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Volumn 19, Issue 17, 2005, Pages 1951-1967

Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal

Author keywords

NAD+; PARP 1; Poly(ADP ribosyl)ation

Indexed keywords

GLYCOSIDASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; POLY(ADENOSINE DIPHOSPHATE RIBOSE); POLY(ADENOSINE DIPHOSPHATE RIBOSE)GLYCOHYDROLASE; UNCLASSIFIED DRUG;

EID: 24344454692     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1331805     Document Type: Review
Times cited : (705)

References (141)
  • 2
    • 0029162298 scopus 로고
    • Dissection of ADP-ribose polymer synthesis into individual steps of initiation, elongation, and branching
    • Alvarez-Gonzalez, R. and Mendoza-Alvarez, H. 1995. Dissection of ADP-ribose polymer synthesis into individual steps of initiation, elongation, and branching. Biochimie 77: 403-407.
    • (1995) Biochimie , vol.77 , pp. 403-407
    • Alvarez-Gonzalez, R.1    Mendoza-Alvarez, H.2
  • 6
    • 0033953753 scopus 로고    scopus 로고
    • Identification of poly(ADP-ribose) polymerase as a transcriptional coactivator of the human T-cell leukemia virus type 1 Tax protein
    • Anderson, M.G., Scoggin, K.E., Simbulan-Rosenthal, C.M., and Steadman, J.A. 2000. Identification of poly(ADP-ribose) polymerase as a transcriptional coactivator of the human T-cell leukemia virus type 1 Tax protein. J. Virol. 74: 2169-2177.
    • (2000) J. Virol. , vol.74 , pp. 2169-2177
    • Anderson, M.G.1    Scoggin, K.E.2    Simbulan-Rosenthal, C.M.3    Steadman, J.A.4
  • 8
    • 0038329323 scopus 로고    scopus 로고
    • Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • Anderson, R.M., Bitterman, K.J., Wood, J.G., Medvedik, O., and Sinclair, D.A. 2003. Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae. Nature 423: 181-185.
    • (2003) Nature , vol.423 , pp. 181-185
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3    Medvedik, O.4    Sinclair, D.A.5
  • 9
    • 0037442006 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 regulates activation of activator protein-1 in murine fibroblasts
    • Andreone, T.L., O'Connor, M., Denenberg, A., Hake, P.W., and Zingarelli, B. 2003. Poly(ADP-ribose) polymerase-1 regulates activation of activator protein-1 in murine fibroblasts. J. Immunol. 170: 2113-2120.
    • (2003) J. Immunol. , vol.170 , pp. 2113-2120
    • Andreone, T.L.1    O'Connor, M.2    Denenberg, A.3    Hake, P.W.4    Zingarelli, B.5
  • 10
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • Araki, T., Sasaki, Y., and Milbrandt, J. 2004. Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 305: 1010-1013.
    • (2004) Science , vol.305 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 13
    • 0036142055 scopus 로고    scopus 로고
    • Detection of poly(ADP-ribose) polymerase activation in oxidatively stressed cells and tissues using biotinylated NAD substrate
    • Bakondi, E., Bai, P., Szabo, E.E., Hunyadi, J., Gergely, P., Szabo, C., and Virag, L. 2002. Detection of poly(ADP-ribose) polymerase activation in oxidatively stressed cells and tissues using biotinylated NAD substrate. J. Histochem. Cytochem. 50: 91-98.
    • (2002) J. Histochem. Cytochem. , vol.50 , pp. 91-98
    • Bakondi, E.1    Bai, P.2    Szabo, E.E.3    Hunyadi, J.4    Gergely, P.5    Szabo, C.6    Virag, L.7
  • 14
    • 0035910395 scopus 로고    scopus 로고
    • Insulators and boundaries: Versatile regulatory elements in the eukaryotic
    • Bell, A.C., West, A.G., and Felsenfeld, G. 2001. Insulators and boundaries: Versatile regulatory elements in the eukaryotic. Science 291: 447-450.
    • (2001) Science , vol.291 , pp. 447-450
    • Bell, A.C.1    West, A.G.2    Felsenfeld, G.3
  • 16
    • 1542346420 scopus 로고    scopus 로고
    • The new life of a centenarian: Signalling functions of NAD(P)
    • Berger, F., Ramirez-Hernandez, M.H., and Ziegler, M. 2004. The new life of a centenarian: Signalling functions of NAD(P). Trends Biochem. Sci. 29: 111-118.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 111-118
    • Berger, F.1    Ramirez-Hernandez, M.H.2    Ziegler, M.3
  • 18
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman, K.J., Anderson, R.M., Cohen, H.Y., Latorre-Esteves, M., and Sinclair, D.A. 2002. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J. Biol. Chem. 277: 45099-45107.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 19
    • 0742323811 scopus 로고    scopus 로고
    • Alteration of poly(ADP-ribose) glycohydrolase nucleocytoplasmic shuttling characteristics upon cleavage by apoptotic proteases
    • Bonicalzi, M.E., Vodenicharov, M., Coulombe, M., Gagne, J.P., and Poirier, G.G. 2003. Alteration of poly(ADP-ribose) glycohydrolase nucleocytoplasmic shuttling characteristics upon cleavage by apoptotic proteases. Biol. Cell 95: 635-644.
    • (2003) Biol. Cell , vol.95 , pp. 635-644
    • Bonicalzi, M.E.1    Vodenicharov, M.2    Coulombe, M.3    Gagne, J.P.4    Poirier, G.G.5
  • 20
    • 0038449141 scopus 로고    scopus 로고
    • PARP-1, a determinant of cell survival in response to DNA damage
    • Bouchard, V.J., Rouleau, M., and Poirier, G.G. 2003. PARP-1, a determinant of cell survival in response to DNA damage. Exp. Hematol. 31: 446-454.
    • (2003) Exp. Hematol. , vol.31 , pp. 446-454
    • Bouchard, V.J.1    Rouleau, M.2    Poirier, G.G.3
  • 22
    • 0035495529 scopus 로고    scopus 로고
    • PARP-1: A regulator of genomic stability linked with mammalian longevity
    • Bürkle, A. 2001a. PARP-1: A regulator of genomic stability linked with mammalian longevity. Chembiochem. 2: 725-728.
    • (2001) Chembiochem. , vol.2 , pp. 725-728
    • Bürkle, A.1
  • 23
    • 0034814670 scopus 로고    scopus 로고
    • Physiology and pathophysiology of poly(ADP-ribosyl)ation
    • _. 2001b. Physiology and pathophysiology of poly(ADP-ribosyl)ation. Bioessays 23: 795-806.
    • (2001) Bioessays , vol.23 , pp. 795-806
  • 26
    • 0034615948 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a B-MYB coactivator
    • Cervellera, M.N. and Sala, A. 2000. Poly(ADP-ribose) polymerase is a B-MYB coactivator. J. Biol. Chem. 275: 10692-10696.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10692-10696
    • Cervellera, M.N.1    Sala, A.2
  • 27
    • 0002160618 scopus 로고
    • Nicotinamide mononucleotide activation of a new DNA-dependent poly-adenylic acid synthesizing enzyme
    • Chambon, P., Weill, J.D., and Mandel, J.L. 1963. Nicotinamide mononucleotide activation of a new DNA-dependent poly-adenylic acid synthesizing enzyme. Biochem. Biophys. Res. Comm. 11: 39-43.
    • (1963) Biochem. Biophys. Res. Comm. , vol.11 , pp. 39-43
    • Chambon, P.1    Weill, J.D.2    Mandel, J.L.3
  • 28
    • 10344234720 scopus 로고    scopus 로고
    • Poly(ADP-ribose) is required for spindle assembly and structure
    • Chang, P., Jacobson, M.K., and Mitchison, T.J. 2004. Poly(ADPribose) is required for spindle assembly and structure. Nature 432: 645-649.
    • (2004) Nature , vol.432 , pp. 645-649
    • Chang, P.1    Jacobson, M.K.2    Mitchison, T.J.3
  • 29
    • 0037067597 scopus 로고    scopus 로고
    • Cell biology. PARP-1 - A perpetrator of apoptotic cell death?
    • Chiarugi, A. and Moskowitz, M.A. 2002. Cell biology. PARP-1 - A perpetrator of apoptotic cell death? Science 297: 200-201.
    • (2002) Science , vol.297 , pp. 200-201
    • Chiarugi, A.1    Moskowitz, M.A.2
  • 31
    • 4744360718 scopus 로고    scopus 로고
    • Neuronal trauma model: In search of Thanatos
    • Cole, K. and Perez-Polo, J.R. 2004. Neuronal trauma model: In search of Thanatos. Int. J. Dev. Neurosci. 22: 485-496.
    • (2004) Int. J. Dev. Neurosci. , vol.22 , pp. 485-496
    • Cole, K.1    Perez-Polo, J.R.2
  • 32
    • 0035796476 scopus 로고    scopus 로고
    • Loss of poly(ADP-ribose) polymerase-1 causes increased tumour latency in p53-deficient mice
    • Conde, C., Mark, M., Oliver, F.J., Huber, A., de Murcia, G., and Menissier de Murcia, J. 2001. Loss of poly(ADP-ribose) polymerase-1 causes increased tumour latency in p53-deficient mice. EMBO J. 20: 3535-3543.
    • (2001) EMBO J. , vol.20 , pp. 3535-3543
    • Conde, C.1    Mark, M.2    Oliver, F.J.3    Huber, A.4    De Murcia, G.5    Menissier De Murcia, J.6
  • 33
    • 0036132673 scopus 로고    scopus 로고
    • Role for the related poly(ADP-ribose) polymerases tankyrase 1 and 2 at human telomeres
    • Cook, B.D., Dynek, J.N., Chang, W., Shostak, G., and Smith, S. 2002. Role for the related poly(ADP-ribose) polymerases tankyrase 1 and 2 at human telomeres. Mol. Cell. Biol. 22: 332-342.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 332-342
    • Cook, B.D.1    Dynek, J.N.2    Chang, W.3    Shostak, G.4    Smith, S.5
  • 35
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours, D., Desnoyers, S., D'Silva, I., and Poirier, G.G. 1999. Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 342 (Pt 2): 249-268.
    • (1999) Biochem. J. , vol.342 , Issue.2 PART , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 37
    • 0035425899 scopus 로고    scopus 로고
    • Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism
    • Davidovic, L., Vodenicharov, M., Affar, E.B., and Poirier, G.G. 2001. Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism. Exp. Cell Res. 268: 7-13.
    • (2001) Exp. Cell Res. , vol.268 , pp. 7-13
    • Davidovic, L.1    Vodenicharov, M.2    Affar, E.B.3    Poirier, G.G.4
  • 38
    • 0036020543 scopus 로고    scopus 로고
    • Modulating poly (ADP-ribose) polymerase activity: Potential for the prevention and therapy of pathogenic situations involving DNA damage and oxidative stress
    • Decker, P. and Muller, S. 2002. Modulating poly (ADP-ribose) polymerase activity: Potential for the prevention and therapy of pathogenic situations involving DNA damage and oxidative stress. Curr. Pharm. Biotechnol. 3: 275-283.
    • (2002) Curr. Pharm. Biotechnol. , vol.3 , pp. 275-283
    • Decker, P.1    Muller, S.2
  • 40
    • 1842424729 scopus 로고    scopus 로고
    • Resolution of sister telomere association is required for progression through mitosis
    • Dynek, J.N. and Smith, S. 2004. Resolution of sister telomere association is required for progression through mitosis. Science 304: 97-100.
    • (2004) Science , vol.304 , pp. 97-100
    • Dynek, J.N.1    Smith, S.2
  • 42
    • 7744235672 scopus 로고    scopus 로고
    • Death by design: Apoptosis, necrosis and autophagy
    • Edinger, A.L. and Thompson, C.B. 2004. Death by design: Apoptosis, necrosis and autophagy. Curr. Opin. Cell Biol. 16: 663-669.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 663-669
    • Edinger, A.L.1    Thompson, C.B.2
  • 44
    • 0038641860 scopus 로고    scopus 로고
    • A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins
    • Gagne, J.P., Hunter, J.M., Labrecque, B., Chabot, B., and Poirier, G.G. 2003. A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins. Biochem. J. 371: 331-340.
    • (2003) Biochem. J. , vol.371 , pp. 331-340
    • Gagne, J.P.1    Hunter, J.M.2    Labrecque, B.3    Chabot, B.4    Poirier, G.G.5
  • 45
    • 0027081044 scopus 로고
    • Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span
    • Grube, K. and Burkle, A. 1992. Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span. Proc. Natl. Acad. Sci. 89: 11759-11763.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 11759-11763
    • Grube, K.1    Burkle, A.2
  • 46
    • 0033830186 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 in the nervous system
    • Ha, H.C. and Snyder, S.H. 2000. Poly(ADP-ribose) polymerase-1 in the nervous system. Neurobiol. Dis. 7: 225-239.
    • (2000) Neurobiol. Dis. , vol.7 , pp. 225-239
    • Ha, H.C.1    Snyder, S.H.2
  • 47
    • 0035906329 scopus 로고    scopus 로고
    • Niacin, poly(ADP-ribose) polymerase-1 and genomic stability
    • Hageman, G.J. and Stierum, R.H. 2001. Niacin, poly(ADP-ribose) polymerase-1 and genomic stability. Mutat. Res. 475: 45-56.
    • (2001) Mutat. Res. , vol.475 , pp. 45-56
    • Hageman, G.J.1    Stierum, R.H.2
  • 48
    • 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., and Uchida, K. 1998. Genomic organization of Drosophila poly(ADP-ribose) polymerase and distribution of its mRNA during development. J. Biol. Chem. 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
  • 49
    • 0347719407 scopus 로고    scopus 로고
    • Loss of poly(ADP-ribose) glycohydrolase causes progressive neurodegeneration in Drosophila melanogaster
    • Hanai, S., Kanai, M., Ohashi, S., Okamoto, K., Yamada, M., Takahashi, H., and Miwa, M. 2004. Loss of poly(ADP-ribose) glycohydrolase causes progressive neurodegeneration in Drosophila melanogaster. Proc. Natl. Acad. Sci. 101: 82-86.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 82-86
    • Hanai, S.1    Kanai, M.2    Ohashi, S.3    Okamoto, K.4    Yamada, M.5    Takahashi, H.6    Miwa, M.7
  • 50
    • 0036710459 scopus 로고    scopus 로고
    • The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-κB in inflammatory disorders
    • Hassa, P.O. and Hottiger, M.O. 2002. The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-κB in inflammatory disorders. Cell Mol. Life Sci. 59: 1534-1553.
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 1534-1553
    • Hassa, P.O.1    Hottiger, M.O.2
  • 51
    • 0035824647 scopus 로고    scopus 로고
    • The enzymatic and DNA binding activity of PARP-1 are not required for NF-κ B coactivator function
    • Hassa, P.O., Covic, M., Hasan, S., Imhof, R., and Hottiger, M.O. 2001. The enzymatic and DNA binding activity of PARP-1 are not required for NF-κ B coactivator function. J. Biol. Chem. 276: 45588-45597.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45588-45597
    • Hassa, P.O.1    Covic, M.2    Hasan, S.3    Imhof, R.4    Hottiger, M.O.5
  • 53
    • 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., and Poirier, G.G. 1989. The effect of poly(ADP-ribosyl)ation on native and H1-depleted chromatin. A role of poly(ADP-ribosyl)ation on core nucleosome structure. J. Biol. Chem. 264: 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
  • 54
    • 10944253639 scopus 로고    scopus 로고
    • Activating the PARP-1 sensor component of the groucho/TLE1 corepressor complex mediates a CaMKinase IIδ-dependent neurogenic gene activation pathway
    • Ju, B.G., Solum, D., Song, E.J., Lee, K.J., Rose, D.W., Glass, C.K., and Rosenfeld, M.G. 2004. Activating the PARP-1 sensor component of the groucho/TLE1 corepressor complex mediates a CaMKinase IIδ-dependent neurogenic gene activation pathway. Cell 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
  • 55
    • 0035929591 scopus 로고    scopus 로고
    • TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression
    • Kaminker, P.G., Kim, S.H., Taylor, R.D., Zebarjadian, Y., Funk, W.D., Morin, G.B., Yaswen, P., and Campisi, J. 2001. TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression. J. Biol. Chem. 276: 35891-35899.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35891-35899
    • Kaminker, P.G.1    Kim, S.H.2    Taylor, R.D.3    Zebarjadian, Y.4    Funk, W.D.5    Morin, G.B.6    Yaswen, P.7    Campisi, J.8
  • 56
    • 0037379179 scopus 로고    scopus 로고
    • Involvement of poly(ADP-ribose) polymerase 1 and poly(ADP-ribosyl)ation in regulation of centrosome function
    • Kanai, M., Tong, W.M., Sugihara, E., Wang, Z.Q., Fukasawa, K., and Miwa, M. 2003. Involvement of poly(ADP-ribose) polymerase 1 and poly(ADP-ribosyl)ation in regulation of centrosome function. Mol. Cell. Biol. 23: 2451-2462.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2451-2462
    • Kanai, M.1    Tong, W.M.2    Sugihara, E.3    Wang, Z.Q.4    Fukasawa, K.5    Miwa, M.6
  • 58
    • 0027255417 scopus 로고
    • Specific proteolytic cleavage of poly-(ADP-ribose) polymerase: An early marker of chemotherapy-induced apoptosis
    • Kaufmann, S.H., Desnoyers, S., Ottaviano, Y., Davidson, N.E., and Poirier, G.G. 1993. Specific proteolytic cleavage of poly-(ADP-ribose) polymerase: An early marker of chemotherapy-induced apoptosis. Cancer Res. 53: 3976-3985.
    • (1993) Cancer Res. , vol.53 , pp. 3976-3985
    • Kaufmann, S.H.1    Desnoyers, S.2    Ottaviano, Y.3    Davidson, N.E.4    Poirier, G.G.5
  • 60
    • 10944227347 scopus 로고    scopus 로고
    • +-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1
    • +-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1. Cell 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
  • 62
    • 0038682011 scopus 로고    scopus 로고
    • PARP goes transcription
    • Kraus, W.L. and Lis, J.T. 2003. PARP goes transcription. Cell 113: 677-683.
    • (2003) Cell , vol.113 , pp. 677-683
    • Kraus, W.L.1    Lis, J.T.2
  • 63
    • 0037131343 scopus 로고    scopus 로고
    • Coenzymatic activity of randomly broken or intact double-stranded DNAs in auto and histone H1 trans-poly(ADP-ribosylation), catalyzed by poly(ADP-ribose) polymerase (PARP I)
    • Kun, E., Kirsten, E., and Ordahl, C.P. 2002. Coenzymatic activity of randomly broken or intact double-stranded DNAs in auto and histone H1 trans-poly(ADP-ribosylation), catalyzed by poly(ADP-ribose) polymerase (PARP I). J. Biol. Chem. 277: 39066-39069.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39066-39069
    • Kun, E.1    Kirsten, E.2    Ordahl, C.P.3
  • 66
    • 0242585417 scopus 로고    scopus 로고
    • Genetic cooperation between the Werner syndrome protein and poly(ADP-ribose) polymerase-1 in preventing chromatid breaks, complex chromosomal rearrangements, and cancer in mice
    • Lebel, M., Lavoie, J., Gaudreault, I., Bronsard, M., and Drouin, R. 2003. Genetic cooperation between the Werner syndrome protein and poly(ADP-ribose) polymerase-1 in preventing chromatid breaks, complex chromosomal rearrangements, and cancer in mice. Am. J. Pathol. 162: 1559-1569.
    • (2003) Am. J. Pathol. , vol.162 , pp. 1559-1569
    • Lebel, M.1    Lavoie, J.2    Gaudreault, I.3    Bronsard, M.4    Drouin, R.5
  • 67
  • 68
    • 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., and Szabo, C. 2001. 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. 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
  • 71
    • 33645621928 scopus 로고    scopus 로고
    • DNA damage signaling through poly(ADP-ribose)
    • ed. A. Burkle, Landes Bioscience, Georgetown, TX
    • Malanga, M. and Althaus, F.R. 2005. DNA damage signaling through poly(ADP-ribose). In Poly(ADP-ribosyl)ation (ed. A. Burkle), pp. 41-50. Landes Bioscience, Georgetown, TX.
    • (2005) Poly(ADP-ribosyl)ation , pp. 41-50
    • Malanga, M.1    Althaus, F.R.2
  • 74
    • 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., and de Murcia, G. 1998. XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol. Cell. Biol. 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
  • 78
    • 0023117437 scopus 로고
    • Release of core DNA from nucleosomal core particles following (ADP-ribose)n-modification in vitro
    • Mathis, G. and Althaus, F.R. 1987. Release of core DNA from nucleosomal core particles following (ADP-ribose)n-modification in vitro. Biochem. Biophys. Res. Commun. 143: 1049-1054.
    • (1987) Biochem. Biophys. Res. Commun. , vol.143 , pp. 1049-1054
    • Mathis, G.1    Althaus, F.R.2
  • 79
    • 0030938581 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase enhances activator-dependent transcription in vitro
    • Meisterernst, M., Stelzer, G., and Roeder, R.G. 1997. Poly(ADP-ribose) polymerase enhances activator-dependent transcription in vitro. Proc. Natl. Acad. Sci. 94: 2261-2265.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 2261-2265
    • Meisterernst, M.1    Stelzer, G.2    Roeder, R.G.3
  • 81
    • 2942707644 scopus 로고    scopus 로고
    • Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments
    • Meyer-Ficca, M.L., Meyer, R.G., Coyle, D.L., Jacobson, E.L., and Jacobson, M.K. 2004. Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments. Exp. Cell Res. 297: 521-532.
    • (2004) Exp. Cell Res. , vol.297 , pp. 521-532
    • Meyer-Ficca, M.L.1    Meyer, R.G.2    Coyle, D.L.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 83
    • 0021099468 scopus 로고
    • Probable helical conformation of poly(ADP-ribose). The effect of cations on spectral properties
    • Minaga, T. and Kun, E. 1983a. Probable helical conformation of poly(ADP-ribose). The effect of cations on spectral properties. J. Biol. Chem. 258: 5726-5730.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5726-5730
    • Minaga, T.1    Kun, E.2
  • 84
    • 0021111550 scopus 로고
    • Spectral analysis of the conformation of polyadenosine diphosphoribose. Evidence indicating secondary structure
    • _. 1983b. Spectral analysis of the conformation of polyadenosine diphosphoribose. Evidence indicating secondary structure. J. Biol. Chem. 258: 725-730.
    • (1983) J. Biol. Chem. , vol.258 , pp. 725-730
  • 85
    • 0032891437 scopus 로고    scopus 로고
    • Functional analysis of poly(ADP-ribose) polymerase in Drosophila melanogaster
    • Miwa, M., Hanai, S., Poltronieri, P., Uchida, M., and Uchida, K. 1999. Functional analysis of poly(ADP-ribose) polymerase in Drosophila melanogaster. Mol. Cell. Biochem. 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
  • 86
    • 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., and Wang, Z.Q. 1997. Genetic interaction between PARP and DNA-PK in V(D)J recombination and tumorigenesis. Nat. Genet. 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
  • 88
    • 3142616449 scopus 로고    scopus 로고
    • The human Rap1 protein complex and modulation of telomere length
    • O'Connor, M.S., Safari, A., Liu, D., Qin, J., and Songyang, Z. 2004. The human Rap1 protein complex and modulation of telomere length. J. Biol. Chem. 279: 28585-28591.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28585-28591
    • O'Connor, M.S.1    Safari, A.2    Liu, D.3    Qin, J.4    Songyang, Z.5
  • 89
    • 0034806128 scopus 로고    scopus 로고
    • Transcription factor Yin Yang 1 stimulates poly(ADP-ribosyl)ation and DNA repair
    • Oei, S.L. and Shi, Y. 2001. Transcription factor Yin Yang 1 stimulates poly(ADP-ribosyl)ation and DNA repair. Biochem. Biophys. Res. Commun. 284: 450-454.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 450-454
    • Oei, S.L.1    Shi, Y.2
  • 90
    • 0019876860 scopus 로고
    • Poly-(ADP-ribose) synthetase, a main acceptor of poly(ADP-ribose) in isolated nuclei
    • Ogata, N., Ueda, K., Kawaichi, M., and Hayaishi, O. 1981. Poly-(ADP-ribose) synthetase, a main acceptor of poly(ADP-ribose) in isolated nuclei. J. Biol. Chem. 256: 4135-4137.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4135-4137
    • Ogata, N.1    Ueda, K.2    Kawaichi, M.3    Hayaishi, O.4
  • 92
    • 0021339860 scopus 로고
    • ADP-ribosyl protein lyase. Purification, properties, and identification of the product
    • Oka, J., Ueda, K., Hayaishi, O., Komura, H., and Nakanishi, K. 1984. ADP-ribosyl protein lyase. Purification, properties, and identification of the product. J. Biol. Chem. 259: 986-995.
    • (1984) J. Biol. Chem. , vol.259 , pp. 986-995
    • Oka, J.1    Ueda, K.2    Hayaishi, O.3    Komura, H.4    Nakanishi, K.5
  • 93
    • 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., and Yasui, A. 2003. Spatial and temporal cellular responses to single-strand breaks in human cells. Mol. Cell. Biol. 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
  • 95
    • 0026506694 scopus 로고
    • Noncovalent interactions of poly(adenosine diphosphate ribose) with histones
    • Panzeter, P.L., Realini, C.A., and Althaus, F.R. 1992. Noncovalent interactions of poly(adenosine diphosphate ribose) with histones. Biochemistry 31: 1379-1385.
    • (1992) Biochemistry , vol.31 , pp. 1379-1385
    • Panzeter, P.L.1    Realini, C.A.2    Althaus, F.R.3
  • 97
    • 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., and Althaus, F.R. 2000. Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 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
  • 99
    • 4844220063 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribose) glycohydrolase by gallotannin selectively up-regulates expression of proinflammatory genes
    • Rapizzi, E., Fossati, S., Moroni, F., and Chiarugi, A. 2004. Inhibition of poly(ADP-ribose) glycohydrolase by gallotannin selectively up-regulates expression of proinflammatory genes. Mol. Pharmacol. 66: 890-898.
    • (2004) Mol. Pharmacol. , vol.66 , pp. 890-898
    • Rapizzi, E.1    Fossati, S.2    Moroni, F.3    Chiarugi, A.4
  • 101
    • 0026730009 scopus 로고
    • Histone shuttling by poly-(ADP-ribosylation)
    • Realini, C.A. and Althaus, F.R. 1992. Histone shuttling by poly-(ADP-ribosylation). J. Biol. Chem. 267: 18858-18865.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18858-18865
    • Realini, C.A.1    Althaus, F.R.2
  • 102
    • 10944270187 scopus 로고    scopus 로고
    • The NAD biosynthesis pathway mediated by nicotinamide phosphoribo-syltransferase regulates Sir2 activity in mammalian cells
    • Revollo, J.R., Grimm, A.A., and Imai, S. 2004. The NAD biosynthesis pathway mediated by nicotinamide phosphoribo-syltransferase regulates Sir2 activity in mammalian cells. J. Biol. Chem. 279: 50754-50763.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50754-50763
    • Revollo, J.R.1    Grimm, A.A.2    Imai, S.3
  • 103
    • 0037068372 scopus 로고    scopus 로고
    • DNA methylation and chromatin - Unraveling the tangled web
    • Robertson, K.D. 2002. DNA methylation and chromatin - Unraveling the tangled web. Oncogene 21: 5361-5379.
    • (2002) Oncogene , vol.21 , pp. 5361-5379
    • Robertson, K.D.1
  • 105
    • 0037829279 scopus 로고    scopus 로고
    • Reconstructing eukaryotic NAD metabolism
    • Rongvaux, A., Andris, F., Van Gool, F., and Leo, O. 2003. Reconstructing eukaryotic NAD metabolism. Bioessays 25: 683-690.
    • (2003) Bioessays , vol.25 , pp. 683-690
    • Rongvaux, A.1    Andris, F.2    Van Gool, F.3    Leo, O.4
  • 106
    • 0025342903 scopus 로고
    • Evidence for an inhibitory effect exerted by yeast NMN adenylyltransferase on poly-(ADP-ribose) polymerase activity
    • Ruggieri, S., Gregori, L., Natalini, P., Vita, A., Emanuelli, M., Raffaelli, N., and Magni, G. 1990. Evidence for an inhibitory effect exerted by yeast NMN adenylyltransferase on poly-(ADP-ribose) polymerase activity. Biochemistry 29: 2501-2506.
    • (1990) Biochemistry , vol.29 , pp. 2501-2506
    • Ruggieri, S.1    Gregori, L.2    Natalini, P.3    Vita, A.4    Emanuelli, M.5    Raffaelli, N.6    Magni, G.7
  • 109
    • 0037178870 scopus 로고    scopus 로고
    • Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose) polymerase-1 protein and are poly(ADP-ribosyl)ated
    • Saxena, A., Saffery, R., Wong, L.H., Kalitsis, P., and Choo, K.H. 2002a. Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose) polymerase-1 protein and are poly(ADP-ribosyl)ated. J. Biol. Chem. 277: 26921-26926.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26921-26926
    • Saxena, A.1    Saffery, R.2    Wong, L.H.3    Kalitsis, P.4    Choo, K.H.5
  • 110
    • 0037106439 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 2 localizes to mammalian active centromeres and interacts with PARP-1, Cenpa, Cenpb and Bub3, but not Cenpc
    • Saxena, A., Wong, L.H., Kalitsis, P., Earle, E., Shaffer, L.G., and Choo, K.H. 2002b. Poly(ADP-ribose) polymerase 2 localizes to mammalian active centromeres and interacts with PARP-1, Cenpa, Cenpb and Bub3, but not Cenpc. Hum. Mol. Genet. 11: 2319-2329.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2319-2329
    • Saxena, A.1    Wong, L.H.2    Kalitsis, P.3    Earle, E.4    Shaffer, L.G.5    Choo, K.H.6
  • 111
    • 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., Ame, J.C., Dolle, P., Schultz, I., Rinaldi, B., Fraulob, V., Menissier de Murcia, J., and de Murcia, G. 2002. Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. J. Biol. Chem. 277: 23028-23036.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23028-23036
    • Schreiber, V.1    Ame, J.C.2    Dolle, P.3    Schultz, I.4    Rinaldi, B.5    Fraulob, V.6    Menissier De Murcia, J.7    De Murcia, G.8
  • 112
    • 0035831109 scopus 로고    scopus 로고
    • Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis
    • Schweiger, M., Hennig, K., Lerner, F., Niere, M., Hirsch-Kauffmann, M., Specht, T., Weise, C., Oei, S.L., and Ziegler, M. 2001. Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis. FEBS Lett. 492: 95-100.
    • (2001) FEBS Lett. , vol.492 , pp. 95-100
    • Schweiger, M.1    Hennig, K.2    Lerner, F.3    Niere, M.4    Hirsch-Kauffmann, M.5    Specht, T.6    Weise, C.7    Oei, S.L.8    Ziegler, M.9
  • 113
    • 0034733928 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1: What have we learned from the deficient mouse model?
    • Shall, S. and de Murcia, G. 2000. Poly(ADP-ribose) polymerase-1: What have we learned from the deficient mouse model? Mutat. Res. 460: 1-15.
    • (2000) Mutat. Res. , vol.460 , pp. 1-15
    • Shall, S.1    De Murcia, G.2
  • 114
    • 20044369162 scopus 로고    scopus 로고
    • Parp-1 deficiency causes an increase of deletion mutations and insertions/rearrangements in vivo after treatment with an alkylating agent
    • Shibata, A., Kamada, N., Masumura, K., Nohmi, T., Kobayashi, S., Teraoka, H., Nakagama, H., Sugimura, T., Suzuki, H., and Masutani, M. 2005. Parp-1 deficiency causes an increase of deletion mutations and insertions/ rearrangements in vivo after treatment with an alkylating agent. Oncogene 24: 1328-1337.
    • (2005) Oncogene , vol.24 , pp. 1328-1337
    • Shibata, A.1    Kamada, N.2    Masumura, K.3    Nohmi, T.4    Kobayashi, S.5    Teraoka, H.6    Nakagama, H.7    Sugimura, T.8    Suzuki, H.9    Masutani, M.10
  • 115
    • 0035281786 scopus 로고    scopus 로고
    • The world according to PARP
    • Smith, S. 2001. The world according to PARP. Trends Biochem. Sci. 26: 174-179.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 174-179
    • Smith, S.1
  • 116
    • 0032721132 scopus 로고    scopus 로고
    • Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes
    • Smith, S. and de Lange, T. 1999. Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes. J. Cell Sci. 112 (Pt 21): 3649-3656.
    • (1999) J. Cell Sci. , vol.112 , Issue.21 PART , pp. 3649-3656
    • Smith, S.1    De Lange, T.2
  • 117
    • 0036022402 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: An update
    • Soldani, C. and Scovassi, A.I. 2002. Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: An update. Apoptosis 7: 321-328.
    • (2002) Apoptosis , vol.7 , pp. 321-328
    • Soldani, C.1    Scovassi, A.I.2
  • 119
    • 0032127666 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) synthetase in inflammation and ischaemia-reperfusion
    • Szabo, C. and Dawson, V.L. 1998. Role of poly(ADP-ribose) synthetase in inflammation and ischaemia-reperfusion. Trends Pharmacol. Sci. 19: 287-298.
    • (1998) Trends Pharmacol. Sci. , vol.19 , pp. 287-298
    • Szabo, C.1    Dawson, V.L.2
  • 120
    • 0021099354 scopus 로고
    • ADP-ribosylation of non-histone high mobility group proteins in intact cells
    • Tanuma, S. and Johnson, G.S. 1983. ADP-ribosylation of non-histone high mobility group proteins in intact cells. J. Biol. Chem. 258: 4067-4070.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4067-4070
    • Tanuma, S.1    Johnson, G.S.2
  • 121
    • 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., and Wang, Z.Q. 2001. DNA strand break-sensing molecule poly(ADP-ribose) polymerase cooperates with p53 in telomere function, chromosome stability, and tumor suppression. Mol. Cell. Biol. 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
  • 123
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly-(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • Tulin, A. and Spradling, A. 2003. Chromatin loosening by poly-(ADP)-ribose polymerase (PARP) at Drosophila puff loci. Science 299: 560-562.
    • (2003) Science , vol.299 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 124
    • 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., and Spradling, A.C. 2002. The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development. Genes & Dev. 16: 2108-2119.
    • (2002) Genes & Dev. , vol.16 , pp. 2108-2119
    • Tulin, A.1    Stewart, D.2    Spradling, A.C.3
  • 125
    • 0036893150 scopus 로고    scopus 로고
    • The relationship between the roles of BRCA genes in DNA repair and cancer predisposition
    • Tutt, A. and Ashworth, A. 2002. The relationship between the roles of BRCA genes in DNA repair and cancer predisposition. Trends Mol. Med. 8: 571-576.
    • (2002) Trends Mol. Med. , vol.8 , pp. 571-576
    • Tutt, A.1    Ashworth, A.2
  • 126
    • 33645632273 scopus 로고    scopus 로고
    • PARP-1 and the shape of cell death
    • ed. A. Burkle, Landes Bioscience, Georgetown, TX
    • Virag, L. 2005. PARP-1 and the shape of cell death. In Poly(ADPribosyl) ation (ed. A. Burkle), pp. 141-154. Landes Bioscience, Georgetown, TX.
    • (2005) Poly(ADP-ribosyl)ation , pp. 141-154
    • Virag, L.1
  • 127
    • 0242721664 scopus 로고    scopus 로고
    • Central role for the Werner syndrome protein/poly(ADP-ribose) polymerase 1 complex in the poly(ADP-ribosyl)ation pathway after DNA damage
    • von Kobbe, C., Harrigan, J.A., May, A., Opresko, P.L., Dawut, L., Cheng, W.H., and Bohr, V.A. 2003. Central role for the Werner syndrome protein/poly(ADP-ribose) polymerase 1 complex in the poly(ADP-ribosyl)ation pathway after DNA damage. Mol. Cell. Biol. 23: 8601-8613.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8601-8613
    • Von Kobbe, C.1    Harrigan, J.A.2    May, A.3    Opresko, P.L.4    Dawut, L.5    Cheng, W.H.6    Bohr, V.A.7
  • 128
    • 0028922462 scopus 로고
    • Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease
    • Wang, Z.Q., Auer, B., Stingl, L., Berghammer, H., Haidacher, D., Schweiger, M., and Wagner, E.F. 1995. Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease. Genes & Dev. 9: 509-520.
    • (1995) Genes & Dev. , vol.9 , pp. 509-520
    • Wang, Z.Q.1    Auer, B.2    Stingl, L.3    Berghammer, H.4    Haidacher, D.5    Schweiger, M.6    Wagner, E.F.7
  • 130
    • 0024276135 scopus 로고
    • The effect of poly(ADP-ribose) on interactions of DNA with histones H1, H3 and H4
    • Wesierska-Gadek, J. and Sauermann, G. 1988. The effect of poly(ADP-ribose) on interactions of DNA with histones H1, H3 and H4. Eur. J. Biochem. 173: 675-679.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 675-679
    • Wesierska-Gadek, J.1    Sauermann, G.2
  • 131
    • 0037685164 scopus 로고    scopus 로고
    • Breast and ovarian cancer
    • Wooster, R. and Weber, B.L. 2003. Breast and ovarian cancer. N. Engl. J. Med. 348: 2339-2347.
    • (2003) N. Engl. J. Med. , vol.348 , pp. 2339-2347
    • Wooster, R.1    Weber, B.L.2
  • 135
    • 0032569020 scopus 로고    scopus 로고
    • The unmethylated state of CpG islands in mouse fibroblasts depends on the poly(ADP-ribosyl) ation process
    • Zardo, G. and Caiafa, P. 1998. The unmethylated state of CpG islands in mouse fibroblasts depends on the poly(ADP-ribosyl) ation process. J. Biol. Chem. 273: 16517-16520.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16517-16520
    • Zardo, G.1    Caiafa, P.2
  • 138
    • 0041589716 scopus 로고    scopus 로고
    • Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked?
    • Zhang, J. 2003. Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked? Bioessays 25: 808-814.
    • (2003) Bioessays , vol.25 , pp. 808-814
    • Zhang, J.1
  • 139
    • 0028294246 scopus 로고
    • Nitric oxide activation of poly(ADP-ribose) synthetase in neurotoxicity
    • Zhang, J., Dawson, V.L., Dawson, T.M., and Snyder, S.H. 1994. Nitric oxide activation of poly(ADP-ribose) synthetase in neurotoxicity. Science 263: 687-689.
    • (1994) Science , vol.263 , pp. 687-689
    • Zhang, J.1    Dawson, V.L.2    Dawson, T.M.3    Snyder, S.H.4
  • 140
    • 0032514225 scopus 로고    scopus 로고
    • Genetic disruption of poly(ADP-ribose) synthetase inhibits the expression of P-selectin and intercellular adhesion molecule-1 in myocardial ischemia/reperfusion injury
    • Zingarelli, B., Salzman, A.L., and Szabo, C. 1998. Genetic disruption of poly(ADP-ribose) synthetase inhibits the expression of P-selectin and intercellular adhesion molecule-1 in myocardial ischemia/reperfusion injury. Circ. Res. 83: 85-94.
    • (1998) Circ. Res. , vol.83 , pp. 85-94
    • Zingarelli, B.1    Salzman, A.L.2    Szabo, C.3
  • 141
    • 2642536197 scopus 로고    scopus 로고
    • Alkylating DNA damage stimulates a regulated form of necrotic cell death
    • Zong, W.X., Ditsworth, D., Bauer, D.E., Wang, Z.Q., and Thompson, C.B. 2004. Alkylating DNA damage stimulates a regulated form of necrotic cell death. Genes & Dev. 18: 1272-1282.
    • (2004) Genes & Dev. , vol.18 , pp. 1272-1282
    • Zong, W.X.1    Ditsworth, D.2    Bauer, D.E.3    Wang, Z.Q.4    Thompson, C.B.5


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