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1

Blin, J., and F. Nowak. "Cancer de l’ovaire et inhibiteur de PARP : parcours des patientes en génétique oncologique." Oncologie 19, no. 5-6 (2017): 191–98. http://dx.doi.org/10.1007/s10269-017-2705-1.

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2

Chabanon, Roman M., and Sophie Postel-Vinay. "Inhibiteurs de PARP." médecine/sciences 35, no. 10 (2019): 728–31. http://dx.doi.org/10.1051/medsci/2019148.

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3

Kempe, Sabrina. "Neuer PARP-Inhibitor verfügbar." InFo Hämatologie + Onkologie 23, no. 7-8 (2020): 53. http://dx.doi.org/10.1007/s15004-020-8165-6.

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4

Hofmann-Aßmus, Marion. "Erhaltungstherapie mit PARP-Inhibitor." InFo Onkologie 21, no. 8 (2018): 73. http://dx.doi.org/10.1007/s15004-018-6357-0.

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5

Dréan, Amy, Christopher J. Lord, and Alan Ashworth. "PARP inhibitor combination therapy." Critical Reviews in Oncology/Hematology 108 (December 2016): 73–85. http://dx.doi.org/10.1016/j.critrevonc.2016.10.010.

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6

Bollet, M. A., F. Pouzoulet, F. Mégnin, V. Favaudon, and J. Hall. "Inhibiteurs de PARP et radiothérapie." Oncologie 14, no. 4 (2012): 267–70. http://dx.doi.org/10.1007/s10269-012-2115-8.

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7

Lindgren, Anders E. G., Tobias Karlberg, Ann-Gerd Thorsell, et al. "PARP Inhibitor with Selectivity Toward ADP-Ribosyltransferase ARTD3/PARP3." ACS Chemical Biology 8, no. 8 (2013): 1698–703. http://dx.doi.org/10.1021/cb4002014.

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8

Juhász, Szilvia, Rebecca Smith, Tamás Schauer, et al. "The chromatin remodeler ALC1 underlies resistance to PARP inhibitor treatment." Science Advances 6, no. 51 (2020): eabb8626. http://dx.doi.org/10.1126/sciadv.abb8626.

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Poly(ADP-ribose) polymerase (PARP) inhibitors are used in the treatment of BRCA-deficient cancers, with treatments currently extending toward other homologous recombination defective tumors. In a genome-wide CRISPR knockout screen with olaparib, we identify ALC1 (Amplified in Liver Cancer 1)—a cancer-relevant poly(ADP-ribose)-regulated chromatin remodeling enzyme—as a key modulator of sensitivity to PARP inhibitor. We found that ALC1 can remove inactive PARP1 indirectly through binding to PARylated chromatin. Consequently, ALC1 deficiency enhances trapping of inhibited PARP1, which then impair
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9

Romero, Diana. "EMBRACing a new PARP inhibitor?" Nature Reviews Clinical Oncology 15, no. 11 (2018): 655. http://dx.doi.org/10.1038/s41571-018-0090-3.

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10

Mullard, Asher. "PARP inhibitor pick-me-up." Nature Reviews Drug Discovery 18, no. 11 (2019): 814. http://dx.doi.org/10.1038/d41573-019-00174-w.

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11

Aujla, Mandy. "PARP inhibitor has antitumor activity." Nature Reviews Clinical Oncology 6, no. 9 (2009): 496. http://dx.doi.org/10.1038/nrclinonc.2009.118.

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12

Turner, Nicholas C., and Alan Ashworth. "Biomarkers of PARP inhibitor sensitivity." Breast Cancer Research and Treatment 127, no. 1 (2011): 283–86. http://dx.doi.org/10.1007/s10549-011-1375-8.

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13

Bischoff, Angelika. "Ovarialkarzinom: PARP-Inhibitor breit wirksam." gynäkologie + geburtshilfe 23, no. 6 (2018): 69. http://dx.doi.org/10.1007/s15013-018-1621-9.

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14

Smith, Hannah Louise, Asima Mukhopadhyay, Yvette Drew, Elaine Willmore, and Nicola Curtin. "Differences in Durability of PARP Inhibition by PARP Inhibitors in Ovarian Cancer Cells." Medical Sciences Forum 3, no. 1 (2021): 11. http://dx.doi.org/10.3390/iecc2021-09194.

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Background: PARP inhibitors (PARPi) exploit defects in homologous recombination repair (HRR) to selectively kill tumour cells. Continuous PARP inhibition is required for cytotoxicity. PARPis rucaparib, olaparib, and niraparib have been approved for use in ovarian cancer on continuous schedules. Previous studies demonstrate prolonged PARP inhibition by rucaparib [1]. Aim: To determine if persistent PARP inhibition is a class effect. Methods: IGROV-1 (human ovarian cancer) cells were treated with 1 µM of rucaparib, olaparib, niraparib, talazoparib, or pamiparib for 1 h before drug was washed off
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15

Kirmizibayrak, Petek Ballar, Recep Ilhan, Sinem Yilmaz, Selin Gunal, and Burcu Erbaykent Tepedelen. "A Src/Abl kinase inhibitor, bosutinib, downregulates and inhibits PARP enzyme and sensitizes cells to the DNA damaging agents." Turkish Journal of Biochemistry 43, no. 2 (2017): 101–9. http://dx.doi.org/10.1515/tjb-2017-0095.

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AbstractBackground:Poly(ADP-ribosyl)ation (PARylation) catalyzed mainly by PARP1 is a highly regulated posttranslational modification associated with several pathways in cellular physiology and genotoxic deoxyribonucleic acid (DNA) damage response. PAR polymers and PARP enzyme function in DNA integrity maintenance and several PARP inhibitors have entered clinical phase studies for cancer therapies.Material and methods:The effect of bosutinib, a dual Src/Abl kinase inhibitor, on PARylation was fluorometrically measured. The cytotoxic and chemosensitizing effects were assessed by 3-(4,5-dimethyl
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16

Sinha, G. "Downfall of Iniparib: A PARP Inhibitor That Doesn't Inhibit PARP After All." JNCI Journal of the National Cancer Institute 106, no. 1 (2014): djt447. http://dx.doi.org/10.1093/jnci/djt447.

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17

Yung, W. K. Alfred, Shaofang Wu, Feng Gao, et al. "EGFR amplification predicted selective sensitivity to PARP inhibitors with high PARP-DNA trapping potential in human GBM." Journal of Clinical Oncology 37, no. 15_suppl (2019): 2047. http://dx.doi.org/10.1200/jco.2019.37.15_suppl.2047.

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2047 Background: Poly-ADP-ribose polymerase (PARP) is an enzyme critical for regulating a variety of DNA damage repair mechanisms such as BER/SSBR, and PARP inhibitors have been shown to have single agent activity in breast and ovarian cancer patients with BRCA ½ mutations. However, PARP inhibitor such as veliparib has limited single agent activity in GBM and identifying markers predicting sensitivity is critical to select individuals or certain groups of patients for PARP inhibitor therapy. Methods: Potency and selectivity of PARP inhibitors were analyzed in a panel of glioma stem cells (GSCs
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18

Nacev, Benjamin A., and William D. Tap. "TOMAS: revisiting PARP inhibitor combination therapy." Lancet Oncology 19, no. 10 (2018): 1269–70. http://dx.doi.org/10.1016/s1470-2045(18)30494-7.

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19

Mullard, Asher. "European regulators approve first PARP inhibitor." Nature Reviews Drug Discovery 13, no. 12 (2014): 877. http://dx.doi.org/10.1038/nrd4508.

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20

Pezaro, Carmel. "PARP inhibitor combinations in prostate cancer." Therapeutic Advances in Medical Oncology 12 (January 2020): 175883591989753. http://dx.doi.org/10.1177/1758835919897537.

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Polyadenosine-diphosphate-ribose polymerase (PARP) inhibitors cause deoxyribonucleic acid (DNA) damage that can be lethal to cells with deficient repair mechanisms. A number of PARP inhibitors are being tested as treatments for men with prostate cancer, both as monotherapies and in combinations that are based on purported synergies in treatment effect. While the initial single-agent development focused on men with identified deficiencies in DNA-repair pathways, broader patient populations are being considered for combination approaches. This review summarizes the current clinical development o
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21

Bradley, Conor A. "Efficacy of a PARP inhibitor combination." Nature Reviews Urology 15, no. 9 (2018): 526. http://dx.doi.org/10.1038/s41585-018-0048-3.

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22

Bebb, D. Gwyn, and Susan P. Lees-Miller. "Predicting PARP inhibitor sensitivity and resistance." Cell Cycle 11, no. 22 (2012): 4110. http://dx.doi.org/10.4161/cc.22604.

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23

Luker, Gary D. "Imaging Pharmacodynamics of a PARP Inhibitor." Radiology: Imaging Cancer 3, no. 3 (2021): e219010. http://dx.doi.org/10.1148/rycan.2021219010.

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24

Kedar, Padmini S., Donna F. Stefanick, Julie K. Horton, and Samuel H. Wilson. "Increased PARP-1 Association with DNA in Alkylation Damaged, PARP-Inhibited Mouse Fibroblasts." Molecular Cancer Research 10, no. 3 (2012): 360–68. http://dx.doi.org/10.1158/1541-7786.mcr-11-0477.

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25

Lazareth, H., N. Delanoy, E. Boissier, et al. "Insuffisance rénale aiguë et inhibiteurs de PARP." Néphrologie & Thérapeutique 15, no. 5 (2019): 356. http://dx.doi.org/10.1016/j.nephro.2019.07.228.

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26

Nilov, Dmitry, Natalya Maluchenko, Tatyana Kurgina, et al. "Molecular Mechanisms of PARP-1 Inhibitor 7-Methylguanine." International Journal of Molecular Sciences 21, no. 6 (2020): 2159. http://dx.doi.org/10.3390/ijms21062159.

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7-Methylguanine (7-MG), a natural compound that inhibits DNA repair enzyme poly(ADP-ribose) polymerase 1 (PARP-1), can be considered as a potential anticancer drug candidate. Here we describe a study of 7-MG inhibition mechanism using molecular dynamics, fluorescence anisotropy and single-particle Förster resonance energy transfer (spFRET) microscopy approaches to elucidate intermolecular interactions between 7-MG, PARP-1 and nucleosomal DNA. It is shown that 7-MG competes with substrate NAD+ and its binding in the PARP-1 active site is mediated by hydrogen bonds and nonpolar interactions with
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27

Gurkan-Alp, A. Selen, Mehmet Alp, Arzu Z. Karabay, Asli Koc, and Erdem Buyukbingol. "Synthesis of Some Benzimidazole-derived Molecules and their Effects on PARP-1 Activity and MDA-MB-231, MDA-MB-436, MDA-MB-468 Breast Cancer Cell Viability." Anti-Cancer Agents in Medicinal Chemistry 20, no. 14 (2020): 1728–38. http://dx.doi.org/10.2174/1871520620666200502001953.

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Background: Poly (ADP-ribosyl) polymerase-1 (PARP-1) inhibitors are compounds that are used to treat cancers, which are defective in DNA-repair and DNA Damage-Response (DDR) pathways. Objective: In this study, a series of potential PARP-1 inhibitor substituted (piperazine-1-carbonyl)phenyl)-1Hbenzo[ d]imidazole-4-carboxamide compounds were synthesised and tested for their PARP-1 inhibitory and anticancer activities. Methods: Compounds were tested by cell-free colorimetric PARP-1 activity and MTT assay in MDA-MB-231, MDA-MB-436, MDA-MB-468 breast cancer, and L929 fibroblast cell lines. Results:
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28

Hu, Hongye, Buran Chen, Danni Zheng, and Guanli Huang. "Revealing the selective mechanisms of inhibitors to PARP-1 and PARP-2 via multiple computational methods." PeerJ 8 (May 25, 2020): e9241. http://dx.doi.org/10.7717/peerj.9241.

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Background Research has shown that Poly-ADP-ribose polymerases 1 (PARP-1) is a potential therapeutic target in the clinical treatment of breast cancer. An increasing number of studies have focused on the development of highly selective inhibitors that target PARP-1 over PARP-2, its closest isoform, to mitigate potential side effects. However, due to the highly conserved and similar binding sites of PARP-1 and PARP-2, there is a huge challenge for the discovery and design of PARP-1 inhibitors. Recently, it was reported that a potent PARP-1 inhibitor named NMS-P118 exhibited greater selectivity
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29

Evans, Tarra, and Ursula Matulonis. "PARP inhibitors in ovarian cancer: evidence, experience and clinical potential." Therapeutic Advances in Medical Oncology 9, no. 4 (2017): 253–67. http://dx.doi.org/10.1177/1758834016687254.

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Inhibitors of poly(ADP-ribose) polymerase (PARP) are considered one of the most active and exciting new therapies for the treatment of ovarian cancer. The anticancer activity of PARP inhibitors is based on the DNA repair vulnerability of many ovarian cancer cells, and multiple mechanisms of action of PARP inhibitors have been identified. As single agents, PARP inhibitors have demonstrated their greatest activity in ovarian cancer cells that harbor mutations in BRCA genes. Additionally, recent phase III studies have shown that single-agent PARP inhibitor activity extends beyond BRCA-related can
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30

Lok, B., J. Laird, J. Ma, E. De Stanchina, J. Poirier, and C. Rudin. "MA22.01 PARP Inhibitor Radiosensitization of Small Cell Lung Cancer Differs by PARP Trapping Potency." Journal of Thoracic Oncology 13, no. 10 (2018): S433. http://dx.doi.org/10.1016/j.jtho.2018.08.501.

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31

Takagi, Masatoshi, Jiuhua Piao, Takahiro Kamiya, Mitsuko Masutani, and Shuki Mizutani. "PARP Inhibitor Selectively Induces Cell Death in E2A-Hlf Positive Leukemia." Blood 124, no. 21 (2014): 2183. http://dx.doi.org/10.1182/blood.v124.21.2183.2183.

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Abstract Background: Defects in homologous recombination repair (HRR) have long been known to contribute to genomic instability leading to tumor development. Poly (ADP-ribose) polymerase (PARP) exerts various cell biological effects, such as maintenance of genomic stability, energy metabolism and cell death. PARP is indispensable in DNA repair machinery, especially in base excision repair (BER). PARP inhibition convert DNA double strand breaks from DNA single strand breaks induced by alkylating agents. These DNA double strand breaks can be repaired by HRR. Therefore, PARP inhibitor induces syn
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32

Gatti, Marco, Ralph Imhof, Qingyao Huang, Michael Baudis, and Matthias Altmeyer. "The Ubiquitin Ligase TRIP12 Limits PARP1 Trapping and Constrains PARP Inhibitor Efficiency." Cell Reports 32, no. 5 (2020): 107985. http://dx.doi.org/10.1016/j.celrep.2020.107985.

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33

Madison, Dana L., Daniel Stauffer, and James R. Lundblad. "The PARP inhibitor PJ34 causes a PARP1-independent, p21 dependent mitotic arrest." DNA Repair 10, no. 10 (2011): 1003–13. http://dx.doi.org/10.1016/j.dnarep.2011.07.006.

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34

Baldwin, Paige, Shifalika Tangutoori, and Srinivas Sridhar. "In vitro analysis of PARP inhibitor nanoformulations." International Journal of Nanomedicine Volume 13 (March 2018): 59–61. http://dx.doi.org/10.2147/ijn.s124992.

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35

Zaremba, Tomasz, and Nicola Curtin. "PARP Inhibitor Development for Systemic Cancer Targeting." Anti-Cancer Agents in Medicinal Chemistry 7, no. 5 (2007): 515–23. http://dx.doi.org/10.2174/187152007781668715.

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36

WACHTER, KERRI. "PARP Inhibitor Delays Progression in Ovarian Ca." Ob.Gyn. News 46, no. 6 (2011): 2. http://dx.doi.org/10.1016/s0029-7437(11)70169-0.

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37

McCluskey, J. D. "PARP-1 Inhibitor Attenuates Cocaine-Induced Hepatotoxicity." Open Toxicology Journal 5, no. 1 (2012): 21–27. http://dx.doi.org/10.2174/1874340401205010021.

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38

Pettitt, Stephen J., and Christopher J. Lord. "Dissecting PARP inhibitor resistance with functional genomics." Current Opinion in Genetics & Development 54 (February 2019): 55–63. http://dx.doi.org/10.1016/j.gde.2019.03.001.

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39

Bennett, Christina. "Investigational PARP Inhibitor Talazoparib Shows Clinical Benefit." Oncology Times 40 (February 2018): 13. http://dx.doi.org/10.1097/01.cot.0000530521.16211.9b.

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40

Goodwin, Peter M. "PARP Inhibitor Success in Refractory Prostate Cancer." Oncology Times 41, no. 22 (2019): 30. http://dx.doi.org/10.1097/01.cot.0000615228.82343.17.

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41

red. "PARP-Inhibitor: Neue Option beim rezidivierten Ovarialkarzinom." Im Focus Onkologie 20, no. 6 (2017): 60. http://dx.doi.org/10.1007/s15015-017-3396-6.

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42

red. "PARP-Inhibitor unabhängig von BRCA-Mutationsstatus zugelassen." Im Focus Onkologie 20, no. 12 (2017): 77. http://dx.doi.org/10.1007/s15015-017-3725-9.

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43

Einecke, Dirk. "Rezidivierendes Ovarialkarzinom: Neuer PARP-Inhibitor verdreifacht PFS." Im Focus Onkologie 21, no. 4 (2018): 85. http://dx.doi.org/10.1007/s15015-018-3945-7.

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44

D’Andrea, Alan D. "Mechanisms of PARP inhibitor sensitivity and resistance." DNA Repair 71 (November 2018): 172–76. http://dx.doi.org/10.1016/j.dnarep.2018.08.021.

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45

OSANAI, Takayuki, Tsuyoshi NAKAGAWA, and Noriaki TAKIGUCHI. "PARP Inhibiter as a Treatment for Breast Cancer." Nihon Rinsho Geka Gakkai Zasshi (Journal of Japan Surgical Association) 80, no. 10 (2019): 1802–6. http://dx.doi.org/10.3919/jjsa.80.1802.

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46

Gomez, Miriam K., Giuditta Illuzzi, Carlota Colomer, et al. "Identifying and Overcoming Mechanisms of PARP Inhibitor Resistance in Homologous Recombination Repair-Deficient and Repair-Proficient High Grade Serous Ovarian Cancer Cells." Cancers 12, no. 6 (2020): 1503. http://dx.doi.org/10.3390/cancers12061503.

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High grade serous ovarian cancer (HGSOC) is a major cause of female cancer mortality. The approval of poly (ADP-ribose) polymerase (PARP) inhibitors for clinical use has greatly improved treatment options for patients with homologous recombination repair (HRR)-deficient HGSOC, although the development of PARP inhibitor resistance in some patients is revealing limitations to outcome. A proportion of patients with HRR-proficient cancers also benefit from PARP inhibitor therapy. Our aim is to compare mechanisms of resistance to the PARP inhibitor olaparib in these two main molecular categories of
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47

Gunderson, Camille C., and Kathleen N. Moore. "Olaparib: an oral PARP-1 and PARP-2 inhibitor with promising activity in ovarian cancer." Future Oncology 11, no. 5 (2015): 747–57. http://dx.doi.org/10.2217/fon.14.313.

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48

Li, Nan, Yifan Wang, Weiye Deng, and Steven H. Lin. "Poly (ADP-Ribose) Polymerases (PARPs) and PARP Inhibitor-Targeted Therapeutics." Anti-Cancer Agents in Medicinal Chemistry 19, no. 2 (2019): 206–12. http://dx.doi.org/10.2174/1871520618666181109164645.

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Background:Poly-ADP-ribosylation, that is, adding ADP-ribose moieties to a protein, is a unique type of protein post-translational modification that regulates various cellular processes such as DNA repair, mitosis, transcription, and cell growth. Small-molecule inhibitors of poly-ADP-ribose polymerase 1 (PARP1) have been developed as anticancer agents because inhibition of PARP enzymes may be a synthetic lethal strategy for cancers with or BRCA2 mutations. However, there are still questions surrounding PARP inhibitors.Methods/Results:Data were collected from Pubmed, Medline, through searching
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49

Gallyas, Ferenc, Balazs Sumegi, and Csaba Szabo. "Role of Akt Activation in PARP Inhibitor Resistance in Cancer." Cancers 12, no. 3 (2020): 532. http://dx.doi.org/10.3390/cancers12030532.

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Poly(ADP-ribose) polymerase (PARP) inhibitors have recently been introduced in the therapy of several types of cancers not responding to conventional treatments. However, de novo and acquired PARP inhibitor resistance is a significant limiting factor in the clinical therapy, and the underlying mechanisms are not fully understood. Activity of the cytoprotective phosphatidylinositol-3 kinase (PI3K)-Akt pathway is often increased in human cancer that could result from mutation, expressional change, or amplification of upstream growth-related factor signaling elements or elements of the Akt pathwa
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50

Curtin, Nicola J. "PARP inhibitors for cancer therapy." Expert Reviews in Molecular Medicine 7, no. 4 (2005): 1–20. http://dx.doi.org/10.1017/s146239940500904x.

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Poly(ADP-ribose) polymerase 1 (PARP-1) is a zinc-finger DNA-binding enzyme that is activated by binding to DNA breaks. Poly(ADP-ribosyl)ation of nuclear proteins by PARP-1 converts DNA damage into intracellular signals that activate either DNA repair by the base-excision pathway or cell death. A family of 18 PARPs has been identified, but only the most abundant, PARP-1 and PARP-2, which are both nuclear enzymes, are activated by DNA damage. PARP inhibitors of ever-increasing potency have been developed in the 40 years since the discovery of PARP-1, both as tools for the investigation of PARP-1
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