Therapeutic applications of PARP inhibitors: Anticancer therapy and beyond

Curtin, Nicola J.; Szabo, Csaba

doi:10.1016/j.mam.2013.01.006

Cited by 391PARP inhibition in cancer therapyDNA Repair MechanismsBRCA gene mutations in cancer

Therapeutic applications of PARP inhibitors: Anticancer therapy and beyond

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Curtin, Nicola J., Szabo, Csaba·2013·Molecular Aspects of Medicine

DOI 10.1016/j.mam.2013.01.006PMC PMC3657315

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Abstract

The aim of this article is to describe the current and potential clinical translation of pharmacological inhibitors of poly(ADP-ribose) polymerase (PARP) for the therapy of various diseases. The first section of the present review summarizes the available preclinical and clinical data with PARP inhibitors in various forms of cancer. In this context, the role of PARP in single-strand DNA break repair is relevant, leading to replication-associated lesions that cannot be repaired if homologous recombination repair (HRR) is defective, and the synthetic lethality of PARP inhibitors in HRR-defective cancer. HRR defects are classically associated with BRCA1 and 2 mutations associated with familial breast and ovarian cancer, but there may be many other causes of HRR defects. Thus, PARP inhibitors may be the drugs of choice for BRCA mutant breast and ovarian cancers, and extend beyond these tumors if appropriate biomarkers can be developed to identify HRR defects. Multiple lines of preclinical data demonstrate that PARP inhibition increases cytotoxicity and tumor growth delay in combination with temozolomide, topoisomerase inhibitors and ionizing radiation. Both single agent and combination clinical trials are underway. The final part of the first section of the present review summarizes the current status of the various PARP inhibitors that are in various stages of clinical development. The second section of the present review summarizes the role of PARP in selected non-oncologic indications. In a number of severe, acute diseases (such as stroke, neurotrauma, circulatory shock and acute myocardial infarction) the clinical translatability of PARP inhibition is supported by multiple lines of preclinical data, as well as observational data demonstrating PARP activation in human tissue samples. In these disease indications, PARP overactivation due to oxidative and nitrative stress drives cell necrosis and pro-inflammatory gene expression, which contributes to disease pathology. Accordingly, multiple lines of preclinical data indicate the efficacy of PARP inhibitors to preserve viable tissue and to down-regulate inflammatory responses. As the clinical trials with PARP inhibitors in various forms of cancer progress, it is hoped that a second line of clinical investigations, aimed at testing of PARP inhibitors for various non-oncologic indications, will be initiated, as well.

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Specific pharmacological inhibitors of PARP1 efficiently delay parthanatos in multiple cell types, in vitro and in vivo.
“specific pharmacological inhibitors of PARP1 efficiently delay parthanatos in multiple cell types, in vitro and in vivo [1, 669].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [669]
PARP1 inhibition by pharmacological or genetic interventions mediates robust cytoprotective effects in multiple animal models of disease.
“PARP1 inhibition by pharmacological or genetic interventions mediates robust cytoprotective effects in multiple animal models of disease [1, 669].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [669]
PARP inhibitors are available and are being tested clinically in cancer.
“PARP inhibitors (Paribs) already exist and are clinically tested in the cancer field (Curtin and Szabo, 2013).”
From Pharmacological Inhibition of poly(ADP-ribose) polymerases improves fitness and mitochondrial function in skeletal muscle (2014) · cites this paper as Curtin and Szabo, 2013
Paribs are currently tested for oncology indications, with positive results in tumors that have defective homologous DNA recombination repair.
“Paribs are currently being tested for oncology indications, with positive outcomes in tumors with dysfunctional homologous DNA recombination repair (Curtin and Szabo, 2013).”
From Pharmacological Inhibition of poly(ADP-ribose) polymerases improves fitness and mitochondrial function in skeletal muscle (2014) · cites this paper as Curtin and Szabo, 2013
The success of Paribs is thought to depend on cancer cells' high reliance on PARP enzymes for DNA repair, but may also involve reprogramming cells toward oxidative metabolism.
“The success of Paribs is thought to rely on the high dependency of these cancer cells on PARP enzymes for DNA repair (Curtin and Szabo, 2013), but could also involve their capacity to reprogram cells towards oxidative metabolism (Bai et al., 2011).”
From Pharmacological Inhibition of poly(ADP-ribose) polymerases improves fitness and mitochondrial function in skeletal muscle (2014) · cites this paper as Curtin and Szabo, 2013

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Elevated Levels of Oxidative DNA Damage and DNA Repair Enzymes in Human Atherosclerotic Plaques
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A Marker of Homologous Recombination Predicts Pathologic Complete Response to Neoadjuvant Chemotherapy in Primary Breast Cancer
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Hydrogen sulfide replacement therapy protects the vascular endothelium in hyperglycemia by preserving mitochondrial function
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Potent Metalloporphyrin Peroxynitrite Decomposition Catalyst Protects Against the Development of Doxorubicin-Induced Cardiac Dysfunction
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Protection against peroxynitrite-induced fibroblast injury and arthritis development by inhibition of poly(ADP-ribose) synthase
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Inhibition of PARP-1 by Olaparib (AZD2281) Increases the Radiosensitivity of a Lung Tumor Xenograft
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A Novel Methionine-Based Signaling Mechanism Regulating the Expression of Thymidylate Synthase
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Aldose Reductase Inhibition Counteracts Oxidative-Nitrosative Stress and Poly(ADP-Ribose) Polymerase Activation in Tissue Sites for Diabetes Complications
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Regulation of microglial expression of integrins by poly(ADP-ribose) polymerase-1
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Part I: Pathogenetic Role of Peroxynitrite in the Development of Diabetes and Diabetic Vascular Complications: Studies With FP15, A Novel Potent Peroxynitrite Decomposition Catalyst
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Potential role of poly(adenosine 5′-diphosphate-ribose) polymerase activation in the pathogenesis of myocardial contractile dysfunction associated with human septic shock
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In vitro and In vivo Radiosensitization of Glioblastoma Cells by the Poly (ADP-Ribose) Polymerase Inhibitor E7016
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Resistance to Acute Septic Peritonitis in Poly(ADP-ribose) Polymerase-1-Deficient Mice
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Poly(ADP-Ribose) Polymerase Is Activated in Subjects at Risk of Developing Type 2 Diabetes and Is Associated With Impaired Vascular Reactivity
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Polymorphisms in DNA Base Excision Repair Genes ADPRT and XRCC1 and Risk of Lung Cancer
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Role of Glutamic Acid 988 of Human Poly-ADP-ribose Polymerase in Polymer Formation
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Role of nitrosative stress in the pathogenesis of diabetic vascular dysfunction
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The ADPRT V762A Genetic Variant Contributes to Prostate Cancer Susceptibility and Deficient Enzyme Function
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Poly(ADP-Ribose) Polymerase Inhibition Reduces Reperfusion Injury After Heart Transplantation
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Safety and tolerability of the poly(ADP-ribose) polymerase (PARP) inhibitor, olaparib (AZD2281) in combination with topotecan for the treatment of patients with advanced solid tumors: a phase I study
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Myocardial Postischemic Injury Is Reduced by PolyADPribose Polymerase-1 Gene Disruption
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Clinical perspectives of PARP inhibitors
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Activation of Microglial Poly(ADP-Ribose)-Polymerase-1 by Cholesterol Breakdown Products during Neuroinflammation
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Ca2+‐dependent generation of mitochondrial reactive oxygen species serves as a signal for poly(ADP‐ribose) polymerase‐1 activation during glutamate excitotoxicity
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Cross-sensitivity of γ-ray-sensitive hamster mutants to cross-linking agents
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Potentiation of anti-cancer agent cytotoxicity by the potent poly(ADP-ribose) polymerase inhibitors NU1025 and NU1064
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GW274150, a potent and highly selective inhibitor of iNOS, reduces experimental renal ischemia/reperfusion injury
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Novel Tricyclic Poly(ADP-ribose) Polymerase-1 Inhibitors with Potent Anticancer Chemopotentiating Activity: Design, Synthesis, and X-ray Cocrystal Structure
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Relationship between the intracellular effects of camptothecin and the inhibition of DNA topoisomerase I in cultured L1210 cells.
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PTEN Deletion in Prostate Cancer Cells Does Not Associate with Loss of RAD51 Function: Implications for Radiotherapy and Chemotherapy
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Poly(ADP-ribose) polymerase-1 (PARP-1) and its therapeutic implications
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Du L Zhang X Han YY Burke NA Kochanek Clark RS Vagni VA Nathaniel PD Jenkins LW Dixon CE Szabo C Local administration of the poly (ADP-ribose) polymerase inhibitor INO-1001 prevents NAD+ depletion and improves water maze performance after traumatic brain injury in mice J Neurotrauma 2007 24 1399 405 17711401
Miknyoczki SJ Jones-Bolin S Prichard S Chemopotentiation of temozlomide, irinotecan and cisplatin activity by CEP-6800, a poly(ADP-ribose) polymerase inhibitor Mol Cancer Ther 2003 2 371 82 12700281
Pacher P Liaudet L Bai P Mabley JG Kaminski PM Virág L Deb A Szabó E Ungvári Z Wolin MS Groves JT Szabó C Potent metalloporphyrin peroxynitrite decomposition catalyst protects against the development of doxorubicin-induced cardiac dysfunction Circulation 2003 107 896 904 12591762
Szabó C Snyder SS Szabo C Cell death by energy depletion: a re-emerging concept via the nitric oxide connection Cell Death: The Role of PARP 2000 1 6 CRC Press Boca Raton, Florida

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Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors
Thorsell, A. G., Ekblad, T., Karlberg, T., Löw, M., Pinto, A. F., Tresaugues, L., Moche, M., Cohen, M. S., & Schuler, H. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00990 · Cited by 369 · see citing works
Chemical Genetic Discovery of PARP Targets Reveals a Role for PARP-1 in Transcription Elongation
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An integrative drug repositioning framework discovered a potential therapeutic agent targeting COVID-19
Ge, Y., Tian, T., Huang, S., Wan, F., Li, J., Li, S., Wang, X., Yang, H., Hong, L., Wu, N., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00568-6 · Cited by 300 · see citing works
Rationale for Poly(ADP-ribose) Polymerase (PARP) Inhibitors in Combination Therapy with Camptothecins or Temozolomide Based on PARP Trapping versus Catalytic Inhibition
Murai, J., Zhang, Y., Morris, J., Ji, J. J., Takeda, S., Doroshow, J. H., & Pommier, Y. G. (2014) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.113.210146 · Cited by 297 · see citing works
Poly(ADP-ribose) signaling in cell death
Virág, L., Robaszkiewicz, A., Rodriguez-Vargas, J. M., & Oliver, F. J. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.007 · Cited by 273 · see citing works
Which cell death modality wins the contest for photodynamic therapy of cancer?
Mishchenko, T. A., Balalaeva, I. V., Gorokhova, A. A., Vedunova, M. V., & Krysko, D. V. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04851-4 · Cited by 290 · see citing works
Mechanistic Dissection of PARP1 Trapping and the Impact on In Vivo Tolerability and Efficacy of PARP Inhibitors
Hopkins, T. A., Shi, Y., Rodriguez, L. E., Solomon, L. R., Donawho, C. K., DiGiammarino, E. L., Panchal, S. C., Wilsbacher, J. L., Gao, W., Olson, A. M., et al. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0191-t · Cited by 270 · see citing works
Pharmacological Inhibition of poly(ADP-ribose) polymerases improves fitness and mitochondrial function in skeletal muscle
Pirinen, E., Cantó, C., Jo, Y. S., Morato, L., Zhang, H., Menzies, K. J., Williams, E. G., Mouchiroud, L., Moullan, N., Hagberg, C., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.002 · Cited by 254 · see citing works
“First, chronic Parib treatment could induce genomic instability (Curtin and Szabo, 2013).”
BackgroundInfluential
Readers of poly(ADP-ribose): designed to be fit for purpose
Teloni, F., & Altmeyer, M. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1383 · Cited by 250 · see citing works
Trapping Poly(ADP-Ribose) Polymerase
Shen, Y., Aoyagi-Scharber, M., & Wang, B. (2015) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.222448 · Cited by 230 · see citing works
Microbiome—Microbial Metabolome—Cancer Cell Interactions in Breast Cancer—Familiar, but Unexplored
Mikó, E., Kovàcs, T., Sebő, É., Tóth, J., Csonka, T., Ujlaki, G., Sipos, A., Szabó, J., Méhes, G., & Bai, P. (2019) · Cells · doi:10.3390/cells8040293 · Cited by 220 · see citing works
Opportunities for the repurposing of PARP inhibitors for the therapy of non‐oncological diseases
Berger, N. A., Besson, V. C., Boulares, A. H., Bürkle, A., Chiarugi, A., Clark, R. S. B., Curtin, N. J., Cuzzocrea, S., Dawson, T. M., Dawson, V. L., et al. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13748 · Cited by 212 · see citing works
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The Promise of Proteomics for the Study of ADP-Ribosylation
Daniels, C. M., Ong, S., & Leung, A. K. L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.012 · Cited by 196 · see citing works
Poly(ADP-ribose): PARadigms and PARadoxes
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Niraparib: A Poly(ADP-ribose) Polymerase (PARP) Inhibitor for the Treatment of Tumors with Defective Homologous Recombination
JONES, P. G., Wilcoxen, K., Rowley, M., & Toniatti, C. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm5018237 · Cited by 189 · see citing works
Tankyrases: Structure, Function and Therapeutic Implications in Cancer
Haikarainen, T., Krauss, S. J. K., & Lehtiö, L. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140630101525 · Cited by 185 · see citing works
Induction of apoptosis in MDA-MB-231 breast cancer cells by a PARP1-targeting PROTAC small molecule
Zhao, Q., Lan, T., Su, S., & Rao, Y. (2018) · Chemical Communications · doi:10.1039/c8cc07813k · Cited by 185 · see citing works
PARPs in lipid metabolism and related diseases
Szántó, M., Gupte, R., Kraus, W. L., Pacher, P., & Bai, P. (2021) · Progress in Lipid Research · doi:10.1016/j.plipres.2021.101117 · Cited by 184 · see citing works
Discovery and Characterization of (8 S ,9 R )-5-Fluoro-8-(4-fluorophenyl)-9-(1-methyl-1 H -1,2,4-triazol-5-yl)-2,7,8,9-tetrahydro-3 H -pyrido[4,3,2-de]phthalazin-3-one (BMN 673, Talazoparib), a Novel, Highly Potent, and Orally Efficacious Poly(ADP-ribose) Polymerase-1/2 Inhibitor, as an Anticancer Agent
Wang, B., Chu, D., Feng, Y., Shen, Y., Aoyagi-Scharber, M., & Post, L. E. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01498 · Cited by 183 · see citing works
PARP inhibition protects against alcoholic and non-alcoholic steatohepatitis
Mukhopadhyay, P., Horváth, B., Rajesh, M., Varga, Z. V., Gariani, K., Ryu, D., Cao, Z., Holovac, E., Park, O., Zhou, Z., et al. (2016) · Journal of Hepatology · doi:10.1016/j.jhep.2016.10.023 · Cited by 168 · see citing works
Targeted therapies in gynecological cancers: a comprehensive review of clinical evidence
Wang, Q., Peng, H., Qi, X., Wu, M., & Zhao, X. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0199-6 · Cited by 157 · see citing works
Poly(ADP-ribose) Polymerase (PARP) and PARP Inhibitors: Mechanisms of Action and Role in Cardiovascular Disorders
Henning, R. J., Bourgeois, M., & Harbison, R. D. (2018) · Cardiovascular Toxicology · doi:10.1007/s12012-018-9462-2 · Cited by 155 · see citing works
Discovery of 2-[1-(4,4-Difluorocyclohexyl)piperidin-4-yl]-6-fluoro-3-oxo-2,3-dihydro-1H-isoindole-4-carboxamide (NMS-P118): A Potent, Orally Available, and Highly Selective PARP-1 Inhibitor for Cancer Therapy
Papeo, G., Posteri, H., Borghi, D., Busel, A. A., Caprera, F., Casale, E., Ciomei, M., Cirla, A., Corti, E., D’Anello, M., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00680 · Cited by 144 · see citing works
The role of the microbiome in ovarian cancer: mechanistic insights into oncobiosis and to bacterial metabolite signaling
Sipos, A., Ujlaki, G., Mikó, E., Maka, E., Szabó, J., Uray, K., Krasznai, Z. T., & Bai, P. (2021) · Molecular Medicine · doi:10.1186/s10020-021-00295-2 · Cited by 150 · see citing works
Chromatin to Clinic: The Molecular Rationale for PARP1 Inhibitor Function
Feng, F. Y.-C., Bono, J. S. D., Rubin, M. A., & Knudsen, K. E. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.04.016 · Cited by 131 · see citing works
From old alkylating agents to new minor groove binders
Puyo, S., Montaudon, D., & Pourquier, P. (2013) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2013.07.006 · Cited by 133 · see citing works
Randomized Trial of Oral Cyclophosphamide and Veliparib in High-Grade Serous Ovarian, Primary Peritoneal, or Fallopian Tube Cancers, or BRCA -Mutant Ovarian Cancer
Kummar, S., Oza, A. M., Fleming, G. F., Sullivan, D. M., Gandara, D. R., Naughton, M. J., Villalona-Calero, M. A., Morgan, R. J., Szabó, P., Youn, A., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2565 · Cited by 130 · see citing works
Inhibition of poly(ADP-ribosyl)ation in cancer: Old and new paradigms revisited
Lupo, B., & Trusolino, L. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.07.004 · Cited by 131 · see citing works
PARP Inhibitors as Therapeutics: Beyond Modulation of PARylation
Min, A., & Im, S. (2020) · Cancers · doi:10.3390/cancers12020394 · Cited by 129 · see citing works
Poly (ADP-Ribose) Polymerase-1 Is a Key Mediator of Liver Inflammation and Fibrosis
Mukhopadhyay, P., Rajesh, M., Cao, Z., Horváth, B., Park, O., Wang, H., Erdélyi, K., Holovac, E., Wang, Y., Liaudet, L., et al. (2013) · Hepatology · doi:10.1002/hep.26763 · Cited by 125 · see citing works
Poly(ADP-ribose) polymerases as modulators of mitochondrial activity
Bai, P., Nagy, L., Fodor, T., Liaudet, L., & Pacher, P. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2014.11.003 · Cited by 119 · see citing works
Recent progress on HDAC inhibitors with dual targeting capabilities for cancer treatment
Peng, X., Sun, Z., Kuang, P., & Chen, J. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112831 · Cited by 119 · see citing works
An update on PARP inhibitors for the treatment of cancer
Hall, M., & Benafif, S. (2015) · OncoTargets and Therapy · doi:10.2147/ott.s30793 · Cited by 112 · see citing works
PARP Trapping Beyond Homologous Recombination and Platinum Sensitivity in Cancers
Murai, J., & Pommier, Y. G. (2018) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030518-055914 · Cited by 112 · see citing works
The Elephant and the Blind Men: Making Sense of PARP Inhibitors in Homologous Recombination Deficient Tumor Cells
Lorenzo, S. B. D., Patel, A. G., Hurley, R. M., & Kaufmann, S. H. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00228 · Cited by 110 · see citing works
PARP1 Inhibitors: Antitumor Drug Design
Maluchenko, N. V., Kotova, E. Y., Kulaeva, O. I., Kirpichnikov, M. P., & Studitskiy, V. M. (2015) · Acta Naturae · doi:10.32607/20758251-2015-7-3-27-37 · Cited by 111 · see citing works
PARP inhibition protects mitochondria and reduces ROS production via PARP-1-ATF4-MKP-1-MAPK retrograde pathway
Hocsák, E., Szabó, V., Kálmán, N., Antus, C., Cseh, A. M., Sümegi, K., Erős, K., Hegedüs, Z., Gallyas, F., Sümegi, B., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.018 · Cited by 110 · see citing works
PARP1 in Carcinomas and PARP1 Inhibitors as Antineoplastic Drugs
Wang, L., Liang, C., Li, F., Guan, D., Wu, X., Fu, X., Lü, A., & Zhang, G. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102111 · Cited by 108 · see citing works
ATM-Deficient Cancers Provide New Opportunities for Precision Oncology
Jette, N., Kumar, M., Radhamani, S., Arthur, G., Goutam, S., Yip, S., Kolinsky, M. P., Williams, G. J., Bose, P., & Lees‐Miller, S. P. (2020) · Cancers · doi:10.3390/cancers12030687 · Cited by 108 · see citing works
The rise and fall of poly(ADP-ribose): An enzymatic perspective
Pascal, J. M., & Ellenberger, T. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.04.008 · Cited by 107 · see citing works
Adipose tissue NAD+-homeostasis, sirtuins and poly(ADP-ribose) polymerases -important players in mitochondrial metabolism and metabolic health
Jokinen, R., Pirnes-Karhu, S., Pietiläinen, K. H., & Pirinen, E. (2017) · Redox Biology · doi:10.1016/j.redox.2017.02.011 · Cited by 103 · see citing works
DNA Damage Signalling and Repair Inhibitors: The Long-Sought-After Achilles’ Heel of Cancer
Velic, D., Couturier, A. M., Ferreira, M., Rodrigue, A., Poirier, G. G., Fleury, F., & Masson, J. (2015) · Biomolecules · doi:10.3390/biom5043204 · Cited by 97 · see citing works
Poly(ADP‐ribose) Polymerase 1 (PARP1) in Atherosclerosis: From Molecular Mechanisms to Therapeutic Implications
Xu, S., Bai, P., Little, P. J., & Liu, P. (2013) · Medicinal Research Reviews · doi:10.1002/med.21300 · Cited by 97 · see citing works
The role of melatonin on doxorubicin-induced cardiotoxicity: A systematic review
Najafi, M., Shayesteh, M. R. H., Mortezaee, K., Farhood, B., & Haghi‐Aminjan, H. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.117173 · Cited by 96 · see citing works
Efficacy of PARP Inhibitor Rucaparib in Orthotopic Glioblastoma Xenografts Is Limited by Ineffective Drug Penetration into the Central Nervous System
Parrish, K. E., Cen, L., Murray, J., Calligaris, D., Kizilbash, S. H., Mittapalli, R. K., Carlson, B. L., Schroeder, M. A., Sludden, J., Boddy, A. V., et al. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0553 · Cited by 91 · see citing works
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Olaparib hydroxamic acid derivatives as dual PARP and HDAC inhibitors for cancer therapy
Yuan, Z., Chen, S., Sun, Q., Wang, N., Li, D., Miao, S., Gao, C., Chen, Y., Tan, C., & Jiang, Y. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.05.058 · Cited by 90 · see citing works
Discovery of SK-575 as a Highly Potent and Efficacious Proteolysis-Targeting Chimera Degrader of PARP1 for Treating Cancers
Cao, C.-G., Yang, J., Chen, Y. X., Zhou, P., Wang, Y., Du, W., Zhao, L., & Chen, Y. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00821 · Cited by 90 · see citing works
PARP inhibitors for anticancer therapy
Curtin, N. J. (2014) · Biochemical Society Transactions · doi:10.1042/bst20130187 · Cited by 88 · see citing works
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Chemical Methods for Encoding and Decoding of Posttranslational Modifications
Chuh, K. N., Batt, A. R., & Pratt, M. R. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2015.11.006 · Cited by 88 · see citing works
The role of ADP-ribose metabolism in metabolic regulation, adipose tissue differentiation, and metabolismPreprint
Szántó, M., & Bai, P. (2020) · Genes & Development · doi:10.1101/gad.334284.119 · Cited by 88 · see citing works
E7449: A dual inhibitor of PARP1/2 and tankyrase1/2 inhibits growth of DNA repair deficient tumors and antagonizes Wnt signaling
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PARP3 controls TGFβ and ROS driven epithelial-to-mesenchymal transition and stemness by stimulating a TG2-Snail-E-cadherin axis
Karicheva, O., Rodríguez-Vargas, J. M., Wadier, N., Martin-Hernandez, K., Vauchelles, R., Magroun, N., Tissier, A., Schreiber, V., & Dantzer, F. (2016) · Oncotarget · doi:10.18632/oncotarget.11627 · Cited by 87 · see citing works
Host-Directed Therapies: Modulating Inflammation to Treat Tuberculosis
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PARP inhibitors: polypharmacology versus selective inhibition
Ekblad, T., Camaioni, E., Schuler, H., & Macchiarulo, A. (2013) · FEBS Journal · doi:10.1111/febs.12298 · Cited by 78 · see citing works
RECQ1 helicase is involved in replication stress survival and drug resistance in multiple myeloma
Viziteu, E., Klein, B., Basbous, J., Lin, Y., Hirtz, C., Gourzonès, C., Tiers, L., Bruyer, A., Vincent, L., Grandmougin, C., et al. (2017) · Leukemia · doi:10.1038/leu.2017.54 · Cited by 77 · see citing works
Drug resistance‐related microRNAs in osteosarcoma: Translating basic evidence into therapeutic strategies
Chen, R., Wang, G., Zheng, Y., Hua, Y., & Cai, Z. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14064 · Cited by 76 · see citing works
Tryptophan metabolism and disposition in cancer biology and immunotherapy
Badawy, A. A. ‐. (2022) · Bioscience Reports · doi:10.1042/bsr20221682 · Cited by 75 · see citing works
Roles of N-Methyl-D-Aspartate Receptors (NMDARs) in Epilepsy
Chen, S., Xu, D., Liu, F., Fang, Z. H., Wang, X., & Li, M. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.797253 · Cited by 75 · see citing works
Randomized phase II trial of cyclophosphamide and the oral poly (ADP-ribose) polymerase inhibitor veliparib in patients with recurrent, advanced triple-negative breast cancer
Kummar, S., Wade, J. L., Oza, A. M., Sullivan, D. M., Chen, A. P., Gandara, D. R., Ji, J. J., Kinders, R. J., Wang, L., Allen, D. E., et al. (2016) · Investigational New Drugs · doi:10.1007/s10637-016-0335-x · Cited by 74 · see citing works
Reverse the Resistance to PARP Inhibitors
Kim, Y., Kim, A., Sharip, A., Sharip, A., Jiang, J., Yang, Q., & Xie, Y. (2017) · International Journal of Biological Sciences · doi:10.7150/ijbs.17240 · Cited by 74 · see citing works
Mitochondrial poly(ADP-ribose) polymerase: The Wizard of Oz at work
Brunyánszki, A., Szczęsny, B., Virág, L., & Szabó, C. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.02.024 · Cited by 73 · see citing works
Tryptophan Metabolism: A Versatile Area Providing Multiple Targets for Pharmacological Intervention
Badawy, A. A.-B. (2019) · Egyptian Journal of Basic and Clinical Pharmacology · doi:10.32527/2019/101415 · Cited by 73 · see citing works
PARP14 inhibits microglial activation via LPAR5 to promote post-stroke functional recovery
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PARP, transcription and chromatin modeling
Marjanović, M. P., Crawford, K., & Ahel, I. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.09.014 · Cited by 70 · see citing works
Transcription and DNA Damage: Holding Hands or Crossing Swords?
D’Alessandro, G., & di Fagagna, F. D. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.11.002 · Cited by 66 · see citing works
Successes and Challenges of PARP Inhibitors in Cancer Therapy
Ricks, T. K., Chiu, H.-J., Ison, G., Kim, G., McKee, A. E., Kluetz, P. G., & Pazdur, R. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00222 · Cited by 69 · see citing works
Discovery of novel functionalized 1,2,4-triazoles as PARP-1 inhibitors in breast cancer: Design, synthesis and antitumor activity evaluation
Boraei, A. T. A., Singh, P. K., Sechi, M., & Satta, S. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111621 · Cited by 69 · see citing works
Nicotinamide adenine dinucleotide homeostasis and signalling in heart disease: Pathophysiological implications and therapeutic potential
Mericskay, M. (2015) · Archives of cardiovascular diseases · doi:10.1016/j.acvd.2015.10.004 · Cited by 67 · see citing works
Metabolic roles of poly(ADP-ribose) polymerases
Vida, A., Márton, J., Mikó, E., & Bai, P. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.12.009 · Cited by 66 · see citing works
The new identified biomarkers determine sensitivity to immune check-point blockade therapies in melanoma
Chen, H., Yang, M., Wang, Q., Song, F., Li, X., & Chen, K. (2019) · OncoImmunology · doi:10.1080/2162402x.2019.1608132 · Cited by 66 · see citing works
Phase I and Pharmacologic Study of Olaparib in Combination with High-dose Radiotherapy with and without Concurrent Cisplatin for Non–Small Cell Lung Cancer
de Haan, R., van den Heuvel, M. M., van Diessen, J., Peulen, H. M. U., van Werkhoven, E. D., de Langen, A. J., Lalezari, F., Pluim, D., Verwijs-Janssen, M., Vens, C., et al. (2020) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-20-2551 · Cited by 64 · see citing works
Nudix hydrolases degrade protein-conjugated ADP-ribose
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Repositioning PARP inhibitors for SARS‐CoV‐2 infection(COVID‐19); a new multi‐pronged therapy for acute respiratory distress syndrome?
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SIRT6 interacts with TRF2 and promotes its degradation in response to DNA damage
Rizzo, A., Iachettini, S., Salvati, E., Zizza, P., Maresca, C., D’Angelo, C., Benarroch, D., Capolupo, A., Gaudio, F. D., Cosconati, S., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1202 · Cited by 64 · see citing works
A Quantitative Assay Reveals Ligand Specificity of the DNA Scaffold Repair Protein XRCC1 and Efficient Disassembly of Complexes of XRCC1 and the Poly(ADP-ribose) Polymerase 1 by Poly(ADP-ribose) Glycohydrolase
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BRCA1 Mutation: A Predictive Marker for Radiation Therapy?
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New paradigms in the repair of oxidative damage in human genome: mechanisms ensuring repair of mutagenic base lesions during replication and involvement of accessory proteins
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NAD+: A key metabolic regulator with great therapeutic potential
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Discovery and Structure–Activity Relationship of Novel 2,3-Dihydrobenzofuran-7-carboxamide and 2,3-Dihydrobenzofuran-3(2 H )-one-7-carboxamide Derivatives as Poly(ADP-ribose)polymerase-1 Inhibitors
Patel, M. R., Bhatt, A., Steffen, J. D., Chergui, A., Murai, J., Pommier, Y. G., Pascal, J. M., Trombetta, L. D., Fronczek, F. R., & Talele, T. T. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5002502 · Cited by 52 · see citing works
Differentiation-Associated Downregulation of Poly(ADP-Ribose) Polymerase-1 Expression in Myoblasts Serves to Increase Their Resistance to Oxidative Stress
Oláh, G., Szczęsny, B., Brunyánszki, A., López-García, I. A., Gerő, D., Radak, Z. O., & Szabó, C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134227 · Cited by 51 · see citing works
Indoleamine 2,3-dioxygenase mediates immune-independent human tumor cell resistance to olaparib, gamma radiation, and cisplatin
Vareki, S. M., Rytelewski, M., Figueredo, R., Chen, D., Ferguson, P. J., Vincent, M. D., Min, W., Zheng, X., & Koropatnick, J. D. (2014) · Oncotarget · doi:10.18632/oncotarget.1916 · Cited by 51 · see citing works
Evaluation and Structural Basis for the Inhibition of Tankyrases by PARP Inhibitors
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Radiosensitization by PARP inhibition to proton beam irradiation in cancer cells
Hirai, T., Saito, S., Fujimori, H., Matsushita, K., Nishio, T., Okayasu, R., & Masutani, M. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.07.062 · Cited by 51 · see citing works
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Authors: Curtin, N. J., & Szabo, C.
Affiliations: Newcastle University (GB)
Corresponding author: Curtin, Nicola J.
ORCID: Curtin, Nicola J.
Venue: Molecular Aspects of Medicine
Publisher: Elsevier BV
Published: 2013-12
Volume: 34
Issue: 6
Pages: 1217-1256
ISSN: 0098-2997 (ISSN-L)
DOI: 10.1016/j.mam.2013.01.006
PMC: PMC3657315
OpenAlex: W2017171454
Cited by: 369
References: 559
Citations by year: 2026: 9 · 2025: 17 · 2024: 12 · 2023: 22 · 2022: 25 · 2021: 25 · 2020: 37 · 2019: 31 · 2018: 26 · 2017: 32 · 2016: 38 · 2015: 50 · 2014: 24 · 2013: 21
FWCI: 4.93
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Molecular Aspects of Medicine (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Newcastle University ePrints (Newcastle Univesity)
Funders: National Institutes of Health
Topics: Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › BRCA gene mutations in cancer
Keywords: PARP inhibitors, poly(ADP-ribose) polymerase, synthetic lethality, homologous recombination deficiency, BRCA mutations, breast cancer, ovarian cancer, temozolomide combination therapy, topoisomerase inhibitors, ionizing radiation, oxidative stress, nitrative stress, necrosis, inflammation, stroke, neurotrauma, shock, acute myocardial infarction, clinical translation
MeSH terms: Poly(ADP-ribose) Polymerase Inhibitors, Animals, Antineoplastic Agents, Cardiovascular Diseases, Clinical Trials as Topic, Enzyme Inhibitors, Humans, Neoplasms, Poly(ADP-ribose) Polymerases, Radiation-Sensitizing Agents, Stroke, Translational Research, Biomedical, Molecular Targeted Therapy

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Therapeutic applications of PARP inhibitors: Anticancer therapy and beyond

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