{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPARP2 is a critical DNA damage response enzyme that rapidly detects and binds to multiple types of DNA lesions. Upon encountering single‐ or double‐strand breaks, it is recruited via its WGR and other accessory domains and becomes catalytically active, synthesizing poly(ADP‐ribose) chains—often in conjunction with the accessory factor HPF1—to modify its substrates predominantly on serine residues. These post‐translational modifications promote local chromatin relaxation and facilitate the assembly of downstream repair complexes. Structural studies further reveal that PARP2 can bridge DNA ends, including within nucleosomal contexts, thereby helping to organize and process damaged chromatin."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its canonical role in direct damage sensing, PARP2 coordinates several aspects of DNA repair and replication fork stability. It collaborates with other repair factors—including PARP1 and the scaffold protein XRCC1—to modulate base excision repair and to support efficient processing of repair intermediates. PARP2 further contributes to the choice of repair pathway by limiting the accumulation of resection barrier factors such as 53BP1 at break sites, thereby promoting resection‐dependent processes. Its dynamic interactions and automodification properties help regulate the length and branching of poly(ADP‐ribose) chains, ultimately fine‐tuning repair complex assembly and disassembly at sites of DNA damage."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond direct DNA repair, PARP2 exerts important non‐canonical functions that impact transcriptional regulation, chromatin remodeling, and metabolic homeostasis. It interacts with key transcription factors—for example, facilitating androgen receptor recruitment in prostate cancer cells and modulating lung‐specific gene expression—to influence differentiation and cell‐type–specific gene programs. Moreover, PARP2 has been implicated in the regulation of hepatic cholesterol metabolism, in processes such as retrotransposition, and even in mitochondrial dynamics, while its own cellular levels are tightly controlled by serum factors and microRNAs. These diverse roles underscore the multifunctional nature of PARP2 in maintaining genomic stability and cellular homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Maria Malanga, Felix R Althaus "}, {"type": "b", "children": [{"type": "t", "text": "Poly(ADP-ribose) reactivates stalled DNA topoisomerase I and Induces DNA strand break resealing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.C300437200"}], "href": "https://doi.org/10.1074/jbc.C300437200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14699148"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14699148"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Tobias Karlberg, Martin Hammarström, Patrick Schütz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Crystal structure of the catalytic domain of human PARP2 in complex with PARP inhibitor ABT-888."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi902079y"}], "href": "https://doi.org/10.1021/bi902079y"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20092359"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20092359"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Amanda A Riccio, Gino Cingolani, John M Pascal "}, {"type": "b", "children": [{"type": "t", "text": "PARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damage."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkv1376"}], "href": "https://doi.org/10.1093/nar/gkv1376"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26704974"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26704974"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Hana Hanzlikova, William Gittens, Katerina Krejcikova, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Overlapping roles for PARP1 and PARP2 in the recruitment of endogenous XRCC1 and PNKP into oxidized chromatin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkw1246"}], "href": "https://doi.org/10.1093/nar/gkw1246"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27965414"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27965414"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Qian Chen, Muzaffer Ahmad Kassab, Françoise Dantzer, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PARP2 mediates branched poly ADP-ribosylation in response to DNA damage."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-018-05588-5"}], "href": "https://doi.org/10.1038/s41467-018-05588-5"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30104678"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30104678"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Marcin J Suskiewicz, Florian Zobel, Tom E H Ogden, et al. "}, {"type": "b", "children": [{"type": "t", "text": "HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41586-020-2013-6"}], "href": "https://doi.org/10.1038/s41586-020-2013-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32028527"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32028527"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Silvija Bilokapic, Marcin J Suskiewicz, Ivan Ahel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41586-020-2725-7"}], "href": "https://doi.org/10.1038/s41586-020-2725-7"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32939087"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32939087"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Guillaume Gaullier, Genevieve Roberts, Uma M Muthurajan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0240932"}], "href": "https://doi.org/10.1371/journal.pone.0240932"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33141820"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33141820"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Christopher A Koczor, Kate M Saville, Joel F Andrews, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Temporal dynamics of base excision/single-strand break repair protein complex assembly/disassembly are modulated by the PARP/NAD"}, {"type": "a", "children": [{"type": "t", "text": "sup"}], "href": "sup"}, {"type": "t", "text": "+"}, {"type": "a", "children": [{"type": "t", "text": "/sup"}], "href": "/sup"}, {"type": "t", "text": "/SIRT6 axis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Rep (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.celrep.2021.109917"}], "href": "https://doi.org/10.1016/j.celrep.2021.109917"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34731617"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34731617"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Rabeya Bilkis, Robert J Lake, Karen L Cooper, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The CSB chromatin remodeler regulates PARP1- and PARP2-mediated single-strand break repair at actively transcribed DNA regions."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkad515"}], "href": "https://doi.org/10.1093/nar/gkad515"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37326017"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37326017"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Delphine Quénet, Véronique Gasser, Laetitia Fouillen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The histone subcode: poly(ADP-ribose) polymerase-1 (Parp-1) and Parp-2 control cell differentiation by regulating the transcriptional intermediary factor TIF1beta and the heterochromatin protein HP1alpha."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FASEB J (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1096/fj.08-113464"}], "href": "https://doi.org/10.1096/fj.08-113464"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18676401"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18676401"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Mikhail M Kutuzov, Svetlana N Khodyreva, Ekaterina S Ilina, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Interaction of PARP-2 with AP site containing DNA."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochimie (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.biochi.2015.02.010"}], "href": "https://doi.org/10.1016/j.biochi.2015.02.010"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25724268"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25724268"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Jean-Philippe Gagné, Chantal Ethier, Daniel Defoy, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Quantitative site-specific ADP-ribosylation profiling of DNA-dependent PARPs."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "DNA Repair (Amst) (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.dnarep.2015.02.004"}], "href": "https://doi.org/10.1016/j.dnarep.2015.02.004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25800440"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25800440"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Sharon McGonigle, Zhihong Chen, Jiayi Wu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "E7449: A dual inhibitor of PARP1/2 and tankyrase1/2 inhibits growth of DNA repair deficient tumors and antagonizes Wnt signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.5846"}], "href": "https://doi.org/10.18632/oncotarget.5846"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26513298"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26513298"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Maria V Sukhanova, Sanae Abrakhi, Vandana Joshi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Single molecule detection of PARP1 and PARP2 interaction with DNA strand breaks and their poly(ADP-ribosyl)ation using high-resolution AFM imaging."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkv1476"}], "href": "https://doi.org/10.1093/nar/gkv1476"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26673720"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26673720"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Florian J Bock, Paul Chang "}, {"type": "b", "children": [{"type": "t", "text": "New directions in poly(ADP-ribose) polymerase biology."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS J (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/febs.13737"}], "href": "https://doi.org/10.1111/febs.13737"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27087568"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27087568"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Ezeogo Obaji, Teemu Haikarainen, Lari Lehtiö "}, {"type": "b", "children": [{"type": "t", "text": "Characterization of the DNA dependent activation of human ARTD2/PARP2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/srep34487"}], "href": "https://doi.org/10.1038/srep34487"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27708353"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27708353"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Ezeogo Obaji, Teemu Haikarainen, Lari Lehtiö "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis for DNA break recognition by ARTD2/PARP2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gky927"}], "href": "https://doi.org/10.1093/nar/gky927"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30321391"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30321391"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Maria V Sukhanova, Loic Hamon, Mikhail M Kutuzov, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A Single-Molecule Atomic Force Microscopy Study of PARP1 and PARP2 Recognition of Base Excision Repair DNA Intermediates."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jmb.2019.05.028"}], "href": "https://doi.org/10.1016/j.jmb.2019.05.028"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31129062"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31129062"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Tomoichiro Miyoshi, Takeshi Makino, John V Moran "}, {"type": "b", "children": [{"type": "t", "text": "Poly(ADP-Ribose) Polymerase 2 Recruits Replication Protein A to Sites of LINE-1 Integration to Facilitate Retrotransposition."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2019.07.018"}], "href": "https://doi.org/10.1016/j.molcel.2019.07.018"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31473101"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31473101"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Olga I Lavrik "}, {"type": "b", "children": [{"type": "t", "text": "PARPs' impact on base excision DNA repair."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "DNA Repair (Amst) (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.dnarep.2020.102911"}], "href": "https://doi.org/10.1016/j.dnarep.2020.102911"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33087277"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33087277"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Upendra Kumar Soni, Sangappa Basanna Chadchan, Rakesh Kumar Gupta, et al. "}, {"type": "b", "children": [{"type": "t", "text": "miRNA-149 targets PARP-2 in endometrial epithelial and stromal cells to regulate the trophoblast attachment process."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Hum Reprod (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/molehr/gaab039"}], "href": "https://doi.org/10.1093/molehr/gaab039"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34051087"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34051087"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Laura Jankó, Tünde Kovács, Miklós Laczik, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Silencing of Poly(ADP-Ribose) Polymerase-2 Induces Mitochondrial Reactive Species Production and Mitochondrial Fragmentation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cells (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/cells10061387"}], "href": "https://doi.org/10.3390/cells10061387"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34199944"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34199944"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Sandra S Haenni, Matthias Altmeyer, Paul O Hassa, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Importin alpha binding and nuclear localization of PARP-2 is dependent on lysine 36, which is located within a predicted classical NLS."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Cell Biol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/1471-2121-9-39"}], "href": "https://doi.org/10.1186/1471-2121-9-39"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18644123"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18644123"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Magdolna Szántó, Attila Brunyánszki, Judit Márton, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deletion of PARP-2 induces hepatic cholesterol accumulation and decrease in HDL levels."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbadis.2013.12.006"}], "href": "https://doi.org/10.1016/j.bbadis.2013.12.006"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24365238"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24365238"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Alexis Fouquin, Josée Guirouilh-Barbat, Bernard Lopez, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PARP2 controls double-strand break repair pathway choice by limiting 53BP1 accumulation at DNA damage sites and promoting end-resection."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkx881"}], "href": "https://doi.org/10.1093/nar/gkx881"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29036662"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29036662"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Qizhi Sun, Mohamed I Gatie, Gregory M Kelly "}, {"type": "b", "children": [{"type": "t", "text": "Serum-dependent and -independent regulation of PARP2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Cell Biol (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1139/bcb-2018-0345"}], "href": "https://doi.org/10.1139/bcb-2018-0345"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30880404"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30880404"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Bin Gui, Fu Gui, Tomoaki Takai, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Selective targeting of PARP-2 inhibits androgen receptor signaling and prostate cancer growth through disruption of FOXA1 function."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1908547116"}], "href": "https://doi.org/10.1073/pnas.1908547116"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31266892"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31266892"}]}, {"type": "r", "ref": 29, "children": [{"type": "t", "text": "Marcin J Suskiewicz, Luca Palazzo, Rebecca Hughes, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Progress and outlook in studying the substrate specificities of PARPs and related enzymes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS J (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/febs.15518"}], "href": "https://doi.org/10.1111/febs.15518"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32785980"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32785980"}]}, {"type": "r", "ref": 30, "children": [{"type": "t", "text": "Inna Vasil'eva, Nina Moor, Rashid Anarbaev, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Functional Roles of PARP2 in Assembling Protein-Protein Complexes Involved in Base Excision DNA Repair."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Mol Sci (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/ijms22094679"}], "href": "https://doi.org/10.3390/ijms22094679"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33925170"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33925170"}]}, {"type": "r", "ref": 31, "children": [{"type": "t", "text": "Lotte van Beek, Éilís McClay, Saleha Patel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Mol Sci (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/ijms22105112"}], "href": "https://doi.org/10.3390/ijms22105112"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34066057"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34066057"}]}, {"type": "r", "ref": 32, "children": [{"type": "t", "text": "Ezeogo Obaji, Mirko M Maksimainen, Albert Galera-Prat, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-021-23800-x"}], "href": "https://doi.org/10.1038/s41467-021-23800-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34108479"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34108479"}]}, {"type": "r", "ref": 33, "children": [{"type": "t", "text": "Evgeniia Prokhorova, Florian Zobel, Rebecca Smith, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Serine-linked PARP1 auto-modification controls PARP inhibitor response."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-021-24361-9"}], "href": "https://doi.org/10.1038/s41467-021-24361-9"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34210965"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34210965"}]}, {"type": "r", "ref": 34, "children": [{"type": "t", "text": "Nicholas A W Bell, Justin E Molloy "}, {"type": "b", "children": [{"type": "t", "text": "Single-molecule force spectroscopy reveals binding and bridging dynamics of PARP1 and PARP2 at DNA double-strand breaks."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.2214209120"}], "href": "https://doi.org/10.1073/pnas.2214209120"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37216533"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37216533"}]}]}]}