PARP inhibition: PARP1 and beyond

Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy

Farmer, H., McCabe, N., Lord, C. J., Tutt, A. N. J., Johnson, D. A., Richardson, T. B., Santarosa, M., Dillon, K. J., Hickson, I., Knights, C., et al. (2005) · Nature · doi:10.1038/nature03445 · Cited by 6,683 · see citing works

Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase

Bryant, H. E., Schultz, N., Thomas, H. D., Parker, K. M., Flower, D., Lopez, E., Kyle, S., Meuth, M., Curtin, N. J., & Helleday, T. (2005) · Nature · doi:10.1038/nature03443 · Cited by 5,198 · see citing works

Inhibition of Poly(ADP-Ribose) Polymerase in Tumors from <i>BRCA</i> Mutation Carriers

Fong, P. C., Boss, D. S., Yap, T. A., Tutt, A., Wu, P., Mergui-Roelvink, M., Mortimer, P., Swaisland, H., Lau, A., O'Connor, M. J., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0900212 · Cited by 3,634 · see citing works

AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy

Hardie, D. G. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2249 · Cited by 2,207 · see citing works

Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling

Huang, S.-M. A., Mishina, Y., Liu, S.-M., Cheung, A. K., Stegmeier, F., Michaud, G., Charlat, O., Wiellette, E., Zhang, Y., Wiessner, S., et al. (2009) · Nature · doi:10.1038/nature08356 · Cited by 2,077 · see citing works

Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions

D’Amours, D., Desnoyers, S., D’Silva, I., & Poirier, G. G. (1999) · Biochemical Journal · doi:10.1042/bj3420249 · Cited by 1,819 · see citing works

Hallmarks of 'BRCAness' in sporadic cancers

Turner, N. C., Tutt, A. N. J., & Ashworth, A. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1457 · Cited by 1,651 · see citing works

The PARP superfamily

Amé, J., Spenlehauer, C., & de MURCIA, G. (2004) · BioEssays · doi:10.1002/bies.20085 · Cited by 1,463 · see citing works

Deficiency in the Repair of DNA Damage by Homologous Recombination and Sensitivity to Poly(ADP-Ribose) Polymerase Inhibition

McCabe, N., Turner, N. C., Lord, C. J., Kluzek, K., Białkowska, A., Swift, S., Giavara, S., O’Connor, M. J., Tutt, A. N. J., Zdzienicka, M. Z., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0140 · Cited by 1,311 · see citing works

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

Satoh, M. S., & Lindahl, T. L. (1992) · Nature · doi:10.1038/356356a0 · Cited by 1,181 · see citing works

(ADP-ribose)n participates in DNA excision repair

Durkacz, B. W., Omidiji, O., Gray, D. A., & Shall, S. (1980) · Nature · doi:10.1038/283593a0 · Cited by 1,123 · see citing works

Secondary mutations as a mechanism of cisplatin resistance in BRCA2-mutated cancers

Sakai, W., Swisher, E. M., Karlan, B. Y., Agarwal, M. K., Higgins, J., Friedman, C., Villegas, E., Jacquemont, C., Farrugia, D. J., Couch, F. J., et al. (2008) · Nature · doi:10.1038/nature06633 · Cited by 1,086 · see citing works

Requirement of poly(ADP-ribose) polymerase in recovery from DNA damage in mice and in cells

Murcia, J. M., Niedergang, C., Trucco, C., Ricoul, M., Dutrillaux, B., Mark, M. P., Oliver, F. J., Masson, M., Dierich, A., LeMeur, M., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7303 · Cited by 1,058 · see citing works

Resistance to therapy caused by intragenic deletion in BRCA2

Edwards, S. L., Brough, R., Lord, C. J., Natrajan, R., Vatcheva, R., Levine, D. A., Boyd, J., Reis-Filho, J. S., & Ashworth, A. (2008) · Nature · doi:10.1038/nature06548 · Cited by 1,011 · see citing works

High sensitivity of BRCA1-deficient mammary tumors to the PARP inhibitor AZD2281 alone and in combination with platinum drugs

Rottenberg, S., Jaspers, J. E., Kersbergen, A. J., van der Burg, E., Nygren, A. O. H., Zander, S. A. L., Derksen, P. W. B., de Bruin, M., Zevenhoven, J., Lau, A., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806092105 · Cited by 958 · see citing works

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., Murcia, J. M., & de MURCIA, G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.6.3563 · Cited by 910 · see citing works

PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways

Wang, M., Wu, W., Wu, W., Rosidi, B., Zhang, L., Wang, H., & Iliakis, G. E. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl840 · Cited by 823 · see citing works

ABT-888, an Orally Active Poly(ADP-Ribose) Polymerase Inhibitor that Potentiates DNA-Damaging Agents in Preclinical Tumor Models

Donawho, C. K., Luo, Y., Luo, Y., Penning, T. D., Bauch, J. L., Bouska, J. J., Bontcheva-Diaz, V., Cox, B. F., DeWeese, T. L., Dillehay, L. E., et al. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-3039 · Cited by 776 · see citing works

Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease.Preprint

Wang, Z. Q., Auer, B., Stingl, L., Berghammer, H., Haidacher, D., Schweiger, M. R., & Wagner, E. F. (1995) · Genes & Development · doi:10.1101/gad.9.5.509 · Cited by 774 · see citing works

PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-ribose) Polymerase

Amé, J., Rolli, V., Schreiber, V., Niedergang, C., Apiou, F., Decker, P., Muller, S., Höger, T. H., Murcia, J. M., & de MURCIA, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17860 · Cited by 744 · see citing works

Involvement of Poly(ADP-ribose) Polymerase-1 and XRCC1/DNA Ligase III in an Alternative Route for DNA Double-strand Breaks Rejoining

Audebert, M., Salles, B., & Calsou, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404524200 · Cited by 709 · see citing works

A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage

El‐Khamisy, S. F. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg761 · Cited by 660 · see citing works

Nicotinamide mononucleotide activation of a new DNA-dependent polyadenylic acid synthesizing nuclear enzyme

Chambon, P., Weill, J. D., & Mandel, P. (1963) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(63)90024-x · Cited by 654 · see citing works

Poly(ADP-ribose) (PAR) polymer is a death signal

Andrabi, S. A., Kim, N. S., Yu, S.-W., Wang, H., Koh, D. W., Sasaki, M., Klaus, J. A., Otsuka, T., Zhang, Z., Koehler, R. C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606526103 · Cited by 644 · see citing works

The Nudix hydrolase superfamily

McLennan, A. G. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5386-7 · Cited by 636 · see citing works

Synthetic lethal targeting of PTEN mutant cells with PARP inhibitors

Mendes‐Pereira, A. M., Martin, S. A., Brough, R., McCarthy, A., Taylor, J. R., Kim, J., Waldman, T. A., Lord, C. J., & Ashworth, A. (2009) · EMBO Molecular Medicine · doi:10.1002/emmm.200900041 · Cited by 630 · see citing works

Functional interaction between PARP‐1 and PARP‐2 in chromosome stability and embryonic development in mouse

Murcia, J. M., Ricoul, M., Tartier, L., Niedergang, C., Huber, A., Dantzer, F., Schreiber, V., Amé, J., Dierich, A., LeMeur, M., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg206 · Cited by 629 · see citing works

Alkylating DNA damage stimulates a regulated form of necrotic cell deathPreprint

Zong, W., Ditsworth, D., Bauer, D. E., Wang, Z., & Thompson, C. B. (2004) · Genes & Development · doi:10.1101/gad.1199904 · Cited by 618 · see citing works

PARP1-dependent Kinetics of Recruitment of MRE11 and NBS1 Proteins to Multiple DNA Damage Sites

Haince, J.-F., McDonald, D., Rodrigue, A., Déry, U., Masson, J., Hendzel, M. J., & Poirier, G. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706734200 · Cited by 609 · see citing works

4-[3-(4-Cyclopropanecarbonylpiperazine-1-carbonyl)-4-fluorobenzyl]-2H-phthalazin-1-one: A Novel Bioavailable Inhibitor of Poly(ADP-ribose) Polymerase-1

Menear, K. A., Adcock, C., Boulter, R., Cockcroft, X. F., Copsey, L., Cranston, A. N., Dillon, K. J., Drzewiecki, J., Garman, S., Gomez, S., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8001263 · Cited by 604 · see citing works

PARP is activated at stalled forks to mediate Mre11‐dependent replication restart and recombination

Bryant, H. E., Petermann, E., Schultz, N., Jemth, A., Loseva, O., Issaeva, N., Johansson, F., Fernandez, S., McGlynn, P., & Helleday, T. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.206 · Cited by 593 · see citing works

Poly(ADP-ribose)–Dependent Regulation of DNA Repair by the Chromatin Remodeling Enzyme ALC1

Ahel, D., Hořejší, Z., Wiechens, N., Polo, S. E., Garcia-Wilson, E., Ahel, I., Flynn, H., Skehel, M., West, S. C., Jackson, S. P., et al. (2009) · Science · doi:10.1126/science.1177321 · Cited by 588 · see citing works

The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases

Paul, O. H. (2007) · Frontiers in bioscience · doi:10.2741/2909 · Cited by 587 · see citing works

Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model?

Shall, S., & de MURCIA, G. (2000) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(00)00016-1 · Cited by 534 · see citing works

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 516 · see citing works

Parthanatos, a messenger of death

David, K. K. (2009) · Frontiers in Bioscience · doi:10.2741/3297 · Cited by 450 · cited 1× · see citing works

Chromatin Loosening by Poly(ADP)-Ribose Polymerase (PARP) at Drosophila Puff Loci

Tulin, A. V., & Spradling, A. C. (2003) · Science · doi:10.1126/science.1078764 · Cited by 443 · see citing works

A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation

Timinszky, G., Till, S., Hassa, P. O., Hothorn, M., Kustatscher, G., Nijmeijer, B., Colombelli, J., Altmeyer, M., Stelzer, E. H. K., Scheffzek, K., et al. (2009) · Nature Structural &amp; Molecular Biology · doi:10.1038/nsmb.1664 · Cited by 416 · see citing works

Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes

Gagné, J., Isabelle, M., Lo, K. S., Bourassa, S., Hendzel, M. J., Dawson, V. L., Dawson, T. M., & Poirier, G. G. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn771 · Cited by 416 · see citing works

Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation

Kraus, W. L. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.006 · Cited by 409 · see citing works

Phase I Study of the Poly(ADP-Ribose) Polymerase Inhibitor, AG014699, in Combination with Temozolomide in Patients with Advanced Solid Tumors

Plummer, R., Jones, C., Middleton, M. R., Wilson, R. H., Evans, J., Olsen, A. L., Curtin, N. J., Boddy, A. V., McHugh, P. J., Newell, D. R., et al. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1223 · Cited by 386 · see citing works

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. (2008) · Science · doi:10.1126/science.1149250 · Cited by 382 · see citing works

ADP-ribosylation in mammalian cell ghosts. Dependence of poly(ADP-ribose) synthesis on strand breakage in DNA.

Benjamin, R. C., & Gill, D. M. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70490-6 · Cited by 379 · see citing works

Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler

Gottschalk, A. J., Timinszky, G., Kong, S. E., Jin, J., Cai, Y., Swanson, S. K., Washburn, M. P., Florens, L. A., Ladurner, A. G., Conaway, J. W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906920106 · Cited by 358 · see citing works

Understanding and treating triple-negative breast cancer

Carey, L., & Anders, C. (2021) · PubMed · doi:10.17615/85ph-f542 · Cited by 352 · see citing works

Poly(ADP-ribose) levels in carcinogen-treated cells

Juarez-Salinas, H., Sims, J. L., & Jacobson, M. K. (1979) · Nature · doi:10.1038/282740a0 · Cited by 349 · see citing works

DNA strand breaks and ADP-ribosyl transferase activation during cell differentiation

Farzaneh, F., Zalin, R. J., Brill, D., & Shall, S. (1982) · Nature · doi:10.1038/300362a0 · Cited by 347 · see citing works

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

Chambon, P., Weill, J., Doly, J., Strosser, M. T., & Mandel, P. (1966) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(66)90502-x · Cited by 345 · see citing works

Substrate-Assisted Catalysis by PARP10 Limits Its Activity to Mono-ADP-Ribosylation

Kleine, H., Poręba, E., Leśniewicz, K., Hassa, P. O., Hottiger, M. O., Litchfield, D. W., Shilton, B. H., & Lüscher, B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.009 · Cited by 340 · see citing works

Selective Inhibition of BRCA2-Deficient Mammary Tumor Cell Growth by AZD2281 and Cisplatin

Evers, B., Drost, R., Schut, E., de Bruin, M., van der Burg, E., Derksen, P. W. B., Holstege, H. H., Liu, X., van Drunen, E., Beverloo, H. B., et al. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-4953 · Cited by 336 · see citing works

Spontaneous Homologous Recombination Is Induced by Collapsed Replication Forks That Are Caused by Endogenous DNA Single-Strand Breaks

Saleh-Gohari, N., Bryant, H. E., Schultz, N., Parker, K. M., Cassel, T. N., & Helleday, T. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.16.7158-7169.2005 · Cited by 334 · see citing works

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. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp229 · Cited by 325 · see citing works

Discovery of 2-{4-[(3S)-Piperidin-3-yl]phenyl}-2H-indazole-7-carboxamide (MK-4827): A Novel Oral Poly(ADP-ribose)polymerase (PARP) Inhibitor Efficacious in BRCA-1 and -2 Mutant Tumors

JONES, P. G., Altamura, S., Boueres, J. K., Ferrigno, F., Fonsi, M., Giomini, C., Lamartina, S., Monteagudo, E. S., Ontoria, J. M., Orsale, M. V., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901188v · Cited by 323 · see citing works

A synthetic lethal siRNA screen identifying genes mediating sensitivity to a PARP inhibitor

Turner, N. C., Lord, C. J., Iorns, E. J., Brough, R., Swift, S., Elliott, R. J. R., Rayter, S., Tutt, A. N. J., & Ashworth, A. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.61 · Cited by 322 · see citing works

Role of Poly(ADP‐ribose) polymerase 1 (PARP‐1) in Cardiovascular Diseases: The Therapeutic Potential of PARP Inhibitors

Pacher, P., & Szabó, C. (2007) · Cardiovascular Drug Reviews · doi:10.1111/j.1527-3466.2007.00018.x · Cited by 317 · see citing works

Studies on the Polymer of Adenosine Diphosphate Ribose

Nishizuka, Y., Ueda, K., Nakazawa, K., & Hayaishi, O. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95947-8 · Cited by 309 · see citing works

Preclinical selection of a novel poly(ADP-ribose) polymerase inhibitor for clinical trial

Thomas, H. D., Calabrese, C. R., Batey, M. A., Canan, S. S., Hostomský, Z., Kyle, S., Maegley, K. A., Newell, D. R., Skalitzky, D. J., Wang, L.-Z., et al. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0552 · Cited by 309 · see citing works

Poly(ADP-ribose) Polymerase Null Mouse Cells Synthesize ADP-ribose Polymers

Shieh, W.-R., Amé, J., Wilson, M. V., Wang, Z., Koh, D. W., Jacobson, M. K., & Jacobson, E. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30069 · Cited by 303 · see citing works

Identification and Characterization of a Mammalian 39-kDa Poly(ADP-ribose) Glycohydrolase

Oka, S., Kato, J., & Moss, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510290200 · Cited by 290 · see citing works

Current Development of Clinical Inhibitors of Poly(ADP-Ribose) Polymerase in Oncology

Ratnam, K., & Low, J. A. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2260 · Cited by 286 · see citing works

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

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

Discovery of the Poly(ADP-ribose) Polymerase (PARP) Inhibitor 2-[(R)-2-methylpyrrolidin-2-yl]-1H-benzimidazole-4-carboxamide (ABT-888) for the Treatment of Cancer

Penning, T. D., Zhu, G., Gandhi, V. B., Gong, J., Liu, X., Shi, Y., Klinghofer, V., Johnson, E. F., Donawho, C. K., Frost, D. J., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm801171j · Cited by 273 · see citing works

Inhibition of Poly(ADP-Ribose) Polymerase Enhances Cell Death and Improves Tumor Growth Delay in Irradiated Lung Cancer Models

Albert, J. M., Cao, C., Kim, K. W., Willey, C. D., Geng, L., Xiao, D., Wang, H., Sandler, A. B., Johnson, D. H., Colevas, A. D., et al. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2872 · Cited by 266 · see citing works

Ataxia Telangiectasia Mutated (ATM) Signaling Network Is Modulated by a Novel Poly(ADP-ribose)-dependent Pathway in the Early Response to DNA-damaging Agents

Haince, J.-F., Kozlov, S., Dawson, V. L., Dawson, T. M., Hendzel, M. J., Lavin, M. F., & Poirier, G. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608406200 · Cited by 261 · see citing works

In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)

Otto, H., Reche, P. A., Bazán, F., Dittmar, K., Haag, F., & Koch‐Nolte, F. (2005) · BMC Genomics · doi:10.1186/1471-2164-6-139 · Cited by 259 · see citing works

Tankyrase function at telomeres, spindle poles, and beyond

Hsiao, S. J., & Smith, S. H. (2007) · Biochimie · doi:10.1016/j.biochi.2007.07.012 · Cited by 249 · see citing works

PARP-1 is involved in autophagy induced by DNA damage

Muñoz‐Gámez, J. A., Rodríguez-Vargas, J. M., Quiles, R., Aguilar‐Quesada, R., Martín‐Oliva, D., de MURCIA, G., Murcia, J. M., Almendros-Ruiz, A., de Almodóvar, J. M. R., & Oliver, F. J. (2009) · Autophagy · doi:10.4161/auto.5.1.7272 · Cited by 248 · see citing works

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

Álvarez-González, R., & Jacobson, M. K. (1987) · Biochemistry · doi:10.1021/bi00385a042 · Cited by 244 · see citing works

Ablation of PARP-1 does not interfere with the repair of DNA double-strand breaks, but compromises the reactivation of stalled replication forks

Yang, Y., Cortes, U., Patnaik, S., Jasin, M., & Wang, Z. (2004) · Oncogene · doi:10.1038/sj.onc.1207491 · Cited by 244 · see citing works

Efficacy of BSI-201, a poly (ADP-ribose) polymerase-1 (PARP1) inhibitor, in combination with gemcitabine/carboplatin (G/C) in patients with metastatic triple-negative breast cancer (TNBC): Results of a randomized phase II trial

O’Shaughnessy, J., Osborne, C. R. C., Pippen, J., Yoffe, M., Patt, D. A., Monaghan, G., Rocha, C., Ossovskaya, V., Sherman, B. M., & Bradley, C. R. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2009.27.15_suppl.3 · Cited by 242 · see citing works

Role of DNA breaks and ADP-ribosyl transferase activity in eukaryotic differentiation demonstrated in human lymphocytes

Johnstone, A. P., & Williams, G. T. (1982) · Nature · doi:10.1038/300368a0 · Cited by 237 · see citing works

Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular.

Mendoza‐Alvarez, H., & Álvarez-González, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41568-2 · Cited by 227 · see citing works

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 · see citing works

Replication-Dependent Radiosensitization of Human Glioma Cells by Inhibition of Poly(ADP-Ribose) Polymerase: Mechanisms and Therapeutic Potential

Dungey, F. A., Löser, D. A., & Chalmers, A. J. (2008) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2008.07.031 · Cited by 221 · see citing works

PARP-1 ensures regulation of replication fork progression by homologous recombination on damaged DNA

Sugimura, K., Takebayashi, S., Taguchi, H., Takeda, S., & Okumura, K. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200806068 · Cited by 213 · see citing works

ADP-ribosylation of histone H1. Identification of glutamic acid residues 2, 14, and the COOH-terminal lysine residue as modification sites.

Ogata, N., Ueda, K., Kagamiyama, H., & Hayaishi, O. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43873-8 · Cited by 212 · see citing works

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., & Jacobson, M. K. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.03.050 · Cited by 209 · see citing works

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. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708558200 · Cited by 206 · see citing works

A Shuttle Mechanism for DNA‐Protein Interactions

Zahradka, P. C., & Ebisuzaki, K. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06912.x · Cited by 180 · see citing works

Genetic interaction between PARP and DNA-PK in V(D)J recombination and tumorigenesis

Morrison, C. G., Smith, G. C. M., Stingl, L., Jackson, S. P., Wagner, E. F., & Wang, Z. (1997) · Nature Genetics · doi:10.1038/ng1297-479 · Cited by 176 · see citing works

Dual Function for Poly(ADP-ribose) Synthesis in Response to DNA Strand Breakage

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The role of BRCA1 in DNA double-strand repair: Past and present

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Integrating the DNA damage and protein stress responses during cancer development and treatment

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PARP inhibition selectively increases sensitivity to cisplatin in ERCC1-low non-small cell lung cancer cells

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Differences in PARP Inhibitors for the Treatment of Ovarian Cancer: Mechanisms of Action, Pharmacology, Safety, and Efficacy

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Evaluation of the pharmacodynamics and pharmacokinetics of the PARP inhibitor olaparib: a phase I multicentre trial in patients scheduled for elective breast cancer surgery

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The histone variant macroH2A1.1 is recruited to DSBs through a mechanism involving PARP1

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AMPKα2 exerts its anti-inflammatory effects through PARP-1 and Bcl-6

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Telomere fusion threshold identifies a poor prognostic subset of breast cancer patients

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Transcriptional and Posttranslational Regulation of Nucleotide Excision Repair: The Guardian of the Genome against Ultraviolet Radiation

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Altered DNA base excision repair profile in brain tissue and blood in Alzheimer’s disease

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Poly(ADP-Ribose) Polymerase-1 Inhibition by Arsenite Promotes the Survival of Cells With Unrepaired DNA Lesions Induced by UV Exposure

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Coordination of DNA repair by NEIL1 and PARP-1: a possible link to aging

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Targeting DNA Damage Response and Immune Checkpoint for Anticancer Therapy

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Cip2a promotes cell cycle progression in triple-negative breast cancer cells by regulating the expression and nuclear export of p27Kip1

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PARP inhibitor rucaparib induces changes in NAD levels in cells and liver tissues as assessed by MRS

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Unsprung traps keep PARP inhibitors effective

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Complete inhibition of poly(ADP-ribose) polymerase activity prevents the recovery of C3H1OT1/2 cells from oxidative stress

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A Review on Poly (ADP-ribose) Polymerase (PARP) - An Enzyme that Share the ability to Catalyze the Transfer of ADP-Ribose to Target Proteins

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NADH can enter into astrocytes and block poly(ADP-ribose) polymerase-1-mediated astrocyte death

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Trapping Poly(ADP-Ribose) Polymerase

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