    • Mammalian DNA single-strand break repair: An X-ra(y)ted affair
    • Caldecott, K. W. Mammalian DNA single-strand break repair: an X-ra(y)ted affair. Bioessays 23, 447-455 (2001).
    • (2001) Bioessays , vol.23 , pp. 447-455
    • Caldecott, K.W.1
  • 122
    • 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, 7-10 (2003).
    • (2003) Cell , vol.112 , pp. 7-10
    • Caldecott, K.W.1
  • 123
    • 3242883361 scopus 로고    scopus 로고
    • DNA single-strand breaks and neurodegeneration
    • Caldecott, K. W. DNA single-strand breaks and neurodegeneration. DNA Repair (Amst.) 3, 875-882 (2004).
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 875-882
    • Caldecott, K.W.1
  • 124
    • 0023684502 scopus 로고
    • Ataxia-ocular motor apraxia: A syndrome mimicking ataxia-telangiectasia
    • Aicardi, J. et al. Ataxia-ocular motor apraxia: a syndrome mimicking ataxia-telangiectasia. Ann. Neurol. 24, 497-502 (1988).
    • (1988) Ann. Neurol , vol.24 , pp. 497-502
    • Aicardi, J.1
  • 125
    • 0028575680 scopus 로고
    • Ataxia-ocular motor apraxia syndrome: An investigation of cellular radiosensitivity of patients and their families
    • Hannan, M. A., Sigut, D., Waghray, M. & Gascon, G. G. Ataxia-ocular motor apraxia syndrome: an investigation of cellular radiosensitivity of patients and their families. J. Med. Genet. 31, 953-956 (1994).
    • (1994) J. Med. Genet , vol.31 , pp. 953-956
    • Hannan, M.A.1    Sigut, D.2    Waghray, M.3    Gascon, G.G.4
  • 126
    • 0035109757 scopus 로고    scopus 로고
    • Recessive ataxia with ocular apraxia: Review of 22 Portuguese patients
    • Barbot, C. et al. Recessive ataxia with ocular apraxia: review of 22 Portuguese patients. Arch. Neurol. 58, 201-205 (2001).
    • (2001) Arch. Neurol , vol.58 , pp. 201-205
    • Barbot, C.1
  • 127
    • 0035125621 scopus 로고    scopus 로고
    • Homozygosity mapping of Portuguese and Japanese forms of ataxia-oculomotor apraxia to 9p13, and evidence for genetic heterogeneity
    • Moreira, M. C. et al. Homozygosity mapping of Portuguese and Japanese forms of ataxia-oculomotor apraxia to 9p13, and evidence for genetic heterogeneity. Am. J. Hum. Genet. 68, 501-508 (2001).
    • (2001) Am. J. Hum. Genet , vol.68 , pp. 501-508
    • Moreira, M.C.1
  • 128
    • 0344875066 scopus 로고    scopus 로고
    • Cerebellar ataxia with oculomotor apraxia type 1: Clinical and genetic studies
    • Le Ber, I. et al. Cerebellar ataxia with oculomotor apraxia type 1: clinical and genetic studies. Brain 126, 2761-2772 (2003).
    • (2003) Brain , vol.126 , pp. 2761-2772
    • Le Ber, I.1
  • 129
    • 33947256186 scopus 로고    scopus 로고
    • Aprataxin (APTX) gene mutations resembling multiple system atrophy
    • Baba, Y. et al. Aprataxin (APTX) gene mutations resembling multiple system atrophy. Parkinsonism Relat. Disord. 13, 139-142 (2006).
    • (2006) Parkinsonism Relat. Disord , vol.13 , pp. 139-142
    • Baba, Y.1
  • 130
    • 13244277454 scopus 로고    scopus 로고
    • Coenzyme Q deficiency and cerebellar ataxia associated with an aprataxin mutation
    • Quinzii, C. M. et al. Coenzyme Q deficiency and cerebellar ataxia associated with an aprataxin mutation. Neurology 64, 539-541 (2005).
    • (2005) Neurology , vol.64 , pp. 539-541
    • Quinzii, C.M.1
  • 131
    • 33846446004 scopus 로고    scopus 로고
    • Muscle coenzyme Q10 deficiencies in ataxia with oculomotor apraxia 1
    • Le Ber, I. et al. Muscle coenzyme Q10 deficiencies in ataxia with oculomotor apraxia 1. Neurology 68, 295-297 (2007).
    • (2007) Neurology , vol.68 , pp. 295-297
    • Le Ber, I.1
  • 132
    • 0034790947 scopus 로고    scopus 로고
    • Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is caused by mutations in a new HIT superfamily gene
    • This paper and reference 133 identified APTX as the protein mutated in AOA1
    • Date, H. et al. Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is caused by mutations in a new HIT superfamily gene. Nature Genet. 29, 184-188 (2001). This paper and reference 133 identified APTX as the protein mutated in AOA1.
    • (2001) Nature Genet , vol.29 , pp. 184-188
    • Date, H.1
  • 133
    • 0034785531 scopus 로고    scopus 로고
    • The gene mutated in ataxia-ocular apraxia 1 encodes the new HIT/Zn-finger protein aprataxin
    • Moreira, M. C. et al. The gene mutated in ataxia-ocular apraxia 1 encodes the new HIT/Zn-finger protein aprataxin. Nature Genet. 29, 189-193 (2001).
    • (2001) Nature Genet , vol.29 , pp. 189-193
    • Moreira, M.C.1
  • 134
    • 2542495194 scopus 로고    scopus 로고
    • Aprataxin mutations are a rare cause of early onset ataxia in Germany
    • Habeck, M. et al. Aprataxin mutations are a rare cause of early onset ataxia in Germany. J. Neurol. 251, 591-594 (2004).
    • (2004) J. Neurol , vol.251 , pp. 591-594
    • Habeck, M.1
  • 135
    • 8844265438 scopus 로고    scopus 로고
    • The FHA domain of aprataxin interacts with the C-terminal region of XRCC1
    • Date, H. et al. The FHA domain of aprataxin interacts with the C-terminal region of XRCC1. Biochem. Biophys. Res. Commun. 325, 1279-1285 (2004).
    • (2004) Biochem. Biophys. Res. Commun , vol.325 , pp. 1279-1285
    • Date, H.1
  • 136
    • 34247245102 scopus 로고    scopus 로고
    • A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses
    • Kanno, S. et al. A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. Embo J. 26, 2094-2103 (2007).
    • (2007) Embo J , vol.26 , pp. 2094-2103
    • Kanno, S.1
  • 137
    • 6344238643 scopus 로고    scopus 로고
    • Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV
    • Koch, C. A. et al. Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV. Embo J. 23, 3874-3885 (2004).
    • (2004) Embo J , vol.23 , pp. 3874-3885
    • Koch, C.A.1
  • 138
    • 33745614891 scopus 로고    scopus 로고
    • Nucleolar localization of aprataxin is dependent on interaction with nucleolin and on active ribosomal DNA transcription
    • Becherel, O. J. et al. Nucleolar localization of aprataxin is dependent on interaction with nucleolin and on active ribosomal DNA transcription. Hum. Mol. Genet. 15, 2239-2249 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 2239-2249
    • Becherel, O.J.1
  • 139
    • 20444419381 scopus 로고    scopus 로고
    • Disease-associated mutations inactivate AMP-lysine hydrolase activity of Aprataxin
    • Seidle, H. F., Bieganowski, P. & Brenner, C. Disease-associated mutations inactivate AMP-lysine hydrolase activity of Aprataxin. J. Biol. Chem. 280, 20927-20931 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 20927-20931
    • Seidle, H.F.1    Bieganowski, P.2    Brenner, C.3
  • 140
    • 34248180071 scopus 로고    scopus 로고
    • Short half-lives of ataxia-associated aprataxin proteins in neuronal cells
    • Hirano, M. et al. Short half-lives of ataxia-associated aprataxin proteins in neuronal cells. Neurosci. Lett. 419, 184-187 (2007).
    • (2007) Neurosci. Lett , vol.419 , pp. 184-187
    • Hirano, M.1
  • 141
    • 18244372434 scopus 로고    scopus 로고
    • Very late onset in ataxia oculomotor apraxia type I
    • Criscuolo, C. et al. Very late onset in ataxia oculomotor apraxia type I. Ann. Neurol. 57, 777 (2005).
    • (2005) Ann. Neurol , vol.57 , pp. 777
    • Criscuolo, C.1
  • 142
    • 10444275312 scopus 로고    scopus 로고
    • Ataxia with oculomotor apraxia type 1 in southern Italy: Late onset and variable phenotype
    • Criscuolo, C. et al. Ataxia with oculomotor apraxia type 1 in southern Italy: late onset and variable phenotype. Neurology 63, 2173-2175 (2004).
    • (2004) Neurology , vol.63 , pp. 2173-2175
    • Criscuolo, C.1
  • 144
    • 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. & 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, 13939-13948 (2006).
    • (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
  • 145
    • 34548614799 scopus 로고    scopus 로고
    • Defective DNA repair and neurodegenerative disease
    • Rass, U., Ahel, I. & West, S. C. Defective DNA repair and neurodegenerative disease. Cell 130, 991-1004 (2007).
    • (2007) Cell , vol.130 , pp. 991-1004
    • Rass, U.1    Ahel, I.2    West, S.C.3
  • 146
    • 18644386254 scopus 로고    scopus 로고
    • Takashima, H. et al. Mutation of TDP1, encoding a topoisomerase I-dependent DNA damage repair enzyme, in spinocerebellar ataxia with axonal neuropathy. Nature Genet. 32, 267-272 (2002). This paper identified TDP1 as the protein mutated in SCAN1.
    • Takashima, H. et al. Mutation of TDP1, encoding a topoisomerase I-dependent DNA damage repair enzyme, in spinocerebellar ataxia with axonal neuropathy. Nature Genet. 32, 267-272 (2002). This paper identified TDP1 as the protein mutated in SCAN1.
  • 147
    • 0030698003 scopus 로고    scopus 로고
    • Trapping of mammalian topoisomerase I and recombinations induced by damaged DNA containing nicks or gaps. Importance of DNA end phosphorylation and camptothecin effects
    • Pourquier, P. et al. Trapping of mammalian topoisomerase I and recombinations induced by damaged DNA containing nicks or gaps. Importance of DNA end phosphorylation and camptothecin effects. J. Biol. Chem. 272, 26441-26447 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 26441-26447
    • Pourquier, P.1
  • 148
    • 0033605675 scopus 로고    scopus 로고
    • Induction of reversible complexes between eukaryotic DNA topoisomerase I and DNAcontaining oxidative base damages. 7,8-dihydro-8-oxoguanine and 5-hydroxycytosine
    • Pourquier, P. et al. Induction of reversible complexes between eukaryotic DNA topoisomerase I and DNAcontaining oxidative base damages. 7,8-dihydro-8-oxoguanine and 5-hydroxycytosine. J. Biol. Chem. 274, 8516-8523 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 8516-8523
    • Pourquier, P.1
  • 149
    • 0031003701 scopus 로고    scopus 로고
    • Effects of uracil incorporation, DNA mismatches, and abasic sites on cleavage and religation activities of mammalian topoisomerase I
    • Pourquier, P. et al. Effects of uracil incorporation, DNA mismatches, and abasic sites on cleavage and religation activities of mammalian topoisomerase I. J. Biol. Chem. 272, 7792-7796 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 7792-7796
    • Pourquier, P.1
  • 150
    • 0035132902 scopus 로고    scopus 로고
    • Topoisomerase I-mediated cytotoxicity of N-methyl-N′-nitro-N-nitrosoguanidine: Trapping of topoisomerase I by the O6-methylguanine
    • Pourquier, P. et al. Topoisomerase I-mediated cytotoxicity of N-methyl-N′-nitro-N-nitrosoguanidine: trapping of topoisomerase I by the O6-methylguanine. Cancer Res. 61, 53-58 (2001).
    • (2001) Cancer Res , vol.61 , pp. 53-58
    • Pourquier, P.1
  • 151
    • 0033663604 scopus 로고    scopus 로고
    • Topoisomerase I-mediated DNA damage
    • Pourquier, P. & Pommier, Y. Topoisomerase I-mediated DNA damage. Adv. Cancer Res. 80, 189-216 (2001).
    • (2001) Adv. Cancer Res , vol.80 , pp. 189-216
    • Pourquier, P.1    Pommier, Y.2
  • 152
    • 33745254448 scopus 로고    scopus 로고
    • Trapping of DNA topoisomerase I on nick-containing DNA in cell free extracts of Saccharomyces cerevisiae
    • Lebedeva, N., Auffret Vander Kemp, P., Bjornsti, M. A., Lavrik, O. & Boiteux, S. Trapping of DNA topoisomerase I on nick-containing DNA in cell free extracts of Saccharomyces cerevisiae. DNA Repair (Amst.) 5, 799-809 (2006).
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 799-809
    • Lebedeva, N.1    Auffret Vander Kemp, P.2    Bjornsti, M.A.3    Lavrik, O.4    Boiteux, S.5
  • 153
    • 2442549621 scopus 로고    scopus 로고
    • Hydrogen peroxide induces topoisomerase I-mediated DNA damage and cell death
    • Daroui, P., Desai, S. D., Li, T. K., Liu, A. A. & Liu, L. F. Hydrogen peroxide induces topoisomerase I-mediated DNA damage and cell death. J. Biol. Chem. 279, 14587-14594 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 14587-14594
    • Daroui, P.1    Desai, S.D.2    Li, T.K.3    Liu, A.A.4    Liu, L.F.5
  • 154
    • 0035854751 scopus 로고    scopus 로고
    • Overexpression of type I topoisomerases sensitizes yeast cells to DNA damage
    • Nitiss, J. L., Nitiss, K. C., Rose, A. & Waltman, J. L. Overexpression of type I topoisomerases sensitizes yeast cells to DNA damage. J. Biol. Chem. 276, 26708-26714 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 26708-26714
    • Nitiss, J.L.1    Nitiss, K.C.2    Rose, A.3    Waltman, J.L.4
  • 155
    • 2342517437 scopus 로고    scopus 로고
    • The role of TDP1 from budding yeast in the repair of DNA damage
    • Liu, C., Pouliot, J. J. & Nash, H. A. The role of TDP1 from budding yeast in the repair of DNA damage. DNA Repair (Amst.) 3, 593-601 (2004).
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 593-601
    • Liu, C.1    Pouliot, J.J.2    Nash, H.A.3
  • 156
    • 34548535219 scopus 로고    scopus 로고
    • TDP1 facilitates repair of ionizing radiation-induced DNA single-strand breaks
    • El-Khamisy, S. F., Hartsuiker, E. & Caldecott, K. W. TDP1 facilitates repair of ionizing radiation-induced DNA single-strand breaks. DNA Repair (Amst.) 6, 1485-1495 (2007).
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 1485-1495
    • El-Khamisy, S.F.1    Hartsuiker, E.2    Caldecott, K.W.3
  • 157
    • 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. et al. 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, 27162-27168 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 27162-27168
    • Inamdar, K.V.1
  • 158
    • 27744521320 scopus 로고    scopus 로고
    • Human Tdp1 cleaves a broad spectrum of substrates, including phosphoamide linkages
    • Interthal, H., Chen, H. J. & Champoux, J. J. Human Tdp1 cleaves a broad spectrum of substrates, including phosphoamide linkages. J. Biol. Chem. 280, 36518-36528 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 36518-36528
    • Interthal, H.1    Chen, H.J.2    Champoux, J.J.3
  • 159
    • 13744253911 scopus 로고    scopus 로고
    • Deficiency in 3′-phosphoglycolate processing in human cells with a hereditary mutation in tyrosyl-DNA phosphodiesterase (TDP1)
    • Zhou, T. et al. Deficiency in 3′-phosphoglycolate processing in human cells with a hereditary mutation in tyrosyl-DNA phosphodiesterase (TDP1). Nucleic Acids Res. 33, 289-297 (2005).
    • (2005) Nucleic Acids Res , vol.33 , pp. 289-297
    • Zhou, T.1
  • 160
    • 33745154128 scopus 로고    scopus 로고
    • Tyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damage
    • Nitiss, K. C., Malik, M., He, X., White, S. W. & Nitiss, J. L. Tyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damage. Proc. Natl Acad. Sci. USA 103, 8953-8958 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8953-8958
    • Nitiss, K.C.1    Malik, M.2    He, X.3    White, S.W.4    Nitiss, J.L.5
  • 161
    • 21844437071 scopus 로고    scopus 로고
    • SCAN1 mutant Tdp1 accumulates the enzyme-DNA intermediate and causes camptothecin hypersensitivity
    • Interthal, H. et al. SCAN1 mutant Tdp1 accumulates the enzyme-DNA intermediate and causes camptothecin hypersensitivity. Embo J. 24, 2224-2233 (2005).
    • (2005) Embo J , vol.24 , pp. 2224-2233
    • Interthal, H.1
  • 162
    • 36249016854 scopus 로고    scopus 로고
    • Spinocerebellar ataxia with axonal neuropathy: Consequence of a Tdp1 recessive neomorphic mutation?
    • Hirano, R. et al. Spinocerebellar ataxia with axonal neuropathy: consequence of a Tdp1 recessive neomorphic mutation? Embo J. 26, 4732-4743 (2007).
    • (2007) Embo J , vol.26 , pp. 4732-4743
    • Hirano, R.1
  • 163
    • 36248984333 scopus 로고    scopus 로고
    • TDP1 facilitates chromosomal single-strand break repair in neurons and is neuroprotective in vivo
    • Katyal, S. et al. TDP1 facilitates chromosomal single-strand break repair in neurons and is neuroprotective in vivo. Embo J. 26, 4720-4731 (2007).
    • (2007) Embo J , vol.26 , pp. 4720-4731
    • Katyal, S.1
  • 164
    • 15044357229 scopus 로고    scopus 로고
    • The novel human gene aprataxin is directly involved in DNA single-strand-break repair
    • Mosesso, P. et al. The novel human gene aprataxin is directly involved in DNA single-strand-break repair. Cell. Mol. Life Sci. 62, 485-491 (2005).
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 485-491
    • Mosesso, P.1
  • 165
    • 33749616036 scopus 로고    scopus 로고
    • TDP1-dependent DNA single-strand break repair and neurodegeneration
    • El-Khamisy, S. F. & Caldecott, K. W. TDP1-dependent DNA single-strand break repair and neurodegeneration. Mutagenesis 21, 219-224 (2006).
    • (2006) Mutagenesis , vol.21 , pp. 219-224
    • El-Khamisy, S.F.1    Caldecott, K.W.2
  • 166
    • 32244435724 scopus 로고    scopus 로고
    • Is base excision repair a tumor suppressor mechanism?
    • Sweasy, J. B., Lang, T. & DiMaio, D. Is base excision repair a tumor suppressor mechanism? Cell Cycle 5, 250-259 (2006).
    • (2006) Cell Cycle , vol.5 , pp. 250-259
    • Sweasy, J.B.1    Lang, T.2    DiMaio, D.3
  • 167
    • 0036012789 scopus 로고    scopus 로고
    • ATM deficiency and oxidative stress: A new dimension of defective response to DNA damage
    • Barzilai, A., Rotman, G. & Shiloh, Y. ATM deficiency and oxidative stress: a new dimension of defective response to DNA damage. DNA Repair (Amst.) 1, 3-25 (2002).
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 3-25
    • Barzilai, A.1    Rotman, G.2    Shiloh, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.