메뉴 건너뛰기




Volumn 63, Issue , 2017, Pages 92-101

Expanding functions of ADP-ribosylation in the maintenance of genome integrity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; POLY(ADENOSINE DIPHOSPHATE RIBOSE); POLYMER;

EID: 84999836310     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2016.09.009     Document Type: Review
Times cited : (74)

References (109)
  • 1
    • 84870400503 scopus 로고    scopus 로고
    • Base excision repair targets for cancer therapy
    • [1] Dianov, G.L., Base excision repair targets for cancer therapy. Am. J. Cancer Res. 1 (2011), 845–851.
    • (2011) Am. J. Cancer Res. , vol.1 , pp. 845-851
    • Dianov, G.L.1
  • 2
    • 84969262470 scopus 로고    scopus 로고
    • DNA double-strand-break repair in higher eukaryotes and its role in genomic instability and cancer: cell cycle and proliferation-dependent regulation
    • [2] Mladenov, E., Magin, S., Soni, A., Iliakis, G., DNA double-strand-break repair in higher eukaryotes and its role in genomic instability and cancer: cell cycle and proliferation-dependent regulation. Semin. Cancer Biol. 37–38 (2016), 51–64.
    • (2016) Semin. Cancer Biol. , vol.37-38 , pp. 51-64
    • Mladenov, E.1    Magin, S.2    Soni, A.3    Iliakis, G.4
  • 3
    • 80755187806 scopus 로고    scopus 로고
    • Double-strand break end resection and repair pathway choice
    • [3] Symington, L.S., Gautier, J., Double-strand break end resection and repair pathway choice. Annu. Rev. Genet. 45 (2011), 247–271.
    • (2011) Annu. Rev. Genet. , vol.45 , pp. 247-271
    • Symington, L.S.1    Gautier, J.2
  • 4
    • 84891014338 scopus 로고    scopus 로고
    • Double-strand break repair: 53BP1 comes into focus
    • [4] Panier, S., Boulton, S.J., Double-strand break repair: 53BP1 comes into focus. Nat. Rev. Mol. Cell Biol. 15 (2014), 7–18.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 7-18
    • Panier, S.1    Boulton, S.J.2
  • 5
    • 84904642416 scopus 로고    scopus 로고
    • Understanding nucleotide excision repair and its roles in cancer and ageing
    • [5] Marteijn, J.A., Lans, H., Vermeulen, W., Hoeijmakers, J.H., Understanding nucleotide excision repair and its roles in cancer and ageing. Nat. Rev. Mol. Cell Biol. 15 (2014), 465–481.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 465-481
    • Marteijn, J.A.1    Lans, H.2    Vermeulen, W.3    Hoeijmakers, J.H.4
  • 6
    • 84974575150 scopus 로고    scopus 로고
    • Chemical genetic discovery of PARP targets reveals a role for PARP-1 in transcription elongation
    • [6] Gibson, B.A., Zhang, Y., Jiang, H., Hussey, K.M., Shrimp, J.H., Lin, H., Schwede, F., Yu, Y., Kraus, W.L., Chemical genetic discovery of PARP targets reveals a role for PARP-1 in transcription elongation. Science 353 (2016), 45–50.
    • (2016) Science , vol.353 , pp. 45-50
    • Gibson, B.A.1    Zhang, Y.2    Jiang, H.3    Hussey, K.M.4    Shrimp, J.H.5    Lin, H.6    Schwede, F.7    Yu, Y.8    Kraus, W.L.9
  • 7
    • 84884906084 scopus 로고    scopus 로고
    • Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
    • [7] Zhang, Y., Wang, J., Ding, M., Yu, Y., Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome. Nat. Methods 10 (2013), 981–984.
    • (2013) Nat. Methods , vol.10 , pp. 981-984
    • Zhang, Y.1    Wang, J.2    Ding, M.3    Yu, Y.4
  • 8
  • 9
    • 84886246082 scopus 로고    scopus 로고
    • Proteome-wide identification of poly(ADP-Ribosyl)ation targets in different genotoxic stress responses
    • [9] Jungmichel, S., Rosenthal, F., Altmeyer, M., Lukas, J., Hottiger, M.O., Nielsen, M.L., Proteome-wide identification of poly(ADP-Ribosyl)ation targets in different genotoxic stress responses. Mol. Cell 52 (2013), 272–285.
    • (2013) Mol. Cell , vol.52 , pp. 272-285
    • Jungmichel, S.1    Rosenthal, F.2    Altmeyer, M.3    Lukas, J.4    Hottiger, M.O.5    Nielsen, M.L.6
  • 10
    • 84937597366 scopus 로고    scopus 로고
    • PARPs and ADP-ribosylation: 50 years and counting
    • [10] Kraus, W.L., PARPs and ADP-ribosylation: 50 years and counting. Mol. Cell 58 (2015), 902–910.
    • (2015) Mol. Cell , vol.58 , pp. 902-910
    • Kraus, W.L.1
  • 12
    • 84937578418 scopus 로고    scopus 로고
    • Structures and mechanisms of enzymes employed in the synthesis and degradation of PARP-dependent protein ADP-ribosylation
    • [12] Barkauskaite, E., Jankevicius, G., Ahel, I., Structures and mechanisms of enzymes employed in the synthesis and degradation of PARP-dependent protein ADP-ribosylation. Mol. Cell 58 (2015), 935–946.
    • (2015) Mol. Cell , vol.58 , pp. 935-946
    • Barkauskaite, E.1    Jankevicius, G.2    Ahel, I.3
  • 14
    • 84938198958 scopus 로고    scopus 로고
    • The rise and fall of poly(ADP-ribose): an enzymatic perspective
    • [14] Pascal, J.M., Ellenberger, T., The rise and fall of poly(ADP-ribose): an enzymatic perspective. DNA Repair (Amst.) 32 (2015), 10–16.
    • (2015) DNA Repair (Amst.) , vol.32 , pp. 10-16
    • Pascal, J.M.1    Ellenberger, T.2
  • 15
    • 84860806404 scopus 로고    scopus 로고
    • Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1
    • [15] Langelier, M.F., Planck, J.L., Roy, S., Pascal, J.M., Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1. Science 336 (2012), 728–732.
    • (2012) Science , vol.336 , pp. 728-732
    • Langelier, M.F.1    Planck, J.L.2    Roy, S.3    Pascal, J.M.4
  • 16
    • 84873524967 scopus 로고    scopus 로고
    • PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis
    • [16] Langelier, M.F., Pascal, J.M., PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis. Curr. Opin. Struct. Biol. 23 (2013), 134–143.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 134-143
    • Langelier, M.F.1    Pascal, J.M.2
  • 18
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • [18] Tulin, A., Spradling, A., Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci. Science 299 (2003), 560–562.
    • (2003) Science , vol.299 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 22
    • 84880557003 scopus 로고    scopus 로고
    • Kdm4b histone demethylase is a DNA damage response protein and confers a survival advantage following gamma-irradiation
    • [22] Young, L.C., McDonald, D.W., Hendzel, M.J., Kdm4b histone demethylase is a DNA damage response protein and confers a survival advantage following gamma-irradiation. J. Biol. Chem. 288 (2013), 21376–21388.
    • (2013) J. Biol. Chem. , vol.288 , pp. 21376-21388
    • Young, L.C.1    McDonald, D.W.2    Hendzel, M.J.3
  • 25
    • 79955507697 scopus 로고    scopus 로고
    • HP1alpha recruitment to DNA damage by p150CAF-1 promotes homologous recombination repair
    • [25] Baldeyron, C., Soria, G., Roche, D., Cook, A.J., Almouzni, G., HP1alpha recruitment to DNA damage by p150CAF-1 promotes homologous recombination repair. J. Cell Biol. 193 (2011), 81–95.
    • (2011) J. Cell Biol. , vol.193 , pp. 81-95
    • Baldeyron, C.1    Soria, G.2    Roche, D.3    Cook, A.J.4    Almouzni, G.5
  • 26
    • 84903446359 scopus 로고    scopus 로고
    • DNA double-strand breaks promote methylation of histone H3 on lysine 9 and transient formation of repressive chromatin
    • [26] Ayrapetov, M.K., Gursoy-Yuzugullu, O., Xu, C., Xu, Y., Price, B.D., DNA double-strand breaks promote methylation of histone H3 on lysine 9 and transient formation of repressive chromatin. Proc. Natl. Acad. Sci. U. S. A. 111 (2014), 9169–9174.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 9169-9174
    • Ayrapetov, M.K.1    Gursoy-Yuzugullu, O.2    Xu, C.3    Xu, Y.4    Price, B.D.5
  • 28
  • 32
    • 84883136968 scopus 로고    scopus 로고
    • The RNA-binding protein fused in sarcoma (FUS) functions downstream of poly(ADP-ribose) polymerase (PARP) in response to DNA damage
    • [32] Mastrocola, A.S., Kim, S.H., Trinh, A.T., Rodenkirch, L.A., Tibbetts, R.S., The RNA-binding protein fused in sarcoma (FUS) functions downstream of poly(ADP-ribose) polymerase (PARP) in response to DNA damage. J. Biol. Chem. 288 (2013), 24731–24741.
    • (2013) J. Biol. Chem. , vol.288 , pp. 24731-24741
    • Mastrocola, A.S.1    Kim, S.H.2    Trinh, A.T.3    Rodenkirch, L.A.4    Tibbetts, R.S.5
  • 36
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • [36] 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:Pt. 2 (1999), 249–268.
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 37
    • 84861231399 scopus 로고    scopus 로고
    • The diverse roles and clinical relevance of PARPs in DNA damage repair: current state of the art
    • [37] De Vos, M., Schreiber, V., Dantzer, F., The diverse roles and clinical relevance of PARPs in DNA damage repair: current state of the art. Biochem. Pharmacol. 84 (2012), 137–146.
    • (2012) Biochem. Pharmacol. , vol.84 , pp. 137-146
    • De Vos, M.1    Schreiber, V.2    Dantzer, F.3
  • 39
    • 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
    • [39] Mortusewicz, O., Ame, J.C., Schreiber, V., Leonhardt, H., Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells. Nucleic Acids Res. 35 (2007), 7665–7675.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 7665-7675
    • Mortusewicz, O.1    Ame, J.C.2    Schreiber, V.3    Leonhardt, H.4
  • 40
    • 38149057387 scopus 로고    scopus 로고
    • PARP1-dependent kinetics of recruitment of MRE11 and NBS1 proteins to multiple DNA damage sites
    • [40] Haince, J.F., McDonald, D., Rodrigue, A., Dery, U., Masson, J.Y., Hendzel, M.J., Poirier, G.G., PARP1-dependent kinetics of recruitment of MRE11 and NBS1 proteins to multiple DNA damage sites. J. Biol. Chem. 283 (2008), 1197–1208.
    • (2008) J. Biol. Chem. , vol.283 , 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
  • 41
    • 80054764341 scopus 로고    scopus 로고
    • PARP-1 enhances the mismatch-dependence of 5'-directed excision in human mismatch repair in vitro
    • [41] Liu, Y., Kadyrov, F.A., Modrich, P., PARP-1 enhances the mismatch-dependence of 5'-directed excision in human mismatch repair in vitro. DNA Repair (Amst.) 10 (2011), 1145–1153.
    • (2011) DNA Repair (Amst.) , vol.10 , pp. 1145-1153
    • Liu, Y.1    Kadyrov, F.A.2    Modrich, P.3
  • 42
    • 84919400644 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerases in double-strand break repair: focus on PARP1 PARP2 and PARP3
    • [42] Beck, C., Robert, I., Reina-San-Martin, B., Schreiber, V., Dantzer, F., Poly(ADP-ribose) polymerases in double-strand break repair: focus on PARP1 PARP2 and PARP3. Exp. Cell Res. 329 (2014), 18–25.
    • (2014) Exp. Cell Res. , vol.329 , pp. 18-25
    • Beck, C.1    Robert, I.2    Reina-San-Martin, B.3    Schreiber, V.4    Dantzer, F.5
  • 43
    • 84886718907 scopus 로고    scopus 로고
    • Functional aspects of PARylation in induced and programmed DNA repair processes: preserving genome integrity and modulating physiological events
    • [43] Robert, I., Karicheva, O., Reina San Martin, B., Schreiber, V., Dantzer, F., Functional aspects of PARylation in induced and programmed DNA repair processes: preserving genome integrity and modulating physiological events. Mol. Aspects Med. 34 (2013), 1138–1152.
    • (2013) Mol. Aspects Med. , vol.34 , pp. 1138-1152
    • Robert, I.1    Karicheva, O.2    Reina San Martin, B.3    Schreiber, V.4    Dantzer, F.5
  • 44
    • 84959367139 scopus 로고    scopus 로고
    • Roles of RNA-binding proteins in DNA damage response
    • [44] Kai, M., Roles of RNA-binding proteins in DNA damage response. Int. J. Mol. Sci., 17, 2016.
    • (2016) Int. J. Mol. Sci. , vol.17
    • Kai, M.1
  • 45
    • 84901207597 scopus 로고    scopus 로고
    • RNA binding protein RBM14 promotes radio-resistance in glioblastoma by regulating DNA repair and cell differentiation
    • [45] Yuan, M., Eberhart, C.G., Kai, M., RNA binding protein RBM14 promotes radio-resistance in glioblastoma by regulating DNA repair and cell differentiation. Oncotarget 5 (2014), 2820–2826.
    • (2014) Oncotarget , vol.5 , pp. 2820-2826
    • Yuan, M.1    Eberhart, C.G.2    Kai, M.3
  • 47
    • 33845657443 scopus 로고    scopus 로고
    • PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways
    • [47] Wang, M., Wu, W., Rosidi, B., Zhang, L., Wang, H., Iliakis, G., PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways. Nucleic Acids Res. 34 (2006), 6170–6182.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 6170-6182
    • Wang, M.1    Wu, W.2    Rosidi, B.3    Zhang, L.4    Wang, H.5    Iliakis, G.6
  • 48
    • 78049446968 scopus 로고    scopus 로고
    • The alternative end-joining pathway for repair of DNA double-strand breaks requires PARP1 but is not dependent upon microhomologies
    • [48] Mansour, W.Y., Rhein, T., Dahm-Daphi, J., The alternative end-joining pathway for repair of DNA double-strand breaks requires PARP1 but is not dependent upon microhomologies. Nucleic Acids Res. 38 (2010), 6065–6077.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 6065-6077
    • Mansour, W.Y.1    Rhein, T.2    Dahm-Daphi, J.3
  • 49
    • 66049143898 scopus 로고    scopus 로고
    • Parp1 facilitates alternative NHEJ, whereas Parp2 suppresses IgH/c-myc translocations during immunoglobulin class switch recombination
    • [49] Robert, I., Dantzer, F., Reina-San-Martin, B., Parp1 facilitates alternative NHEJ, whereas Parp2 suppresses IgH/c-myc translocations during immunoglobulin class switch recombination. J. Exp. Med. 206 (2009), 1047–1056.
    • (2009) J. Exp. Med. , vol.206 , pp. 1047-1056
    • Robert, I.1    Dantzer, F.2    Reina-San-Martin, B.3
  • 50
    • 84878117602 scopus 로고    scopus 로고
    • Touching base with PARPs: moonlighting in the repair of UV lesions and double-strand breaks
    • [50] Pines, A., Mullenders, L.H., van Attikum, H., Luijsterburg, M.S., Touching base with PARPs: moonlighting in the repair of UV lesions and double-strand breaks. Trends Biochem. Sci. 38 (2013), 321–330.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 321-330
    • Pines, A.1    Mullenders, L.H.2    van Attikum, H.3    Luijsterburg, M.S.4
  • 51
    • 14644404266 scopus 로고    scopus 로고
    • Mechanism of early biphasic activation of poly(ADP-ribose) polymerase-1 in response to ultraviolet B radiation
    • [51] Vodenicharov, M.D., Ghodgaonkar, M.M., Halappanavar, S.S., Shah, R.G., Shah, G.M., Mechanism of early biphasic activation of poly(ADP-ribose) polymerase-1 in response to ultraviolet B radiation. J. Cell Sci. 118 (2005), 589–599.
    • (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
  • 55
    • 2342524565 scopus 로고    scopus 로고
    • Ablation of PARP-1 does not interfere with the repair of DNA double-strand breaks, but compromises the reactivation of stalled replication forks
    • [55] Yang, Y.G., Cortes, U., Patnaik, S., Jasin, M., Wang, Z.Q., Ablation of PARP-1 does not interfere with the repair of DNA double-strand breaks, but compromises the reactivation of stalled replication forks. Oncogene 23 (2004), 3872–3882.
    • (2004) Oncogene , vol.23 , pp. 3872-3882
    • Yang, Y.G.1    Cortes, U.2    Patnaik, S.3    Jasin, M.4    Wang, Z.Q.5
  • 57
    • 84861888851 scopus 로고    scopus 로고
    • Mre11-dependent degradation of stalled DNA replication forks is prevented by BRCA2 and PARP1
    • [57] Ying, S., Hamdy, F.C., Helleday, T., Mre11-dependent degradation of stalled DNA replication forks is prevented by BRCA2 and PARP1. Cancer Res. 72 (2012), 2814–2821.
    • (2012) Cancer Res. , vol.72 , pp. 2814-2821
    • Ying, S.1    Hamdy, F.C.2    Helleday, T.3
  • 60
    • 84877823968 scopus 로고    scopus 로고
    • Function of BRCA1 in the DNA damage response is mediated by ADP-ribosylation
    • [60] Li, M., Yu, X., Function of BRCA1 in the DNA damage response is mediated by ADP-ribosylation. Cancer Cell 23 (2013), 693–704.
    • (2013) Cancer Cell , vol.23 , pp. 693-704
    • Li, M.1    Yu, X.2
  • 61
    • 84873855937 scopus 로고    scopus 로고
    • BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM MDC1, and RNF8
    • [61] Yan, Q., Xu, R., Zhu, L., Cheng, X., Wang, Z., Manis, J., Shipp, M.A., BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM MDC1, and RNF8. Mol. Cell. Biol. 33 (2013), 845–857.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 845-857
    • Yan, Q.1    Xu, R.2    Zhu, L.3    Cheng, X.4    Wang, Z.5    Manis, J.6    Shipp, M.A.7
  • 62
    • 84945559598 scopus 로고    scopus 로고
    • Poly(ADP-Ribose) mediates the BRCA2-dependent early DNA damage response
    • [62] Zhang, F., Shi, J., Bian, C., Yu, X., Poly(ADP-Ribose) mediates the BRCA2-dependent early DNA damage response. Cell Rep. 13 (2015), 678–689.
    • (2015) Cell Rep. , vol.13 , pp. 678-689
    • Zhang, F.1    Shi, J.2    Bian, C.3    Yu, X.4
  • 63
    • 41549155890 scopus 로고    scopus 로고
    • Toward specific functions of poly(ADP-ribose) polymerase-2
    • [63] Yelamos, J., Schreiber, V., Dantzer, F., Toward specific functions of poly(ADP-ribose) polymerase-2. Trends Mol. Med. 14 (2008), 169–178.
    • (2008) Trends Mol. Med. , vol.14 , pp. 169-178
    • Yelamos, J.1    Schreiber, V.2    Dantzer, F.3
  • 64
    • 84892384683 scopus 로고    scopus 로고
    • Structural implications for selective targeting of PARPs
    • [64] Steffen, J.D., Brody, J.R., Armen, R.S., Pascal, J.M., Structural implications for selective targeting of PARPs. Front. Oncol., 3, 2013, 301.
    • (2013) Front. Oncol. , vol.3 , pp. 301
    • Steffen, J.D.1    Brody, J.R.2    Armen, R.S.3    Pascal, J.M.4
  • 65
    • 84960493553 scopus 로고    scopus 로고
    • PARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damage
    • [65] Riccio, A.A., Cingolani, G., Pascal, J.M., PARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damage. Nucleic Acids Res. 44 (2016), 1691–1702.
    • (2016) Nucleic Acids Res. , vol.44 , pp. 1691-1702
    • Riccio, A.A.1    Cingolani, G.2    Pascal, J.M.3
  • 66
    • 84979687732 scopus 로고    scopus 로고
    • Common and unique genetic interactions of the poly(ADP-ribose) polymerases PARP1 and PARP2 with DNA double-strand break repair pathways
    • [66] Ghosh, R., Roy, S., Kamyab, J., Dantzer, F., Franco, S., Common and unique genetic interactions of the poly(ADP-ribose) polymerases PARP1 and PARP2 with DNA double-strand break repair pathways. DNA Repair (Amst). 45 (2016), 56–62.
    • (2016) DNA Repair (Amst). , vol.45 , pp. 56-62
    • Ghosh, R.1    Roy, S.2    Kamyab, J.3    Dantzer, F.4    Franco, S.5
  • 71
    • 84903977632 scopus 로고    scopus 로고
    • PARP-2 and PARP-3 are selectively activated by 5’ phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1
    • [71] Langelier, M.F., Riccio, A.A., Pascal, J.M., PARP-2 and PARP-3 are selectively activated by 5’ phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1. Nucleic Acids Res. 42 (2014), 7762–7775.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 7762-7775
    • Langelier, M.F.1    Riccio, A.A.2    Pascal, J.M.3
  • 72
    • 84876528414 scopus 로고    scopus 로고
    • The PARP3- and ATM-dependent phosphorylation of APLF facilitates DNA double-strand break repair
    • [72] Fenton, A.L., Shirodkar, P., Macrae, C.J., Meng, L., Koch, C.A., The PARP3- and ATM-dependent phosphorylation of APLF facilitates DNA double-strand break repair. Nucleic Acids Res. 41 (2013), 4080–4092.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 4080-4092
    • Fenton, A.L.1    Shirodkar, P.2    Macrae, C.J.3    Meng, L.4    Koch, C.A.5
  • 75
    • 0032553473 scopus 로고    scopus 로고
    • Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
    • [75] Smith, S., Giriat, I., Schmitt, A., de Lange, T., Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. Science 282 (1998), 1484–1487.
    • (1998) Science , vol.282 , pp. 1484-1487
    • Smith, S.1    Giriat, I.2    Schmitt, A.3    de Lange, T.4
  • 76
    • 1842424729 scopus 로고    scopus 로고
    • Resolution of sister telomere association is required for progression through mitosis
    • [76] Dynek, J.N., Smith, S., Resolution of sister telomere association is required for progression through mitosis. Science 304 (2004), 97–100.
    • (2004) Science , vol.304 , pp. 97-100
    • Dynek, J.N.1    Smith, S.2
  • 78
    • 61449168034 scopus 로고    scopus 로고
    • Sister telomeres rendered dysfunctional by persistent cohesion are fused by NHEJ
    • [78] Hsiao, S.J., Smith, S., Sister telomeres rendered dysfunctional by persistent cohesion are fused by NHEJ. J. Cell Biol. 184 (2009), 515–526.
    • (2009) J. Cell Biol. , vol.184 , pp. 515-526
    • Hsiao, S.J.1    Smith, S.2
  • 79
    • 79953322962 scopus 로고    scopus 로고
    • Regulatory roles of tankyrase 1 at telomeres and in DNA repair: suppression of T-SCE and stabilization of DNA-PKcs
    • [79] Dregalla, R.C., Zhou, J., Idate, R.R., Battaglia, C.L., Liber, H.L., Bailey, S.M., Regulatory roles of tankyrase 1 at telomeres and in DNA repair: suppression of T-SCE and stabilization of DNA-PKcs. Aging (Milano) 2 (2010), 691–708.
    • (2010) Aging (Milano) , vol.2 , pp. 691-708
    • Dregalla, R.C.1    Zhou, J.2    Idate, R.R.3    Battaglia, C.L.4    Liber, H.L.5    Bailey, S.M.6
  • 80
    • 61549087513 scopus 로고    scopus 로고
    • The DNA damage-inducible C. elegans tankyrase is a nuclear protein closely linked to chromosomes
    • [80] White, C., Gagnon, S.N., St-Laurent, J.F., Gravel, C., Proulx, L.I., Desnoyers, S., The DNA damage-inducible C. elegans tankyrase is a nuclear protein closely linked to chromosomes. Mol. Cell. Biochem. 324 (2009), 73–83.
    • (2009) Mol. Cell. Biochem. , vol.324 , pp. 73-83
    • White, C.1    Gagnon, S.N.2    St-Laurent, J.F.3    Gravel, C.4    Proulx, L.I.5    Desnoyers, S.6
  • 81
    • 83255171058 scopus 로고    scopus 로고
    • Structural basis and sequence rules for substrate recognition by Tankyrase explain the basis for cherubism disease
    • [81] Guettler, S., LaRose, J., Petsalaki, E., Gish, G., Scotter, A., Pawson, T., Rottapel, R., Sicheri, F., Structural basis and sequence rules for substrate recognition by Tankyrase explain the basis for cherubism disease. Cell 147 (2011), 1340–1354.
    • (2011) Cell , vol.147 , pp. 1340-1354
    • Guettler, S.1    LaRose, J.2    Petsalaki, E.3    Gish, G.4    Scotter, A.5    Pawson, T.6    Rottapel, R.7    Sicheri, F.8
  • 82
    • 84959894091 scopus 로고    scopus 로고
    • Tankyrases promote homologous recombination and check point activation in response to DSBs
    • [82] Nagy, Z., Kalousi, A., Furst, A., Koch, M., Fischer, B., Soutoglou, E., Tankyrases promote homologous recombination and check point activation in response to DSBs. PLoS Genet., 12, 2016, e1005791.
    • (2016) PLoS Genet. , vol.12 , pp. e1005791
    • Nagy, Z.1    Kalousi, A.2    Furst, A.3    Koch, M.4    Fischer, B.5    Soutoglou, E.6
  • 84
    • 84930756708 scopus 로고    scopus 로고
    • MERIT40 is an akt substrate that promotes resolution of DNA damage induced by chemotherapy
    • [84] Brown, K.K., Montaser-Kouhsari, L., Beck, A.H., Toker, A., MERIT40 is an akt substrate that promotes resolution of DNA damage induced by chemotherapy. Cell Rep. 11 (2015), 1358–1366.
    • (2015) Cell Rep. , vol.11 , pp. 1358-1366
    • Brown, K.K.1    Montaser-Kouhsari, L.2    Beck, A.H.3    Toker, A.4
  • 85
    • 0034672418 scopus 로고    scopus 로고
    • BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration
    • [85] Aguiar, R.C., Yakushijin, Y., Kharbanda, S., Salgia, R., Fletcher, J.A., Shipp, M.A., BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration. Blood 96 (2000), 4328–4334.
    • (2000) Blood , vol.96 , pp. 4328-4334
    • Aguiar, R.C.1    Yakushijin, Y.2    Kharbanda, S.3    Salgia, R.4    Fletcher, J.A.5    Shipp, M.A.6
  • 86
    • 84878644504 scopus 로고    scopus 로고
    • BAL1/ARTD9 represses the anti-proliferative and pro-apoptotic IFNgamma-STAT1-IRF1-p53 axis in diffuse large B-cell lymphoma
    • [86] Camicia, R., Bachmann, S.B., Winkler, H.C., Beer, M., Tinguely, M., Haralambieva, E., Hassa, P.O., BAL1/ARTD9 represses the anti-proliferative and pro-apoptotic IFNgamma-STAT1-IRF1-p53 axis in diffuse large B-cell lymphoma. J. Cell Sci. 126 (2013), 1969–1980.
    • (2013) J. Cell Sci. , vol.126 , pp. 1969-1980
    • Camicia, R.1    Bachmann, S.B.2    Winkler, H.C.3    Beer, M.4    Tinguely, M.5    Haralambieva, E.6    Hassa, P.O.7
  • 87
    • 26644446700 scopus 로고    scopus 로고
    • B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity
    • [87] Aguiar, R.C., Takeyama, K., He, C., Kreinbrink, K., Shipp, M.A., B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity. J. Biol. Chem. 280 (2005), 33756–33765.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33756-33765
    • Aguiar, R.C.1    Takeyama, K.2    He, C.3    Kreinbrink, K.4    Shipp, M.A.5
  • 88
    • 70349759491 scopus 로고    scopus 로고
    • BBAP monoubiquitylates histone H4 at lysine 91 and selectively modulates the DNA damage response
    • [88] Yan, Q., Dutt, S., Xu, R., Graves, K., Juszczynski, P., Manis, J.P., Shipp, M.A., BBAP monoubiquitylates histone H4 at lysine 91 and selectively modulates the DNA damage response. Mol. Cell. 36 (2009), 110–120.
    • (2009) Mol. Cell. , vol.36 , pp. 110-120
    • Yan, Q.1    Dutt, S.2    Xu, R.3    Graves, K.4    Juszczynski, P.5    Manis, J.P.6    Shipp, M.A.7
  • 89
    • 84900458533 scopus 로고    scopus 로고
    • The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell nuclear antigen (PCNA) and is required for DNA damage tolerance
    • [89] Nicolae, C.M., Aho, E.R., Vlahos, A.H., Choe, K.N., De, S., Karras, G.I., Moldovan, G.L., The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell nuclear antigen (PCNA) and is required for DNA damage tolerance. J. Biol. Chem. 289 (2014), 13627–13637.
    • (2014) J. Biol. Chem. , vol.289 , pp. 13627-13637
    • Nicolae, C.M.1    Aho, E.R.2    Vlahos, A.H.3    Choe, K.N.4    De, S.5    Karras, G.I.6    Moldovan, G.L.7
  • 90
    • 84942239332 scopus 로고    scopus 로고
    • A novel role for the mono-ADP-ribosyltransferase PARP14/ARTD8 in promoting homologous recombination and protecting against replication stress
    • [90] Nicolae, C.M., Aho, E.R., Choe, K.N., Constantin, D., Hu, H.J., Lee, D., Myung, K., Moldovan, G.L., A novel role for the mono-ADP-ribosyltransferase PARP14/ARTD8 in promoting homologous recombination and protecting against replication stress. Nucleic Acids Res. 43 (2015), 3143–3153.
    • (2015) Nucleic Acids Res. , vol.43 , pp. 3143-3153
    • Nicolae, C.M.1    Aho, E.R.2    Choe, K.N.3    Constantin, D.4    Hu, H.J.5    Lee, D.6    Myung, K.7    Moldovan, G.L.8
  • 93
    • 84863974838 scopus 로고    scopus 로고
    • Sirtuin 6 (SIRT6) rescues the decline of homologous recombination repair during replicative senescence
    • [93] Mao, Z., Tian, X., Van Meter, M., Ke, Z., Gorbunova, V., Seluanov, A., Sirtuin 6 (SIRT6) rescues the decline of homologous recombination repair during replicative senescence. Proc. Natl. Acad. Sci. U. S. A. 109 (2012), 11800–11805.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 11800-11805
    • Mao, Z.1    Tian, X.2    Van Meter, M.3    Ke, Z.4    Gorbunova, V.5    Seluanov, A.6
  • 95
    • 2942707644 scopus 로고    scopus 로고
    • Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments
    • [95] Meyer-Ficca, M.L., Meyer, R.G., Coyle, D.L., Jacobson, E.L., Jacobson, M.K., Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments. Exp. Cell Res. 297 (2004), 521–532.
    • (2004) Exp. Cell Res. , vol.297 , pp. 521-532
    • Meyer-Ficca, M.L.1    Meyer, R.G.2    Coyle, D.L.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 96
    • 79960206370 scopus 로고    scopus 로고
    • PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-dependent mechanisms
    • [96] Mortusewicz, O., Fouquerel, E., Ame, J.C., Leonhardt, H., Schreiber, V., PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-dependent mechanisms. Nucleic Acids Res. 39 (2011), 5045–5056.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 5045-5056
    • Mortusewicz, O.1    Fouquerel, E.2    Ame, J.C.3    Leonhardt, H.4    Schreiber, V.5
  • 97
    • 78649815064 scopus 로고    scopus 로고
    • Deletion of the nuclear isoform of poly(ADP-ribose) glycohydrolase (PARG) reveals its function in DNA repair, genomic stability and tumorigenesis
    • [97] Min, W., Cortes, U., Herceg, Z., Tong, W.M., Wang, Z.Q., Deletion of the nuclear isoform of poly(ADP-ribose) glycohydrolase (PARG) reveals its function in DNA repair, genomic stability and tumorigenesis. Carcinogenesis 31 (2010), 2058–2065.
    • (2010) Carcinogenesis , vol.31 , pp. 2058-2065
    • Min, W.1    Cortes, U.2    Herceg, Z.3    Tong, W.M.4    Wang, Z.Q.5
  • 100
    • 70349658096 scopus 로고    scopus 로고
    • Dual role of poly(ADP-ribose) glycohydrolase in the regulation of cell death in oxidatively stressed A549 cells
    • [100] Erdelyi, K., Bai, P., Kovacs, I., Szabo, E., Mocsar, G., Kakuk, A., Szabo, C., Gergely, P., Virag, L., Dual role of poly(ADP-ribose) glycohydrolase in the regulation of cell death in oxidatively stressed A549 cells. FASEB J. 23 (2009), 3553–3563.
    • (2009) FASEB J. , vol.23 , pp. 3553-3563
    • Erdelyi, K.1    Bai, P.2    Kovacs, I.3    Szabo, E.4    Mocsar, G.5    Kakuk, A.6    Szabo, C.7    Gergely, P.8    Virag, L.9
  • 101
    • 84903954677 scopus 로고    scopus 로고
    • PARG is dispensable for recovery from transient replicative stress but required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress
    • (in press)
    • [101] Illuzzi, G., Fouquerel, E., Amé, J.-C., Noll, A., Rehmet, K., Nasheuer, H.-P., Dantzer, F., Schreiber, V., PARG is dispensable for recovery from transient replicative stress but required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress. Nucleic Acids Res., 2014 (in press).
    • (2014) Nucleic Acids Res.
    • Illuzzi, G.1    Fouquerel, E.2    Amé, J.-C.3    Noll, A.4    Rehmet, K.5    Nasheuer, H.-P.6    Dantzer, F.7    Schreiber, V.8
  • 102
    • 84879641430 scopus 로고    scopus 로고
    • PARG dysfunction enhances DNA double strand break formation in S-phase after alkylation DNA damage and augments different cell death pathways
    • [102] Shirai, H., Poetsch, A.R., Gunji, A., Maeda, D., Fujimori, H., Fujihara, H., Yoshida, T., Ogino, H., Masutani, M., PARG dysfunction enhances DNA double strand break formation in S-phase after alkylation DNA damage and augments different cell death pathways. Cell. Death. Dis., 4, 2013, e656.
    • (2013) Cell. Death. Dis. , vol.4 , pp. e656
    • Shirai, H.1    Poetsch, A.R.2    Gunji, A.3    Maeda, D.4    Fujimori, H.5    Fujihara, H.6    Yoshida, T.7    Ogino, H.8    Masutani, M.9
  • 103
    • 84922196613 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl) glycohydrolase prevents the accumulation of unusual replication structures during unperturbed S phase
    • [103] Ray Chaudhuri, A., Ahuja, A.K., Herrador, R., Lopes, M., Poly(ADP-ribosyl) glycohydrolase prevents the accumulation of unusual replication structures during unperturbed S phase. Mol. Cell. Biol. 35 (2015), 856–865.
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 856-865
    • Ray Chaudhuri, A.1    Ahuja, A.K.2    Herrador, R.3    Lopes, M.4
  • 104
    • 33644849513 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase
    • [104] Oka, S., Kato, J., Moss, J., Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 281 (2006), 705–713.
    • (2006) J. Biol. Chem. , vol.281 , pp. 705-713
    • Oka, S.1    Kato, J.2    Moss, J.3
  • 105
    • 84860844237 scopus 로고    scopus 로고
    • ADP-ribosylhydrolase 3 (ARH3) not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose)
    • [105] Niere, M., Mashimo, M., Agledal, L., Dolle, C., Kasamatsu, A., Kato, J., Moss, J., Ziegler, M., ADP-ribosylhydrolase 3 (ARH3) not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose). J. Biol. Chem. 287 (2012), 16088–16102.
    • (2012) J. Biol. Chem. , vol.287 , pp. 16088-16102
    • Niere, M.1    Mashimo, M.2    Agledal, L.3    Dolle, C.4    Kasamatsu, A.5    Kato, J.6    Moss, J.7    Ziegler, M.8
  • 106
    • 84888110477 scopus 로고    scopus 로고
    • ADP-ribosyl-acceptor hydrolase 3 regulates poly (ADP-ribose) degradation and cell death during oxidative stress
    • [106] Mashimo, M., Kato, J., Moss, J., ADP-ribosyl-acceptor hydrolase 3 regulates poly (ADP-ribose) degradation and cell death during oxidative stress. Proc. Natl. Acad. Sci. U. S. A. 110 (2013), 18964–18969.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 18964-18969
    • Mashimo, M.1    Kato, J.2    Moss, J.3
  • 108
    • 84921367731 scopus 로고    scopus 로고
    • Synthetic lethality and cancer therapy: lessons learned from the development of PARP inhibitors
    • [108] Lord, C.J., Tutt, A.N., Ashworth, A., Synthetic lethality and cancer therapy: lessons learned from the development of PARP inhibitors. Annu. Rev. Med. 66 (2015), 455–470.
    • (2015) Annu. Rev. Med. , vol.66 , pp. 455-470
    • Lord, C.J.1    Tutt, A.N.2    Ashworth, A.3
  • 109
    • 84944741450 scopus 로고    scopus 로고
    • From poly(ADP-ribose) discovery to PARP inhibitors in cancer therapy
    • [109] Schreiber, V., Illuzzi, G., Heberle, E., Dantzer, F., From poly(ADP-ribose) discovery to PARP inhibitors in cancer therapy. Bull. Cancer 102 (2015), 863–873.
    • (2015) Bull. Cancer , vol.102 , pp. 863-873
    • Schreiber, V.1    Illuzzi, G.2    Heberle, E.3    Dantzer, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.