메뉴 건너뛰기




Volumn 44, Issue 19, 2016, Pages 9279-9295

Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro

Author keywords

[No Author keywords available]

Indexed keywords

CORDYCEPIN; DNA FRAGMENT; DOUBLE STRANDED DNA; GLYCOSIDASE; MONOMER; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 2; OLIGONUCLEOTIDE; PHOSPHATE; POLY(ADP RIBOSE)GLYCOSIDASE; UNCLASSIFIED DRUG; DNA; DNA ADDUCT; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PARP2 PROTEIN, MOUSE; PROTEIN BINDING;

EID: 84994817680     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkw675     Document Type: Article
Times cited : (117)

References (66)
  • 1
    • 84875185107 scopus 로고    scopus 로고
    • DNA base damage by reactive oxygen species, oxidizing agents, and UV radiation
    • Cadet, J. and Wagner, J.R. (2013) DNA base damage by reactive oxygen species, oxidizing agents, and UV radiation. Cold Spring Harb. Perspect. Biol., 5, a012559
    • (2013) Cold Spring Harb. Perspect. Biol , vol.5 , pp. a012559
    • Cadet, J.1    Wagner, J.R.2
  • 2
    • 77954187741 scopus 로고    scopus 로고
    • DNA topoisomerases and their poisoning by anticancer and antibacterial drugs
    • Pommier, Y., Leo, E., Zhang, H. and Marchand, C. (2010) DNA topoisomerases and their poisoning by anticancer and antibacterial drugs. Chem. Biol., 17, 421-433
    • (2010) Chem. Biol , vol.17 , pp. 421-433
    • Pommier, Y.1    Leo, E.2    Zhang, H.3    Marchand, C.4
  • 4
    • 24344454692 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal
    • Kim, M.Y., Zhang, T. and Kraus, W.L. (2005) Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal. Genes Dev., 19, 1951-1967
    • (2005) Genes Dev , vol.19 , pp. 1951-1967
    • Kim, M.Y.1    Zhang, T.2    Kraus, W.L.3
  • 6
    • 0000102949 scopus 로고
    • Poly(ADP-ribose) polymerase: A molecular nick-sensor
    • de Murcia, G. and Menissier de Murcia, J. (1994) Poly(ADP-ribose) polymerase: A molecular nick-sensor. Trends Biochem. Sci., 19, 172-176
    • (1994) Trends Biochem. Sci , vol.19 , pp. 172-176
    • De Murcia, G.1    Menissier De Murcia, J.2
  • 7
    • 0021287371 scopus 로고
    • Mechanism of the inhibition of Ca2+, Mg2+-dependent endonuclease of bull seminal plasma induced by ADP-ribosylation
    • Tanaka, Y., Yoshihara, K., Itaya, A., Kamiya, T. and Koide, S.S. (1984) Mechanism of the inhibition of Ca2+, Mg2+-dependent endonuclease of bull seminal plasma induced by ADP-ribosylation. J. Biol. Chem., 259, 6579-6585
    • (1984) J. Biol. Chem , vol.259 , pp. 6579-6585
    • Tanaka, Y.1    Yoshihara, K.2    Itaya, A.3    Kamiya, T.4    Koide, S.S.5
  • 8
    • 0028365745 scopus 로고
    • Dual function for poly(ADP-ribose) synthesis in response to DNA strand breakage
    • Satoh, M.S., Poirier, G.G. and Lindahl, T. (1994) Dual function for poly(ADP-ribose) synthesis in response to DNA strand breakage. Biochemistry, 33, 7099-7106
    • (1994) Biochemistry , vol.33 , pp. 7099-7106
    • Satoh, M.S.1    Poirier, G.G.2    Lindahl, T.3
  • 9
    • 84902086815 scopus 로고    scopus 로고
    • Protein ADP-ribosylation and the cellular response to DNA strand breaks
    • Caldecott, K.W. (2014) Protein ADP-ribosylation and the cellular response to DNA strand breaks. DNA Repair, 19, 108-113
    • (2014) DNA Repair , vol.19 , pp. 108-113
    • Caldecott, K.W.1
  • 10
    • 17044365726 scopus 로고    scopus 로고
    • Nucleosome and chromatin fiber dynamics
    • Luger, K. and Hansen, J.C. (2005) Nucleosome and chromatin fiber dynamics. Curr. Opin. Struct. Biol., 15, 188-196
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 188-196
    • Luger, K.1    Hansen, J.C.2
  • 11
    • 77949528928 scopus 로고    scopus 로고
    • Rotational dynamics of DNA on the nucleosome surface markedly impact accessibility to a DNA repair enzyme
    • Hinz, J.M., Rodriguez, Y. and Smerdon, M.J. (2010) Rotational dynamics of DNA on the nucleosome surface markedly impact accessibility to a DNA repair enzyme. Proc. Natl. Acad. Sci. U.S.A 107, 4646-4651
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 4646-4651
    • Hinz, J.M.1    Rodriguez, Y.2    Smerdon, M.J.3
  • 13
    • 84886719040 scopus 로고    scopus 로고
    • PARP-1 and gene regulation: Progress and puzzles
    • Kraus, W.L. and Hottiger, M.O. (2013) PARP-1 and gene regulation: progress and puzzles. Mol. Aspects Med., 34, 1109-1123
    • (2013) Mol. Aspects Med , vol.34 , pp. 1109-1123
    • Kraus, W.L.1    Hottiger, M.O.2
  • 14
    • 33847618236 scopus 로고    scopus 로고
    • Mammalian single-strand break repair: Mechanisms and links with chromatin
    • Caldecott, K.W. (2007) Mammalian single-strand break repair: mechanisms and links with chromatin. DNA Repair, 6, 443-453
    • (2007) DNA Repair , vol.6 , pp. 443-453
    • Caldecott, K.W.1
  • 16
    • 84873524967 scopus 로고    scopus 로고
    • PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis
    • Langelier, M.F. and Pascal, J.M. (2013) PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis. Curr. Opin. Struct. Biol., 23, 134-143
    • (2013) Curr. Opin. Struct. Biol , vol.23 , pp. 134-143
    • Langelier, M.F.1    Pascal, J.M.2
  • 19
    • 1342286058 scopus 로고    scopus 로고
    • Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2
    • Oliver, A.W., Ame, J.C., Roe, S.M., Good, V., de Murcia, G. and Pearl, L.H. (2004) Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2. Nucleic Acids Res., 32, 456-464
    • (2004) Nucleic Acids Res , vol.32 , pp. 456-464
    • Oliver, A.W.1    Ame, J.C.2    Roe, S.M.3    Good, V.4    De Murcia, G.5    Pearl, L.H.6
  • 20
    • 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
    • Langelier, M.F., Riccio, A.A. and Pascal, J.M. (2014) 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, 7762-7775
    • (2014) Nucleic Acids Res , vol.42 , pp. 7762-7775
    • Langelier, M.F.1    Riccio, A.A.2    Pascal, J.M.3
  • 22
    • 84877738664 scopus 로고    scopus 로고
    • Interaction of PARP-2 with DNA structures mimicking DNA repair intermediates and consequences on activity of base excision repair proteins
    • Kutuzov, M.M., Khodyreva, S.N., Ame, J.C., Ilina, E.S., Sukhanova, M.V., Schreiber, V. and Lavrik, O.I. (2013) Interaction of PARP-2 with DNA structures mimicking DNA repair intermediates and consequences on activity of base excision repair proteins. Biochimie, 95, 1208-1215
    • (2013) Biochimie , vol.95 , pp. 1208-1215
    • Kutuzov, M.M.1    Khodyreva, S.N.2    Ame, J.C.3    Ilina, E.S.4    Sukhanova, M.V.5    Schreiber, V.6    Lavrik, O.I.7
  • 23
    • 84878930839 scopus 로고    scopus 로고
    • Alternative excision repair pathways
    • Yasui, A. (2013) Alternative excision repair pathways. Cold Spring Harb. Perspect. Biol., 5, a012617
    • (2013) Cold Spring Harb. Perspect. Biol , vol.5 , pp. a012617
    • Yasui, A.1
  • 24
    • 33847673237 scopus 로고    scopus 로고
    • The intricate structural chemistry of base excision repair machinery: Implications for DNA damage recognition, removal, and repair
    • Hitomi, K., Iwai, S. and Tainer, J.A. (2007) The intricate structural chemistry of base excision repair machinery: implications for DNA damage recognition, removal, and repair. DNA Repair (Amst), 6, 410-428
    • (2007) DNA Repair (Amst) , vol.6 , pp. 410-428
    • Hitomi, K.1    Iwai, S.2    Tainer, J.A.3
  • 26
    • 84888129073 scopus 로고    scopus 로고
    • The mechanism of human tyrosyl-DNA phosphodiesterase 1 in the cleavage of AP site and its synthetic analogs
    • Lebedeva, N.A., Rechkunova, N.I., Ishchenko, A.A., Saparbaev, M. and Lavrik, O.I. (2013) The mechanism of human tyrosyl-DNA phosphodiesterase 1 in the cleavage of AP site and its synthetic analogs. DNA Repair, 12, 1037-1042
    • (2013) DNA Repair , vol.12 , pp. 1037-1042
    • Lebedeva, N.A.1    Rechkunova, N.I.2    Ishchenko, A.A.3    Saparbaev, M.4    Lavrik, O.I.5
  • 28
    • 0037049975 scopus 로고    scopus 로고
    • Alternative nucleotide incision repair pathway for oxidative DNA damage
    • Ischenko, A.A. and Saparbaev, M.K. (2002) Alternative nucleotide incision repair pathway for oxidative DNA damage. Nature, 415, 183-187
    • (2002) Nature , vol.415 , pp. 183-187
    • Ischenko, A.A.1    Saparbaev, M.K.2
  • 29
    • 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. and Caldecott, K.W. (2003) A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage. Nucleic Acids Res., 31, 5526-5533
    • (2003) Nucleic Acids Res , vol.31 , pp. 5526-5533
    • El-Khamisy, S.F.1    Masutani, M.2    Suzuki, H.3    Caldecott, K.W.4
  • 31
    • 79956053314 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase and XPF-ERCC1 participate in distinct pathways for the repair of topoisomerase I-induced DNA damage in mammalian cells
    • Zhang, Y.W., Regairaz, M., Seiler, J.A., Agama, K.K., Doroshow, J.H. and Pommier, Y. (2011) Poly(ADP-ribose) polymerase and XPF-ERCC1 participate in distinct pathways for the repair of topoisomerase I-induced DNA damage in mammalian cells. Nucleic Acids Res., 39, 3607-3620
    • (2011) Nucleic Acids Res , vol.39 , pp. 3607-3620
    • Zhang, Y.W.1    Regairaz, M.2    Seiler, J.A.3    Agama, K.K.4    Doroshow, J.H.5    Pommier, Y.6
  • 32
    • 84919400644 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerases in double-strand break repair: Focus on PARP1, PARP2 and PARP3
    • Beck, C., Robert, I., Reina-San-Martin, B., Schreiber, V. and Dantzer, F. (2014) Poly(ADP-ribose) polymerases in double-strand break repair: focus on PARP1, PARP2 and PARP3. Exp. Cell Res., 329, 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
  • 33
    • 38149057387 scopus 로고    scopus 로고
    • PARP1-dependent kinetics of recruitment of MRE11 and NBS1 proteins to multiple DNA damage sites
    • Haince, J.F., McDonald, D., Rodrigue, A., Dery, U., Masson, J.Y., Hendzel, M.J. and Poirier, G.G. (2008) PARP1-dependent kinetics of recruitment of MRE11 and NBS1 proteins to multiple DNA damage sites. J. Biol. Chem., 283, 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
  • 35
    • 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
    • Mortusewicz, O., Ame, J.C., Schreiber, V. and Leonhardt, H. (2007) Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells. Nucleic Acids Res., 35, 7665-7675
    • (2007) Nucleic Acids Res , vol.35 , pp. 7665-7675
    • Mortusewicz, O.1    Ame, J.C.2    Schreiber, V.3    Leonhardt, H.4
  • 36
    • 18544384491 scopus 로고    scopus 로고
    • Regulation of poly(ADP-ribose) metabolism by poly(ADP-ribose) glycohydrolase: Where and when?
    • Bonicalzi, M.E., Haince, J.F., Droit, A. and Poirier, G.G. (2005) Regulation of poly(ADP-ribose) metabolism by poly(ADP-ribose) glycohydrolase: where and when? Cell. Mol. Life Sci., 62, 739-750
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 739-750
    • Bonicalzi, M.E.1    Haince, J.F.2    Droit, A.3    Poirier, G.G.4
  • 37
    • 33750940806 scopus 로고    scopus 로고
    • The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-Acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases
    • Ono, T., Kasamatsu, A., Oka, S. and Moss, J. (2006) The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-Acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases. Proc. Natl. Acad. Sci. U.S.A., 103, 16687-16691
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 16687-16691
    • Ono, T.1    Kasamatsu, A.2    Oka, S.3    Moss, J.4
  • 41
    • 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., Hochegger, H., Takeda, S. and Caldecott, K.W. (2007) Poly(ADP-ribose) polymerase 1 accelerates single-strand break repair in concert with poly(ADP-ribose) glycohydrolase. Mol. Cell. Biol., 27, 5597-5605
    • (2007) Mol. Cell. Biol , vol.27 , pp. 5597-5605
    • Fisher, A.E.1    Hochegger, H.2    Takeda, S.3    Caldecott, K.W.4
  • 43
    • 0002160618 scopus 로고
    • Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme
    • Chambon, P., Weill, J.D. and Mandel, P. (1963) Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme. Biochem. Biophys. Res. Commun., 11, 39-43
    • (1963) Biochem. Biophys. Res. Commun , vol.11 , pp. 39-43
    • Chambon, P.1    Weill, J.D.2    Mandel, P.3
  • 44
    • 84862878460 scopus 로고    scopus 로고
    • Tyrosyl-DNA phosphodiesterase 1 initiates repair of apurinic/apyrimidinic sites
    • Lebedeva, N.A., Rechkunova, N.I., El-Khamisy, S.F. and Lavrik, O.I. (2012) Tyrosyl-DNA phosphodiesterase 1 initiates repair of apurinic/apyrimidinic sites. Biochimie, 94, 1749-1753
    • (2012) Biochimie , vol.94 , pp. 1749-1753
    • Lebedeva, N.A.1    Rechkunova, N.I.2    El-Khamisy, S.F.3    Lavrik, O.I.4
  • 45
    • 79960737838 scopus 로고    scopus 로고
    • New insights in the removal of the hydantoins, oxidation product of pyrimidines, via the base excision and nucleotide incision repair pathways
    • Redrejo-Rodriguez, M., Saint-Pierre, C., Couve, S., Mazouzi, A., Ishchenko, A.A., Gasparutto, D. and Saparbaev, M. (2011) New insights in the removal of the hydantoins, oxidation product of pyrimidines, via the base excision and nucleotide incision repair pathways. PLoS One, 6, e21039
    • (2011) PLoS One , vol.6 , pp. e21039
    • Redrejo-Rodriguez, M.1    Saint-Pierre, C.2    Couve, S.3    Mazouzi, A.4    Ishchenko, A.A.5    Gasparutto, D.6    Saparbaev, M.7
  • 46
    • 0017240221 scopus 로고
    • Purification and properties of calf thymus polyadenosine diphosphate ribose polymerase
    • Okazaki, H., Niedergang, C. and Mandel, P. (1976) Purification and properties of calf thymus polyadenosine diphosphate ribose polymerase. FEBS Lett., 62, 255-258
    • (1976) FEBS Lett , vol.62 , pp. 255-258
    • Okazaki, H.1    Niedergang, C.2    Mandel, P.3
  • 47
    • 0345824718 scopus 로고    scopus 로고
    • Regulation of the enzymatic catalysis of poly(ADP-ribose) polymerase by dsDNA, polyamines, Mg2+, Ca2+, histones H1 and H3, and ATP
    • Kun, E., Kirsten, E., Mendeleyev, J. and Ordahl, C.P. (2004) Regulation of the enzymatic catalysis of poly(ADP-ribose) polymerase by dsDNA, polyamines, Mg2+, Ca2+, histones H1 and H3, and ATP. Biochemistry, 43, 210-216
    • (2004) Biochemistry , vol.43 , pp. 210-216
    • Kun, E.1    Kirsten, E.2    Mendeleyev, J.3    Ordahl, C.P.4
  • 49
    • 0020671387 scopus 로고
    • Poly(ADP-ribose) polymerase auto-modification and interaction with DNA: Electron microscopic visualization
    • de Murcia, G., Jongstra-Bilen, J., Ittel, M.E., Mandel, P. and Delain, E. (1983) Poly(ADP-ribose) polymerase auto-modification and interaction with DNA: electron microscopic visualization. EMBO J., 2, 543-548
    • (1983) EMBO J , vol.2 , pp. 543-548
    • De Murcia, G.1    Jongstra-Bilen, J.2    Ittel, M.E.3    Mandel, P.4    Delain, E.5
  • 50
    • 0023191708 scopus 로고
    • Characterization of polymers of adenosine diphosphate ribose generated in vitro and in vivo
    • Alvarez-Gonzalez, R. and Jacobson, M.K. (1987) Characterization of polymers of adenosine diphosphate ribose generated in vitro and in vivo. Biochemistry, 26, 3218-3224
    • (1987) Biochemistry , vol.26 , pp. 3218-3224
    • Alvarez-Gonzalez, R.1    Jacobson, M.K.2
  • 51
    • 0017799391 scopus 로고
    • Structure of a poly (adenosine diphosphoribose) monomer: 2-(5-hosphoribosyl)-5--Adenosine monophosphate
    • Ferro, A.M. and Oppenheimer, N.J. (1978) Structure of a poly (adenosine diphosphoribose) monomer: 2-(5-hosphoribosyl)-5-Adenosine monophosphate. Proc. Natl. Acad. Sci. U.S.A., 75, 809-813
    • (1978) Proc. Natl. Acad. Sci. U.S.A , vol.75 , pp. 809-813
    • Ferro, A.M.1    Oppenheimer, N.J.2
  • 54
    • 79956330964 scopus 로고    scopus 로고
    • CpG islands and the regulation of transcription
    • Deaton, A.M. and Bird, A. (2011) CpG islands and the regulation of transcription. Genes Dev., 25, 1010-1022
    • (2011) Genes Dev , vol.25 , pp. 1010-1022
    • Deaton, A.M.1    Bird, A.2
  • 60
    • 84866534208 scopus 로고    scopus 로고
    • Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes
    • Clark, N.J., Kramer, M., Muthurajan, U.M. and Luger, K. (2012) Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes. J. Biol. Chem., 287, 32430-32439
    • (2012) J. Biol. Chem , vol.287 , pp. 32430-32439
    • Clark, N.J.1    Kramer, M.2    Muthurajan, U.M.3    Luger, K.4
  • 61
    • 84963813216 scopus 로고    scopus 로고
    • Single molecule detection of PARP1 and PARP2 interaction with DNA strand breaks and their poly(ADP-ribosyl)ation using high-resolution AFM imaging
    • Sukhanova, M.V., Abrakhi, S., Joshi, V., Pastre, D., Kutuzov, M.M., Anarbaev, R.O., Curmi, P.A., Hamon, L. and Lavrik, O.I. (2016) Single molecule detection of PARP1 and PARP2 interaction with DNA strand breaks and their poly(ADP-ribosyl)ation using high-resolution AFM imaging. Nucleic Acids Res., 44, e60.
    • (2016) Nucleic Acids Res , vol.44 , pp. e60
    • Sukhanova, M.V.1    Abrakhi, S.2    Joshi, V.3    Pastre, D.4    Kutuzov, M.M.5    Anarbaev, R.O.6    Curmi, P.A.7    Hamon, L.8    Lavrik, O.I.9
  • 62
    • 0025696463 scopus 로고
    • Use of two-dimensional thin-layer chromatography for the components study of poly(adenosine diphosphate ribose
    • Keith, G., Desgres, J. and de Murcia, G. (1990) Use of two-dimensional thin-layer chromatography for the components study of poly(adenosine diphosphate ribose). Anal. Biochem., 191, 309-313
    • (1990) Anal. Biochem , vol.191 , pp. 309-313
    • Keith, G.1    Desgres, J.2    De Murcia, G.3
  • 63
    • 0020981536 scopus 로고
    • Correlation between endogenous nucleosomal hyper(ADP-ribosyl)ation of histone H1 and the induction of chromatin relaxation
    • Aubin, R.J., Frechette, A., de Murcia, G., Mandel, P., Lord, A., Grondin, G. and Poirier, G.G. (1983) Correlation between endogenous nucleosomal hyper(ADP-ribosyl)ation of histone H1 and the induction of chromatin relaxation. EMBO J., 2, 1685-1693
    • (1983) EMBO J , vol.2 , pp. 1685-1693
    • Aubin, R.J.1    Frechette, A.2    De Murcia, G.3    Mandel, P.4    Lord, A.5    Grondin, G.6    Poirier, G.G.7
  • 64
    • 79960206370 scopus 로고    scopus 로고
    • PARG is recruited to DNA damage sites through poly(ADP-ribose)-and PCNA-dependent mechanisms
    • Mortusewicz, O., Fouquerel, E., Ame, J.C., Leonhardt, H. and Schreiber, V. (2011) PARG is recruited to DNA damage sites through poly(ADP-ribose)-and PCNA-dependent mechanisms. Nucleic Acids Res., 39, 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
  • 65
    • 0015816206 scopus 로고
    • Identification of poly (ADP-ribose) covalently bound to histone F1 in vivo
    • Smith, J.A. and Stocken, L.A. (1973) Identification of poly (ADP-ribose) covalently bound to histone F1 in vivo. Biochem. Biophys. Res. Commun., 54, 297-300
    • (1973) Biochem. Biophys. Res. Commun , vol.54 , pp. 297-300
    • Smith, J.A.1    Stocken, L.A.2
  • 66
    • 0016792818 scopus 로고
    • Chemical and metabolic properties of adenosine diphosphate ribose derivatives of nuclear proteins
    • Smith, J.A. and Stocken, L.A. (1975) Chemical and metabolic properties of adenosine diphosphate ribose derivatives of nuclear proteins. Biochem. J., 147, 523-529.
    • (1975) Biochem. J , vol.147 , pp. 523-529
    • Smith, J.A.1    Stocken, L.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.