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Volumn 19, Issue , 2014, Pages 108-113

Protein ADP-ribosylation and the cellular response to DNA strand breaks

Author keywords

Base excision repair; DNA double strand break; DNA single strand break; Homologous recombination; Non homologous end joining; Poly(ADP ribose) polymerase; Single strand break repair

Indexed keywords

NAKED DNA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN; XRCC1 PROTEIN; DNA BINDING PROTEIN;

EID: 84902086815     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2014.03.021     Document Type: Article
Times cited : (105)

References (91)
  • 2
    • 84873524967 scopus 로고    scopus 로고
    • PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis
    • Langelier M.-F., Pascal J.M. PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis. Curr. Opin. Struct. Biol. 2013, 23:134-143.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 134-143
    • Langelier, M.-F.1    Pascal, J.M.2
  • 3
    • 84870392591 scopus 로고    scopus 로고
    • Towards a structural understanding of PARP1 activation and related signalling ADP-ribosyl-transferases
    • Hassler M., Ladurner A.G. Towards a structural understanding of PARP1 activation and related signalling ADP-ribosyl-transferases. Curr. Opin. Struct. Biol. 2012, 22:721-729.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 721-729
    • Hassler, M.1    Ladurner, A.G.2
  • 5
    • 84876715061 scopus 로고    scopus 로고
    • A genetic screen using the PiggyBac transposon in haploid cells identifies PARP1 as a mediator of olaparib toxicity
    • Pettitt S.J., Rehman F.L., Bajrami I., Brough R., Wallberg F., Kozarewa I., et al. A genetic screen using the PiggyBac transposon in haploid cells identifies PARP1 as a mediator of olaparib toxicity. PLoS One 2013, 8:e61520.
    • (2013) PLoS One , vol.8
    • Pettitt, S.J.1    Rehman, F.L.2    Bajrami, I.3    Brough, R.4    Wallberg, F.5    Kozarewa, I.6
  • 7
    • 84861231399 scopus 로고    scopus 로고
    • The diverse roles and clinical relevance of PARPs in DNA damage repair: current state of the art
    • 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. 2012, 84:137-146.
    • (2012) Biochem. Pharmacol. , vol.84 , pp. 137-146
    • De Vos, M.1    Schreiber, V.2    Dantzer, F.3
  • 8
    • 48249095920 scopus 로고    scopus 로고
    • Single-strand break repair and genetic disease
    • Caldecott K.W. Single-strand break repair and genetic disease. Nat. Rev. Genet. 2008, 9:619-631.
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 619-631
    • Caldecott, K.W.1
  • 9
    • 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., Amé J.-C., Dollé P., Schultz I., Rinaldi B., Fraulob 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. 2002, 277:23028-23036.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23028-23036
    • Schreiber, V.1    Amé, J.-C.2    Dollé, P.3    Schultz, I.4    Rinaldi, B.5    Fraulob, V.6
  • 12
    • 0033539651 scopus 로고    scopus 로고
    • Chromosomal aberrations in PARP(-/-) mice: genome stabilization in immortalized cells by reintroduction of poly(ADP-ribose) polymerase cDNA
    • Simbulan-Rosenthal C.M., Haddad B.R., Rosenthal D.S., Weaver Z., Coleman A., Luo R., et al. Chromosomal aberrations in PARP(-/-) mice: genome stabilization in immortalized cells by reintroduction of poly(ADP-ribose) polymerase cDNA. Proc. Nat. Acad. Sci. U.S.A. 1999, 96:13191-13196.
    • (1999) Proc. Nat. Acad. Sci. U.S.A. , vol.96 , pp. 13191-13196
    • Simbulan-Rosenthal, C.M.1    Haddad, B.R.2    Rosenthal, D.S.3    Weaver, Z.4    Coleman, A.5    Luo, R.6
  • 14
    • 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.) 2002, 1:547-558.
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 547-558
    • Sanderson, R.J.1    Lindahl, T.2
  • 15
    • 84886719040 scopus 로고    scopus 로고
    • PARP-1 and gene regulation: progress and puzzles
    • Kraus W.L., Hottiger M.O. PARP-1 and gene regulation: progress and puzzles. Mol. Aspects Med. 2013, 34:1109-1123.
    • (2013) Mol. Aspects Med. , vol.34 , pp. 1109-1123
    • Kraus, W.L.1    Hottiger, M.O.2
  • 16
    • 0020479276 scopus 로고
    • Poly(ADP-ribosylation) in vitro. Reaction parameters and enzyme mechanism
    • Ferro A.M., Olivera B.M. Poly(ADP-ribosylation) in vitro. Reaction parameters and enzyme mechanism. J. Biol. Chem. 1982, 257:7808-7813.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7808-7813
    • Ferro, A.M.1    Olivera, B.M.2
  • 17
    • 0020200025 scopus 로고
    • A shuttle mechanism for DNA-protein interactions. The regulation of poly(ADP-ribose) polymerase
    • Zahradka P., Ebisuzaki K. A shuttle mechanism for DNA-protein interactions. The regulation of poly(ADP-ribose) polymerase. Eur. J. Biochem. 1982, 127:579-585.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 579-585
    • Zahradka, P.1    Ebisuzaki, K.2
  • 18
    • 84879566553 scopus 로고    scopus 로고
    • Roles of poly(ADP-ribose) glycohydrolase in DNA damage and apoptosis
    • Feng X., Koh D.W. Roles of poly(ADP-ribose) glycohydrolase in DNA damage and apoptosis. Int. Rev. Cell Mol. Biol. 2013, 304:227-281.
    • (2013) Int. Rev. Cell Mol. Biol. , vol.304 , pp. 227-281
    • Feng, X.1    Koh, D.W.2
  • 19
    • 0026507413 scopus 로고
    • Role of poly(ADP-ribose) formation in DNA repair
    • Satoh M.S., Lindahl T. Role of poly(ADP-ribose) formation in DNA repair. Nature 1992, 356:356-358.
    • (1992) Nature , vol.356 , pp. 356-358
    • Satoh, M.S.1    Lindahl, T.2
  • 20
    • 34547225606 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 accelerates single-strand break repair in concert with poly(ADP-ribose) glycohydrolase
    • Fisher A.E.O., 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. 2007, 27:5597-5605.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5597-5605
    • Fisher, A.E.O.1    Hochegger, H.2    Takeda, S.3    Caldecott, K.W.4
  • 21
    • 43849110460 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 modulates DNA repair capacity and prevents formation of DNA double strand breaks
    • Woodhouse B.C., Dianova I.I., Parsons J.L., Dianov G.L. Poly(ADP-ribose) polymerase-1 modulates DNA repair capacity and prevents formation of DNA double strand breaks. DNA Repair (Amst.) 2008, 7:932-940.
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 932-940
    • Woodhouse, B.C.1    Dianova, I.I.2    Parsons, J.L.3    Dianov, G.L.4
  • 22
    • 84860113578 scopus 로고    scopus 로고
    • Differential effects of poly(ADP-ribose) polymerase inhibition on DNA break repair in human cells are revealed with Epstein-Barr virus
    • Ma W., Halweg C.J., Menendez D., Resnick M.A. Differential effects of poly(ADP-ribose) polymerase inhibition on DNA break repair in human cells are revealed with Epstein-Barr virus. Proc. Nat. Acad. Sci. U.S.A. 2012, 109:6590-6595.
    • (2012) Proc. Nat. Acad. Sci. U.S.A. , vol.109 , pp. 6590-6595
    • Ma, W.1    Halweg, C.J.2    Menendez, D.3    Resnick, M.A.4
  • 23
    • 0041378046 scopus 로고    scopus 로고
    • XRCC1 and DNA strand break repair
    • Caldecott K.W. XRCC1 and DNA strand break repair. DNA Repair (Amst.) 2003, 2:955-969.
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 955-969
    • Caldecott, K.W.1
  • 24
    • 0033955346 scopus 로고    scopus 로고
    • XRCC1 keeps DNA from getting stranded
    • Thompson L.H., West M.G. XRCC1 keeps DNA from getting stranded. Mutat. Res. 2000, 459:1-18.
    • (2000) Mutat. Res. , vol.459 , pp. 1-18
    • Thompson, L.H.1    West, M.G.2
  • 25
    • 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. 1996, 24:4387-4394.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4387-4394
    • Caldecott, K.W.1    Aoufouchi, S.2    Johnson, P.3    Shall, S.4
  • 26
    • 0031844311 scopus 로고    scopus 로고
    • XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
    • Masson M., Niedergang C., Schreiber V., Muller S., Menissier-de Murcia J., de Murcia G. XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol. Cell. Biol. 1998, 18:3563-3571.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3563-3571
    • Masson, M.1    Niedergang, C.2    Schreiber, V.3    Muller, S.4    Menissier-de Murcia, J.5    de Murcia, G.6
  • 27
    • 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. 2003, 31:5526-5533.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5526-5533
    • El-Khamisy, S.F.1    Masutani, M.2    Suzuki, H.3    Caldecott, K.W.4
  • 28
    • 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. 2003, 23:3974-3981.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3974-3981
    • Okano, S.1    Lan, L.2    Caldecott, K.W.3    Mori, T.4    Yasui, A.5
  • 29
    • 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. 2000, 275:40974-40980.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 30
    • 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.) 2007, 6:443-453.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 443-453
    • Caldecott, K.W.1
  • 31
    • 34248157719 scopus 로고    scopus 로고
    • APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks
    • 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. 2007, 27:3793-3803.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3793-3803
    • Iles, N.1    Rulten, S.2    El-Khamisy, S.F.3    Caldecott, K.W.4
  • 32
    • 47049104588 scopus 로고    scopus 로고
    • APLF (C2orf13) is a novel component of poly(ADP-ribose) signaling in mammalian cells
    • Rulten S.L., Cortes Ledesma F., Guo L., Iles N.J., Caldecott K.W. APLF (C2orf13) is a novel component of poly(ADP-ribose) signaling in mammalian cells. Mol. Cell. Biol. 2008, 28:4620-4628.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4620-4628
    • Rulten, S.L.1    Cortes Ledesma, F.2    Guo, L.3    Iles, N.J.4    Caldecott, K.W.5
  • 34
    • 34247245102 scopus 로고    scopus 로고
    • A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses
    • Kanno S.-I., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S., et al. A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. EMBO J. 2007, 26:2094-2103.
    • (2007) EMBO J. , vol.26 , pp. 2094-2103
    • Kanno, S.-I.1    Kuzuoka, H.2    Sasao, S.3    Hong, Z.4    Lan, L.5    Nakajima, S.6
  • 36
    • 84871605560 scopus 로고    scopus 로고
    • Activation of the SNF2 family ATPase ALC1 by poly(ADP-ribose) in a stable ALC1·PARP1·nucleosome intermediate
    • Gottschalk A.J., Trivedi R.D., Conaway J.W., Conaway R.C. Activation of the SNF2 family ATPase ALC1 by poly(ADP-ribose) in a stable ALC1·PARP1·nucleosome intermediate. J. Biol. Chem. 2012, 287:43527-43532.
    • (2012) J. Biol. Chem. , vol.287 , pp. 43527-43532
    • Gottschalk, A.J.1    Trivedi, R.D.2    Conaway, J.W.3    Conaway, R.C.4
  • 37
    • 69549083315 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler
    • Gottschalk A.J., Timinszky G., Kong S.E., Jin J., Cai Y., Swanson S.K., et al. Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler. Proc. Nat. Acad. Sci. U.S.A. 2009, 106:13770-13774.
    • (2009) Proc. Nat. Acad. Sci. U.S.A. , vol.106 , pp. 13770-13774
    • Gottschalk, A.J.1    Timinszky, G.2    Kong, S.E.3    Jin, J.4    Cai, Y.5    Swanson, S.K.6
  • 38
    • 69949123856 scopus 로고    scopus 로고
    • Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1
    • Ahel D., Horejsí Z., Wiechens N., Polo S.E., Garcia-Wilson E., Ahel I., et al. Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1. Science 2009, 325:1240-1243.
    • (2009) Science , vol.325 , pp. 1240-1243
    • Ahel, D.1    Horejsí, Z.2    Wiechens, N.3    Polo, S.E.4    Garcia-Wilson, E.5    Ahel, I.6
  • 39
    • 78650399787 scopus 로고    scopus 로고
    • Substrate channeling in mammalian base excision repair pathways: passing the baton
    • Prasad R., Shock D.D., Beard W.A., Wilson S.H. Substrate channeling in mammalian base excision repair pathways: passing the baton. J. Biol. Chem. 2010, 285:40479-40488.
    • (2010) J. Biol. Chem. , vol.285 , pp. 40479-40488
    • Prasad, R.1    Shock, D.D.2    Beard, W.A.3    Wilson, S.H.4
  • 41
    • 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. 1992, 267:12804-12812.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12804-12812
    • Ding, R.1    Pommier, Y.2    Kang, V.H.3    Smulson, M.4
  • 43
    • 79955588797 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase (PARP) is not involved in base excision repair but PARP inhibition traps a single-strand intermediate
    • Ström C.E., Johansson F., Uhlén M., Szigyarto C.A.-K., Erixon K., Helleday T. Poly(ADP-ribose) polymerase (PARP) is not involved in base excision repair but PARP inhibition traps a single-strand intermediate. Nucleic Acids Res. 2011, 39:3166-3175.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 3166-3175
    • Ström, C.E.1    Johansson, F.2    Uhlén, M.3    Szigyarto, C.A.-K.4    Erixon, K.5    Helleday, T.6
  • 44
    • 0034667921 scopus 로고    scopus 로고
    • Base excision repair is efficient in cells lacking poly(ADP-ribose) polymerase 1
    • Vodenicharov M.D., Sallmann F.R., Satoh M.S., Poirier G.G. Base excision repair is efficient in cells lacking poly(ADP-ribose) polymerase 1. Nucleic Acids Res. 2000, 28:3887-3896.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3887-3896
    • Vodenicharov, M.D.1    Sallmann, F.R.2    Satoh, M.S.3    Poirier, G.G.4
  • 45
    • 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. 2003, 278:18471-18477.
    • (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
  • 46
    • 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., Lavrik O.I., Kim S.J., Kedar P., Yang X.P., Vande Berg B.J., et al. DNA polymerase beta -mediated long patch base excision repair. Poly(ADP-ribose)polymerase-1 stimulates strand displacement DNA synthesis. J. Biol. Chem. 2001, 276:32411-32414.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32411-32414
    • Prasad, R.1    Lavrik, O.I.2    Kim, S.J.3    Kedar, P.4    Yang, X.P.5    Vande Berg, B.J.6
  • 48
    • 59449101071 scopus 로고    scopus 로고
    • PARP-1 ensures regulation of replication fork progression by homologous recombination on damaged DNA
    • Sugimura K., Takebayashi S.-I., Taguchi H., Takeda S., Okumura K. PARP-1 ensures regulation of replication fork progression by homologous recombination on damaged DNA. J. Cell Biol. 2008, 183:1203-1212.
    • (2008) J. Cell Biol. , vol.183 , pp. 1203-1212
    • Sugimura, K.1    Takebayashi, S.-I.2    Taguchi, H.3    Takeda, S.4    Okumura, K.5
  • 49
    • 33645288259 scopus 로고    scopus 로고
    • Parp-1 protects homologous recombination from interference by Ku and Ligase IV in vertebrate cells
    • Hochegger H., Dejsuphong D., Fukushima T., Morrison C., Sonoda E., Schreiber V., et al. Parp-1 protects homologous recombination from interference by Ku and Ligase IV in vertebrate cells. EMBO J. 2006, 25:1305-1314.
    • (2006) EMBO J. , vol.25 , pp. 1305-1314
    • Hochegger, H.1    Dejsuphong, D.2    Fukushima, T.3    Morrison, C.4    Sonoda, E.5    Schreiber, V.6
  • 50
    • 77950958141 scopus 로고    scopus 로고
    • 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks
    • Bunting S.F., Callén E., Wong N., Chen H.-T., Polato F., Gunn A., et al. 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks. Cell 2010, 141:243-254.
    • (2010) Cell , vol.141 , pp. 243-254
    • Bunting, S.F.1    Callén, E.2    Wong, N.3    Chen, H.-T.4    Polato, F.5    Gunn, A.6
  • 51
    • 79952747328 scopus 로고    scopus 로고
    • Nonhomologous end joining drives poly(ADP-ribose) polymerase (PARP) inhibitor lethality in homologous recombination-deficient cells
    • Patel A.G., Sarkaria J.N., Kaufmann S.H. Nonhomologous end joining drives poly(ADP-ribose) polymerase (PARP) inhibitor lethality in homologous recombination-deficient cells. Proc. Nat. Acad. Sci. U.S.A. 2011, 108:3406-3411.
    • (2011) Proc. Nat. Acad. Sci. U.S.A. , vol.108 , pp. 3406-3411
    • Patel, A.G.1    Sarkaria, J.N.2    Kaufmann, S.H.3
  • 52
    • 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
    • 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 2004, 23:3872-3882.
    • (2004) Oncogene , vol.23 , pp. 3872-3882
    • Yang, Y.-G.1    Cortes, U.2    Patnaik, S.3    Jasin, M.4    Wang, Z.-Q.5
  • 53
    • 69849097500 scopus 로고    scopus 로고
    • PARP is activated at stalled forks to mediate Mre11-dependent replication restart and recombination
    • Bryant H.E., Petermann E., Schultz N., Jemth A.-S., Loseva O., Issaeva N., et al. PARP is activated at stalled forks to mediate Mre11-dependent replication restart and recombination. EMBO J. 2009, 28:2601-2615.
    • (2009) EMBO J. , vol.28 , pp. 2601-2615
    • Bryant, H.E.1    Petermann, E.2    Schultz, N.3    Jemth, A.-S.4    Loseva, O.5    Issaeva, N.6
  • 54
    • 84861888851 scopus 로고    scopus 로고
    • Mre11-dependent degradation of stalled DNA replication forks is prevented by BRCA2 and PARP1
    • Ying S., Hamdy F.C., Helleday T. Mre11-dependent degradation of stalled DNA replication forks is prevented by BRCA2 and PARP1. Cancer Res. 2012, 72:2814-2821.
    • (2012) Cancer Res. , vol.72 , pp. 2814-2821
    • Ying, S.1    Hamdy, F.C.2    Helleday, T.3
  • 55
    • 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 2001, 23:447-455.
    • (2001) Bioessays , vol.23 , pp. 447-455
    • Caldecott, K.W.1
  • 56
    • 0019956767 scopus 로고
    • A CHO-cell strain having hypersensitivity to mutagens, a defect in DNA strand-break repair, and an extraordinary baseline frequency of sister-chromatid exchange
    • Thompson L.H., Brookman K.W., Dillehay L.E., Carrano A.V., Mazrimas J.A., Mooney C.L., et al. A CHO-cell strain having hypersensitivity to mutagens, a defect in DNA strand-break repair, and an extraordinary baseline frequency of sister-chromatid exchange. Mutat. Res. 1982, 95:427-440.
    • (1982) Mutat. Res. , vol.95 , pp. 427-440
    • Thompson, L.H.1    Brookman, K.W.2    Dillehay, L.E.3    Carrano, A.V.4    Mazrimas, J.A.5    Mooney, C.L.6
  • 58
    • 81955161844 scopus 로고    scopus 로고
    • DNA double-strand break repair pathways, chromosomal rearrangements and cancer
    • Kasparek T.R., Humphrey T.C. DNA double-strand break repair pathways, chromosomal rearrangements and cancer. Semin. Cell Dev. Biol. 2011, 22:886-897.
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 886-897
    • Kasparek, T.R.1    Humphrey, T.C.2
  • 59
    • 79956215808 scopus 로고    scopus 로고
    • Induction and repair of DNA double strand breaks: the increasing spectrum of non-homologous end joining pathways
    • Mladenov E., Iliakis G. Induction and repair of DNA double strand breaks: the increasing spectrum of non-homologous end joining pathways. Mutat. Res. 2011, 711:61-72.
    • (2011) Mutat. Res. , vol.711 , pp. 61-72
    • Mladenov, E.1    Iliakis, G.2
  • 60
    • 0025640847 scopus 로고
    • The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA
    • Ikejima M., Noguchi S., Yamashita R., Ogura T., Sugimura T., Gill D.M., et al. The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA. J. Biol. Chem. 1990, 265:21907-21913.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21907-21913
    • Ikejima, M.1    Noguchi, S.2    Yamashita, R.3    Ogura, T.4    Sugimura, T.5    Gill, D.M.6
  • 62
    • 0033575278 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase and Ku autoantigen form a complex and synergistically bind to matrix attachment sequences
    • Galande S., Kohwi-Shigematsu T. Poly(ADP-ribose) polymerase and Ku autoantigen form a complex and synergistically bind to matrix attachment sequences. J. Biol. Chem. 1999, 274:20521-20528.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20521-20528
    • Galande, S.1    Kohwi-Shigematsu, T.2
  • 64
    • 84876328368 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation links the chromatin remodeler SMARCA5/SNF2H to RNF168-dependent DNA damage signaling
    • Smeenk G., Wiegant W.W., Marteijn J.A., Luijsterburg M.S., Sroczynski N., Costelloe T., et al. Poly(ADP-ribosyl)ation links the chromatin remodeler SMARCA5/SNF2H to RNF168-dependent DNA damage signaling. J. Cell Sci. 2013, 126:889-903.
    • (2013) J. Cell Sci. , vol.126 , pp. 889-903
    • Smeenk, G.1    Wiegant, W.W.2    Marteijn, J.A.3    Luijsterburg, M.S.4    Sroczynski, N.5    Costelloe, T.6
  • 66
    • 2342657887 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase (PARP-1) is not involved in DNA double-strand break recovery
    • Noël G., Giocanti N., Fernet M., Mégnin-Chanet F., Favaudon V. Poly(ADP-ribose) polymerase (PARP-1) is not involved in DNA double-strand break recovery. BMC Cell Biol. 2003, 4:7.
    • (2003) BMC Cell Biol. , vol.4 , pp. 7
    • Noël, G.1    Giocanti, N.2    Fernet, M.3    Mégnin-Chanet, F.4    Favaudon, V.5
  • 67
    • 78650756134 scopus 로고    scopus 로고
    • PARP-3 and APLF function together to accelerate nonhomologous end-joining
    • Rulten S.L., Fisher A.E.O., Robert I., Zuma M.C., Rouleau M., Ju L., et al. PARP-3 and APLF function together to accelerate nonhomologous end-joining. Mol. Cell 2011, 41:33-45.
    • (2011) Mol. Cell , vol.41 , pp. 33-45
    • Rulten, S.L.1    Fisher, A.E.O.2    Robert, I.3    Zuma, M.C.4    Rouleau, M.5    Ju, L.6
  • 68
    • 38049064044 scopus 로고    scopus 로고
    • Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins
    • Ahel I., Ahel D., Matsusaka T., Clark A.J., Pines J., Boulton S.J., et al. Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Nature 2008, 451:81-85.
    • (2008) Nature , vol.451 , pp. 81-85
    • Ahel, I.1    Ahel, D.2    Matsusaka, T.3    Clark, A.J.4    Pines, J.5    Boulton, S.J.6
  • 69
    • 76349105464 scopus 로고    scopus 로고
    • Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)
    • Eustermann S., Brockmann C., Mehrotra P.V., Yang J.-C., Loakes D., West S.C., et al. Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose). Nat. Struct. Mol. Biol. 2010, 17:241-243.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 241-243
    • Eustermann, S.1    Brockmann, C.2    Mehrotra, P.V.3    Yang, J.-C.4    Loakes, D.5    West, S.C.6
  • 70
    • 77952716489 scopus 로고    scopus 로고
    • Structure and identification of ADP-ribose recognition motifs of APLF and role in the DNA damage response
    • Li G.-Y., McCulloch R.D., Fenton A.L., Cheung M., Meng L., Ikura M., et al. Structure and identification of ADP-ribose recognition motifs of APLF and role in the DNA damage response. Proc. Nat. Acad. Sci. U.S.A. 2010, 107:9129-9134.
    • (2010) Proc. Nat. Acad. Sci. U.S.A. , vol.107 , pp. 9129-9134
    • Li, G.-Y.1    McCulloch, R.D.2    Fenton, A.L.3    Cheung, M.4    Meng, L.5    Ikura, M.6
  • 71
    • 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)
    • Oberoi J., Richards M.W., Crumpler S., Brown N., Blagg J., Bayliss R. Structural basis of poly(ADP-ribose) recognition by the multizinc binding domain of checkpoint with forkhead-associated and RING Domains (CHFR). J. Biol. Chem. 2010, 285:39348-39358.
    • (2010) J. Biol. Chem. , vol.285 , pp. 39348-39358
    • Oberoi, J.1    Richards, M.W.2    Crumpler, S.3    Brown, N.4    Blagg, J.5    Bayliss, R.6
  • 73
    • 80054683238 scopus 로고    scopus 로고
    • Polynucleotide kinase and aprataxin-like forkhead-associated protein (PALF) acts as both a single-stranded DNA endonuclease and a single-stranded DNA 3' exonuclease and can participate in DNA end joining in a biochemical system
    • Li S., Kanno S.-I., Watanabe R., Ogiwara H., Kohno T., Watanabe G., et al. Polynucleotide kinase and aprataxin-like forkhead-associated protein (PALF) acts as both a single-stranded DNA endonuclease and a single-stranded DNA 3' exonuclease and can participate in DNA end joining in a biochemical system. J. Biol. Chem. 2011, 286:36368-36377.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36368-36377
    • Li, S.1    Kanno, S.-I.2    Watanabe, R.3    Ogiwara, H.4    Kohno, T.5    Watanabe, G.6
  • 76
    • 33845657443 scopus 로고    scopus 로고
    • PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways
    • Wang M., Wu W., Wu W., Rosidi B., Zhang L., Wang H., et al. PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways. Nucleic Acids Res. 2006, 34:6170-6182.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 6170-6182
    • Wang, M.1    Wu, W.2    Wu, W.3    Rosidi, B.4    Zhang, L.5    Wang, H.6
  • 77
    • 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. 2004, 279:55117-55126.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55117-55126
    • Audebert, M.1    Salles, B.2    Calsou, P.3
  • 78
    • 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
    • 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. 2010, 38:6065-6077.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 6065-6077
    • Mansour, W.Y.1    Rhein, T.2    Dahm-Daphi, J.3
  • 79
    • 79959814259 scopus 로고    scopus 로고
    • DNA ligase III promotes alternative nonhomologous end-joining during chromosomal translocation formation
    • Simsek D., Brunet E., Wong S.Y.-W., Katyal S., Gao Y., McKinnon P.J., et al. DNA ligase III promotes alternative nonhomologous end-joining during chromosomal translocation formation. PLoS Genet. 2011, 7:e1002080.
    • (2011) PLoS Genet. , vol.7
    • Simsek, D.1    Brunet, E.2    Wong, S.Y.-W.3    Katyal, S.4    Gao, Y.5    McKinnon, P.J.6
  • 80
    • 20144363082 scopus 로고    scopus 로고
    • DNA ligase III as a candidate component of backup pathways of nonhomologous end joining
    • Wang H., Rosidi B., Perrault R., Wang M., Zhang L., Windhofer F., et al. DNA ligase III as a candidate component of backup pathways of nonhomologous end joining. Cancer Res. 2005, 65:4020-4030.
    • (2005) Cancer Res. , vol.65 , pp. 4020-4030
    • Wang, H.1    Rosidi, B.2    Perrault, R.3    Wang, M.4    Zhang, L.5    Windhofer, F.6
  • 81
    • 37549006429 scopus 로고    scopus 로고
    • Repair of radiation induced DNA double strand breaks by backup NHEJ is enhanced in G2
    • Wu W., Wang M., Wu W., Singh S.K., Mussfeldt T., Iliakis G. Repair of radiation induced DNA double strand breaks by backup NHEJ is enhanced in G2. DNA Repair (Amst.) 2008, 7:329-338.
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 329-338
    • Wu, W.1    Wang, M.2    Wu, W.3    Singh, S.K.4    Mussfeldt, T.5    Iliakis, G.6
  • 82
    • 69949173301 scopus 로고    scopus 로고
    • Backup pathways of NHEJ in cells of higher eukaryotes: cell cycle dependence
    • Iliakis G. Backup pathways of NHEJ in cells of higher eukaryotes: cell cycle dependence. Radiother. Oncol. 2009, 92:310-315.
    • (2009) Radiother. Oncol. , vol.92 , pp. 310-315
    • Iliakis, G.1
  • 83
    • 84863411679 scopus 로고    scopus 로고
    • Time-dependent predominance of nonhomologous DNA end-joining pathways during embryonic development in mice
    • Chiruvella K.K., Sebastian R., Sharma S., Karande A.A., Choudhary B., Raghavan S.C. Time-dependent predominance of nonhomologous DNA end-joining pathways during embryonic development in mice. J. Mol. Biol. 2012, 417:197-211.
    • (2012) J. Mol. Biol. , vol.417 , pp. 197-211
    • Chiruvella, K.K.1    Sebastian, R.2    Sharma, S.3    Karande, A.A.4    Choudhary, B.5    Raghavan, S.C.6
  • 84
    • 34547589577 scopus 로고    scopus 로고
    • Formation of NHEJ-derived reciprocal chromosomal translocations does not require Ku70
    • Weinstock D.M., Brunet E., Jasin M. Formation of NHEJ-derived reciprocal chromosomal translocations does not require Ku70. Nat. Cell Biol. 2007, 9:978-981.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 978-981
    • Weinstock, D.M.1    Brunet, E.2    Jasin, M.3
  • 85
    • 77950462986 scopus 로고    scopus 로고
    • Alternative end-joining is suppressed by the canonical NHEJ component XRCC4-ligase IV during chromosomal translocation formation
    • Simsek D., Jasin M. Alternative end-joining is suppressed by the canonical NHEJ component XRCC4-ligase IV during chromosomal translocation formation. Nat. Struct. Mol. Biol. 2010, 17:410-416.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 410-416
    • Simsek, D.1    Jasin, M.2
  • 86
    • 77649267656 scopus 로고    scopus 로고
    • Alternative end-joining catalyzes robust IgH locus deletions and translocations in the combined absence of ligase 4 and Ku70
    • Boboila C., Jankovic M., Yan C.T., Wang J.H., Wesemann D.R., Zhang T., et al. Alternative end-joining catalyzes robust IgH locus deletions and translocations in the combined absence of ligase 4 and Ku70. Proc. Nat. Acad. Sci. U.S.A. 2010, 107:3034-3039.
    • (2010) Proc. Nat. Acad. Sci. U.S.A. , vol.107 , pp. 3034-3039
    • Boboila, C.1    Jankovic, M.2    Yan, C.T.3    Wang, J.H.4    Wesemann, D.R.5    Zhang, T.6
  • 87
    • 34748863465 scopus 로고    scopus 로고
    • IgH class switching and translocations use a robust non-classical end-joining pathway
    • Yan C.T., Boboila C., Souza E.K., Franco S., Hickernell T.R., Murphy M., et al. IgH class switching and translocations use a robust non-classical end-joining pathway. Nature 2007, 449:478-482.
    • (2007) Nature , vol.449 , pp. 478-482
    • Yan, C.T.1    Boboila, C.2    Souza, E.K.3    Franco, S.4    Hickernell, T.R.5    Murphy, M.6
  • 88
    • 84860456242 scopus 로고    scopus 로고
    • Removal of shelterin reveals the telomere end-protection problem
    • Sfeir A., de Lange T. Removal of shelterin reveals the telomere end-protection problem. Science 2012, 336:593-597.
    • (2012) Science , vol.336 , pp. 593-597
    • Sfeir, A.1    de Lange, T.2
  • 89
    • 66049143898 scopus 로고    scopus 로고
    • PARP1 facilitates alternative NHEJ, whereas PARP2 suppresses IgH/c-myc translocations during immunoglobulin class switch recombination
    • 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. 2009, 206:1047-1056.
    • (2009) J. Exp. Med. , vol.206 , pp. 1047-1056
    • Robert, I.1    Dantzer, F.2    Reina-San-Martin, B.3
  • 90
    • 84858636333 scopus 로고    scopus 로고
    • X-ray repair cross-complementing protein 1 (XRCC1) deficiency enhances class switch recombination is permissive for alternative end joining
    • Han L., Mao W., Yu K. X-ray repair cross-complementing protein 1 (XRCC1) deficiency enhances class switch recombination is permissive for alternative end joining. Proc. Nat. Acad. Sci. U.S.A. 2012.
    • (2012) Proc. Nat. Acad. Sci. U.S.A.
    • Han, L.1    Mao, W.2    Yu, K.3
  • 91
    • 84863116082 scopus 로고    scopus 로고
    • Robust chromosomal DNA repair via alternative end-joining in the absence of X-ray repair cross-complementing protein 1 (XRCC1)
    • Boboila C., Oksenych V., Gostissa M., Wang J.H., Zha S., Zhang Y., et al. Robust chromosomal DNA repair via alternative end-joining in the absence of X-ray repair cross-complementing protein 1 (XRCC1). Proc. Nat. Acad. Sci. U.S.A. 2012, 109:2473-2478.
    • (2012) Proc. Nat. Acad. Sci. U.S.A. , vol.109 , pp. 2473-2478
    • Boboila, C.1    Oksenych, V.2    Gostissa, M.3    Wang, J.H.4    Zha, S.5    Zhang, Y.6


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