메뉴 건너뛰기




Volumn 20, Issue 3, 2015, Pages 440-457

Poly-ADP-ribosylation signaling during DNA damage repair

Author keywords

Chromatin; DNA damage response; PARP; Poly ADP ribose; Review

Indexed keywords

CHROMATIN; POLY(ADENOSINE DIPHOSPHATE RIBOSE);

EID: 84918769390     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/4318     Document Type: Review
Times cited : (21)

References (133)
  • 1
    • 79956215808 scopus 로고    scopus 로고
    • Induction and repair of DNA double strand breaks: The increasing spectrum of non-homologous end joining pathways
    • E. Mladenov and G. Iliakis: Induction and repair of DNA double strand breaks: the increasing spectrum of non-homologous end joining pathways. Mutat Res, 711(1-2), 61-72 (2011) DOI: 10.1016/j.mrfmmm.2011.02.005
    • (2011) Mutat Res , vol.711 , Issue.1-2 , pp. 61-72
    • Mladenov, E.1    Iliakis, G.2
  • 2
    • 70350504453 scopus 로고    scopus 로고
    • The DNA-damage response in human biology and disease
    • S. P. Jackson and J. Bartek: The DNA-damage response in human biology and disease. Nature, 461(7267), 1071-8 (2009) DOI: 10.1038/nature08467
    • (2009) Nature , vol.461 , Issue.7267 , pp. 1071-1078
    • Jackson, S.P.1    Bartek, J.2
  • 4
    • 79952314830 scopus 로고    scopus 로고
    • Double-strand breaks in heterochromatin move outside of a dynamic HP1a domain to complete recombinational repair
    • I. Chiolo, A. Minoda, S. U. Colmenares, A. Polyzos, S. V. Costes and G. H. Karpen: Double-strand breaks in heterochromatin move outside of a dynamic HP1a domain to complete recombinational repair. Cell, 144(5), 732-44 (2011) DOI: 10.1016/j.cell.2011.02.012
    • (2011) Cell , vol.144 , Issue.5 , pp. 732-744
    • Chiolo, I.1    Minoda, A.2    Colmenares, S.U.3    Polyzos, A.4    Costes, S.V.5    Karpen, G.H.6
  • 5
    • 84865248380 scopus 로고    scopus 로고
    • Chromatin organization is a major influence on regional mutation rates in human cancer cells
    • B. Schuster-Bockler and B. Lehner: Chromatin organization is a major influence on regional mutation rates in human cancer cells. Nature, 488(7412), 504-7 (2012) DOI: 10.1038/nature11273
    • (2012) Nature , vol.488 , Issue.7412 , pp. 504-507
    • Schuster-Bockler, B.1    Lehner, B.2
  • 7
    • 84861231399 scopus 로고    scopus 로고
    • The diverse roles and clinical relevance of PARPs in DNA damage repair: Current state of the art
    • M. De Vos, V. Schreiber and F. Dantzer: The diverse roles and clinical relevance of PARPs in DNA damage repair: current state of the art. Biochem Pharmacol, 84(2), 137-46 (2012) DOI: 10.1016/j.bcp.2012.03.018
    • (2012) Biochem Pharmacol , vol.84 , Issue.2 , pp. 137-146
    • De Vos, M.1    Schreiber, V.2    Dantzer, F.3
  • 8
    • 84878117602 scopus 로고    scopus 로고
    • Touching base with PARPs: Moonlighting in the repair of UV lesions and double-strand breaks
    • A. Pines, L. H. Mullenders, H. van Attikum and M. S. Luijsterburg: Touching base with PARPs: moonlighting in the repair of UV lesions and double-strand breaks. Trends Biochem Sci, 38(6), 321-30 (2013) DOI: 10.1016/j.tibs.2013.03.002
    • (2013) Trends Biochem Sci , vol.38 , Issue.6 , pp. 321-330
    • Pines, A.1    Mullenders, L.H.2    Van Attikum, H.3    Luijsterburg, M.S.4
  • 9
    • 0019876860 scopus 로고
    • Poly(ADP-ribose) synthetase, a main acceptor of poly(ADP-ribose) in isolated nuclei
    • No DOI Found
    • N. Ogata, K. Ueda, M. Kawaichi and O. Hayaishi: Poly(ADP-ribose) synthetase, a main acceptor of poly(ADP-ribose) in isolated nuclei. J Biol Chem, 256(9), 4135-7 (1981) No DOI Found
    • (1981) J Biol Chem , vol.256 , Issue.9 , pp. 4135-4137
    • Ogata, N.1    Ueda, K.2    Kawaichi, M.3    Hayaishi, O.4
  • 10
    • 84886246082 scopus 로고    scopus 로고
    • Proteome-wide identification of poly(ADP-Ribosyl) ation targets in different genotoxic stress responses
    • S. Jungmichel, F. Rosenthal, M. Altmeyer, J. Lukas, M. O. Hottiger and M. L. Nielsen: Proteome-wide identification of poly(ADP-Ribosyl) ation targets in different genotoxic stress responses. Mol Cell, 52(2), 272-85 (2013) DOI: 10.1016/j.molcel.2013.08.026
    • (2013) Mol Cell , vol.52 , Issue.2 , pp. 272-285
    • Jungmichel, S.1    Rosenthal, F.2    Altmeyer, M.3    Lukas, J.4    Hottiger, M.O.5    Nielsen, M.L.6
  • 11
    • 84884906084 scopus 로고    scopus 로고
    • Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
    • Y. Zhang, J. Wang, M. Ding and Y. Yu: Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome. Nat Methods, 10(10), 981-4 (2013) DOI: 10.1038/nmeth.2603
    • (2013) Nat Methods , vol.10 , Issue.10 , pp. 981-984
    • Zhang, Y.1    Wang, J.2    Ding, M.3    Yu, Y.4
  • 12
    • 38149057387 scopus 로고    scopus 로고
    • PARP1-dependent kinetics of recruitment of MRE11 and NBS1 proteins to multiple DNA damage sites
    • J. F. Haince, D. McDonald, A. Rodrigue, U. Dery, J. Y. Masson, M. J. Hendzel and G. G. Poirier: PARP1-dependent kinetics of recruitment of MRE11 and NBS1 proteins to multiple DNA damage sites. J Biol Chem, 283(2), 1197-208 (2008) DOI: 10.1074/jbc.M706734200
    • (2008) J Biol Chem , vol.283 , Issue.2 , pp. 1197-1208
    • Haince, J.F.1    McDonald, D.2    Rodrigue, A.3    Dery, U.4    Masson, J.Y.5    Hendzel, M.J.6    Poirier, G.G.7
  • 14
    • 84860806404 scopus 로고    scopus 로고
    • Structural basis for DNA damage-dependent poly(ADP-ribosyl) ation by human PARP-1
    • M. F. Langelier, J. L. Planck, S. Roy and J. M. Pascal: Structural basis for DNA damage-dependent poly(ADP-ribosyl) ation by human PARP-1. Science, 336(6082), 728-32 (2012) DOI: 10.1126/science.1216338
    • (2012) Science , vol.336 , Issue.6082 , pp. 728-732
    • Langelier, M.F.1    Planck, J.L.2    Roy, S.3    Pascal, J.M.4
  • 15
    • 79952008439 scopus 로고    scopus 로고
    • The DNA-binding domain of human PARP-1 interacts with DNA single-strand breaks as a monomer through its second zinc finger
    • S. Eustermann, H. Videler, J. C. Yang, P. T. Cole, D. Gruszka, D. Veprintsev and D. Neuhaus: The DNA-binding domain of human PARP-1 interacts with DNA single-strand breaks as a monomer through its second zinc finger. J Mol Biol, 407(1), 149-70 (2011) DOI: 10.1016/j.jmb.2011.01.034
    • (2011) J Mol Biol , vol.407 , Issue.1 , pp. 149-170
    • Eustermann, S.1    Videler, H.2    Yang, J.C.3    Cole, P.T.4    Gruszka, D.5    Veprintsev, D.6    Neuhaus, D.7
  • 16
    • 0016228090 scopus 로고
    • Purification and properties of glycohydrolase from calf thymus splitting ribose-ribose linkages of poly(adenosine diphosphate ribose)
    • No DOI Found
    • M. Miwa, M. Tanaka, T. Matsushima and T. Sugimura: Purification and properties of glycohydrolase from calf thymus splitting ribose-ribose linkages of poly(adenosine diphosphate ribose). J Biol Chem, 249(11), 3475-82 (1974) No DOI Found
    • (1974) J Biol Chem , vol.249 , Issue.11 , pp. 3475-3482
    • Miwa, M.1    Tanaka, M.2    Matsushima, T.3    Sugimura, T.4
  • 17
    • 0023688678 scopus 로고
    • Poly(ADP-ribose) degradation by glycohydrolase starts with an endonucleolytic incision
    • No DOI Found
    • M. Ikejima and D. M. Gill: Poly(ADP-ribose) degradation by glycohydrolase starts with an endonucleolytic incision. J Biol Chem, 263(23), 11037-40 (1988) No DOI Found
    • (1988) J Biol Chem , vol.263 , Issue.23 , pp. 11037-11040
    • Ikejima, M.1    Gill, D.M.2
  • 18
    • 33644849513 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase
    • S. Oka, J. Kato and J. Moss: Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase. J Biol Chem, 281(2), 705-13 (2006) DOI: 10.1074/jbc.M510290200
    • (2006) J Biol Chem , vol.281 , Issue.2 , pp. 705-713
    • Oka, S.1    Kato, J.2    Moss, J.3
  • 19
    • 84888110477 scopus 로고    scopus 로고
    • ADP-ribosyl-acceptor hydrolase 3 regulates poly (ADP-ribose) degradation and cell death during oxidative stress
    • M. Mashimo, J. Kato and J. Moss: ADP-ribosyl-acceptor hydrolase 3 regulates poly (ADP-ribose) degradation and cell death during oxidative stress. Proc Natl Acad Sci U S A, 110(47), 18964-9 (2013) DOI: 10.1073/pnas.1312783110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.47 , pp. 18964-18969
    • Mashimo, M.1    Kato, J.2    Moss, J.3
  • 23
    • 84880333185 scopus 로고    scopus 로고
    • The recognition and removal of cellular poly(ADP-ribose) signals
    • E. Barkauskaite, G. Jankevicius, A. G. Ladurner, I. Ahel and G. Timinszky: The recognition and removal of cellular poly(ADP-ribose) signals. FEBS J, 280(15), 3491-507 (2013) DOI: 10.1111/febs.12358
    • (2013) FEBS J , vol.280 , Issue.15 , pp. 3491-3507
    • Barkauskaite, E.1    Jankevicius, G.2    Ladurner, A.G.3    Ahel, I.4    Timinszky, G.5
  • 24
    • 84901397700 scopus 로고    scopus 로고
    • ADP-Ribosylation: Activation, Recognition, and Removal
    • N. Li and J. Chen: ADP-Ribosylation: Activation, Recognition, and Removal. Mol Cells, 37(1), 9-16 (2014) DOI: 10.14348/molcells.2014.2245
    • (2014) Mol Cells , vol.37 , Issue.1 , pp. 9-16
    • Li, N.1    Chen, J.2
  • 25
    • 2942703171 scopus 로고
    • Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure
    • G. G. Poirier, G. de Murcia, J. Jongstra-Bilen, C. Niedergang and P. Mandel: Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure. Proc Natl Acad Sci U S A, 79(11), 3423-7 (1982) DOI: 10.1073/pnas.79.11.3423
    • (1982) Proc Natl Acad Sci U S A , vol.79 , Issue.11 , pp. 3423-3427
    • Poirier, G.G.1    De Murcia, G.2    Jongstra-Bilen, J.3    Niedergang, C.4    Mandel, P.5
  • 26
    • 10944227347 scopus 로고    scopus 로고
    • NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1
    • M. Y. Kim, S. Mauro, N. Gevry, J. T. Lis and W. L. Kraus: NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1. Cell, 119(6), 803-14 (2004) DOI: 10.1016/j.cell.2004.11.002
    • (2004) Cell , vol.119 , Issue.6 , pp. 803-814
    • Kim, M.Y.1    Mauro, S.2    Gevry, N.3    Lis, J.T.4    Kraus, W.L.5
  • 27
    • 0024406764 scopus 로고
    • The effect of poly(ADP-ribosyl) ation on native and H1-depleted chromatin. A role of poly(ADP-ribosyl) ation on core nucleosome structure
    • No DOI Found
    • A. Huletsky, G. de Murcia, S. Muller, M. Hengartner, L. Menard, D. Lamarre and G. G. Poirier: The effect of poly(ADP-ribosyl) ation on native and H1-depleted chromatin. A role of poly(ADP-ribosyl) ation on core nucleosome structure. J Biol Chem, 264(15), 8878-86 (1989) No DOI Found
    • (1989) J Biol Chem , vol.264 , Issue.15 , pp. 8878-8886
    • Huletsky, A.1    De Murcia, G.2    Muller, S.3    Hengartner, M.4    Menard, L.5    Lamarre, D.6    Poirier, G.G.7
  • 28
    • 77954274504 scopus 로고    scopus 로고
    • The PARP side of the nucleus: Molecular actions, physiological outcomes, and clinical targets
    • R. Krishnakumar and W. L. Kraus: The PARP side of the nucleus: molecular actions, physiological outcomes, and clinical targets. Mol Cell, 39(1), 8-24 (2010) DOI: 10.1016/j.molcel.2010.06.017
    • (2010) Mol Cell , vol.39 , Issue.1 , pp. 8-24
    • Krishnakumar, R.1    Kraus, W.L.2
  • 29
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
    • J. M. Pleschke, H. E. Kleczkowska, M. Strohm and F. R. Althaus: Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J Biol Chem, 275(52), 40974-80 (2000) DOI: 10.1074/jbc.M006520200
    • (2000) J Biol Chem , vol.275 , Issue.52 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 31
    • 38049064044 scopus 로고    scopus 로고
    • Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins
    • I. Ahel, D. Ahel, T. Matsusaka, A. J. Clark, J. Pines, S. J. Boulton and S. C. West: Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Nature, 451(7174), 81-5 (2008) DOI: 10.1038/nature06420
    • (2008) Nature , vol.451 , Issue.7174 , pp. 81-85
    • Ahel, I.1    Ahel, D.2    Matsusaka, T.3    Clark, A.J.4    Pines, J.5    Boulton, S.J.6    West, S.C.7
  • 32
    • 0035338814 scopus 로고    scopus 로고
    • The WWE domain: A common interaction module in protein ubiquitination and ADP ribosylation
    • L. Aravind: The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation. Trends Biochem Sci, 26(5), 273-5 (2001) DOI: 10.1016/S0968-0004(01)01787-X
    • (2001) Trends Biochem Sci , vol.26 , Issue.5 , pp. 273-275
    • Aravind, L.1
  • 33
    • 84877823968 scopus 로고    scopus 로고
    • Function of BRCA1 in the DNA damage response is mediated by ADP-ribosylation
    • M. Li and X. Yu: Function of BRCA1 in the DNA damage response is mediated by ADP-ribosylation. Cancer Cell, 23(5), 693-704 (2013) DOI: 10.1016/j.ccr.2013.03.025
    • (2013) Cancer Cell , vol.23 , Issue.5 , pp. 693-704
    • Li, M.1    Yu, X.2
  • 34
    • 84882724418 scopus 로고    scopus 로고
    • The FHA and BRCT domains recognize ADP-ribosylation during DNA damage response
    • M. Li, L. Y. Lu, C. Y. Yang, S. Wang and X. Yu: The FHA and BRCT domains recognize ADP-ribosylation during DNA damage response. Genes Dev, 27(16), 1752-68 (2013) DOI: 10.1101/gad.226357.113
    • (2013) Genes Dev , vol.27 , Issue.16 , pp. 1752-1768
    • Li, M.1    Lu, L.Y.2    Yang, C.Y.3    Wang, S.4    Yu, X.5
  • 36
    • 84901044576 scopus 로고    scopus 로고
    • The oligonucleotide/oligosaccharide-binding fold motif is a poly(ADP-ribose)-binding domain that mediates DNA damage response
    • F. Zhang, Y. Chen, M. Li and X. Yu: The oligonucleotide/oligosaccharide-binding fold motif is a poly(ADP-ribose)-binding domain that mediates DNA damage response. Proc Natl Acad Sci U S A, 111(20), 7278-83 (2014) DOI: 10.1073/pnas.1318367111
    • (2014) Proc Natl Acad Sci U S A , vol.111 , Issue.20 , pp. 7278-7283
    • Zhang, F.1    Chen, Y.2    Li, M.3    Yu, X.4
  • 37
    • 53849133471 scopus 로고    scopus 로고
    • Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins
    • Q. Deng and J. T. Barbieri: Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins. Annu Rev Microbiol, 62, 271-88 (2008) DOI: 10.1146/annurev.micro.62.081307. 162848
    • (2008) Annu Rev Microbiol , vol.62 , pp. 271-288
    • Deng, Q.1    Barbieri, J.T.2
  • 39
  • 41
    • 84873631924 scopus 로고    scopus 로고
    • CHFR is important for the first wave of ubiquitination at DNA damage sites
    • C. Liu, J. Wu, S. C. Paudyal, Z. You and X. Yu: CHFR is important for the first wave of ubiquitination at DNA damage sites. Nucleic Acids Res, 41(3), 1698-710 (2013) DOI: 10.1093/nar/gks1278
    • (2013) Nucleic Acids Res , vol.41 , Issue.3 , pp. 1698-1710
    • Liu, C.1    Wu, J.2    Paudyal, S.C.3    You, Z.4    Yu, X.5
  • 42
    • 84863010981 scopus 로고    scopus 로고
    • Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination
    • Z. Wang, G. A. Michaud, Z. Cheng, Y. Zhang, T. R. Hinds, E. Fan, F. Cong and W. Xu: Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination. Genes Dev, 26(3), 235-40 (2012) DOI: 10.1101/gad.182618.111
    • (2012) Genes Dev , vol.26 , Issue.3 , pp. 235-240
    • Wang, Z.1    Michaud, G.A.2    Cheng, Z.3    Zhang, Y.4    Hinds, T.R.5    Fan, E.6    Cong, F.7    Xu, W.8
  • 43
    • 78649874455 scopus 로고    scopus 로고
    • Structural basis of poly(ADP-ribose) recognition by the multizinc binding domain of checkpoint with forkhead-associated and RING Domains (CHFR)
    • J. Oberoi, M. W. Richards, S. Crumpler, N. Brown, J. Blagg and R. Bayliss: Structural basis of poly(ADP-ribose) recognition by the multizinc binding domain of checkpoint with forkhead-associated and RING Domains (CHFR). J Biol Chem, 285(50), 39348-58 (2010) DOI: 10.1074/jbc.M110.159855
    • (2010) J Biol Chem , vol.285 , Issue.50 , pp. 39348-39358
    • Oberoi, J.1    Richards, M.W.2    Crumpler, S.3    Brown, N.4    Blagg, J.5    Bayliss, R.6
  • 45
    • 38949198773 scopus 로고    scopus 로고
    • Reciprocal binding of PARP-1 and histone H1 at promoters specifies transcriptional outcomes
    • R. Krishnakumar, M. J. Gamble, K. M. Frizzell, J. G. Berrocal, M. Kininis and W. L. Kraus: Reciprocal binding of PARP-1 and histone H1 at promoters specifies transcriptional outcomes. Science, 319(5864), 819-21 (2008) DOI: 10.1126/science.1149250
    • (2008) Science , vol.319 , Issue.5864 , pp. 819-821
    • Krishnakumar, R.1    Gamble, M.J.2    Frizzell, K.M.3    Berrocal, J.G.4    Kininis, M.5    Kraus, W.L.6
  • 49
    • 78649349810 scopus 로고    scopus 로고
    • A chromatin localization screen reveals poly (ADP ribose)-regulated recruitment of the repressive polycomb and NuRD complexes to sites of DNA damage
    • D. M. Chou, B. Adamson, N. E. Dephoure, X. Tan, A. C. Nottke, K. E. Hurov, S. P. Gygi, M. P. Colaiacovo and S. J. Elledge: A chromatin localization screen reveals poly (ADP ribose)-regulated recruitment of the repressive polycomb and NuRD complexes to sites of DNA damage. Proc Natl Acad Sci U S A, 107(43), 18475-80 (2010) DOI: 10.1073/pnas.1012946107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.43 , pp. 18475-18480
    • Chou, D.M.1    Adamson, B.2    Dephoure, N.E.3    Tan, X.4    Nottke, A.C.5    Hurov, K.E.6    Gygi, S.P.7    Colaiacovo, M.P.8    Elledge, S.J.9
  • 50
    • 77956870690 scopus 로고    scopus 로고
    • Regulation of DNA-damage responses and cell-cycle progression by the chromatin remodelling factor CHD4
    • S. E. Polo, A. Kaidi, L. Baskcomb, Y. Galanty and S. P. Jackson: Regulation of DNA-damage responses and cell-cycle progression by the chromatin remodelling factor CHD4. EMBO J, 29(18), 3130-9 (2010) DOI: 10.1038/emboj.2010.188
    • (2010) EMBO J , vol.29 , Issue.18 , pp. 3130-3139
    • Polo, S.E.1    Kaidi, A.2    Baskcomb, L.3    Galanty, Y.4    Jackson, S.P.5
  • 51
    • 0031022784 scopus 로고    scopus 로고
    • Recurrent chromosomal abnormalities in hepatocellular carcinoma detected by comparative genomic hybridization
    • A. Marchio, M. Meddeb, P. Pineau, G. Danglot, P. Tiollais, A. Bernheim and A. Dejean: Recurrent chromosomal abnormalities in hepatocellular carcinoma detected by comparative genomic hybridization. Genes Chromosomes Cancer, 18(1), 59-65 (1997) DOI: 10.1002/(SICI)1098-2264(199701) 18:1〈59::AID-GCC7〉3.0.CO;2-0
    • (1997) Genes Chromosomes Cancer , vol.18 , Issue.1 , pp. 59-65
    • Marchio, A.1    Meddeb, M.2    Pineau, P.3    Danglot, G.4    Tiollais, P.5    Bernheim, A.6    Dejean, A.7
  • 52
    • 51349135630 scopus 로고    scopus 로고
    • Inflammatory stress exacerbates lipid accumulation in hepatic cells and fatty livers of apolipoprotein E knockout mice
    • K. L. Ma, X. Z. Ruan, S. H. Powis, Y. Chen, J. F. Moorhead and Z. Varghese: Inflammatory stress exacerbates lipid accumulation in hepatic cells and fatty livers of apolipoprotein E knockout mice. Hepatology, 48(3), 770-81 (2008) DOI: 10.1002/hep.22423
    • (2008) Hepatology , vol.48 , Issue.3 , pp. 770-781
    • Ma, K.L.1    Ruan, X.Z.2    Powis, S.H.3    Chen, Y.4    Moorhead, J.F.5    Varghese, Z.6
  • 53
    • 77951176116 scopus 로고    scopus 로고
    • CHD1L promotes hepatocellular carcinoma progression and metastasis in mice and is associated with these processes in human patients
    • L. Chen, T. H. Chan, Y. F. Yuan, L. Hu, J. Huang, S. Ma, J. Wang, S. S. Dong, K. H. Tang, D. Xie, Y. Li and X. Y. Guan: CHD1L promotes hepatocellular carcinoma progression and metastasis in mice and is associated with these processes in human patients. J Clin Invest, 120(4), 1178-91 (2010) DOI: 10.1172/JCI40665
    • (2010) J Clin Invest , vol.120 , Issue.4 , pp. 1178-1191
    • Chen, L.1    Chan, T.H.2    Yuan, Y.F.3    Hu, L.4    Huang, J.5    Ma, S.6    Wang, J.7    Dong, S.S.8    Tang, K.H.9    Xie, D.10    Li, Y.11    Guan, X.Y.12
  • 54
    • 69249208771 scopus 로고    scopus 로고
    • Transgenic CHD1L expression in mouse induces spontaneous tumors
    • M. Chen, J. D. Huang, L. Hu, B. J. Zheng, L. Chen, S. L. Tsang and X. Y. Guan: Transgenic CHD1L expression in mouse induces spontaneous tumors. PLoS One, 4(8), e6727 (2009) DOI: 10.1371/journal.pone.0006727
    • (2009) PLoS One , vol.4 , Issue.8 , pp. e6727
    • Chen, M.1    Huang, J.D.2    Hu, L.3    Zheng, B.J.4    Chen, L.5    Tsang, S.L.6    Guan, X.Y.7
  • 55
    • 84887503435 scopus 로고    scopus 로고
    • Tripartite Motif-containing 33 (TRIM33) protein functions in the poly(ADP-ribose) polymerase (PARP)-dependent DNA damage response through interaction with Amplified in Liver Cancer 1 (ALC1) protein
    • A. Kulkarni, J. Oza, M. Yao, H. Sohail, V. Ginjala, A. Tomas-Loba, Z. Horejsi, A. R. Tan, S. J. Boulton and S. Ganesan: Tripartite Motif-containing 33 (TRIM33) protein functions in the poly(ADP-ribose) polymerase (PARP)-dependent DNA damage response through interaction with Amplified in Liver Cancer 1 (ALC1) protein. J Biol Chem, 288(45), 32357-69 (2013) DOI: 10.1074/jbc.M113.459164
    • (2013) J Biol Chem , vol.288 , Issue.45 , pp. 32357-32369
    • Kulkarni, A.1    Oza, J.2    Yao, M.3    Sohail, H.4    Ginjala, V.5    Tomas-Loba, A.6    Horejsi, Z.7    Tan, A.R.8    Boulton, S.J.9    Ganesan, S.10
  • 62
    • 79959363092 scopus 로고    scopus 로고
    • SIRT6 promotes DNA repair under stress by activating PARP1
    • Z. Mao, C. Hine, X. Tian, M. Van Meter, M. Au, A. Vaidya, A. Seluanov and V. Gorbunova: SIRT6 promotes DNA repair under stress by activating PARP1. Science, 332(6036), 1443-6 (2011) DOI: 10.1126/science.1202723
    • (2011) Science , vol.332 , Issue.6036 , pp. 1443-1446
    • Mao, Z.1    Hine, C.2    Tian, X.3    Van Meter, M.4    Au, M.5    Vaidya, A.6    Seluanov, A.7    Gorbunova, V.8
  • 63
    • 67650725820 scopus 로고    scopus 로고
    • The biology of chromatin remodeling complexes
    • C. R. Clapier and B. R. Cairns: The biology of chromatin remodeling complexes. Annu Rev Biochem, 78, 273-304 (2009) DOI: 10.1146/annurev.biochem.77.062706.153223
    • (2009) Annu Rev Biochem , vol.78 , pp. 273-304
    • Clapier, C.R.1    Cairns, B.R.2
  • 64
    • 0032538293 scopus 로고    scopus 로고
    • The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities
    • Y. Zhang, G. LeRoy, H. P. Seelig, W. S. Lane and D. Reinberg: The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell, 95(2), 279-89 (1998) DOI: 10.1016/S0092-8674(00)81758-4
    • (1998) Cell , vol.95 , Issue.2 , pp. 279-289
    • Zhang, Y.1    LeRoy, G.2    Seelig, H.P.3    Lane, W.S.4    Reinberg, D.5
  • 65
    • 0035875298 scopus 로고    scopus 로고
    • Mi2, an auto-antigen for dermatomyositis, is an ATP-dependent nucleosome remodeling factor
    • H. B. Wang and Y. Zhang: Mi2, an auto-antigen for dermatomyositis, is an ATP-dependent nucleosome remodeling factor. Nucleic Acids Res, 29(12), 2517-21 (2001) DOI: 10.1093/nar/29.12.2517
    • (2001) Nucleic Acids Res , vol.29 , Issue.12 , pp. 2517-2521
    • Wang, H.B.1    Zhang, Y.2
  • 68
    • 0033551430 scopus 로고    scopus 로고
    • Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase alpha
    • J. Wittmeyer, L. Joss and T. Formosa: Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase alpha. Biochemistry, 38(28), 8961-71 (1999) DOI: 10.1021/bi982851d
    • (1999) Biochemistry , vol.38 , Issue.28 , pp. 8961-8971
    • Wittmeyer, J.1    Joss, L.2    Formosa, T.3
  • 69
    • 0041828953 scopus 로고    scopus 로고
    • Transcription elongation factors repress transcription initiation from cryptic sites
    • C. D. Kaplan, L. Laprade and F. Winston: Transcription elongation factors repress transcription initiation from cryptic sites. Science, 301(5636), 1096-9 (2003) DOI: 10.1126/science.1087374
    • (2003) Science , vol.301 , Issue.5636 , pp. 1096-1099
    • Kaplan, C.D.1    Laprade, L.2    Winston, F.3
  • 71
    • 41549112501 scopus 로고    scopus 로고
    • FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16
    • K. Heo, H. Kim, S. H. Choi, J. Choi, K. Kim, J. Gu, M. R. Lieber, A. S. Yang and W. An: FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16. Mol Cell, 30(1), 86-97 (2008) DOI: 10.1016/j.molcel.2008.02.029
    • (2008) Mol Cell , vol.30 , Issue.1 , pp. 86-97
    • Heo, K.1    Kim, H.2    Choi, S.H.3    Choi, J.4    Kim, K.5    Gu, J.6    Lieber, M.R.7    Yang, A.S.8    An, W.9
  • 73
    • 70349230854 scopus 로고    scopus 로고
    • A role for SSRP1 in recombination-mediated DNA damage response
    • A. Kumari, O. M. Mazina, U. Shinde, A. V. Mazin and H. Lu: A role for SSRP1 in recombination-mediated DNA damage response. J Cell Biochem, 108(2), 508-18 (2009) DOI: 10.1002/jcb.22280
    • (2009) J Cell Biochem , vol.108 , Issue.2 , pp. 508-518
    • Kumari, A.1    Mazina, O.M.2    Shinde, U.3    Mazin, A.V.4    Lu, H.5
  • 74
    • 0033566129 scopus 로고    scopus 로고
    • The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins
    • G. Orphanides, W. H. Wu, W. S. Lane, M. Hampsey and D. Reinberg: The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. Nature, 400(6741), 284-8 (1999) DOI: 10.1038/22350
    • (1999) Nature , vol.400 , Issue.6741 , pp. 284-288
    • Orphanides, G.1    Wu, W.H.2    Lane, W.S.3    Hampsey, M.4    Reinberg, D.5
  • 75
    • 33646841045 scopus 로고    scopus 로고
    • Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl) ation
    • J. Y. Huang, W. H. Chen, Y. L. Chang, H. T. Wang, W. T. Chuang and S. C. Lee: Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl) ation. Nucleic Acids Res, 34(8), 2398-407 (2006) DOI: 10.1093/nar/gkl241
    • (2006) Nucleic Acids Res , vol.34 , Issue.8 , pp. 2398-2407
    • Huang, J.Y.1    Chen, W.H.2    Chang, Y.L.3    Wang, H.T.4    Chuang, W.T.5    Lee, S.C.6
  • 76
    • 84876016461 scopus 로고    scopus 로고
    • Mammalian base excision repair: The forgotten archangel
    • G. L. Dianov and U. Hubscher: Mammalian base excision repair: the forgotten archangel. Nucleic Acids Res, 41(6), 3483-90 (2013) DOI: 10.1093/nar/gkt076
    • (2013) Nucleic Acids Res , vol.41 , Issue.6 , pp. 3483-3490
    • Dianov, G.L.1    Hubscher, U.2
  • 77
  • 78
    • 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
    • F. Le Page, V. Schreiber, C. Dherin, G. De Murcia and S. Boiteux: 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(20), 18471-7 (2003) DOI: 10.1074/jbc.M212905200
    • (2003) J Biol Chem , vol.278 , Issue.20 , pp. 18471-18477
    • Le Page, F.1    Schreiber, V.2    Dherin, C.3    De Murcia, G.4    Boiteux, S.5
  • 79
    • 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
    • S. F. El-Khamisy, M. Masutani, H. Suzuki and K. W. Caldecott: A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage. Nucleic Acids Res, 31(19), 5526-33 (2003) DOI: 10.1093/nar/gkg761
    • (2003) Nucleic Acids Res , vol.31 , Issue.19 , pp. 5526-5533
    • El-Khamisy, S.F.1    Masutani, M.2    Suzuki, H.3    Caldecott, K.W.4
  • 80
    • 0038583869 scopus 로고    scopus 로고
    • Spatial and temporal cellular responses to single-strand breaks in human cells
    • S. Okano, L. Lan, K. W. Caldecott, T. Mori and A. Yasui: Spatial and temporal cellular responses to single-strand breaks in human cells. Mol Cell Biol, 23(11), 3974-81 (2003) DOI: 10.1128/MCB.23.11.3974-3981.2003
    • (2003) Mol Cell Biol , vol.23 , Issue.11 , pp. 3974-3981
    • Okano, S.1    Lan, L.2    Caldecott, K.W.3    Mori, T.4    Yasui, A.5
  • 81
    • 70349978979 scopus 로고    scopus 로고
    • Aprataxin, poly-ADP ribose polymerase 1 (PARP-1) and apurinic endonuclease 1 (APE1) function together to protect the genome against oxidative damage
    • J. L. Harris, B. Jakob, G. Taucher-Scholz, G. L. Dianov, O. J. Becherel and M. F. Lavin: Aprataxin, poly-ADP ribose polymerase 1 (PARP-1) and apurinic endonuclease 1 (APE1) function together to protect the genome against oxidative damage. Hum Mol Genet, 18(21), 4102-17 (2009) DOI: 10.1093/hmg/ddp359
    • (2009) Hum Mol Genet , vol.18 , Issue.21 , pp. 4102-4117
    • Harris, J.L.1    Jakob, B.2    Taucher-Scholz, G.3    Dianov, G.L.4    Becherel, O.J.5    Lavin, M.F.6
  • 82
    • 84455161816 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 (PARP-1) binds to 8-oxoguanine-DNA glycosylase (OGG1)
    • N. Noren Hooten, K. Kompaniez, J. Barnes, A. Lohani and M. K. Evans: Poly(ADP-ribose) polymerase 1 (PARP-1) binds to 8-oxoguanine-DNA glycosylase (OGG1). J Biol Chem, 286(52), 44679-90 (2011) DOI: 10.1074/jbc.M111.255869
    • (2011) J Biol Chem , vol.286 , Issue.52 , pp. 44679-44690
    • Noren Hooten, N.1    Kompaniez, K.2    Barnes, J.3    Lohani, A.4    Evans, M.K.5
  • 84
    • 84876393023 scopus 로고    scopus 로고
    • Distinct spatiotemporal patterns and PARP dependence of XRCC1 recruitment to single-strand break and base excision repair
    • A. Campalans, T. Kortulewski, R. Amouroux, H. Menoni, W. Vermeulen and J. P. Radicella: Distinct spatiotemporal patterns and PARP dependence of XRCC1 recruitment to single-strand break and base excision repair. Nucleic Acids Res, 41(5), 3115-29 (2013) DOI: 10.1093/nar/gkt025
    • (2013) Nucleic Acids Res , vol.41 , Issue.5 , pp. 3115-3129
    • Campalans, A.1    Kortulewski, T.2    Amouroux, R.3    Menoni, H.4    Vermeulen, W.5    Radicella, J.P.6
  • 85
    • 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
    • V. Schreiber, J. C. Ame, P. Dolle, I. Schultz, B. Rinaldi, V. Fraulob, J. Menissier-de Murcia and G. de Murcia: 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(25), 23028-36 (2002) DOI: 10.1074/jbc.M202390200
    • (2002) J Biol Chem , vol.277 , Issue.25 , pp. 23028-23036
    • Schreiber, V.1    Ame, J.C.2    Dolle, P.3    Schultz, I.4    Rinaldi, B.5    Fraulob, V.6    Menissier-De Murcia, J.7    De Murcia, G.8
  • 86
    • 38049007502 scopus 로고    scopus 로고
    • Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells
    • O. Mortusewicz, J. C. Ame, V. Schreiber and H. Leonhardt: Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells. Nucleic Acids Res, 35(22), 7665-75 (2007) DOI: 10.1093/nar/gkm933
    • (2007) Nucleic Acids Res , vol.35 , Issue.22 , pp. 7665-7675
    • Mortusewicz, O.1    Ame, J.C.2    Schreiber, V.3    Leonhardt, H.4
  • 87
    • 0031844311 scopus 로고    scopus 로고
    • XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
    • No DOI Found
    • M. Masson, C. Niedergang, V. Schreiber, S. Muller, J. Menissier-de Murcia and G. de Murcia: XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol Cell Biol, 18(6), 3563-71 (1998) No DOI Found
    • (1998) Mol Cell Biol , vol.18 , Issue.6 , pp. 3563-3571
    • Masson, M.1    Niedergang, C.2    Schreiber, V.3    Muller, S.4    Menissier-De Murcia, J.5    De Murcia, G.6
  • 88
    • 33644858558 scopus 로고    scopus 로고
    • Condensin I interacts with the PARP-1-XRCC1 complex and functions in DNA single-strand break repair
    • J. T. Heale, A. R. Ball, Jr., J. A. Schmiesing, J. S. Kim, X. Kong, S. Zhou, D. F. Hudson, W. C. Earnshaw and K. Yokomori: Condensin I interacts with the PARP-1-XRCC1 complex and functions in DNA single-strand break repair. Mol Cell, 21(6), 837-48 (2006) DOI: 10.1016/j.molcel.2006.01.036
    • (2006) Mol Cell , vol.21 , Issue.6 , pp. 837-848
    • Heale, J.T.1    Ball, A.R.2    Schmiesing, J.A.3    Kim, J.S.4    Kong, X.5    Zhou, S.6    Hudson, D.F.7    Earnshaw, W.C.8    Yokomori, K.9
  • 89
    • 80051655790 scopus 로고    scopus 로고
    • Condensin I recruitment to base damage-enriched DNA lesions is modulated by PARP1
    • X. Kong, J. Stephens, A. R. Ball, Jr., J. T. Heale, D. A. Newkirk, M. W. Berns and K. Yokomori: Condensin I recruitment to base damage-enriched DNA lesions is modulated by PARP1. PLoS One, 6(8), e23548 (2011) DOI: 10.1371/journal.pone.0023548
    • (2011) PLoS One , vol.6 , Issue.8 , pp. e23548
    • Kong, X.1    Stephens, J.2    Ball, A.R.3    Heale, J.T.4    Newkirk, D.A.5    Berns, M.W.6    Yokomori, K.7
  • 91
    • 63249109714 scopus 로고    scopus 로고
    • Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK
    • A. A. Ali, R. M. Jukes, L. H. Pearl and A. W. Oliver: Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK. Nucleic Acids Res, 37(5), 1701-12 (2009) DOI: 10.1093/nar/gkn1086
    • (2009) Nucleic Acids Res , vol.37 , Issue.5 , pp. 1701-1712
    • Ali, A.A.1    Jukes, R.M.2    Pearl, L.H.3    Oliver, A.W.4
  • 93
    • 0032742715 scopus 로고    scopus 로고
    • DNA damage recognition during nucleotide excision repair in mammalian cells
    • R. D. Wood: DNA damage recognition during nucleotide excision repair in mammalian cells. Biochimie, 81(1-2), 39-44 (1999) DOI: 10.1016/S0300-9084(99)80036-4
    • (1999) Biochimie , vol.81 , Issue.1-2 , pp. 39-44
    • Wood, R.D.1
  • 94
    • 70350065725 scopus 로고    scopus 로고
    • Disorders of nucleotide excision repair: The genetic and molecular basis of heterogeneity
    • J. E. Cleaver, E. T. Lam and I. Revet: Disorders of nucleotide excision repair: the genetic and molecular basis of heterogeneity. Nat Rev Genet, 10(11), 756-68 (2009) DOI: 10.1038/nrg2663
    • (2009) Nat Rev Genet , vol.10 , Issue.11 , pp. 756-768
    • Cleaver, J.E.1    Lam, E.T.2    Revet, I.3
  • 95
    • 14644404266 scopus 로고    scopus 로고
    • Mechanism of early biphasic activation of poly(ADP-ribose) polymerase-1 in response to ultraviolet B radiation
    • M. D. Vodenicharov, M. M. Ghodgaonkar, S. S. Halappanavar, R. G. Shah and G. M. Shah: Mechanism of early biphasic activation of poly(ADP-ribose) polymerase-1 in response to ultraviolet B radiation. J Cell Sci, 118(Pt 3), 589-99 (2005) DOI: 10.1242/jcs.01636
    • (2005) J Cell Sci , vol.118 , pp. 589-599
    • Vodenicharov, M.D.1    Ghodgaonkar, M.M.2    Halappanavar, S.S.3    Shah, R.G.4    Shah, G.M.5
  • 98
    • 33751583362 scopus 로고    scopus 로고
    • Conditional deletion of Nbs1 in murine cells reveals its role in branching repair pathways of DNA double-strand breaks
    • Y. G. Yang, A. Saidi, P. O. Frappart, W. Min, C. Barrucand, V. Dumon-Jones, J. Michelon, Z. Herceg and Z. Q. Wang: Conditional deletion of Nbs1 in murine cells reveals its role in branching repair pathways of DNA double-strand breaks. EMBO J, 25(23), 5527-38 (2006) DOI: 10.1038/sj.emboj.7601411
    • (2006) EMBO J , vol.25 , Issue.23 , pp. 5527-5538
    • Yang, Y.G.1    Saidi, A.2    Frappart, P.O.3    Min, W.4    Barrucand, C.5    Dumon-Jones, V.6    Michelon, J.7    Herceg, Z.8    Wang, Z.Q.9
  • 99
    • 0034162719 scopus 로고    scopus 로고
    • DNA-dependent protein kinase stimulates an independently active, nonhomologous, end-joining apparatus
    • No DOI Found
    • S. J. DiBiase, Z. C. Zeng, R. Chen, T. Hyslop, W. J. Curran, Jr. and G. Iliakis: DNA-dependent protein kinase stimulates an independently active, nonhomologous, end-joining apparatus. Cancer Res, 60(5), 1245-53 (2000) No DOI Found
    • (2000) Cancer Res , vol.60 , Issue.5 , pp. 1245-1253
    • DiBiase, S.J.1    Zeng, Z.C.2    Chen, R.3    Hyslop, T.4    Curran, W.J.5    Iliakis, G.6
  • 100
    • 84900439412 scopus 로고    scopus 로고
    • Alternative end-joining pathway(s): Bricolage at DNA breaks
    • P. Frit, N. Barboule, Y. Yuan, D. Gomez and P. Calsou: Alternative end-joining pathway(s): Bricolage at DNA breaks. DNA Repair (2014) DOI: 10.1016/j.dnarep.2014.02.007
    • (2014) DNA Repair
    • Frit, P.1    Barboule, N.2    Yuan, Y.3    Gomez, D.4    Calsou, P.5
  • 103
    • 79952747328 scopus 로고    scopus 로고
    • Nonhomologous end joining drives poly(ADP-ribose) polymerase (PARP) inhibitor lethality in homologous recombination-deficient cells
    • A. G. Patel, J. N. Sarkaria and S. H. Kaufmann: Nonhomologous end joining drives poly(ADP-ribose) polymerase (PARP) inhibitor lethality in homologous recombination-deficient cells. Proc Natl Acad Sci U S A, 108(8), 3406-11 (2011) DOI: 10.1073/pnas.1013715108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.8 , pp. 3406-3411
    • Patel, A.G.1    Sarkaria, J.N.2    Kaufmann, S.H.3
  • 104
    • 0026046440 scopus 로고
    • Stimulation of intrachromosomal homologous recombination in mammalian cells by an inhibitor of poly(ADP-ribosylation)
    • A. S. Waldman and B. C. Waldman: Stimulation of intrachromosomal homologous recombination in mammalian cells by an inhibitor of poly(ADP-ribosylation). Nucleic Acids Res, 19(21), 5943-7 (1991) DOI: 10.1093/nar/19.21.5943
    • (1991) Nucleic Acids Res , vol.19 , Issue.21 , pp. 5943-5947
    • Waldman, A.S.1    Waldman, B.C.2
  • 105
    • 0033570903 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribose) polymerase stimulates extrachromosomal homologous recombination in mouse Ltk-fibroblasts
    • A. Semionov, D. Cournoyer and T. Y. Chow: Inhibition of poly(ADP-ribose) polymerase stimulates extrachromosomal homologous recombination in mouse Ltk-fibroblasts. Nucleic Acids Res, 27(22), 4526-31 (1999) DOI: 10.1093/nar/27.22.4526
    • (1999) Nucleic Acids Res , vol.27 , Issue.22 , pp. 4526-4531
    • Semionov, A.1    Cournoyer, D.2    Chow, T.Y.3
  • 106
    • 0344875495 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase (PARP-1) has a controlling role in homologous recombination
    • N. Schultz, E. Lopez, N. Saleh-Gohari and T. Helleday: Poly(ADP-ribose) polymerase (PARP-1) has a controlling role in homologous recombination. Nucleic Acids Res, 31(17), 4959-64 (2003) DOI: 10.1093/nar/gkg703
    • (2003) Nucleic Acids Res , vol.31 , Issue.17 , pp. 4959-4964
    • Schultz, N.1    Lopez, E.2    Saleh-Gohari, N.3    Helleday, T.4
  • 107
    • 0029000890 scopus 로고
    • A dominant-negative mutant of human poly(ADP-ribose) polymerase affects cell recovery, apoptosis, and sister chromatid exchange following DNA damage
    • V. Schreiber, D. Hunting, C. Trucco, B. Gowans, D. Grunwald, G. De Murcia and J. M. De Murcia: A dominant-negative mutant of human poly(ADP-ribose) polymerase affects cell recovery, apoptosis, and sister chromatid exchange following DNA damage. Proc Natl Acad Sci U S A, 92(11), 4753-7 (1995) DOI: 10.1073/pnas.92.11.4753
    • (1995) Proc Natl Acad Sci U S A , vol.92 , Issue.11 , pp. 4753-4757
    • Schreiber, V.1    Hunting, D.2    Trucco, C.3    Gowans, B.4    Grunwald, D.5    De Murcia, G.6    De Murcia, J.M.7
  • 108
    • 34447548569 scopus 로고    scopus 로고
    • Ataxia telangiectasia mutated (ATM) signaling network is modulated by a novel poly(ADP-ribose)-dependent pathway in the early response to DNA-damaging agents
    • J. F. Haince, S. Kozlov, V. L. Dawson, T. M. Dawson, M. J. Hendzel, M. F. Lavin and G. G. Poirier: Ataxia telangiectasia mutated (ATM) signaling network is modulated by a novel poly(ADP-ribose)-dependent pathway in the early response to DNA-damaging agents. J Biol Chem, 282(22), 16441-53 (2007) DOI: 10.1074/jbc.M608406200
    • (2007) J Biol Chem , vol.282 , Issue.22 , pp. 16441-16453
    • Haince, J.F.1    Kozlov, S.2    Dawson, V.L.3    Dawson, T.M.4    Hendzel, M.J.5    Lavin, M.F.6    Poirier, G.G.7
  • 110
    • 79956004104 scopus 로고    scopus 로고
    • hSSB1 interacts directly with the MRN complex stimulating its recruitment to DNA double-strand breaks and its endo-nuclease activity
    • D. J. Richard, L. Cubeddu, A. J. Urquhart, A. Bain, E. Bolderson, D. Menon, M. F. White and K. K. Khanna: hSSB1 interacts directly with the MRN complex stimulating its recruitment to DNA double-strand breaks and its endo-nuclease activity. Nucleic Acids Res, 39(9), 3643-51 (2011) DOI: 10.1093/nar/gkq1340
    • (2011) Nucleic Acids Res , vol.39 , Issue.9 , pp. 3643-3651
    • Richard, D.J.1    Cubeddu, L.2    Urquhart, A.J.3    Bain, A.4    Bolderson, E.5    Menon, D.6    White, M.F.7    Khanna, K.K.8
  • 112
    • 84875423827 scopus 로고    scopus 로고
    • The ATM protein kinase: Regulating the cellular response to genotoxic stress, and more
    • Y. Shiloh and Y. Ziv: The ATM protein kinase: regulating the cellular response to genotoxic stress, and more. Nat Rev Mol Cell Biol, 14(4), 197-210 (2013) DOI: 10.1038/nrm3546
    • (2013) Nat Rev Mol Cell Biol , vol.14 , Issue.4 , pp. 197-210
    • Shiloh, Y.1    Ziv, Y.2
  • 113
    • 0032475904 scopus 로고    scopus 로고
    • In vivo phosphorylation of poly(ADP-ribose) polymerase is independent of its activation
    • Y. Ariumi, K. Ueda, M. Masutani, T. D. Copeland, M. Noda, M. Hatanaka and K. Shimotohno: In vivo phosphorylation of poly(ADP-ribose) polymerase is independent of its activation. FEBS Lett, 436(2), 288-92 (1998) DOI: 10.1016/S0014-5793(98)01144-2
    • (1998) FEBS Lett , vol.436 , Issue.2 , pp. 288-292
    • Ariumi, Y.1    Ueda, K.2    Masutani, M.3    Copeland, T.D.4    Noda, M.5    Hatanaka, M.6    Shimotohno, K.7
  • 114
    • 0033549860 scopus 로고    scopus 로고
    • Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro
    • Y. Ariumi, M. Masutani, T. D. Copeland, T. Mimori, T. Sugimura, K. Shimotohno, K. Ueda, M. Hatanaka and M. Noda: Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro. Oncogene, 18(32), 4616-25 (1999) DOI: 10.1038/sj.onc.1202823
    • (1999) Oncogene , vol.18 , Issue.32 , pp. 4616-4625
    • Ariumi, Y.1    Masutani, M.2    Copeland, T.D.3    Mimori, T.4    Sugimura, T.5    Shimotohno, K.6    Ueda, K.7    Hatanaka, M.8    Noda, M.9
  • 115
    • 0033575278 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase and Ku autoantigen form a complex and synergistically bind to matrix attachment sequences
    • S. Galande and T. Kohwi-Shigematsu: Poly(ADP-ribose) polymerase and Ku autoantigen form a complex and synergistically bind to matrix attachment sequences. J Biol Chem, 274(29), 20521-8 (1999) DOI: 10.1074/jbc.274.29.20521
    • (1999) J Biol Chem , vol.274 , Issue.29 , pp. 20521-20528
    • Galande, S.1    Kohwi-Shigematsu, T.2
  • 116
    • 33845657443 scopus 로고    scopus 로고
    • PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways
    • M. Wang, W. Wu, B. Rosidi, L. Zhang, H. Wang and G. Iliakis: PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways. Nucleic Acids Res, 34(21), 6170-82 (2006) DOI: 10.1093/nar/gkl840
    • (2006) Nucleic Acids Res , vol.34 , Issue.21 , pp. 6170-6182
    • Wang, M.1    Wu, W.2    Rosidi, B.3    Zhang, L.4    Wang, H.5    Iliakis, G.6
  • 118
    • 0037415379 scopus 로고    scopus 로고
    • Lethality in PARP-1/Ku80 double mutant mice reveals physiological synergy during early embryogenesis
    • M. S. Henrie, A. Kurimasa, S. Burma, J. Menissier-de Murcia, G. de Murcia, G. C. Li and D. J. Chen: Lethality in PARP-1/Ku80 double mutant mice reveals physiological synergy during early embryogenesis. DNA Repair (Amst), 2(2), 151-8 (2003) DOI: 10.1016/S1568-7864(02)00199-4
    • (2003) DNA Repair (Amst) , vol.2 , Issue.2 , pp. 151-158
    • Henrie, M.S.1    Kurimasa, A.2    Burma, S.3    Menissier-De Murcia, J.4    De Murcia, G.5    Li, G.C.6    Chen, D.J.7
  • 119
    • 71649091348 scopus 로고    scopus 로고
    • Poly(ADP-Ribose) polymerase-1 and DNA-dependent protein kinase have equivalent roles in double strand break repair following ionizing radiation
    • J. Mitchell, G. C. Smith and N. J. Curtin: Poly(ADP-Ribose) polymerase-1 and DNA-dependent protein kinase have equivalent roles in double strand break repair following ionizing radiation. Int J Radiat Oncol Biol Phys, 75(5), 1520-7 (2009) DOI: 10.1016/j.ijrobp.2009.07.1722
    • (2009) Int J Radiat Oncol Biol Phys , vol.75 , Issue.5 , pp. 1520-1527
    • Mitchell, J.1    Smith, G.C.2    Curtin, N.J.3
  • 120
    • 0030679762 scopus 로고    scopus 로고
    • Genetic interaction between PARP and DNA-PK in V(D)J recombination and tumorigenesis
    • C. Morrison, G. C. Smith, L. Stingl, S. P. Jackson, E. F. Wagner and Z. Q. Wang: Genetic interaction between PARP and DNA-PK in V(D)J recombination and tumorigenesis. Nat Genet, 17(4), 479-82 (1997) DOI: 10.1038/ng1297-479
    • (1997) Nat Genet , vol.17 , Issue.4 , pp. 479-482
    • Morrison, C.1    Smith, G.C.2    Stingl, L.3    Jackson, S.P.4    Wagner, E.F.5    Wang, Z.Q.6
  • 121
    • 34248157719 scopus 로고    scopus 로고
    • APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks
    • N. Iles, S. Rulten, S. F. El-Khamisy and K. W. Caldecott: APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks. Mol Cell Biol, 27(10), 3793-803 (2007) DOI: 10.1128/MCB.02269-06
    • (2007) Mol Cell Biol , vol.27 , Issue.10 , pp. 3793-3803
    • Iles, N.1    Rulten, S.2    El-Khamisy, S.F.3    Caldecott, K.W.4
  • 123
    • 76349105464 scopus 로고    scopus 로고
    • Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)
    • S. Eustermann, C. Brockmann, P. V. Mehrotra, J. C. Yang, D. Loakes, S. C. West, I. Ahel and D. Neuhaus: Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose). Nat Struct Mol Biol, 17(2), 241-3 (2010) DOI: 10.1038/nsmb.1747
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.2 , pp. 241-243
    • Eustermann, S.1    Brockmann, C.2    Mehrotra, P.V.3    Yang, J.C.4    Loakes, D.5    West, S.C.6    Ahel, I.7    Neuhaus, D.8
  • 124
    • 37549023517 scopus 로고    scopus 로고
    • APLF (C2orf13) facilitates nonhomologous end-joining and undergoes ATM-dependent hyperphosphorylation following ionizing radiation
    • C. J. Macrae, R. D. McCulloch, J. Ylanko, D. Durocher and C. A. Koch: APLF (C2orf13) facilitates nonhomologous end-joining and undergoes ATM-dependent hyperphosphorylation following ionizing radiation. DNA Repair (Amst), 7(2), 292-302 (2008) DOI: 10.1016/j.dnarep.2007.10.008
    • (2008) DNA Repair (Amst) , vol.7 , Issue.2 , pp. 292-302
    • Macrae, C.J.1    McCulloch, R.D.2    Ylanko, J.3    Durocher, D.4    Koch, C.A.5
  • 126
    • 84876528414 scopus 로고    scopus 로고
    • The PARP3- and ATM-dependent phosphorylation of APLF facilitates DNA double-strand break repair
    • A. L. Fenton, P. Shirodkar, C. J. Macrae, L. Meng and C. A. Koch: The PARP3- and ATM-dependent phosphorylation of APLF facilitates DNA double-strand break repair. Nucleic Acids Res, 41(7), 4080-92 (2013) DOI: 10.1093/nar/gkt134
    • (2013) Nucleic Acids Res , vol.41 , Issue.7 , pp. 4080-4092
    • Fenton, A.L.1    Shirodkar, P.2    Macrae, C.J.3    Meng, L.4    Koch, C.A.5
  • 127
    • 11244277456 scopus 로고    scopus 로고
    • Backup pathways of NHEJ are suppressed by DNA-PK
    • R. Perrault, H. Wang, M. Wang, B. Rosidi and G. Iliakis: Backup pathways of NHEJ are suppressed by DNA-PK. J Cell Biochem, 92(4), 781-94 (2004) DOI: 10.1002/jcb.20104
    • (2004) J Cell Biochem , vol.92 , Issue.4 , pp. 781-794
    • Perrault, R.1    Wang, H.2    Wang, M.3    Rosidi, B.4    Iliakis, G.5
  • 129
    • 77649225150 scopus 로고    scopus 로고
    • Ku regulates the non-homologous end joining pathway choice of DNA double-strand break repair in human somatic cells
    • F. Fattah, E. H. Lee, N. Weisensel, Y. Wang, N. Lichter and E. A. Hendrickson: Ku regulates the non-homologous end joining pathway choice of DNA double-strand break repair in human somatic cells. PLoS Genet, 6(2), e1000855 (2010) DOI: 10.1371/journal.pgen.1000855
    • (2010) PLoS Genet , vol.6 , Issue.2 , pp. e1000855
    • Fattah, F.1    Lee, E.H.2    Weisensel, N.3    Wang, Y.4    Lichter, N.5    Hendrickson, E.A.6
  • 130
    • 79951850302 scopus 로고    scopus 로고
    • Competition between PARP-1 and Ku70 control the decision between high-fidelity and mutagenic DNA repair
    • M. N. Paddock, A. T. Bauman, R. Higdon, E. Kolker, S. Takeda and A. M. Scharenberg: Competition between PARP-1 and Ku70 control the decision between high-fidelity and mutagenic DNA repair. DNA Repair (Amst), 10(3), 338-43 (2011) DOI: 10.1016/j.dnarep.2010.12.005
    • (2011) DNA Repair (Amst) , vol.10 , Issue.3 , pp. 338-343
    • Paddock, M.N.1    Bauman, A.T.2    Higdon, R.3    Kolker, E.4    Takeda, S.5    Scharenberg, A.M.6
  • 131
    • 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
    • M. Audebert, B. Salles and P. Calsou: 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(53), 55117-26 (2004) DOI: 10.1074/jbc.M404524200
    • (2004) J Biol Chem , vol.279 , Issue.53 , pp. 55117-55126
    • Audebert, M.1    Salles, B.2    Calsou, P.3
  • 132
    • 82755183606 scopus 로고    scopus 로고
    • Correct end use during end joining of multiple chromosomal double strand breaks is influenced by repair protein RAD50, DNA-dependent protein kinase DNA-PKcs, and transcription context
    • A. Gunn, N. Bennardo, A. Cheng and J. M. Stark: Correct end use during end joining of multiple chromosomal double strand breaks is influenced by repair protein RAD50, DNA-dependent protein kinase DNA-PKcs, and transcription context. J Biol Chem, 286(49), 42470-82 (2011) DOI: 10.1074/jbc.M111.309252
    • (2011) J Biol Chem , vol.286 , Issue.49 , pp. 42470-42482
    • Gunn, A.1    Bennardo, N.2    Cheng, A.3    Stark, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.