{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T09:55:10Z","timestamp":1791194110533,"version":"4.1.0"},"reference-count":88,"publisher":"Oxford University Press (OUP)","issue":"18","license":[{"start":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T00:00:00Z","timestamp":1791158400000},"content-version":"vor","delay-in-days":13,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R35GM154859"],"award-info":[{"award-number":["R35GM154859"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["S10OD03243701"],"award-info":[{"award-number":["S10OD03243701"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["UM1TR004528"],"award-info":[{"award-number":["UM1TR004528"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R35GM154859"],"award-info":[{"award-number":["R35GM154859"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100001229","name":"Mathers Foundation","doi-asserted-by":"publisher","award":["MF-2310-04968"],"award-info":[{"award-number":["MF-2310-04968"]}],"id":[{"id":"10.13039\/100001229","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000048","name":"American Cancer Society","doi-asserted-by":"publisher","award":["IRG-16-186-21"],"award-info":[{"award-number":["IRG-16-186-21"]}],"id":[{"id":"10.13039\/100000048","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,22]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Single-strand DNA breaks are among the most frequent forms of DNA damage, yet how PARP2 recognizes these lesions within the constrained geometry of chromatin remains unclear. Here we use cryogenic electron microscopy (cryo-EM) to determine structures of PARP2 and HPF1 bound to nucleosomes containing a site-specific single-strand break (SSB) at superhelical location + 5.3. The structures reveal a multivalent binding mode in which the Trp-Gly-Arg (WGR) domain engages the break while the helical domain and HPF1 contact the opposing DNA gyre, spanning both DNA gyres of the nucleosome. This configuration explains the higher affinity of PARP2 for nucleosomal SSBs relative to free DNA. 3D classification resolves multiple PARP2-bound states with distinct WGR orientations and DNA backbone distortions, revealing structural plasticity during damage recognition. Comparative analysis shows that HPF1 constrains the conformational ensemble of PARP2 and promotes a defined catalytic domain architecture compatible with histone PARylation. PARP inhibitors (olaparib, talazoparib, EB-47) stabilize WGR\u2013helical domain interfaces and make the ADP-ribosyltransferase\u2013HPF1 catalytic module dynamic, consistent with reverse allosteric retention on damaged chromatin, while also promoting asymmetric nucleosomal DNA unwrapping. Together, these structures provide a chromatin-context framework for understanding PARP2 recognition of nucleosomal DNA breaks and how PARPis reshape these interactions to promote PARP retention and local chromatin remodeling.<\/jats:p>","DOI":"10.1093\/nar\/gkag939","type":"journal-article","created":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T18:22:33Z","timestamp":1789755753000},"source":"Crossref","is-referenced-by-count":0,"title":["Structural basis of PARP2 recognition of nucleosomal DNA breaks and inhibitor trapping"],"prefix":"10.1093","volume":"54","author":[{"given":"Chathuni","family":"Jayathilake","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University , Cleveland 44106, OH ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emily R","family":"Gregory-Lott","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University , Cleveland 44106, OH ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajbinder K","family":"Virk","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University , Cleveland 44106, OH ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Grace K","family":"Koh","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University , Cleveland 44106, OH ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eun","family":"Cho","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University , Cleveland 44106, OH ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0344-6265","authenticated-orcid":false,"given":"Tae Hun","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University , Cleveland 44106, OH ,","place":["United States"]},{"name":"Case Comprehensive Cancer Center , Cleveland, OH, 44106 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2026,10,5]]},"reference":[{"key":"2026100505230553000_B1","doi-asserted-by":"publisher","first-page":"644","DOI":"10.1016\/j.cell.2017.01.002","article-title":"Endogenous DNA damage as a source of genomic instability in cancer","volume":"168","author":"Tubbs","year":"2017","journal-title":"Cell"},{"key":"2026100505230553000_B2","doi-asserted-by":"publisher","first-page":"709","DOI":"10.1038\/362709a0","article-title":"Instability and decay of the primary structure of DNA","volume":"362","author":"Lindahl","year":"1993","journal-title":"Nature"},{"key":"2026100505230553000_B3","doi-asserted-by":"publisher","first-page":"366","DOI":"10.1038\/35077232","article-title":"Genome maintenance mechanisms for preventing cancer","volume":"411","author":"Hoeijmakers","year":"2001","journal-title":"Nature"},{"key":"2026100505230553000_B4","doi-asserted-by":"publisher","first-page":"101084","DOI":"10.1016\/j.redox.2018.101084","article-title":"ROS and the DNA damage response in cancer","volume":"25","author":"Srinivas","year":"2019","journal-title":"Redox Biol"},{"key":"2026100505230553000_B5","doi-asserted-by":"publisher","first-page":"733","DOI":"10.1016\/j.tcb.2022.04.010","article-title":"DNA single-strand break repair and human genetic disease","volume":"32","author":"Caldecott","year":"2022","journal-title":"Trends Cell Biol"},{"key":"2026100505230553000_B6","doi-asserted-by":"publisher","first-page":"619","DOI":"10.1038\/nrg2380","article-title":"Single-strand break repair and genetic disease","volume":"9","author":"Caldecott","year":"2008","journal-title":"Nat Rev Genet"},{"key":"2026100505230553000_B7","doi-asserted-by":"publisher","first-page":"3483","DOI":"10.1093\/nar\/gkt076","article-title":"Mammalian base excision repair: the forgotten Archangel","volume":"41","author":"Dianov","year":"2013","journal-title":"Nucleic Acids Res"},{"key":"2026100505230553000_B8","doi-asserted-by":"publisher","first-page":"EMBR201846263","DOI":"10.15252\/embr.201846263","article-title":"Mechanisms for stalled replication fork stabilization: new targets for synthetic lethality strategies in cancer treatments","volume":"19","author":"Liao","year":"2018","journal-title":"EMBO Rep"},{"key":"2026100505230553000_B9","doi-asserted-by":"publisher","first-page":"a012583","DOI":"10.1101\/cshperspect.a012583","article-title":"Base excision repair","volume":"5","author":"Krokan","year":"2013","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"2026100505230553000_B10","doi-asserted-by":"publisher","first-page":"4720","DOI":"10.1038\/sj.emboj.7601869","article-title":"TDP1 facilitates chromosomal single-strand break repair in neurons and is neuroprotective in vivo","volume":"26","author":"Katyal","year":"2007","journal-title":"EMBO J"},{"key":"2026100505230553000_B11","doi-asserted-by":"publisher","first-page":"1189","DOI":"10.1038\/nsmb.2146","article-title":"Structure of an aprataxin\u2013DNA complex with insights into AOA1 neurodegenerative disease","volume":"18","author":"Tumbale","year":"2011","journal-title":"Nat Struct Mol Biol"},{"key":"2026100505230553000_B12","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1016\/j.yexcr.2014.08.027","article-title":"DNA single-strand break repair","volume":"329","author":"Caldecott","year":"2014","journal-title":"Exp Cell Res"},{"key":"2026100505230553000_B13","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1016\/j.dnarep.2014.03.020","article-title":"Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2)","volume":"19","author":"Pommier","year":"2014","journal-title":"DNA Repair"},{"key":"2026100505230553000_B14","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1016\/j.tibs.2011.01.006","article-title":"Tidying up loose ends: the role of polynucleotide kinase\/phosphatase in DNA strand break repair","volume":"36","author":"Weinfeld","year":"2011","journal-title":"Trends Biochem Sci"},{"key":"2026100505230553000_B15","doi-asserted-by":"publisher","first-page":"108","DOI":"10.1016\/j.dnarep.2014.03.021","article-title":"Protein ADP-ribosylation and the cellular response to DNA strand breaks","volume":"19","author":"Caldecott","year":"2014","journal-title":"DNA Repair"},{"key":"2026100505230553000_B16","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1016\/j.dnarep.2015.04.008","article-title":"The rise and fall of poly(ADP-ribose): an enzymatic perspective","volume":"32","author":"Pascal","year":"2015","journal-title":"DNA Repair"},{"key":"2026100505230553000_B17","doi-asserted-by":"publisher","first-page":"7762","DOI":"10.1093\/nar\/gku474","article-title":"PARP-2 and PARP-3 are selectively activated by 5\u2019 phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1","volume":"42","author":"Langelier","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"2026100505230553000_B18","doi-asserted-by":"publisher","first-page":"609","DOI":"10.1038\/s41586-020-2725-7","article-title":"Bridging of DNA breaks activates PARP2\u2013HPF1 to modify chromatin","volume":"585","author":"Bilokapic","year":"2020","journal-title":"Nature"},{"key":"2026100505230553000_B19","doi-asserted-by":"publisher","first-page":"308","DOI":"10.1186\/1471-2148-10-308","article-title":"Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes","volume":"10","author":"Citarelli","year":"2010","journal-title":"BMC Evol Biol"},{"key":"2026100505230553000_B20","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1016\/j.dnarep.2014.05.003","article-title":"Distribution of protein poly(ADP-ribosyl)ation systems across all domains of life","volume":"23","author":"Perina","year":"2014","journal-title":"DNA Repair"},{"key":"2026100505230553000_B21","doi-asserted-by":"crossref","first-page":"2255","DOI":"10.1093\/emboj\/cdg206","article-title":"Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse","volume":"22","author":"M\u00e9nissier\u00a0de\u00a0Murcia","year":"2003","journal-title":"EMBO J"},{"key":"2026100505230553000_B22","doi-asserted-by":"publisher","first-page":"23028","DOI":"10.1074\/jbc.M202390200","article-title":"Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1","volume":"277","author":"Schreiber","year":"2002","journal-title":"J Biol Chem"},{"key":"2026100505230553000_B23","doi-asserted-by":"publisher","first-page":"e1005200","DOI":"10.1371\/journal.pgen.1005200","article-title":"PARP2 Is the predominant poly(ADP-Ribose) polymerase in Arabidopsis DNA damage and immune responses","volume":"11","author":"Song","year":"2015","journal-title":"PLoS Genet"},{"key":"2026100505230553000_B24","doi-asserted-by":"publisher","first-page":"1638","DOI":"10.3390\/ijms20071638","article-title":"Poly(ADP-Ribose) polymerases in plants and their Human counterparts: parallels and peculiarities","volume":"20","author":"Rissel","year":"2019","journal-title":"Int J Mol Sci"},{"key":"2026100505230553000_B25","doi-asserted-by":"publisher","first-page":"2783","DOI":"10.1073\/pnas.1016574108","article-title":"Poly(ADP-ribose) polymerase 3 (PARP3), a newcomer in cellular response to DNA damage and mitotic progression","volume":"108","author":"Boehler","year":"2011","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026100505230553000_B26","doi-asserted-by":"publisher","first-page":"5616","DOI":"10.1093\/nar\/gku174","article-title":"PARP3 affects the relative contribution of homologous recombination and nonhomologous end-joining pathways","volume":"42","author":"Beck","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"2026100505230553000_B27","doi-asserted-by":"publisher","first-page":"12404","DOI":"10.1038\/ncomms12404","article-title":"PARP3 is a sensor of nicked nucleosomes and monoribosylates histone H2BGlu2","volume":"7","author":"Grundy","year":"2016","journal-title":"Nat Commun"},{"key":"2026100505230553000_B28","doi-asserted-by":"crossref","first-page":"5112","DOI":"10.3390\/ijms22105112","article-title":"PARP power: a structural perspective on PARP1, PARP2, and PARP3 in DNA damage repair and nucleosome remodelling","volume":"22","author":"van\u00a0Beek","year":"2021","journal-title":"Int J Mol Sci"},{"key":"2026100505230553000_B29","doi-asserted-by":"publisher","first-page":"e2121979119","DOI":"10.1073\/pnas.2121979119","article-title":"Inhibitors of PARP: number crunching and structure gazing","volume":"119","author":"Rudolph","year":"2022","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026100505230553000_B30","doi-asserted-by":"publisher","first-page":"8217","DOI":"10.1093\/nar\/gkad514","article-title":"Updated protein domain annotation of the PARP protein family sheds new light on biological function","volume":"51","author":"Suskiewicz","year":"2023","journal-title":"Nucleic Acids Res"},{"key":"2026100505230553000_B31","doi-asserted-by":"publisher","first-page":"1259","DOI":"10.1038\/s42003-021-02780-0","article-title":"Dual function of HPF1 in the modulation of PARP1 and PARP2 activities","volume":"4","author":"Kurgina","year":"2021","journal-title":"Commun Biol"},{"key":"2026100505230553000_B32","doi-asserted-by":"publisher","first-page":"432","DOI":"10.1016\/j.molcel.2016.03.008","article-title":"HPF1\/C4orf27 Is a PARP-1-interacting protein that regulates PARP-1 ADP-ribosylation activity","volume":"62","author":"Gibbs-Seymour","year":"2016","journal-title":"Mol Cell"},{"key":"2026100505230553000_B33","doi-asserted-by":"publisher","first-page":"932","DOI":"10.1016\/j.molcel.2017.01.003","article-title":"Serine ADP-ribosylation depends on HPF1","volume":"65","author":"Bonfiglio","year":"2017","journal-title":"Mol Cell"},{"key":"2026100505230553000_B34","doi-asserted-by":"publisher","first-page":"1028","DOI":"10.1038\/s41467-021-21302-4","article-title":"HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones","volume":"12","author":"Sun","year":"2021","journal-title":"Nat Commun"},{"key":"2026100505230553000_B35","doi-asserted-by":"publisher","first-page":"598","DOI":"10.1038\/s41586-020-2013-6","article-title":"HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation","volume":"579","author":"Suskiewicz","year":"2020","journal-title":"Nature"},{"key":"2026100505230553000_B36","doi-asserted-by":"publisher","first-page":"917","DOI":"10.1038\/nature03445","article-title":"Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy","volume":"434","author":"Farmer","year":"2005","journal-title":"Nature"},{"key":"2026100505230553000_B37","doi-asserted-by":"publisher","first-page":"913","DOI":"10.1038\/nature03443","article-title":"Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase","volume":"434","author":"Bryant","year":"2005","journal-title":"Nature"},{"key":"2026100505230553000_B38","doi-asserted-by":"publisher","first-page":"1152","DOI":"10.1126\/science.aam7344","article-title":"PARP inhibitors: synthetic lethality in the clinic","volume":"355","author":"Lord","year":"2017","journal-title":"Science"},{"key":"2026100505230553000_B39","first-page":"2091","article-title":"Olaparib for metastatic castration-resistant prostate cancer","volume-title":"New Engl J Med","author":"Bono","year":"2020"},{"key":"2026100505230553000_B40","first-page":"317","article-title":"Maintenance olaparib for germline BRCA-mutated metastatic pancreatic cancer","volume-title":"New Engl J Med","author":"Golan","year":"2019"},{"key":"2026100505230553000_B41","first-page":"523","article-title":"Olaparib for metastatic breast cancer in patients with a germline BRCA mutation","volume-title":"New Engl J Med","author":"Robson","year":"2017"},{"key":"2026100505230553000_B42","first-page":"1382","article-title":"Olaparib maintenance therapy in platinum-sensitive relapsed ovarian cancer","volume-title":"New Engl J Med","author":"Ledermann","year":"2012"},{"key":"2026100505230553000_B43","doi-asserted-by":"publisher","first-page":"1802","DOI":"10.1001\/jamaoncol.2022.5074","article-title":"Concurrent olaparib and radiotherapy in patients with triple-negative breast cancer: the phase 1 olaparib and radiation therapy for triple-negative breast cancer trial","volume":"8","author":"Loap","year":"2022","journal-title":"JAMA Oncol"},{"key":"2026100505230553000_B44","doi-asserted-by":"publisher","first-page":"5380","DOI":"10.3390\/cancers13215380","article-title":"PARP inhibitors in combination with radiotherapy: to do or not to do?","volume":"13","author":"Barcellini","year":"2021","journal-title":"Cancers"},{"key":"2026100505230553000_B45","doi-asserted-by":"publisher","first-page":"1372","DOI":"10.1158\/2159-8290.CD-19-0582","article-title":"Combination olaparib and temozolomide in relapsed small-cell lung cancer","volume":"9","author":"Farago","year":"2019","journal-title":"Cancer Discov"},{"key":"2026100505230553000_B46","doi-asserted-by":"publisher","first-page":"1371","DOI":"10.1016\/j.ijrobp.2024.01.011","article-title":"Concurrent olaparib and radiation therapy in older patients with newly diagnosed glioblastoma: the phase 1 dose-escalation PARADIGM trial","volume":"118","author":"Derby","year":"2024","journal-title":"Int J Radiat Oncol Biol Physics"},{"key":"2026100505230553000_B47","doi-asserted-by":"publisher","first-page":"100698","DOI":"10.1016\/j.ctro.2023.100698","article-title":"Phase I feasibility study of olaparib in combination with loco-regional radiotherapy in head and neck squamous cell carcinoma","volume":"44","author":"Navran","year":"2024","journal-title":"Clin Transl Radiat Oncol"},{"key":"2026100505230553000_B48","doi-asserted-by":"publisher","first-page":"1212","DOI":"10.1158\/1078-0432.CCR-24-2974","article-title":"Olaparib, temozolomide, and concomitant radiotherapy for partially resected or biopsy-only glioblastoma first-line treatment: results from the OLA-TMZ-RTE-01 phase I study","volume":"31","author":"Stefan","year":"2025","journal-title":"Clin Cancer Res"},{"key":"2026100505230553000_B49","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.3390\/cells13121058","article-title":"Potential benefits of combining proton or carbon ion therapy with DNA damage repair inhibitors","volume":"13","author":"R\u00f8dland","year":"2024","journal-title":"Cells"},{"key":"2026100505230553000_B50","doi-asserted-by":"publisher","first-page":"728","DOI":"10.1126\/science.1216338","article-title":"Structural basis for DNA damage\u2013dependent poly(ADP-ribosyl)ation by Human PARP-1","volume":"336","author":"Langelier","year":"2012","journal-title":"Science"},{"key":"2026100505230553000_B51","doi-asserted-by":"publisher","first-page":"2266","DOI":"10.1093\/nar\/gkab020","article-title":"Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition","volume":"49","author":"Ogden","year":"2021","journal-title":"Nucleic Acids Res"},{"key":"2026100505230553000_B52","doi-asserted-by":"publisher","first-page":"742","DOI":"10.1016\/j.molcel.2015.10.032","article-title":"Structural basis of detection and signaling of DNA single-strand breaks by Human PARP-1","volume":"60","author":"Eustermann","year":"2015","journal-title":"Mol Cell"},{"key":"2026100505230553000_B53","doi-asserted-by":"publisher","first-page":"755","DOI":"10.1016\/j.molcel.2015.10.013","article-title":"PARP-1 activation requires local unfolding of an autoinhibitory domain","volume":"60","author":"Dawicki-McKenna","year":"2015","journal-title":"Mol Cell"},{"key":"2026100505230553000_B54","doi-asserted-by":"publisher","first-page":"2825","DOI":"10.1038\/s41467-026-69375-3","article-title":"PARP1-HPF1 structure and dynamics on nicked DNA suggest a mechanism for acute and localized ADP-ribosylation","volume":"17","author":"Sverzhinsky","year":"2026","journal-title":"Nat Commun"},{"key":"2026100505230553000_B55","doi-asserted-by":"publisher","first-page":"12154","DOI":"10.1093\/nar\/gky927","article-title":"Structural basis for DNA break recognition by ARTD2\/PARP2","volume":"46","author":"Obaji","year":"2018","journal-title":"Nucleic Acids Res"},{"key":"2026100505230553000_B56","doi-asserted-by":"publisher","first-page":"3479","DOI":"10.1038\/s41467-021-23800-x","article-title":"Activation of PARP2\/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition","volume":"12","author":"Obaji","year":"2021","journal-title":"Nat Commun"},{"key":"2026100505230553000_B57","doi-asserted-by":"publisher","first-page":"e0240932","DOI":"10.1371\/journal.pone.0240932","article-title":"Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1","volume":"15","author":"Gaullier","year":"2020","journal-title":"PLoS One"},{"key":"2026100505230553000_B58","doi-asserted-by":"publisher","first-page":"865","DOI":"10.1016\/j.molcel.2025.01.004","article-title":"A PARP2 active site helix melts to permit DNA damage-induced enzymatic activation","volume":"85","author":"Smith-Pillet","year":"2025","journal-title":"Mol Cell"},{"key":"2026100505230553000_B59","doi-asserted-by":"publisher","first-page":"169753","DOI":"10.1016\/j.jmb.2026.169753","article-title":"High-yield production of modified DNA enables structural analysis of PARP2 recognition of nucleosomal single-strand breaks","volume":"438","author":"Jayathilake","year":"2026","journal-title":"J Mol Biol"},{"key":"2026100505230553000_B60","doi-asserted-by":"publisher","first-page":"e2301063120","DOI":"10.1073\/pnas.2301063120","article-title":"Correlating histone acetylation with nucleosome core particle dynamics and function","volume":"120","author":"Kim","year":"2023","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026100505230553000_B61","doi-asserted-by":"crossref","first-page":"100396","DOI":"10.1016\/j.xpro.2021.100396","article-title":"Preparation of scFv stabilized chromatosomes for single-particle cryo-EM structure determination","volume":"2","author":"Zhou","year":"2021","journal-title":"STAR Protoc"},{"key":"2026100505230553000_B62","doi-asserted-by":"publisher","first-page":"290","DOI":"10.1038\/nmeth.4169","article-title":"CryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination","volume":"14","author":"Punjani","year":"2017","journal-title":"Nat Methods"},{"key":"2026100505230553000_B63","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate structure prediction of biomolecular interactions with AlphaFold 3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"2026100505230553000_B64","doi-asserted-by":"publisher","first-page":"166","DOI":"10.1016\/j.molcel.2020.10.038","article-title":"Distinct structures and dynamics of chromatosomes with different Human linker histone isoforms","volume":"81","author":"Zhou","year":"2021","journal-title":"Mol Cell"},{"key":"2026100505230553000_B65","doi-asserted-by":"publisher","first-page":"e4792","DOI":"10.1002\/pro.4792","article-title":"UCSF ChimeraX: tools for structure building and analysis","volume":"32","author":"Meng","year":"2023","journal-title":"Protein Sci"},{"key":"2026100505230553000_B66","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1107\/S2059798318002425","article-title":"ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps","volume":"74","author":"Croll","year":"2018","journal-title":"Acta Crystallogr D Struct Biol"},{"key":"2026100505230553000_B67","first-page":"2126","article-title":"Coot: model-building tools for molecular graphics","volume-title":"Acta Crystallogr D Struct Biol","author":"Emsley","year":"2004"},{"key":"2026100505230553000_B68","first-page":"531","article-title":"Real-space refinement in PHENIX for cryo-EM and crystallography","volume-title":"Acta Crystallogr DStruct Biol","author":"Afonine","year":"2018"},{"key":"2026100505230553000_B69","doi-asserted-by":"publisher","first-page":"34487","DOI":"10.1038\/srep34487","article-title":"Characterization of the DNA dependent activation of human ARTD2\/PARP2","volume":"6","author":"Obaji","year":"2016","journal-title":"Sci Rep"},{"key":"2026100505230553000_B70","doi-asserted-by":"publisher","first-page":"1691","DOI":"10.1093\/nar\/gkv1376","article-title":"PARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damage","volume":"44","author":"Riccio","year":"2016","journal-title":"Nucleic Acids Res"},{"key":"2026100505230553000_B71","doi-asserted-by":"publisher","first-page":"429","DOI":"10.1016\/j.molcel.2023.12.019","article-title":"Poly(ADP-ribosyl)ation enhances nucleosome dynamics and organizes DNA damage repair components within biomolecular condensates","volume":"84","author":"Nosella","year":"2024","journal-title":"Mol Cell"},{"key":"2026100505230553000_B72","first-page":"1","article-title":"Atomic resolution cryo-EM structure of a native-like CENP-A nucleosome aided by an antibody fragment","volume":"10","author":"Zhou","year":"2019","journal-title":"Nat Commun"},{"key":"2026100505230553000_B73","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1038\/s41594-017-0005-5","article-title":"Histone octamer rearranges to adapt to DNA unwrapping","volume":"25","author":"Bilokapic","year":"2018","journal-title":"Nat Struct Mol Biol"},{"key":"2026100505230553000_B74","doi-asserted-by":"publisher","first-page":"eadf7175","DOI":"10.1126\/sciadv.adf7175","article-title":"Clinical PARP inhibitors allosterically induce PARP2 retention on DNA","volume":"9","author":"Langelier","year":"2024","journal-title":"Sci Adv"},{"key":"2026100505230553000_B75","doi-asserted-by":"publisher","first-page":"3958","DOI":"10.1093\/nar\/gkac188","article-title":"PARP inhibitors trap PARP2 and alter the mode of recruitment of PARP2 at DNA damage sites","volume":"50","author":"Lin","year":"2022","journal-title":"Nucleic Acids Res"},{"key":"2026100505230553000_B76","first-page":"1842","article-title":"Understanding specific functions of PARP-2: new lessons for cancer therapy","volume":"6","author":"Ali","year":"2016","journal-title":"Am J Cancer Res"},{"key":"2026100505230553000_B77","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1002\/bies.20085","article-title":"The PARP superfamily","volume":"26","author":"Am\u00e9","year":"2004","journal-title":"Bioessays"},{"key":"2026100505230553000_B78","doi-asserted-by":"crossref","first-page":"17860","DOI":"10.1074\/jbc.274.25.17860","article-title":"PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase*","volume":"274","author":"Am\u00e9","year":"1999","journal-title":"J Biol Chem"},{"key":"2026100505230553000_B79","doi-asserted-by":"publisher","first-page":"228","DOI":"10.1182\/blood.2021012805","article-title":"Distinct roles for PARP-1 and PARP-2 in c-Myc\u2013driven B-cell lymphoma in mice","volume":"139","author":"Galindo-Campos","year":"2022","journal-title":"Blood"},{"key":"2026100505230553000_B80","doi-asserted-by":"publisher","first-page":"3233","DOI":"10.1038\/s41467-018-05588-5","article-title":"PARP2 mediates branched poly ADP-ribosylation in response to DNA damage","volume":"9","author":"Chen","year":"2018","journal-title":"Nat Commun"},{"key":"2026100505230553000_B81","doi-asserted-by":"publisher","first-page":"844","DOI":"10.1038\/s41467-018-03234-8","article-title":"NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains","volume":"9","author":"Langelier","year":"2018","journal-title":"Nat Commun"},{"key":"2026100505230553000_B82","doi-asserted-by":"publisher","first-page":"eaax6367","DOI":"10.1126\/science.aax6367","article-title":"Structural basis for allosteric PARP-1 retention on DNA breaks","volume":"368","author":"Zandarashvili","year":"2020","journal-title":"Science"},{"key":"2026100505230553000_B83","doi-asserted-by":"publisher","first-page":"384","DOI":"10.1038\/s41467-025-67071-2","article-title":"Nucleosome unwrapping and PARP1 allostery drive affinities for chromatin and DNA breaks","volume":"17","author":"Schaich","year":"2025","journal-title":"Nat Commun"},{"key":"2026100505230553000_B84","doi-asserted-by":"publisher","first-page":"105779","DOI":"10.1016\/j.isci.2022.105779","article-title":"Dynamics of endogenous PARP1 and PARP2 during DNA damage revealed by live-cell single-molecule imaging","volume":"26","author":"Mahadevan","year":"2023","journal-title":"iScience"},{"key":"2026100505230553000_B85","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1038\/nsmb801","article-title":"Nucleosomes facilitate their own invasion","volume":"11","author":"Li","year":"2004","journal-title":"Nat Struct Mol Biol"},{"key":"2026100505230553000_B86","doi-asserted-by":"publisher","first-page":"772","DOI":"10.1016\/j.jmb.2008.04.025","article-title":"Spontaneous access to DNA target sites in folded chromatin fibers","volume":"379","author":"Poirier","year":"2008","journal-title":"J Mol Biol"},{"key":"2026100505230553000_B87","doi-asserted-by":"publisher","first-page":"46","DOI":"10.1038\/nsmb869","article-title":"Rapid spontaneous accessibility of nucleosomal DNA","volume":"12","author":"Li","year":"2005","journal-title":"Nat Struct Mol Biol"},{"key":"2026100505230553000_B88","doi-asserted-by":"publisher","first-page":"3123","DOI":"10.1038\/sj.emboj.7601196","article-title":"Rapid accessibility of nucleosomal DNA in yeast on a second time scale","volume":"25","author":"Bucceri","year":"2006","journal-title":"EMBO J"}],"container-title":["Nucleic Acids Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/nar\/article-pdf\/54\/18\/gkag939\/71595458\/gkag939.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/nar\/article-pdf\/54\/18\/gkag939\/71595458\/gkag939.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T09:23:17Z","timestamp":1791192197000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/nar\/article\/doi\/10.1093\/nar\/gkag939\/8863817"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,22]]},"references-count":88,"journal-issue":{"issue":"18","published-print":{"date-parts":[[2026,9,22]]}},"URL":"https:\/\/doi.org\/10.1093\/nar\/gkag939","relation":{},"ISSN":["0305-1048","1362-4962"],"issn-type":[{"value":"0305-1048","type":"print"},{"value":"1362-4962","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2026,10,14]]},"published":{"date-parts":[[2026,9,22]]},"article-number":"gkag939"}}