Molecular and biochemical features of poly (ADP-ribose) metabolism

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

Walker, J. E., Saraste, M., Runswick, M. J., & Gay, N. J. (1982) · The EMBO Journal · doi:10.1002/j.1460-2075.1982.tb01276.x · Cited by 5,312

A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation

Shaw, G., & Kamen, R. (1986) · Cell · doi:10.1016/0092-8674(86)90341-7 · Cited by 4,012

Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes.

Miller, J., McLachlan, A. D., & Klug, A. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03825.x · Cited by 2,476

Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles

Kozak, M. (1983) · Microbiological Reviews · doi:10.1128/mmbr.47.1.1-45.1983 · Cited by 1,502

Sequence requirements for nuclear location of simian virus 40 large-T antigen

Kalderon, D., Richardson, W. D., Markham, A. F., & Smith, A. E. (1984) · Nature · doi:10.1038/311033a0 · Cited by 1,286

EUKARYOTIC TRANSCRIPTIONAL REGULATORY PROTEINS

Johnson, P. F., & McKnight, S. L. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.004055 · Cited by 1,234

Role of poly(ADP-ribose) formation in DNA repair

Satoh, M. S., & Lindahl, T. (1992) · Nature · doi:10.1038/356356a0 · Cited by 1,174

DNA bending at adenine · thymine tracts

Koo, H.-S., Wu, H.-M., & Crothers, D. M. (1986) · Nature · doi:10.1038/320501a0 · Cited by 1,022

Mechanism of transcriptional activation by Sp1: Evidence for coactivators

Pugh, B. F., & Tjian, R. (1990) · Cell · doi:10.1016/0092-8674(90)90683-6 · Cited by 1,001

Poly(ADP-Ribose) in the Cellular Response to DNA Damage

Berger, N. A. (1985) · Radiation Research · doi:10.2307/3576299 · Cited by 775

ADP-RIBOSYLATION

Ueda, K., & Hayaishi, O. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.000445 · Cited by 724

Transcription activation by the adenovirus E1a protein

Lillie, J. W., & Green, M. R. (1989) · Nature · doi:10.1038/338039a0 · Cited by 632

The helix-turn-helix DNA binding motif

Brennan, R. G., & Matthews, B. W. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94115-3 · Cited by 613

GENE AMPLIFICATION

Stark, G. R., & Wahl, G. M. (1984) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.53.070184.002311 · Cited by 583

Novel inhibitors of poly(ADP-ribose) synthetase

Purnell, M. R., & Whish, W. J. (1980) · Biochemical Journal · doi:10.1042/bj1850775 · Cited by 527

Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure.

Poirier, G. G., de Murcia, G., Jongstra-Bilen, J., Niedergang, C., & Mandel, P. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.11.3423 · Cited by 515

Zinc fingers and other metal-binding domains. Elements for interactions between macromolecules.

Berg, J. M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39172-0 · Cited by 505

Poly(ADP-ribose) synthesis in vitro programmed by damaged DNA. A comparison of DNA molecules containing different types of strand breaks.

Benjamin, R. C., & Gill, D. M. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70491-8 · Cited by 487

Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase.

Banasik, M., Komura, H., Shimoyama, M., & Ueda, K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45983-2 · Cited by 476

Phagocytes as Carcinogens: Malignant Transformation Produced by Human Neutrophils

Weitzman, S. A., Weitberg, A. B., Clark, E. P., & Stossel, T. P. (1985) · Science · doi:10.1126/science.3975611 · Cited by 441

The primary structure of transcription factor TFIIIA has 12 consecutive repeats

Brown, R. S., Sander, C., & Argos, P. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)80723-7 · Cited by 407

Determinants of messenger RNA stability

Brawerman, G. (1987) · Cell · doi:10.1016/0092-8674(87)90346-1 · Cited by 400

ADP-ribosylation of proteins. Enzymology and biological significance.

Althaus, F. R., & Richter, C. (1987) · PubMed · Cited by 371

Transcriptionally active chromatin

Reeves, R. (1984) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(84)90044-7 · Cited by 355

On the formation of a novel adenylic compound by enzymatic extracts of liver nuclei

Chambon, P., Weill, J. D., Doly, J., Strosser, M. T., & Mandel, P. (1966) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(66)90502-x · Cited by 344

ADP-Ribosylation of Proteins

Althaus, F. R., & Richter, C. (1987) · Molecular Biology Biochemistry and Biophysics · doi:10.1007/978-3-642-83077-8 · Cited by 289

The Involvement of Poly(ADP‐ribose) Polymerase in the Degradation of NAD Caused by γ‐Radiation and N‐Methyl‐N‐Nitrosourea

SKIDMORE, C. J., DAVIES, M. I., GOODWIN, P. M., HALLDORSSON, H., LEWIS, P. J., SHALL, S., & ZIA'EE, A. (1979) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1979.tb04225.x · Cited by 278

The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.

Gradwohl, G., Ménissier de Murcia, J. M., Molinete, M., Simonin, F., Koken, M., Hoeijmakers, J. H., & de Murcia, G. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.8.2990 · Cited by 277

MOLECULAR MECHANISMS OF TRANSCRIPTIONAL REGULATION IN YEAST

Struhl, K. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.005155 · Cited by 271

Quantitative studies of inhibitors of ADP-ribosylation in vitro and in vivo

Rankin, P. W., Jacobson, E. L., Benjamin, R. C., Moss, J., & Jacobson, M. K. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83741-3 · Cited by 264

Characterization of polymers of adenosine diphosphate ribose generated in vitro and in vivo

Alvarez-Gonzalez, R., & Jacobson, M. K. (1987) · Biochemistry · doi:10.1021/bi00385a042 · Cited by 242

Inhibitors of Poly(Adenosine Diphosphate-Ribose) Synthesis: Effect on Other Metabolic Processes

Milam, K. M., & Cleaver, J. E. (1984) · Science · doi:10.1126/science.6420886 · Cited by 241

The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA.

Ikejima, M., Noguchi, S., Yamashita, R., Ogura, T., Sugimura, T., Gill, D. M., & Miwa, M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45824-3 · Cited by 238

Direct Evidence for DNA Bending at the Lambda Replication Origin

Zahn, K., & Blattner, F. R. (1987) · Science · doi:10.1126/science.2951850 · Cited by 228

Poly (ADP-Ribose) synthetase. Separation and identification of three proteolytic fragments as the substrate-binding domain, the DNA-binding domain, and the automodification domain.

Kameshita, I., Matsuda, Z., Taniguchi, T., & Shizuta, Y. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42913-9 · Cited by 225

Molecular mechanisms of transcriptional regulation in yeast

STRUHL, K. (1990) · Cell Biology International Reports · doi:10.1016/0309-1651(90)90128-l · Cited by 225

Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents

Alvarez-Gonzalez, R., & Althaus, F. R. (1989) · Mutation Research/DNA Repair · doi:10.1016/0921-8777(89)90012-8 · Cited by 224

Conformational change in the DNA associated with an unusual promoter mutation in a tRNA operon of Salmonella

Bossi, L., & Smith, D. M. (1984) · Cell · doi:10.1016/0092-8674(84)90471-9 · Cited by 223

Purification and Properties of a Glycohydrolase from Calf Thymus Splitting Ribose-Ribose Linkages of Poly(Adenosine Diphosphate Ribose)

Miwa, M., Tanaka, M., Matsushima, T., & Sugimura, T. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42597-0 · Cited by 209

Restoration of ultraviolet-induced unscheduled DNA synthesis of xeroderma pigmentosum cells by the concomitant treatment with bacteriophage T4 endonuclease V and HVJ (Sendai virus).

Tanaka, K., Sekiguchi, M., & Okada, Y. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.10.4071 · Cited by 209

Modulation of chromatin superstructure induced by poly(ADP-ribose) synthesis and degradation.

de Murcia, G., Huletsky, A., Lamarre, D., Gaudreau, A., Pouyet, J., Daune, M., & Poirier, G. G. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62715-8 · Cited by 201

Poly(ADP-ribose) polymerase inhibitors preserve oxidized nicotinamide adenine dinucleotide and adenosine 5'-triphosphate pools in DNA-damaged cells: mechanism of stimulation of unscheduled DNA synthesis

Sims, J. L., Berger, S. J., & Berger, N. A. (1983) · Biochemistry · doi:10.1021/bi00291a019 · Cited by 198

Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNA

Ménissier-de Murcia, J., Molinete, M., Gradwohl, G., Simonin, F., & de Murcia, G. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90302-1 · Cited by 193

NAD(+)-dependent repair of damaged DNA by human cell extracts.

Satoh, M. S., Poirier, G. G., & Lindahl, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53346-9 · Cited by 188

A Shuttle Mechanism for DNA‐Protein Interactions: The Regulation of Poly(ADP‐ribose) Polymerase

ZAHRADKA, P., & EBISUZAKI, K. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06912.x · Cited by 182

cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase.

Cherney, B. W., McBride, O. W., Chen, D. F., Alkhatib, H., Bhatia, K., Hensley, P., & Smulson, M. E. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8370 · Cited by 180

Poly(ADP-ribosylation) of DNA topoisomerase I from calf thymus.

Ferro, A. M., & Olivera, B. M. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43696-9 · Cited by 178

Multiple autopoly(ADP-ribosyl)ation of rat liver poly(ADP-ribose) synthetase. Mode of modification and properties of automodified synthetase.

Kawaichi, M., Ueda, K., & Hayaishi, O. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68788-0 · Cited by 172

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. O., Ménard, L., Lamarre, D., & Poirier, G. G. (1989) · PubMed · Cited by 168

Evidence for adenosine diphosphate ribosylation of Ca2+, Mg2+-dependent endonuclease.

Yoshihara, K., Tanigawa, Y., Burzio, L., & KOIDE, S. S. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.1.289 · Cited by 165

Purification and characterization of poly(ADP-ribose) glycohydrolase. Different modes of action on large and small poly(ADP-ribose).

Hatakeyama, K., Nemoto, Y., Ueda, K., & Hayaishi, O. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66802-4 · Cited by 164

Reconstitution of simian virus 40 DNA replication with purified proteins.

Weinberg, D. H., Collins, K. L., Simancek, P., et al. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.22.8692 · Cited by 161

Structure of poly(adenosine diphosphate ribose): identification of 2'-[1''-ribosyl-2''-(or 3''-)(1'''-ribosyl)]adenosine-5',5'',5'''-tris(phosphate) as a branch linkage.

Miwa, M., Saikawa, N., Yamaizumi, Z., Nishimura, S., & Sugimura, T. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.2.595 · Cited by 158

Purification and analysis of a factor which suppresses nick-induced transcription by RNA polymerase II and its identity with poly(ADP-ribose) polymerase.

Slattery, E., Dignam, J. D., Matsui, T., & Roeder, R. G. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)81989-9 · Cited by 157

Induction of beta-polymerase mRNA by DNA-damaging agents in Chinese hamster ovary cells.

Fornace, A. J., Zmudzka, B. Z., Hollander, M. C., & Wilson, S. H. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.2.851 · Cited by 155

Poly(ADP-ribosylation) in vitro. Reaction parameters and enzyme mechanism.

Ferro, A. M., & Olivera, B. M. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34453-3 · Cited by 153

Specific Saccharomyces cerevisiae genes are expressed in response to DNA-damaging agents.

Ruby, S. W., & Szostak, J. W. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.1.75 · Cited by 153

Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase

Uchida, K., Morita, T., Sato, T., Ogura, T., Yamashita, R., Noguchi, S., Suzuki, H., Nyunoya, H., Miwa, M., & Sügimura, T. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90921-1 · Cited by 150

ADP-ribosylation of nuclear proteins in vivo. Identification of histone H2B as a major acceptor for mono- and poly(ADP-ribose) in dimethyl sulfate-treated hepatoma AH 7974 cells.

Adamietz, P., & Rudolph, A. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39804-6 · Cited by 142

The Effect of poly(ADP-ribosyl)ation on Native and H1-depleted Chromatin

Huletsky, A., de MURCIA, G., Muller, S., Hengartner, M. O., Ménard, L., Lamarre, D., & Poirier, G. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81875-0 · Cited by 140

Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence.

Kurosaki, T., Ushiro, H., Mitsuuchi, Y., Suzuki, S., Matsuda, M., Matsuda, Y., Katunuma, N., Kangawa, K., Matsuo, H., & Hirose, T. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47687-9 · Cited by 129

Review: Modulation of chromatin structure by poly(ADP-ribosyl)ation

de MURCIA, G., Huletsky, A., & Poirier, G. G. (1988) · Biochemistry and Cell Biology · doi:10.1139/o88-072 · Cited by 128

ADP-ribosyl protein lyase. Purification, properties, and identification of the product.

Oka, J., Ueda, K., Hayaishi, O., et al. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43555-1 · Cited by 122

Structural and functional analysis of poly(ADP ribose) polymerase: an immunological study

Lamarre, D., Talbot, B. G., de Murica, G., Laplante, C., Leduc, Y., Mazen, A., & Poirier, G. G. (1988) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(88)90007-3 · Cited by 120

Poly(ADP-ribose)polymerase: a novel finger protein

Mazen, A., Murcia, J. M., Molinete, M., Simonin, F., Gradwohl, G., Poirier, G. G., & de MURCIA, G. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.12.4689 · Cited by 114

Relation between carcinogenesis, chromatin structure and poly(ADP-ribosylation) (review).

Boulikas, T. (1991) · PubMed · Cited by 114

The human poly(ADP‐ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity.

Schreiber, V., Molinete, M., Bœuf, H., de MURCIA, G., & Murcia, J. M. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05404.x · Cited by 113

Inhibition of DNA polymerase α, DNA polymerase β, terminal deoxynucleotidyl transferase, and DNA ligase II by poly(ADP-ribosyl)ation reaction in vitro

Yoshihara, K., Itaya, A., Tanaka, Y., Ohashi, Y., Ito, K., Teraoka, H., Tsukada, K., Matsukage, A., & Kamiya, T. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)91644-4 · Cited by 111

Effect of carcinogenic N-alkyl-N-nitroso compounds on nicotinamide adenine dinucleotide metabolism.

Jacobson, M. K., Levi, V., Juarez-Salinas, H., Barton, R. A., & Jacobson, E. L. (1980) · PubMed · Cited by 109

Enzymological properties of poly(ADP-ribose)polymerase: characterization of automodification sites and NADase activity

Desmarais, Y., Ménard, L., Lagueux, J., & Poirier, G. G. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)99007-f · Cited by 103

Cloning and expression of cDNA for human poly(ADP-ribose) polymerase.

Alkhatib, H., Chen, D. F., Cherney, B., Bhatia, K. G., Notario, V., Giri, C., Stein, G. S., Slattery, E., Roeder, R. G., & Smulson, M. E. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.5.1224 · Cited by 101

The branching and linear portions of poly(adenosine diphosphate ribose) have the same alpha(1 leads to 2) ribose-ribose linkage.

Miwa, M., Ishihara, M., Takishima, S., Takasuka, N., Maeda, M., Yamaizumi, Z., Sügimura, T., Yokoyama, S., & Miyazawa, T. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69701-2 · Cited by 98

Stimulation of poly(ADP-ribosyl)ation during Ehrlich ascites tumor cell "starvation" and suppression of concomitant DNA fragmentation by benzamide.

Wielckens, K., George, E., Pless, T., & Hilz, H. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32589-4 · Cited by 97

Poly ADP-ribosylation of DNA-dependent RNA polymerase I from quail oviduct. Dependence on progesterone stimulation.

Müller, W. E. G., & Zahn, R. K. (1976) · Molecular and Cellular Biochemistry · doi:10.1007/bf01741713 · Cited by 97

Hydrogen peroxide insult in cultured mammalian cells: relationships between DNA single-strand breakage, poly(ADP-ribose) metabolism and cell killing

Cantoni, O., Cattabeni, F., Stocchi, V., Meyn, R. E., Cerutti, P., & Murray, D. L. (1989) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(89)90234-6 · Cited by 97

ADP-ribosylation of chromosomal proteins and mouse mammary tumor virus gene expression. Glucocorticoids rapidly decrease endogenous ADP-ribosylation of nonhistone high mobility group 14 and 17 proteins.

Tanuma, S.-I., Johnson, L. D., & Johnson, G. S. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43816-6 · Cited by 89

Macromolecular enzymatic product of NAD+ in liver mitochondria.

Kun, É., Zimber, P., Chang, A. C. Y., Puschendorf, B., & Grunicke, H. H. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.4.1436 · Cited by 88

Lymphocyte dysfunction after DNA damage by toxic oxygen species. A model of immunodeficiency.

Carson, D. A., Seto, S., & Wasson, D. B. (1986) · The Journal of Experimental Medicine · doi:10.1084/jem.163.3.746 · Cited by 80

Sequential ADP‐ribosylation pattern of nucleosomal histones

Huletsky, A., Niedergang, C., Fréchette, A., Aubin, R. A., Gaudreau, A., & Poirier, G. G. (1985) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1985.tb08650.x · Cited by 73

Novel enzyme from rat liver that cleaves an ADP-ribosyl histone linkage.

Okayama, H., Honda, M., & Hayaishi, O. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.5.2254 · Cited by 69

Release of core DNA from nucleosomal core particles following (ADP-ribose)n-modification invitro

Mathis, G. A., & Althaus, F. R. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90358-5 · Cited by 68

Influence of poly(ADP-ribose) polymerase on the enzymatic synthesis of SV40 DNA.

Eki, T., & Hurwitz, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)49958-9 · Cited by 65

ADP-ribosylation of ADPR-transferase and topoisomerase I in intact mouse epidermal cells JB6

Krupitza, G., & Cerutti, P. (1989) · Biochemistry · doi:10.1021/bi00431a011 · Cited by 61

Poly(adenosine diphosphoribose) synthesis in ultraviolet-irradiated xeroderma pigmentosum cells reconstituted with Micrococcus luteus UV endonuclease

Berger, N. A., & Sikorski, G. W. (1981) · Biochemistry · doi:10.1021/bi00515a047 · Cited by 60

Human autoantibodies to poly(adenosine diphosphate-ribose) polymerase.

Yamanaka, H., Willis, E. H., Penning, C. A., et al. (1987) · Journal of Clinical Investigation · doi:10.1172/jci113150 · Cited by 58

Poly(ADP-ribose) synthetase. The DNA binding domain and the automodification domain.

Nishikimi, M., Ogasawara, K., Kameshita, I., et al. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)65111-0 · Cited by 55

Association of poly(ADP-ribose) polymerase with the nuclear matrix: The role intermolecular disulfide bond formation, RNA retention, and cell type

Kaufmann, S. H., Brunet, G., Talbot, B. G., Lamarr, D., Dumas, C., Shaper, J. H., & Poirier, G. G. (1991) · Experimental Cell Research · doi:10.1016/0014-4827(91)90072-3 · Cited by 55

Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation

Suzuki, H., Uchida, K., Shima, H., Sato, T., Okamoto, T., Kimura, T., & Miwa, M. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90543-2 · Cited by 53

Size and shape of poly(ADP-ribose): Examination by gel filtration, gel electrophoresis and electron microscopy

Hayashi, K., Tanaka, M., Shimada, T., Miwa, M., & Sügimura, T. (1983) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(83)91803-x · Cited by 52

Poly(ADP-ribose) may signal changing metabolic conditions to the chromatin of mammalian cells.

Loetscher, P., Álvarez-González, R., & Althaus, F. R. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.5.1286 · Cited by 50

Cell cycle perturbations following DNA damage in the presence of ADP-ribosylation inhibitors

Jacobson, E. L., Meadows, R. Y., & Measel, J. W. (1985) · Carcinogenesis · doi:10.1093/carcin/6.5.711 · Cited by 50

Expression of the poly(ADP-ribose) polymerase gene following natural and induced DNA strand breakage and effect of hyperexpression on DNA repair

Bhatia, K. G., Pommer, Y., Giri, Y., Fornace, A. J., Imaizumi, M., Breitman, T. R., Cherney, B., & Smulson, M. E. (1990) · Carcinogenesis · doi:10.1093/carcin/11.1.123 · Cited by 50

Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene: Structural similarity to that of the DNA polymerase β gene

Ogura, T., Nyunoya, H., Takahashi-Masutani, M., Miwa, M., Sugimura, T., & Esumi, H. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)92082-b · Cited by 44

Human nuclear NAD+ ADP-ribosyltransferase: localization of the gene on chromosome 1q41-q42 and expression of an active human enzyme in Escherichia coli.

Herzog, H., Zabel, B. U., Schneider, R., Auer, B., Hirsch‐Kauffmann, M., & Schweiger, M. R. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.10.3514 · Cited by 42

Specific Saccharomyces cerevisiae Genes Are Expressed in Response to DNA-Damaging Agents

Ruby, S. W., & Szostak, J. W. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.1.75-84.1985 · Cited by 41

Human Nuclear NAD + ADP-Ribosyltransferase(polymerizing): Organization of the Gene

Auer, B., Nagl, U. O., Herzog, H., Schneider, R., & Schweiger, M. (1989) · DNA · doi:10.1089/dna.1989.8.575 · Cited by 39

Changes in mRNA levels of poly(ADP-ribose) polymerase during activation of human lymphocytes

McNerney, R., Tavasolli, M., Shall, S., et al. (1989) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(89)90099-7 · Cited by 37

Poly(ADP-ribose) degradation by glycohydrolase starts with an endonucleolytic incision.

Ikejima, M., & Gill, D. M. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37913-4 · Cited by 37

Inhibition of carcinogen‐induced cellular transformation of human fibroblasts by drugs that interact with the poly(ADP‐ribose) polymerase system

Milo, G. E., Kurian, P., Kirsten, E., & Kun, E. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)80546-9 · Cited by 35

3‐Aminobenzamide is lethal to MMS‐damaged human fibroblasts primarily during s phase

Boorstein, R. J., & Pardee, A. B. (1984) · Journal of Cellular Physiology · doi:10.1002/jcp.1041200313 · Cited by 33

Human poly(ADP‐ribose) polymerase gene

Yokoyama, Y., Kawamoto, T., Mitsuuchi, Y., Kurosaki, T., Toda, K., Ushiro, H., Terashima, M., Sumimoto, H., Kuribayashi, I., Yamamoto, Y., et al. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15647.x · Cited by 32

Polypeptide domains of ADP-ribosyltransferase obtained by digestion with plasmin

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Reconstitution of an in vitro poly(ADP-ribose) turnover system

Ménard, L., Thibault, L., & Poirier, G. G. (1990) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(90)90083-e · Cited by 32

Uncoupling of DNA excision repair and nucleosomal unfolding in poly (ADP-ribose)-depleted mammalian cells

Mathis, G. A., & Althaus, F. R. (1990) · Carcinogenesis · doi:10.1093/carcin/11.7.1237 · Cited by 26

Stimulation of poly(ADP-ribose) synthesis by free radicals in C3H10T1/2 cells: relationship with NAD metabolism and DNA breakage

Lautier, D., Poirier, D., Boudreau, A. C., et al. (1990) · Biochemistry and Cell Biology · doi:10.1139/o90-085 · Cited by 26

DNA replication and poly(ADP-ribosyl)ation of chromatin.

Anachkova, B., Russev, G., & Poirier, G. G. (1989) · PubMed · Cited by 25

Poly(ADP-ribosyl)ation of chromatin: kinetics of relaxation and its effect on chromatin solubility

Fréchette, A., Huletsky, A., Aubin, R. J., de MURCIA, G., Mandel, P., Lord, A., Grondin, G., & Poirier, G. G. (1985) · Canadian Journal of Biochemistry and Cell Biology · doi:10.1139/o85-096 · Cited by 19

Factors modifying 3‐aminobenzamide cytotoxicity in normal and repair‐deficient human fibroblasts

Boorstein, R. J., & Pardee, A. B. (1984) · Journal of Cellular Physiology · doi:10.1002/jcp.1041200312 · Cited by 18

Poly(ADP-ribose) polymerase inhibits DNA synthesis initiation in the absence of NAD+

Nobori, T., Yamanaka, H., & Carson, D. A. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)92336-x · Cited by 11

Mediation of Poly(ADP-Ribose) Polymerase-1-Dependent Cell Death by Apoptosis-Inducing Factor

Yu, S.-W., Wang, H., Poitras, M. F., Coombs, C., Bowers, W. J., Federoff, H. J., Poirier, G. G., Dawson, T. M., & Dawson, V. L. (2002) · Science · doi:10.1126/science.1072221 · Cited by 1,826

Antioxidant Therapy: A New Pharmacological Approach in Shock, Inflammation, and Ischemia/Reperfusion Injury

Cuzzocrea, S., Riley, D. P., Caputi, A. P., & Salvemini, D. (2001) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01484-4 · Cited by 1,087

Poly(ADP-ribose) polymerase gene disruption renders mice resistant to cerebral ischemia

Eliasson, M. J. L., Sampei, K., Mandir, A. S., Hurn, P. D., Traystman, R. J., Bao, J., Pieper, A., Wang, Z.-Q., Dawson, T. M., Snyder, S. H., et al. (1997) · Nature Medicine · doi:10.1038/nm1097-1089 · Cited by 1,018

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. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.6.3563 · Cited by 910

Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion

Ha, H. C., & Snyder, S. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13978 · Cited by 907