메뉴 건너뛰기




Volumn 39, Issue 1, 2010, Pages 8-24

The PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets

Author keywords

[No Author keywords available]

Indexed keywords

1,5 ISOQUINOLINEDIOL; 2 (2 METHYL 2 PYRROLIDINYL) 1H BENZIMIDAZOLE 4 CARBOXAMIDE; 3 AMINOBENZAMIDE; DOXORUBICIN; N (5,6 DIHYDRO 6 OXO 2 PHENANTHRIDINYL) 2 DIMETHYLAMINOACETAMIDE; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 2; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE INHIBITOR; OLAPARIB; POLY(ADENOSINE DIPHOSPHATE RIBOSE); SIRTUIN 1; UNCLASSIFIED DRUG; XAV 939;

EID: 77954274504     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2010.06.017     Document Type: Review
Times cited : (726)

References (161)
  • 4
    • 67649888368 scopus 로고    scopus 로고
    • Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites
    • Altmeyer M., Messner S., Hassa P.O., Fey M., Hottiger M.O. Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites. Nucleic Acids Res. 2009, 37:3723-3738.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3723-3738
    • Altmeyer, M.1    Messner, S.2    Hassa, P.O.3    Fey, M.4    Hottiger, M.O.5
  • 5
    • 0023191708 scopus 로고
    • Characterization of polymers of adenosine diphosphate ribose generated in vitro and in vivo
    • Alvarez-Gonzalez R., Jacobson M.K. Characterization of polymers of adenosine diphosphate ribose generated in vitro and in vivo. Biochemistry 1987, 26:3218-3224.
    • (1987) Biochemistry , vol.26 , pp. 3218-3224
    • Alvarez-Gonzalez, R.1    Jacobson, M.K.2
  • 6
    • 0029162298 scopus 로고
    • Dissection of ADP-ribose polymer synthesis into individual steps of initiation, elongation, and branching
    • Alvarez-Gonzalez R., Mendoza-Alvarez H. Dissection of ADP-ribose polymer synthesis into individual steps of initiation, elongation, and branching. Biochimie 1995, 77:403-407.
    • (1995) Biochimie , vol.77 , pp. 403-407
    • Alvarez-Gonzalez, R.1    Mendoza-Alvarez, H.2
  • 9
  • 10
    • 38049129655 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-2 controls adipocyte differentiation and adipose tissue function through the regulation of the activity of the retinoid X receptor/peroxisome proliferator-activated receptor-gamma heterodimer
    • Bai P., Houten S.M., Huber A., Schreiber V., Watanabe M., Kiss B., de Murcia G., Auwerx J., Menissier-de Murcia J. Poly(ADP-ribose) polymerase-2 controls adipocyte differentiation and adipose tissue function through the regulation of the activity of the retinoid X receptor/peroxisome proliferator-activated receptor-gamma heterodimer. J. Biol. Chem. 2007, 282:37738-37746.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37738-37746
    • Bai, P.1    Houten, S.M.2    Huber, A.3    Schreiber, V.4    Watanabe, M.5    Kiss, B.6    de Murcia, G.7    Auwerx, J.8    Menissier-de Murcia, J.9
  • 14
    • 34247278118 scopus 로고    scopus 로고
    • Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1
    • Berger F., Lau C., Ziegler M. Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1. Proc. Natl. Acad. Sci. USA 2007, 104:3765-3770.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 3765-3770
    • Berger, F.1    Lau, C.2    Ziegler, M.3
  • 15
    • 0038449141 scopus 로고    scopus 로고
    • PARP-1, a determinant of cell survival in response to DNA damage
    • Bouchard V.J., Rouleau M., Poirier G.G. PARP-1, a determinant of cell survival in response to DNA damage. Exp. Hematol. 2003, 31:446-454.
    • (2003) Exp. Hematol. , vol.31 , pp. 446-454
    • Bouchard, V.J.1    Rouleau, M.2    Poirier, G.G.3
  • 19
    • 18444361838 scopus 로고    scopus 로고
    • DNA methylation and chromatin structure: the puzzling CpG islands
    • Caiafa P., Zampieri M. DNA methylation and chromatin structure: the puzzling CpG islands. J. Cell. Biochem. 2005, 94:257-265.
    • (2005) J. Cell. Biochem. , vol.94 , pp. 257-265
    • Caiafa, P.1    Zampieri, M.2
  • 20
    • 62149087062 scopus 로고    scopus 로고
    • CCCTC-binding factor meets poly(ADP-ribose) polymerase-1
    • Caiafa P., Zlatanova J. CCCTC-binding factor meets poly(ADP-ribose) polymerase-1. J. Cell. Physiol. 2009, 219:265-270.
    • (2009) J. Cell. Physiol. , vol.219 , pp. 265-270
    • Caiafa, P.1    Zlatanova, J.2
  • 21
    • 61449261908 scopus 로고    scopus 로고
    • Epigenetics: poly(ADP-ribosyl)ation of PARP-1 regulates genomic methylation patterns
    • Caiafa P., Guastafierro T., Zampieri M. Epigenetics: poly(ADP-ribosyl)ation of PARP-1 regulates genomic methylation patterns. FASEB J. 2009, 23:672-678.
    • (2009) FASEB J. , vol.23 , pp. 672-678
    • Caiafa, P.1    Guastafierro, T.2    Zampieri, M.3
  • 22
    • 10344234720 scopus 로고    scopus 로고
    • Poly(ADP-ribose) is required for spindle assembly and structure
    • Chang P., Jacobson M.K., Mitchison T.J. Poly(ADP-ribose) is required for spindle assembly and structure. Nature 2004, 432:645-649.
    • (2004) Nature , vol.432 , pp. 645-649
    • Chang, P.1    Jacobson, M.K.2    Mitchison, T.J.3
  • 23
    • 85047693635 scopus 로고    scopus 로고
    • Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function
    • Chang P., Coughlin M., Mitchison T.J. Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function. Nat. Cell Biol. 2005, 7:1133-1139.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1133-1139
    • Chang, P.1    Coughlin, M.2    Mitchison, T.J.3
  • 24
    • 50249090605 scopus 로고    scopus 로고
    • Tankyrase 1 and tankyrase 2 are essential but redundant for mouse embryonic development
    • Chiang Y.J., Hsiao S.J., Yver D., Cushman S.W., Tessarollo L., Smith S., Hodes R.J. Tankyrase 1 and tankyrase 2 are essential but redundant for mouse embryonic development. PLoS ONE 2008, 3:e2639. 10.1371/journal.pone.0002639.
    • (2008) PLoS ONE , vol.3
    • Chiang, Y.J.1    Hsiao, S.J.2    Yver, D.3    Cushman, S.W.4    Tessarollo, L.5    Smith, S.6    Hodes, R.J.7
  • 27
    • 19444363980 scopus 로고    scopus 로고
    • Shock, inflammation and PARP
    • Cuzzocrea S. Shock, inflammation and PARP. Pharmacol. Res. 2005, 52:72-82.
    • (2005) Pharmacol. Res. , vol.52 , pp. 72-82
    • Cuzzocrea, S.1
  • 28
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours D., Desnoyers S., D'Silva I., Poirier G.G. Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 1999, 342:249-268.
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 31
    • 77952577473 scopus 로고    scopus 로고
    • Parp-1 deficiency exacerbates diet-induced obesity in mice
    • Devalaraja-Narashimha K., Padanilam B. Parp-1 deficiency exacerbates diet-induced obesity in mice. J. Endocrinol. 2010, 205:243-252.
    • (2010) J. Endocrinol. , vol.205 , pp. 243-252
    • Devalaraja-Narashimha, K.1    Padanilam, B.2
  • 32
    • 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
  • 35
    • 69049084375 scopus 로고    scopus 로고
    • Toll-like receptor 2 and poly(ADP-ribose) polymerase 1 promote central nervous system neuroinflammation in progressive EAE
    • Farez M.F., Quintana F.J., Gandhi R., Izquierdo G., Lucas M., Weiner H.L. Toll-like receptor 2 and poly(ADP-ribose) polymerase 1 promote central nervous system neuroinflammation in progressive EAE. Nat. Immunol. 2009, 10:958-964.
    • (2009) Nat. Immunol. , vol.10 , pp. 958-964
    • Farez, M.F.1    Quintana, F.J.2    Gandhi, R.3    Izquierdo, G.4    Lucas, M.5    Weiner, H.L.6
  • 37
    • 76749171311 scopus 로고    scopus 로고
    • Mutational analysis of the poly(ADP-ribosyl)ation sites of the transcription factor CTCF provides an insight into the mechanism of its regulation by poly(ADP-ribosyl)ation
    • Farrar D., Rai S., Chernukhin I., Jagodic M., Ito Y., Yammine S., Ohlsson R., Murrell A., Klenova E. Mutational analysis of the poly(ADP-ribosyl)ation sites of the transcription factor CTCF provides an insight into the mechanism of its regulation by poly(ADP-ribosyl)ation. Mol. Cell. Biol. 2010, 30:1199-1216.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1199-1216
    • Farrar, D.1    Rai, S.2    Chernukhin, I.3    Jagodic, M.4    Ito, Y.5    Yammine, S.6    Ohlsson, R.7    Murrell, A.8    Klenova, E.9
  • 38
    • 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., 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.1    Hochegger, H.2    Takeda, S.3    Caldecott, K.W.4
  • 40
    • 71749119589 scopus 로고    scopus 로고
    • Global analysis of transcriptional regulation by poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in MCF-7 human breast cancer cells
    • Frizzell K.M., Gamble M.J., Berrocal J.G., Zhang T., Krishnakumar R., Cen Y., Sauve A.A., Kraus W.L. Global analysis of transcriptional regulation by poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in MCF-7 human breast cancer cells. J. Biol. Chem. 2009, 284:33926-33938.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33926-33938
    • Frizzell, K.M.1    Gamble, M.J.2    Berrocal, J.G.3    Zhang, T.4    Krishnakumar, R.5    Cen, Y.6    Sauve, A.A.7    Kraus, W.L.8
  • 41
    • 33644850114 scopus 로고    scopus 로고
    • The expanding role of poly(ADP-ribose) metabolism: current challenges and new perspectives
    • Gagne J.P., Hendzel M.J., Droit A., Poirier G.G. The expanding role of poly(ADP-ribose) metabolism: current challenges and new perspectives. Curr. Opin. Cell Biol. 2006, 18:145-151.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 145-151
    • Gagne, J.P.1    Hendzel, M.J.2    Droit, A.3    Poirier, G.G.4
  • 44
    • 34249898088 scopus 로고    scopus 로고
    • SET and PARP1 remove DEK from chromatin to permit access by the transcription machinery
    • Gamble M.J., Fisher R.P. SET and PARP1 remove DEK from chromatin to permit access by the transcription machinery. Nat. Struct. Mol. Biol. 2007, 14:548-555.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 548-555
    • Gamble, M.J.1    Fisher, R.P.2
  • 45
    • 69249093784 scopus 로고    scopus 로고
    • PARP1 poly(ADP-ribosyl)ates Sox2 to control Sox2 protein levels and FGF4 expression during embryonic stem cell differentiation
    • Gao F., Kwon S.W., Zhao Y., Jin Y. PARP1 poly(ADP-ribosyl)ates Sox2 to control Sox2 protein levels and FGF4 expression during embryonic stem cell differentiation. J. Biol. Chem. 2009, 284:22263-22273.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22263-22273
    • Gao, F.1    Kwon, S.W.2    Zhao, Y.3    Jin, Y.4
  • 47
    • 19444362951 scopus 로고    scopus 로고
    • Clinical perspectives of PARP inhibitors
    • Graziani G., Szabo C. Clinical perspectives of PARP inhibitors. Pharmacol. Res. 2005, 52:109-118.
    • (2005) Pharmacol. Res. , vol.52 , pp. 109-118
    • Graziani, G.1    Szabo, C.2
  • 49
    • 1842687173 scopus 로고    scopus 로고
    • Defective transcription factor activation for proinflammatory gene expression in poly(ADP-ribose) polymerase 1-deficient glia
    • Ha H.C. Defective transcription factor activation for proinflammatory gene expression in poly(ADP-ribose) polymerase 1-deficient glia. Proc. Natl. Acad. Sci. USA 2004, 101:5087-5092.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5087-5092
    • Ha, H.C.1
  • 50
  • 52
    • 55549139051 scopus 로고    scopus 로고
    • The expanding field of poly(ADP-ribosyl)ation reactions. 'Protein Modifications: Beyond the Usual Suspects' Review Series
    • Hakme A., Wong H.K., Dantzer F., Schreiber V. The expanding field of poly(ADP-ribosyl)ation reactions. 'Protein Modifications: Beyond the Usual Suspects' Review Series. EMBO Rep. 2008, 9:1094-1100.
    • (2008) EMBO Rep. , vol.9 , pp. 1094-1100
    • Hakme, A.1    Wong, H.K.2    Dantzer, F.3    Schreiber, V.4
  • 53
    • 0032496140 scopus 로고    scopus 로고
    • Genomic organization of Drosophila poly(ADP-ribose) polymerase and distribution of its mRNA during development
    • Hanai S., Uchida M., Kobayashi S., Miwa M., Uchida K. Genomic organization of Drosophila poly(ADP-ribose) polymerase and distribution of its mRNA during development. J. Biol. Chem. 1998, 273:11881-11886.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11881-11886
    • Hanai, S.1    Uchida, M.2    Kobayashi, S.3    Miwa, M.4    Uchida, K.5
  • 54
    • 0036710459 scopus 로고    scopus 로고
    • The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-kappaB in inflammatory disorders
    • Hassa P.O., Hottiger M.O. The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-kappaB in inflammatory disorders. Cell. Mol. Life Sci. 2002, 59:1534-1553.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1534-1553
    • Hassa, P.O.1    Hottiger, M.O.2
  • 55
    • 38449088040 scopus 로고    scopus 로고
    • The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases
    • Hassa P.O., Hottiger M.O. The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases. Front. Biosci. 2008, 13:3046-3082.
    • (2008) Front. Biosci. , vol.13 , pp. 3046-3082
    • Hassa, P.O.1    Hottiger, M.O.2
  • 56
    • 0242496900 scopus 로고    scopus 로고
    • Transcriptional coactivation of nuclear factor-kappaB-dependent gene expression by p300 is regulated by poly(ADP)-ribose polymerase-1
    • Hassa P.O., Buerki C., Lombardi C., Imhof R., Hottiger M.O. Transcriptional coactivation of nuclear factor-kappaB-dependent gene expression by p300 is regulated by poly(ADP)-ribose polymerase-1. J. Biol. Chem. 2003, 278:45145-45153.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45145-45153
    • Hassa, P.O.1    Buerki, C.2    Lombardi, C.3    Imhof, R.4    Hottiger, M.O.5
  • 57
    • 28844493947 scopus 로고    scopus 로고
    • Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-kappaB-dependent transcription
    • Hassa P.O., Haenni S.S., Buerki C., Meier N.I., Lane W.S., Owen H., Gersbach M., Imhof R., Hottiger M.O. Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-kappaB-dependent transcription. J. Biol. Chem. 2005, 280:40450-40464.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40450-40464
    • Hassa, P.O.1    Haenni, S.S.2    Buerki, C.3    Meier, N.I.4    Lane, W.S.5    Owen, H.6    Gersbach, M.7    Imhof, R.8    Hottiger, M.O.9
  • 58
    • 33749260519 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?
    • Hassa P.O., Haenni S.S., Elser M., Hottiger M.O. Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?. Microbiol. Mol. Biol. Rev. 2006, 70:789-829.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 789-829
    • Hassa, P.O.1    Haenni, S.S.2    Elser, M.3    Hottiger, M.O.4
  • 60
    • 41549112501 scopus 로고    scopus 로고
    • FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16
    • Heo K., Kim H., Choi S.H., Choi J., Kim K., Gu J., Lieber M.R., Yang A.S., An W. FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16. Mol. Cell 2008, 30:86-97.
    • (2008) Mol. Cell , vol.30 , pp. 86-97
    • Heo, K.1    Kim, H.2    Choi, S.H.3    Choi, J.4    Kim, K.5    Gu, J.6    Lieber, M.R.7    Yang, A.S.8    An, W.9
  • 62
    • 33644774924 scopus 로고    scopus 로고
    • Tankyrase 2 poly(ADP-ribose) polymerase domain-deleted mice exhibit growth defects but have normal telomere length and capping
    • Hsiao S.J., Poitras M.F., Cook B.D., Liu Y., Smith S. Tankyrase 2 poly(ADP-ribose) polymerase domain-deleted mice exhibit growth defects but have normal telomere length and capping. Mol. Cell. Biol. 2006, 26:2044-2054.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2044-2054
    • Hsiao, S.J.1    Poitras, M.F.2    Cook, B.D.3    Liu, Y.4    Smith, S.5
  • 64
    • 0024406764 scopus 로고
    • The effect of poly(ADP-ribosyl)ation on native and H1-depleted chromatin. A role of poly(ADP-ribosyl)ation on core nucleosome structure
    • Huletsky A., de Murcia G., Muller S., Hengartner M., Menard L., Lamarre D., Poirier G.G. The effect of poly(ADP-ribosyl)ation on native and H1-depleted chromatin. A role of poly(ADP-ribosyl)ation on core nucleosome structure. J. Biol. Chem. 1989, 264:8878-8886.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8878-8886
    • Huletsky, A.1    de Murcia, G.2    Muller, S.3    Hengartner, M.4    Menard, L.5    Lamarre, D.6    Poirier, G.G.7
  • 65
  • 67
    • 67649855305 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation of heterogeneous nuclear ribonucleoproteins modulates splicing
    • Ji Y., Tulin A.V. Poly(ADP-ribosyl)ation of heterogeneous nuclear ribonucleoproteins modulates splicing. Nucleic Acids Res. 2009, 37:3501-3513.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3501-3513
    • Ji, Y.1    Tulin, A.V.2
  • 68
    • 10944253639 scopus 로고    scopus 로고
    • Activating the PARP-1 sensor component of the groucho/TLE1 corepressor complex mediates a CaMKinase IIdelta-dependent neurogenic gene activation pathway
    • Ju B.G., Solum D., Song E.J., Lee K.J., Rose D.W., Glass C.K., Rosenfeld M.G. Activating the PARP-1 sensor component of the groucho/TLE1 corepressor complex mediates a CaMKinase IIdelta-dependent neurogenic gene activation pathway. Cell 2004, 119:815-829.
    • (2004) Cell , vol.119 , pp. 815-829
    • Ju, B.G.1    Solum, D.2    Song, E.J.3    Lee, K.J.4    Rose, D.W.5    Glass, C.K.6    Rosenfeld, M.G.7
  • 73
    • 33646481320 scopus 로고    scopus 로고
    • Direct phosphorylation and regulation of poly(ADP-ribose) polymerase-1 by extracellular signal-regulated kinases 1/2
    • Kauppinen T.M., Chan W.Y., Suh S.W., Wiggins A.K., Huang E.J., Swanson R.A. Direct phosphorylation and regulation of poly(ADP-ribose) polymerase-1 by extracellular signal-regulated kinases 1/2. Proc. Natl. Acad. Sci. USA 2006, 103:7136-7141.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7136-7141
    • Kauppinen, T.M.1    Chan, W.Y.2    Suh, S.W.3    Wiggins, A.K.4    Huang, E.J.5    Swanson, R.A.6
  • 74
    • 10944227347 scopus 로고    scopus 로고
    • NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1
    • Kim M.Y., Mauro S., Gevry N., Lis J.T., Kraus W.L. NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1. Cell 2004, 119:803-814.
    • (2004) Cell , vol.119 , pp. 803-814
    • Kim, M.Y.1    Mauro, S.2    Gevry, N.3    Lis, J.T.4    Kraus, W.L.5
  • 75
    • 24344454692 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal
    • Kim M.Y., Zhang T., Kraus W.L. Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal. Genes Dev. 2005, 19:1951-1967.
    • (2005) Genes Dev. , vol.19 , pp. 1951-1967
    • Kim, M.Y.1    Zhang, T.2    Kraus, W.L.3
  • 76
    • 70349451172 scopus 로고    scopus 로고
    • Learning how to read ADP-ribosylation
    • Kleine H., Luscher B. Learning how to read ADP-ribosylation. Cell 2009, 139:17-19.
    • (2009) Cell , vol.139 , pp. 17-19
    • Kleine, H.1    Luscher, B.2
  • 79
    • 33744475759 scopus 로고    scopus 로고
    • Control of AIF-mediated cell death by the functional interplay of SIRT1 and PARP-1 in response to DNA damage
    • Kolthur-Seetharam U., Dantzer F., McBurney M.W., de Murcia G., Sassone-Corsi P. Control of AIF-mediated cell death by the functional interplay of SIRT1 and PARP-1 in response to DNA damage. Cell Cycle 2006, 5:873-877.
    • (2006) Cell Cycle , vol.5 , pp. 873-877
    • Kolthur-Seetharam, U.1    Dantzer, F.2    McBurney, M.W.3    de Murcia, G.4    Sassone-Corsi, P.5
  • 80
    • 61449101465 scopus 로고    scopus 로고
    • Poly (ADP-ribose) polymerase 1 is required for protein localization to Cajal body
    • Kotova E., Jarnik M., Tulin A.V. Poly (ADP-ribose) polymerase 1 is required for protein localization to Cajal body. PLoS Genet. 2009, 5:e1000387. 10.1371/journal.pgen.1000387.
    • (2009) PLoS Genet. , vol.5
    • Kotova, E.1    Jarnik, M.2    Tulin, A.V.3
  • 81
    • 44649130038 scopus 로고    scopus 로고
    • Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation
    • Kraus W.L. Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation. Curr. Opin. Cell Biol. 2008, 20:294-302.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 294-302
    • Kraus, W.L.1
  • 82
    • 69949184069 scopus 로고    scopus 로고
    • New functions for an ancient domain
    • Kraus W.L. New functions for an ancient domain. Nat. Struct. Mol. Biol. 2009, 16:904-907.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 904-907
    • Kraus, W.L.1
  • 83
    • 0038682011 scopus 로고    scopus 로고
    • PARP goes transcription
    • Kraus W.L., Lis J.T. PARP goes transcription. Cell 2003, 113:677-683.
    • (2003) Cell , vol.113 , pp. 677-683
    • Kraus, W.L.1    Lis, J.T.2
  • 84
    • 38949198773 scopus 로고    scopus 로고
    • Reciprocal binding of PARP-1 and histone H1 at promoters specifies transcriptional outcomes
    • Krishnakumar R., Gamble M.J., Frizzell K.M., Berrocal J.G., Kininis M., Kraus W.L. Reciprocal binding of PARP-1 and histone H1 at promoters specifies transcriptional outcomes. Science 2008, 319:819-821.
    • (2008) Science , vol.319 , pp. 819-821
    • Krishnakumar, R.1    Gamble, M.J.2    Frizzell, K.M.3    Berrocal, J.G.4    Kininis, M.5    Kraus, W.L.6
  • 86
    • 41549108573 scopus 로고    scopus 로고
    • A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation
    • Langelier M.F., Servent K.M., Rogers E.E., Pascal J.M. A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation. J. Biol. Chem. 2008, 283:4105-4114.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4105-4114
    • Langelier, M.F.1    Servent, K.M.2    Rogers, E.E.3    Pascal, J.M.4
  • 87
    • 77953305213 scopus 로고    scopus 로고
    • The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction
    • Langelier M.F., Ruhl D.D., Planck J.L., Kraus W.L., Pascal J.M. The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction. J. Biol. Chem. 2010, 285:18877-18887.
    • (2010) J. Biol. Chem. , vol.285 , pp. 18877-18887
    • Langelier, M.F.1    Ruhl, D.D.2    Planck, J.L.3    Kraus, W.L.4    Pascal, J.M.5
  • 88
    • 0034885522 scopus 로고    scopus 로고
    • Inhibition of poly (ADP-ribose) synthetase by gene disruption or inhibition with 5-iodo-6-amino-1,2-benzopyrone protects mice from multiple-low-dose-streptozotocin-induced diabetes
    • Mabley J.G., Suarez-Pinzon W.L., Hasko G., Salzman A.L., Rabinovitch A., Kun E., Szabo C. Inhibition of poly (ADP-ribose) synthetase by gene disruption or inhibition with 5-iodo-6-amino-1,2-benzopyrone protects mice from multiple-low-dose-streptozotocin-induced diabetes. Br. J. Pharmacol. 2001, 133:909-919.
    • (2001) Br. J. Pharmacol. , vol.133 , pp. 909-919
    • Mabley, J.G.1    Suarez-Pinzon, W.L.2    Hasko, G.3    Salzman, A.L.4    Rabinovitch, A.5    Kun, E.6    Szabo, C.7
  • 89
    • 24744447821 scopus 로고    scopus 로고
    • The role of poly(ADP-ribose) in the DNA damage signaling network
    • Malanga M., Althaus F.R. The role of poly(ADP-ribose) in the DNA damage signaling network. Biochem. Cell Biol. 2005, 83:354-364.
    • (2005) Biochem. Cell Biol. , vol.83 , pp. 354-364
    • Malanga, M.1    Althaus, F.R.2
  • 91
    • 0032041737 scopus 로고    scopus 로고
    • Conceptually driven encoding episodes create perceptual misattributions
    • Masson M.E., Caldwell J.I. Conceptually driven encoding episodes create perceptual misattributions. Acta Psychol. (Amst.) 1998, 98:183-210.
    • (1998) Acta Psychol. (Amst.) , vol.98 , pp. 183-210
    • Masson, M.E.1    Caldwell, J.I.2
  • 92
    • 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
  • 94
    • 0023117437 scopus 로고
    • Release of core DNA from nucleosomal core particles following (ADP-ribose)n-modification in vitro
    • Mathis G., Althaus F.R. Release of core DNA from nucleosomal core particles following (ADP-ribose)n-modification in vitro. Biochem. Biophys. Res. Commun. 1987, 143:1049-1054.
    • (1987) Biochem. Biophys. Res. Commun. , vol.143 , pp. 1049-1054
    • Mathis, G.1    Althaus, F.R.2
  • 95
    • 62649157236 scopus 로고    scopus 로고
    • Targeting Tankyrase 1 as a therapeutic strategy for BRCA-associated cancer
    • McCabe N., Cerone M.A., Ohishi T., Seimiya H., Lord C.J., Ashworth A. Targeting Tankyrase 1 as a therapeutic strategy for BRCA-associated cancer. Oncogene 2009, 28:1465-1470.
    • (2009) Oncogene , vol.28 , pp. 1465-1470
    • McCabe, N.1    Cerone, M.A.2    Ohishi, T.3    Seimiya, H.4    Lord, C.J.5    Ashworth, A.6
  • 96
    • 0027441894 scopus 로고
    • Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular
    • Mendoza-Alvarez H., Alvarez-Gonzalez R. Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular. J. Biol. Chem. 1993, 268:22575-22580.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22575-22580
    • Mendoza-Alvarez, H.1    Alvarez-Gonzalez, R.2
  • 97
    • 0033616626 scopus 로고    scopus 로고
    • Biochemical characterization of mono(ADP-ribosyl)ated poly(ADP-ribose) polymerase
    • Mendoza-Alvarez H., Alvarez-Gonzalez R. Biochemical characterization of mono(ADP-ribosyl)ated poly(ADP-ribose) polymerase. Biochemistry 1999, 38:3948-3953.
    • (1999) Biochemistry , vol.38 , pp. 3948-3953
    • Mendoza-Alvarez, H.1    Alvarez-Gonzalez, R.2
  • 98
    • 0035965257 scopus 로고    scopus 로고
    • Regulation of p53 sequence-specific DNA-binding by covalent poly(ADP-ribosyl)ation
    • Mendoza-Alvarez H., Alvarez-Gonzalez R. Regulation of p53 sequence-specific DNA-binding by covalent poly(ADP-ribosyl)ation. J. Biol. Chem. 2001, 276:36425-36430.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36425-36430
    • Mendoza-Alvarez, H.1    Alvarez-Gonzalez, R.2
  • 99
    • 0035131124 scopus 로고    scopus 로고
    • Early embryonic lethality in PARP-1 Atm double-mutant mice suggests a functional synergy in cell proliferation during development
    • Menisser-de Murcia J., Mark M., Wendling O., Wynshaw-Boris A., de Murcia G. Early embryonic lethality in PARP-1 Atm double-mutant mice suggests a functional synergy in cell proliferation during development. Mol. Cell. Biol. 2001, 21:1828-1832.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1828-1832
    • Menisser-de Murcia, J.1    Mark, M.2    Wendling, O.3    Wynshaw-Boris, A.4    de Murcia, G.5
  • 101
    • 70350548179 scopus 로고    scopus 로고
    • Sumoylation of poly(ADP-ribose) polymerase 1 inhibits its acetylation and restrains transcriptional coactivator function
    • Messner S., Schuermann D., Altmeyer M., Kassner I., Schmidt D., Schar P., Muller S., Hottiger M.O. Sumoylation of poly(ADP-ribose) polymerase 1 inhibits its acetylation and restrains transcriptional coactivator function. FASEB J. 2009, 23:3978-3989.
    • (2009) FASEB J. , vol.23 , pp. 3978-3989
    • Messner, S.1    Schuermann, D.2    Altmeyer, M.3    Kassner, I.4    Schmidt, D.5    Schar, P.6    Muller, S.7    Hottiger, M.O.8
  • 102
    • 63849177643 scopus 로고    scopus 로고
    • Poly (ADP-ribose) glycohydrolase (PARG) and its therapeutic potential
    • Min W., Wang Z.Q. Poly (ADP-ribose) glycohydrolase (PARG) and its therapeutic potential. Front. Biosci. 2009, 14:1619-1626.
    • (2009) Front. Biosci. , vol.14 , pp. 1619-1626
    • Min, W.1    Wang, Z.Q.2
  • 103
    • 0032891437 scopus 로고    scopus 로고
    • Functional analysis of poly(ADP-ribose) polymerase in Drosophila melanogaster
    • Miwa M., Hanai S., Poltronieri P., Uchida M., Uchida K. Functional analysis of poly(ADP-ribose) polymerase in Drosophila melanogaster. Mol. Cell. Biochem. 1999, 193:103-107.
    • (1999) Mol. Cell. Biochem. , vol.193 , pp. 103-107
    • Miwa, M.1    Hanai, S.2    Poltronieri, P.3    Uchida, M.4    Uchida, K.5
  • 105
    • 38649092421 scopus 로고    scopus 로고
    • Poly(ADP-ribose)polymerase 1 (PARP-1) and postischemic brain damage
    • Moroni F. Poly(ADP-ribose)polymerase 1 (PARP-1) and postischemic brain damage. Curr. Opin. Pharmacol. 2008, 8:96-103.
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 96-103
    • Moroni, F.1
  • 106
    • 0030679762 scopus 로고    scopus 로고
    • Genetic interaction between PARP and DNA-PK in V(D)J recombination and tumorigenesis
    • Morrison C., Smith G.C., Stingl L., Jackson S.P., Wagner E.F., Wang Z.Q. Genetic interaction between PARP and DNA-PK in V(D)J recombination and tumorigenesis. Nat. Genet. 1997, 17:479-482.
    • (1997) Nat. Genet. , vol.17 , pp. 479-482
    • Morrison, C.1    Smith, G.C.2    Stingl, L.3    Jackson, S.P.4    Wagner, E.F.5    Wang, Z.Q.6
  • 107
    • 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., 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. 2007, 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
  • 109
    • 77951634464 scopus 로고    scopus 로고
    • Increased Foxp3+ regulatory T cells in poly(ADP-Ribose) polymerase-1 deficiency
    • Nasta F., Laudisi F., Sambucci M., Rosado M.M., Pioli C. Increased Foxp3+ regulatory T cells in poly(ADP-Ribose) polymerase-1 deficiency. J. Immunol. 2010, 184:3470-3477.
    • (2010) J. Immunol. , vol.184 , pp. 3470-3477
    • Nasta, F.1    Laudisi, F.2    Sambucci, M.3    Rosado, M.M.4    Pioli, C.5
  • 110
    • 57749190795 scopus 로고    scopus 로고
    • Differential activities of cellular and viral macro domain proteins in binding of ADP-ribose metabolites
    • Neuvonen M., Ahola T. Differential activities of cellular and viral macro domain proteins in binding of ADP-ribose metabolites. J. Mol. Biol. 2009, 385:212-225.
    • (2009) J. Mol. Biol. , vol.385 , pp. 212-225
    • Neuvonen, M.1    Ahola, T.2
  • 112
    • 34250359929 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 is inhibited by a histone H2A variant, MacroH2A, and contributes to silencing of the inactive X chromosome
    • Nusinow D.A., Hernandez-Munoz I., Fazzio T.G., Shah G.M., Kraus W.L., Panning B. Poly(ADP-ribose) polymerase 1 is inhibited by a histone H2A variant, MacroH2A, and contributes to silencing of the inactive X chromosome. J. Biol. Chem. 2007, 282:12851-12859.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12851-12859
    • Nusinow, D.A.1    Hernandez-Munoz, I.2    Fazzio, T.G.3    Shah, G.M.4    Kraus, W.L.5    Panning, B.6
  • 115
    • 33644849513 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase
    • Oka S., Kato J., Moss J. Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 2006, 281:705-713.
    • (2006) J. Biol. Chem. , vol.281 , pp. 705-713
    • Oka, S.1    Kato, J.2    Moss, J.3
  • 116
    • 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
  • 118
    • 27644577665 scopus 로고    scopus 로고
    • In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)
    • Otto H., Reche P.A., Bazan F., Dittmar K., Haag F., Koch-Nolte F. In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs). BMC Genomics 2005, 6:139.
    • (2005) BMC Genomics , vol.6 , pp. 139
    • Otto, H.1    Reche, P.A.2    Bazan, F.3    Dittmar, K.4    Haag, F.5    Koch-Nolte, F.6
  • 120
    • 35148896262 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) polymerase 1 (PARP-1) in cardiovascular diseases: the therapeutic potential of PARP inhibitors
    • Pacher P., Szabo C. Role of poly(ADP-ribose) polymerase 1 (PARP-1) in cardiovascular diseases: the therapeutic potential of PARP inhibitors. Cardiovasc. Drug Rev. 2007, 25:235-260.
    • (2007) Cardiovasc. Drug Rev. , vol.25 , pp. 235-260
    • Pacher, P.1    Szabo, C.2
  • 122
    • 51649091688 scopus 로고    scopus 로고
    • Poly(ADP-ribose)polymerase-1 (PARP-1) in carcinogenesis: potential role of PARP inhibitors in cancer treatment
    • Peralta-Leal A., Rodriguez M.I., Oliver F.J. Poly(ADP-ribose)polymerase-1 (PARP-1) in carcinogenesis: potential role of PARP inhibitors in cancer treatment. Clin. Transl. Oncol. 2008, 10:318-323.
    • (2008) Clin. Transl. Oncol. , vol.10 , pp. 318-323
    • Peralta-Leal, A.1    Rodriguez, M.I.2    Oliver, F.J.3
  • 123
    • 46149108345 scopus 로고    scopus 로고
    • Rapid, transcription-independent loss of nucleosomes over a large chromatin domain at Hsp70 loci
    • Petesch S.J., Lis J.T. Rapid, transcription-independent loss of nucleosomes over a large chromatin domain at Hsp70 loci. Cell 2008, 134:74-84.
    • (2008) Cell , vol.134 , pp. 74-84
    • Petesch, S.J.1    Lis, J.T.2
  • 124
    • 30044443515 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1-dependent cardiac myocyte cell death during heart failure is mediated by NAD+ depletion and reduced Sir2alpha deacetylase activity
    • Pillai J.B., Isbatan A., Imai S., Gupta M.P. Poly(ADP-ribose) polymerase-1-dependent cardiac myocyte cell death during heart failure is mediated by NAD+ depletion and reduced Sir2alpha deacetylase activity. J. Biol. Chem. 2005, 280:43121-43130.
    • (2005) J. Biol. Chem. , vol.280 , pp. 43121-43130
    • Pillai, J.B.1    Isbatan, A.2    Imai, S.3    Gupta, M.P.4
  • 125
    • 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
  • 127
    • 55549119952 scopus 로고    scopus 로고
    • The histone subcode: poly(ADP-ribose) polymerase-1 (Parp-1) and Parp-2 control cell differentiation by regulating the transcriptional intermediary factor TIF1beta and the heterochromatin protein HP1alpha
    • Quenet D., Gasser V., Fouillen L., Cammas F., Sanglier-Cianferani S., Losson R., Dantzer F. The histone subcode: poly(ADP-ribose) polymerase-1 (Parp-1) and Parp-2 control cell differentiation by regulating the transcriptional intermediary factor TIF1beta and the heterochromatin protein HP1alpha. FASEB J. 2008, 22:3853-3865.
    • (2008) FASEB J. , vol.22 , pp. 3853-3865
    • Quenet, D.1    Gasser, V.2    Fouillen, L.3    Cammas, F.4    Sanglier-Cianferani, S.5    Losson, R.6    Dantzer, F.7
  • 129
    • 33947380240 scopus 로고    scopus 로고
    • Current development of clinical inhibitors of poly(ADP-ribose) polymerase in oncology
    • Ratnam K., Low J.A. Current development of clinical inhibitors of poly(ADP-ribose) polymerase in oncology. Clin. Cancer Res. 2007, 13:1383-1388.
    • (2007) Clin. Cancer Res. , vol.13 , pp. 1383-1388
    • Ratnam, K.1    Low, J.A.2
  • 131
    • 10944270187 scopus 로고    scopus 로고
    • The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells
    • Revollo J.R., Grimm A.A., Imai S. The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells. J. Biol. Chem. 2004, 279:50754-50763.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50754-50763
    • Revollo, J.R.1    Grimm, A.A.2    Imai, S.3
  • 132
  • 134
    • 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
  • 137
  • 140
    • 70449102637 scopus 로고    scopus 로고
    • A nuclear poly(ADP-ribose)-dependent signalosome confers DNA damage-induced IkappaB kinase activation
    • Stilmann M., Hinz M., Arslan S.C., Zimmer A., Schreiber V., Scheidereit C. A nuclear poly(ADP-ribose)-dependent signalosome confers DNA damage-induced IkappaB kinase activation. Mol. Cell 2009, 36:365-378.
    • (2009) Mol. Cell , vol.36 , pp. 365-378
    • Stilmann, M.1    Hinz, M.2    Arslan, S.C.3    Zimmer, A.4    Schreiber, V.5    Scheidereit, C.6
  • 141
    • 33847313804 scopus 로고    scopus 로고
    • Altered DNA damage response in Caenorhabditis elegans with impaired poly(ADP-ribose) glycohydrolases genes expression
    • St-Laurent J.F., Gagnon S.N., Dequen F., Hardy I., Desnoyers S. Altered DNA damage response in Caenorhabditis elegans with impaired poly(ADP-ribose) glycohydrolases genes expression. DNA Repair (Amst.) 2007, 6:329-343.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 329-343
    • St-Laurent, J.F.1    Gagnon, S.N.2    Dequen, F.3    Hardy, I.4    Desnoyers, S.5
  • 143
    • 0035012606 scopus 로고    scopus 로고
    • DNA strand break-sensing molecule poly(ADP-Ribose) polymerase cooperates with p53 in telomere function, chromosome stability, and tumor suppression
    • Tong W.M., Hande M.P., Lansdorp P.M., Wang Z.Q. DNA strand break-sensing molecule poly(ADP-Ribose) polymerase cooperates with p53 in telomere function, chromosome stability, and tumor suppression. Mol. Cell. Biol. 2001, 21:4046-4054.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4046-4054
    • Tong, W.M.1    Hande, M.P.2    Lansdorp, P.M.3    Wang, Z.Q.4
  • 144
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • Tulin A., Spradling A. Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci. Science 2003, 299:560-562.
    • (2003) Science , vol.299 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 145
    • 0037102454 scopus 로고    scopus 로고
    • The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development
    • Tulin A., Stewart D., Spradling A.C. The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development. Genes Dev. 2002, 16:2108-2119.
    • (2002) Genes Dev. , vol.16 , pp. 2108-2119
    • Tulin, A.1    Stewart, D.2    Spradling, A.C.3
  • 146
    • 2142829614 scopus 로고    scopus 로고
    • Regulation of chromatin structure and gene activity by poly(ADP-ribose) polymerases
    • Tulin A., Chinenov Y., Spradling A. Regulation of chromatin structure and gene activity by poly(ADP-ribose) polymerases. Curr. Top. Dev. Biol. 2003, 56:55-83.
    • (2003) Curr. Top. Dev. Biol. , vol.56 , pp. 55-83
    • Tulin, A.1    Chinenov, Y.2    Spradling, A.3
  • 147
    • 33644777616 scopus 로고    scopus 로고
    • Drosophila poly(ADP-ribose) glycohydrolase mediates chromatin structure and SIR2-dependent silencing
    • Tulin A., Naumova N.M., Menon A.K., Spradling A.C. Drosophila poly(ADP-ribose) glycohydrolase mediates chromatin structure and SIR2-dependent silencing. Genetics 2006, 172:363-371.
    • (2006) Genetics , vol.172 , pp. 363-371
    • Tulin, A.1    Naumova, N.M.2    Menon, A.K.3    Spradling, A.C.4
  • 149
    • 35648955118 scopus 로고    scopus 로고
    • The DNA binding and catalytic domains of poly(ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription
    • Wacker D.A., Ruhl D.D., Balagamwala E.H., Hope K.M., Zhang T., Kraus W.L. The DNA binding and catalytic domains of poly(ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription. Mol. Cell. Biol. 2007, 27:7475-7485.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7475-7485
    • Wacker, D.A.1    Ruhl, D.D.2    Balagamwala, E.H.3    Hope, K.M.4    Zhang, T.5    Kraus, W.L.6
  • 150
  • 152
    • 46449122616 scopus 로고    scopus 로고
    • Polyubiquitylation of PARP-1 through ubiquitin K48 is modulated by activated DNA, NAD+, and dipeptides
    • Wang T., Simbulan-Rosenthal C.M., Smulson M.E., Chock P.B., Yang D.C. Polyubiquitylation of PARP-1 through ubiquitin K48 is modulated by activated DNA, NAD+, and dipeptides. J. Cell. Biochem. 2008, 104:318-328.
    • (2008) J. Cell. Biochem. , vol.104 , pp. 318-328
    • Wang, T.1    Simbulan-Rosenthal, C.M.2    Smulson, M.E.3    Chock, P.B.4    Yang, D.C.5
  • 155
    • 44949253890 scopus 로고    scopus 로고
    • Poly ADP-ribose polymerase-1: an international molecule of mystery
    • Woodhouse B.C., Dianov G.L. Poly ADP-ribose polymerase-1: an international molecule of mystery. DNA Repair (Amst.) 2008, 7:1077-1086.
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 1077-1086
    • Woodhouse, B.C.1    Dianov, G.L.2
  • 157
    • 41549155890 scopus 로고    scopus 로고
    • Toward specific functions of poly(ADP-ribose) polymerase-2
    • Yelamos J., Schreiber V., Dantzer F. Toward specific functions of poly(ADP-ribose) polymerase-2. Trends Mol. Med. 2008, 14:169-178.
    • (2008) Trends Mol. Med. , vol.14 , pp. 169-178
    • Yelamos, J.1    Schreiber, V.2    Dantzer, F.3
  • 159
    • 77953290752 scopus 로고    scopus 로고
    • SIRT1-dependent regulation of chromatin and transcription: linking NAD(+) metabolism and signaling to the control of cellular functions
    • Zhang T., Kraus W.L. SIRT1-dependent regulation of chromatin and transcription: linking NAD(+) metabolism and signaling to the control of cellular functions. Biochim. Biophys. Acta. 2009, 1804:1666-1675.
    • (2009) Biochim. Biophys. Acta. , vol.1804 , pp. 1666-1675
    • Zhang, T.1    Kraus, W.L.2
  • 160
    • 34247383146 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase mediates hydrogen peroxide-induced cell death via sustained poly(ADP-ribose) polymerase-1 activation
    • Zhang S., Lin Y., Kim Y.S., Hande M.P., Liu Z.G., Shen H.M. c-Jun N-terminal kinase mediates hydrogen peroxide-induced cell death via sustained poly(ADP-ribose) polymerase-1 activation. Cell Death Differ. 2007, 14:1001-1010.
    • (2007) Cell Death Differ. , vol.14 , pp. 1001-1010
    • Zhang, S.1    Lin, Y.2    Kim, Y.S.3    Hande, M.P.4    Liu, Z.G.5    Shen, H.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.