{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T16:24:27Z","timestamp":1787243067750,"version":"build-2736575974"},"reference-count":51,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007129","name":"Shandong Province Natural Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100007129","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell Chemical Biology"],"published-print":{"date-parts":[[2026,8]]},"DOI":"10.1016\/j.chembiol.2026.06.011","type":"journal-article","created":{"date-parts":[[2026,7,20]],"date-time":"2026-07-20T15:10:50Z","timestamp":1784560250000},"page":"1165-1178.e5","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Aptamer targeting HMGB1 attenuates inflammatory disease via domain-specific antagonism"],"prefix":"10.1016","volume":"33","author":[{"given":"Hui","family":"Zhang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lele","family":"Ma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shaoju","family":"Gan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mengyuan","family":"Jiang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zheng","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weidi","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wanlin","family":"Xie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peiyu","family":"Xi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fengli","family":"Qu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weihong","family":"Tan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.chembiol.2026.06.011_bib1","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1126\/science.285.5425.248","article-title":"HMG-1 as a late mediator of endotoxin lethality in mice","volume":"285","author":"Wang","year":"1999","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.06.011_bib2","doi-asserted-by":"crossref","DOI":"10.1002\/iid3.1124","article-title":"High-mobility group box 1 emerges as a therapeutic target for asthma","volume":"11","author":"Yang","year":"2023","journal-title":"Immun. Inflamm. Dis."},{"key":"10.1016\/j.chembiol.2026.06.011_bib3","doi-asserted-by":"crossref","first-page":"1959","DOI":"10.1128\/MCB.01862-08","article-title":"Chromatin-Specific Remodeling by HMGB1 and Linker Histone H1 Silences Proinflammatory Genes during Endotoxin Tolerance","volume":"29","author":"Gazzar","year":"2023","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib4","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1038\/s41577-023-00894-6","article-title":"The multifunctional protein HMGB1: 50 years of discovery","volume":"23","author":"Tang","year":"2023","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib5","doi-asserted-by":"crossref","first-page":"5551","DOI":"10.1093\/emboj\/cdg516","article-title":"Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion","volume":"22","author":"Bonaldi","year":"2003","journal-title":"EMBO J."},{"key":"10.1016\/j.chembiol.2026.06.011_bib6","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1038\/s12276-022-00736-w","article-title":"The mechanism of HMGB1 secretion and release","volume":"54","author":"Chen","year":"2022","journal-title":"Exp. Mol. Med."},{"key":"10.1016\/j.chembiol.2026.06.011_bib7","doi-asserted-by":"crossref","first-page":"5800","DOI":"10.4049\/jimmunol.0801873","article-title":"HMGB1 Is Phosphorylated by Classical Protein Kinase C and Is Secreted by a Calcium-Dependent Mechanism","volume":"182","author":"Oh","year":"2009","journal-title":"J. Immunol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib8","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1097\/01.shk.0000225404.51320.82","article-title":"HMGB1 signals through toll-like receptor (TLR) 4 and TLR2","volume":"26","author":"Yu","year":"2006","journal-title":"Shock"},{"key":"10.1016\/j.chembiol.2026.06.011_bib9","doi-asserted-by":"crossref","first-page":"2652","DOI":"10.1182\/blood-2002-05-1300","article-title":"Inflammation-promoting activity of HMGB1 on human microvascular endothelial cells","volume":"101","author":"Fiuza","year":"2003","journal-title":"Blood"},{"key":"10.1016\/j.chembiol.2026.06.011_bib10","doi-asserted-by":"crossref","DOI":"10.1186\/cc6184","article-title":"Inhibition of the RAGE products increases survival in experimental models of severe sepsis and systemic infection","volume":"11","author":"Lutterloh","year":"2007","journal-title":"Crit. Care"},{"key":"10.1016\/j.chembiol.2026.06.011_bib11","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1182\/blood.V122.21.8.8","article-title":"HMGB1 Is a Key Modulator Of Stress Erythropoiesis During Sepsis","volume":"122","author":"Vald\u00e9s-Ferrer","year":"2013","journal-title":"Blood"},{"key":"10.1016\/j.chembiol.2026.06.011_bib12","doi-asserted-by":"crossref","first-page":"1158","DOI":"10.1002\/hep.31324","article-title":"Disulfide High-Mobility Group Box 1 Drives Ischemia-Reperfusion Injury in Human Liver Transplantation","volume":"73","author":"Sosa","year":"2021","journal-title":"Hepatology"},{"key":"10.1016\/j.chembiol.2026.06.011_bib13","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1038\/nrrheum.2011.222","article-title":"HMGB1: A multifunctional alarmin driving autoimmune and inflammatory disease","volume":"8","author":"Harris","year":"2012","journal-title":"Nat. Rev. Rheumatol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib14","doi-asserted-by":"crossref","DOI":"10.3390\/pharmaceutics13122014","article-title":"Current and Emerging Strategies for Enhancing Antibody Delivery to the Brain","volume":"13","author":"Bajracharya","year":"2021","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.chembiol.2026.06.011_bib15","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1146\/annurev-immunol-030409-101323","article-title":"HMGB1 Is a Therapeutic Target for Sterile Inflammation and Infection","volume":"29","author":"Andersson","year":"2011","journal-title":"Annu. Rev. Immunol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib16","doi-asserted-by":"crossref","first-page":"11942","DOI":"10.1073\/pnas.1003893107","article-title":"A critical cysteine is required for HMGB1 binding to Toll-like receptor 4 and activation of macrophage cytokine release","volume":"107","author":"Yang","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.06.011_bib17","doi-asserted-by":"crossref","first-page":"5299","DOI":"10.1038\/onc.2010.261","article-title":"HMGB1 release and redox regulates autophagy and apoptosis in cancer cells","volume":"29","author":"Tang","year":"2010","journal-title":"Oncogene"},{"key":"10.1016\/j.chembiol.2026.06.011_bib18","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/j.chembiol.2007.03.007","article-title":"Glycyrrhizin binds to high-mobility group box 1 protein and inhibits its cytokine activities","volume":"14","author":"Mollica","year":"2007","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib19","doi-asserted-by":"crossref","first-page":"1628","DOI":"10.1093\/clinchem\/45.9.1628","article-title":"Aptamers: An emerging class of molecules that rival antibodies in diagnostics","volume":"45","author":"Jayasena","year":"1999","journal-title":"Clin. Chem."},{"key":"10.1016\/j.chembiol.2026.06.011_bib20","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1038\/nprot.2010.66","article-title":"Development of DNA aptamers using Cell-SELEX","volume":"5","author":"Sefah","year":"2010","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.chembiol.2026.06.011_bib21","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/j.chembiol.2022.01.009","article-title":"Generation of an anticoagulant aptamer that targets factor V\/Va and disrupts the FVa-membrane interaction in normal and COVID-19 patient samples","volume":"29","author":"Soule","year":"2022","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib22","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.addr.2018.04.007","article-title":"Aptamer chemistry","volume":"134","author":"R\u00f6thlisberger","year":"2018","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.chembiol.2026.06.011_bib23","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1016\/j.addr.2010.03.003","article-title":"Molecular diagnostic and drug delivery agents based on aptamer-nanomaterial conjugates","volume":"62","author":"Lee","year":"2010","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.chembiol.2026.06.011_bib24","doi-asserted-by":"crossref","DOI":"10.1038\/s41570-017-0076","article-title":"Analysis of aptamer discovery and technology","volume":"1","author":"Dunn","year":"2017","journal-title":"Nat. Rev. Chem"},{"key":"10.1016\/j.chembiol.2026.06.011_bib25","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1007\/BF03402105","article-title":"Structural basis for the proinflammatory cytokine activity of high mobility group box 1","volume":"9","author":"Li","year":"2003","journal-title":"Mol. Med."},{"key":"10.1016\/j.chembiol.2026.06.011_bib26","doi-asserted-by":"crossref","first-page":"1235","DOI":"10.3390\/pathogens10101235","article-title":"Targeting Inflammation Driven by HMGB1 in Bacterial Keratitis-A Review","volume":"10","author":"Hazlett","year":"2021","journal-title":"Pathogens"},{"key":"10.1016\/j.chembiol.2026.06.011_bib27","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1038\/s41592-020-0848-2","article-title":"Macromolecular modeling and design in Rosetta: recent methods and frameworks","volume":"17","author":"Leman","year":"2020","journal-title":"Nat. Methods"},{"key":"10.1016\/j.chembiol.2026.06.011_bib28","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1016\/j.molcel.2018.03.008","article-title":"Cracking the DNA Code for V(D)J Recombination","volume":"70","author":"Kim","year":"2018","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.06.011_bib29","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1038\/s41419-021-03652-5","article-title":"A small molecule binding HMGB1 inhibits caspase-11-mediated lethality in sepsis","volume":"12","author":"Wang","year":"2021","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.chembiol.2026.06.011_bib30","doi-asserted-by":"crossref","first-page":"35699","DOI":"10.1074\/jbc.M007167200","article-title":"A Role of Basic Residues and the Putative Intercalating Phenylalanine of the HMG-1 Box B in DNA Supercoiling and Binding to Four-way DNA Junctions","volume":"275","author":"\u0160tros","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.06.011_bib31","doi-asserted-by":"crossref","first-page":"4769","DOI":"10.1021\/bi002741i","article-title":"Two mutations of basic residues within the N-terminus of HMG-1 B domain with different effects on DNA supercoiling and binding to bent DNA","volume":"40","author":"\u0160tros","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2026.06.011_bib32","doi-asserted-by":"crossref","first-page":"526","DOI":"10.2119\/molmed.2015.00148","article-title":"Aspirin's Active Metabolite Salicylic Acid Targets High Mobility Group Box 1 to Modulate Inflammatory Responses","volume":"21","author":"Choi","year":"2015","journal-title":"Mol. Med."},{"key":"10.1016\/j.chembiol.2026.06.011_bib33","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1039\/D4CB00062E","article-title":"Natural triterpenoid-aided identification of the druggable interface of HMGB1 occupied by TLR4","volume":"5","author":"Shen","year":"2024","journal-title":"RSC Chem. Biol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib34","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1007\/s10456-008-9093-5","article-title":"Convergence and amplification of toll-like receptor (TLR) and receptor for advanced glycation end products (RAGE) signaling pathways via high mobility group B1 (HMGB1)","volume":"11","author":"van Beijnum","year":"2008","journal-title":"Angiogenesis"},{"key":"10.1016\/j.chembiol.2026.06.011_bib35","doi-asserted-by":"crossref","first-page":"2006","DOI":"10.1002\/jcp.22541","article-title":"HMGB-1 Induces IL-6 Production in Human Synovial Fibroblasts Through c-Src, Akt and NF-\u03baB Pathways","volume":"226","author":"Hou","year":"2011","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib36","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1016\/j.molmed.2007.09.002","article-title":"Signaling to NF-\u03baB by Toll-like receptors","volume":"13","author":"Kawai","year":"2007","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.chembiol.2026.06.011_bib37","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1084\/jem.192.4.565","article-title":"High mobility group 1 protein (HMG-1) stimulates proinflammatory cytokine synthesis in human monocytes","volume":"192","author":"Andersson","year":"2000","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.chembiol.2026.06.011_bib38","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1186\/s12935-020-01289-6","article-title":"HMGB1 mediates lipopolysaccharide-induced inflammation via interacting with GPX4 in colon cancer cells","volume":"20","author":"Yang","year":"2020","journal-title":"Cancer Cell Int."},{"key":"10.1016\/j.chembiol.2026.06.011_bib39","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/nri1594","article-title":"High-mobility group box 1 protein (HMGB): Nuclear weapon in the immune arsenal","volume":"5","author":"Lotze","year":"2005","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib40","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1073\/pnas.2434651100","article-title":"Reversing established sepsis with antagonists of endogenous high-mobility group box 1","volume":"101","author":"Yang","year":"2004","journal-title":"P Natl Acad Sci USA"},{"key":"10.1016\/j.chembiol.2026.06.011_bib41","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.tim.2011.01.001","article-title":"Cecal ligation and puncture: the gold standard model for polymicrobial sepsis?","volume":"19","author":"Dejager","year":"2011","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib42","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1038\/nrd1854","article-title":"Animal models of sepsis: Setting the stage","volume":"4","author":"Buras","year":"2005","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.chembiol.2026.06.011_bib43","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1038\/nature01661","article-title":"Evolving concepts of rheumatoid arthritis","volume":"423","author":"Firestein","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2026.06.011_bib44","doi-asserted-by":"crossref","first-page":"18001","DOI":"10.1038\/nrdp.2018.1","article-title":"Rheumatoid arthritis","volume":"4","author":"Smolen","year":"2018","journal-title":"Nat. Rev. Dis. Primers"},{"key":"10.1016\/j.chembiol.2026.06.011_bib45","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1038\/s41584-020-0373-9","article-title":"Methotrexate and its mechanisms of action in inflammatory arthritis","volume":"16","author":"Cronstein","year":"2020","journal-title":"Nat. Rev. Rheumatol."},{"key":"10.1016\/j.chembiol.2026.06.011_bib46","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1124\/pr.57.2.3","article-title":"Low-dose methotrexate: A mainstay in the treatment of rheumatoid arthritis","volume":"57","author":"Cronstein","year":"2005","journal-title":"Pharmacol. Rev."},{"key":"10.1016\/j.chembiol.2026.06.011_bib47","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.bbagrm.2009.11.019","article-title":"Targeting HMGB1 in inflammation","volume":"1799","author":"Yang","year":"2010","journal-title":"Biochim. Biophys. Acta, Gene Regul. Mech."},{"key":"10.1016\/j.chembiol.2026.06.011_bib48","doi-asserted-by":"crossref","first-page":"952","DOI":"10.3324\/haematol.2024.286484","article-title":"A novel CCL3-HMGB1 signaling axis regulating osteocyte RANKL expression in multiple myeloma","volume":"110","author":"Anloague","year":"2024","journal-title":"Haematologica"},{"key":"10.1016\/j.chembiol.2026.06.011_bib49","doi-asserted-by":"crossref","DOI":"10.1186\/s12974-015-0360-2","article-title":"HMGB1 promotes the activation of NLRP3 and caspase-8 inflammasomes via NF-\u03baB pathway in acute glaucoma","volume":"12","author":"Chi","year":"2015","journal-title":"J. Neuroinflammation"},{"key":"10.1016\/j.chembiol.2026.06.011_bib50","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1093\/nar\/23.9.1604","article-title":"The Hmg-1 Box Protein Family - Classification and Functional-Relationships","volume":"23","author":"Baxevanis","year":"1995","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.chembiol.2026.06.011_bib51","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.bbagrm.2009.09.008","article-title":"HMGB proteins: Interactions with DNA and chromatin","volume":"1799","author":"\u0160tros","year":"2010","journal-title":"Biochim. Biophys. Acta Gene Regul. Mech."}],"container-title":["Cell Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2451945626002357?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2451945626002357?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T15:34:07Z","timestamp":1787240047000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2451945626002357"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8]]},"references-count":51,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2026,8]]}},"alternative-id":["S2451945626002357"],"URL":"https:\/\/doi.org\/10.1016\/j.chembiol.2026.06.011","relation":{},"ISSN":["2451-9456"],"issn-type":[{"value":"2451-9456","type":"print"}],"subject":[],"published":{"date-parts":[[2026,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Aptamer targeting HMGB1 attenuates inflammatory disease via domain-specific antagonism","name":"articletitle","label":"Article Title"},{"value":"Cell Chemical Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.chembiol.2026.06.011","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}