{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,11]],"date-time":"2026-10-11T03:27:19Z","timestamp":1791689239072,"version":"4.3.4"},"reference-count":52,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Fish &amp; Shellfish Immunology"],"published-print":{"date-parts":[[2025,2]]},"DOI":"10.1016\/j.fsi.2024.110043","type":"journal-article","created":{"date-parts":[[2024,11,26]],"date-time":"2024-11-26T16:02:34Z","timestamp":1732636954000},"page":"110043","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"special_numbering":"C","title":["Hemolysis-associated release of hemoglobin induces mitochondrial oxidative phosphorylation (OXPHOS) disturbance and aggravates cell oxidative damage in grass carp (Ctenopharyngodon idella)"],"prefix":"10.1016","volume":"157","author":[{"given":"Yan","family":"Yang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ningjing","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jialing","family":"Song","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ye","family":"Tian","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bing","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiangtao","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li","family":"Lin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhendong","family":"Qin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"8","key":"10.1016\/j.fsi.2024.110043_bib1","doi-asserted-by":"crossref","first-page":"4061","DOI":"10.1021\/pr100252e","article-title":"Quantitative mass spectrometry defines an oxidative hotspot in hemoglobin that is specifically protected by haptoglobin","volume":"9","author":"Pimenova","year":"2010","journal-title":"J. Proteome Res."},{"issue":"45","key":"10.1016\/j.fsi.2024.110043_bib2","doi-asserted-by":"crossref","first-page":"17387","DOI":"10.1074\/jbc.RA118.003840","article-title":"ROS-induced HSP70 promotes cytoplasmic translocation of high-mobility group box 1b and stimulates antiviral autophagy in grass carp kidney cells","volume":"293","author":"Rao","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.fsi.2024.110043_bib3","doi-asserted-by":"crossref","DOI":"10.3389\/fvets.2022.1023784","article-title":"Role of phytobiotics in relieving the impacts of Aeromonas hydrophila infection on aquatic animals: a mini-review","volume":"9","author":"Abdul Kari","year":"2022","journal-title":"Front. Vet. Sci."},{"key":"10.1016\/j.fsi.2024.110043_bib4","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1007\/978-3-030-41769-7_14","article-title":"Hemoglobin: structure, function and allostery","author":"Ahmed","year":"2020","journal-title":"Vertebrate and invertebrate respiratory proteins, lipoproteins and other body fluid proteins"},{"issue":"4","key":"10.1016\/j.fsi.2024.110043_bib5","doi-asserted-by":"crossref","first-page":"1702","DOI":"10.1021\/cr500495x","article-title":"New look at hemoglobin allostery","volume":"115","author":"Yuan","year":"2015","journal-title":"Chemical reviews"},{"issue":"40","key":"10.1016\/j.fsi.2024.110043_bib6","doi-asserted-by":"crossref","first-page":"13112","DOI":"10.1021\/bi960737u","article-title":"Role of hemopexin in protection of low-density lipoprotein against hemoglobin-induced oxidation","volume":"35","author":"Miller","year":"1996","journal-title":"Biochemistry"},{"issue":"6","key":"10.1016\/j.fsi.2024.110043_bib7","doi-asserted-by":"crossref","first-page":"1224","DOI":"10.1271\/bbb.66.1224","article-title":"Monoamine-dependent production of reactive oxygen species catalyzed by pseudoperoxidase activity of human hemoglobin","volume":"66","author":"Kawano","year":"2002","journal-title":"Bioscience, biotechnology, and biochemistry"},{"key":"10.1016\/j.fsi.2024.110043_bib8","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.3389\/fimmu.2020.01323","article-title":"Pro-inflammatory Actions of heme and other hemoglobin-derived DAMPs","volume":"11","author":"Bozza","year":"2020","journal-title":"Front. Immunol."},{"issue":"11","key":"10.1016\/j.fsi.2024.110043_bib9","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/s41581-019-0181-0","article-title":"Mechanisms of haemolysis-induced kidney injury","volume":"15","author":"Van Avondt","year":"2019","journal-title":"Nat. Rev. Nephrol."},{"key":"10.1016\/j.fsi.2024.110043_bib10","doi-asserted-by":"crossref","DOI":"10.1016\/j.dci.2021.104207","article-title":"Hemeprotein amplifies the innate immune receptors of Ctenopharyngodon idellus kidney cells through NF-\u03baB-and MAPK-dependent reactive oxygen species generation","volume":"126","author":"Lu","year":"2022","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.fsi.2024.110043_bib11","doi-asserted-by":"crossref","DOI":"10.1016\/j.aquaculture.2022.738281","article-title":"Hemoglobin mediates inflammation and apoptosis in the head-kidney macrophages of grass carp (Ctenopharyngodon idella)","volume":"557","author":"Qin","year":"2022","journal-title":"Aquaculture"},{"key":"10.1016\/j.fsi.2024.110043_bib12","article-title":"The oxidative injury of extracellular hemoglobin is associated with reactive oxygen species generation of grass carp (Ctenopharyngodon idella)","volume":"13","author":"Qin","year":"2022","journal-title":"Front. Immunol."},{"key":"10.1016\/j.fsi.2024.110043_bib13","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2022.1044299","article-title":"Hemoglobin induces inflammation through NF-kB signaling pathway and causes cell oxidative damage in grass carp (Ctenopharyngodon idella)","volume":"13","author":"Tang","year":"2022","journal-title":"Front. Immunol."},{"issue":"2","key":"10.1016\/j.fsi.2024.110043_bib14","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1002\/jat.4537","article-title":"Environmentally relevant lead alters nuclear integrity in erythrocytes and generates oxidative stress in liver of Anabas testudineus: involvement of Nrf2\u2010Keap1 regulation and expression of biomarker genes","volume":"44","author":"Dey","year":"2024","journal-title":"J. Appl. Toxicol."},{"key":"10.1016\/j.fsi.2024.110043_bib15","doi-asserted-by":"crossref","DOI":"10.1016\/j.aquatox.2020.105676","article-title":"Interplay between dietary lipids and cadmium exposure in rainbow trout liver: influence on fatty acid metabolism, metal accumulation and stress response","volume":"231","author":"Ferain","year":"2021","journal-title":"Aquat. Toxicol."},{"key":"10.1016\/j.fsi.2024.110043_bib16","article-title":"Innate and adaptive immunity gene expression profiles induced by virulent Aeromonas hydrophila infection in the immune-related organs of channel catfish","author":"Gomaa","year":"2024","journal-title":"Dev. Comp. Immunol."},{"issue":"1","key":"10.1016\/j.fsi.2024.110043_bib17","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1186\/s12964-024-01829-x","article-title":"ER\u2013mitochondria contact sites regulate hepatic lipogenesis via Ip3r-Grp75-Vdac complex recruiting Seipin","volume":"22","author":"Chi","year":"2024","journal-title":"Cell Commun. Signal."},{"issue":"4","key":"10.1016\/j.fsi.2024.110043_bib18","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1002\/tox.22699","article-title":"Overview of the toxic effects of titanium dioxide nanoparticles in blood, liver, muscles, and brain of a Neotropical detritivorous fish","volume":"34","author":"Carmo","year":"2019","journal-title":"Environ. Toxicol."},{"issue":"11","key":"10.1016\/j.fsi.2024.110043_bib19","doi-asserted-by":"crossref","first-page":"906","DOI":"10.1016\/j.molmed.2022.08.005","article-title":"Erythrophagocytes in hemolytic anemia, wound healing, and cancer","volume":"28","author":"Schaer","year":"2022","journal-title":"Trends Mol. Med."},{"issue":"12","key":"10.1016\/j.fsi.2024.110043_bib20","doi-asserted-by":"crossref","first-page":"2119","DOI":"10.1089\/ars.2007.1787","article-title":"Heme, heme oxygenase, and ferritin: how the vascular endothelium survives (and dies) in an iron-rich environment","volume":"9","author":"Balla","year":"2007","journal-title":"Antioxidants Redox Signal."},{"issue":"11","key":"10.1016\/j.fsi.2024.110043_bib21","doi-asserted-by":"crossref","first-page":"3796","DOI":"10.1016\/S0021-9258(19)43804-0","article-title":"Binding of porphyrins to rabbit hemopexin and albumin","volume":"248","author":"Seery","year":"1973","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.fsi.2024.110043_bib22","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1089\/ars.2009.2787","article-title":"Heme scavenging and the other facets of hemopexin","volume":"12","author":"Tolosano","year":"2010","journal-title":"Antioxidants Redox Signal."},{"issue":"4","key":"10.1016\/j.fsi.2024.110043_bib23","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1111\/j.1365-2141.2011.08738.x","article-title":"Methaemalbumin formation in sickle cell disease: effect on oxidative protein modification and HO\u20101 induction","volume":"154","author":"Hanson","year":"2011","journal-title":"Br. J. Haematol."},{"issue":"10","key":"10.1016\/j.fsi.2024.110043_bib24","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1038\/13294","article-title":"Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two \u03b2-propeller domains","volume":"6","author":"Paoli","year":"1999","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.fsi.2024.110043_bib25","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1146\/annurev-nutr-062320-112625","article-title":"Molecular mechanisms of iron and heme metabolism","volume":"42","author":"Dutt","year":"2022","journal-title":"Annu. Rev. Nutr."},{"issue":"10","key":"10.1016\/j.fsi.2024.110043_bib26","doi-asserted-by":"crossref","first-page":"5267","DOI":"10.4049\/jimmunol.1202648","article-title":"CD163 and IgG codefend against cytotoxic hemoglobin via autocrine and paracrine mechanisms","volume":"190","author":"Subramanian","year":"2013","journal-title":"J. Immunol."},{"issue":"1","key":"10.1016\/j.fsi.2024.110043_bib27","doi-asserted-by":"crossref","first-page":"175","DOI":"10.2215\/CJN.01970211","article-title":"AKI associated with macroscopic glomerular hematuria: clinical and pathophysiologic consequences","volume":"7","author":"Moreno","year":"2012","journal-title":"Clin. J. Am. Soc. Nephrol."},{"issue":"7","key":"10.1016\/j.fsi.2024.110043_bib28","doi-asserted-by":"crossref","DOI":"10.1172\/jci.insight.90777","article-title":"Inhibition of neuronal ferroptosis protects hemorrhagic brain","volume":"2","author":"Li","year":"2017","journal-title":"JCI Insight"},{"key":"10.1016\/j.fsi.2024.110043_bib29","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/B978-0-12-385118-5.00006-2","article-title":"Quantitative real-time PCR-based analysis of gene expression","author":"Jozefczuk","year":"2011","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.fsi.2024.110043_bib30","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1007\/978-1-4939-8935-5_33","article-title":"Sample preparation for transmission electron microscopy","author":"Tizro","year":"2019","journal-title":"Biobanking: methods and protocols"},{"issue":"3","key":"10.1016\/j.fsi.2024.110043_bib31","article-title":"Preparing paraffin tissue sections for staining","volume":"2021","author":"Rodig","year":"2021","journal-title":"Cold Spring Harbor Protocols"},{"issue":"4","key":"10.1016\/j.fsi.2024.110043_bib32","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/j.jphs.2021.09.001","article-title":"Reduced mitochondrial complex II activity enhances cell death via intracellular reactive oxygen species in STHdhQ111 striatal neurons with mutant huntingtin","volume":"147","author":"Okada","year":"2021","journal-title":"J. Pharmacol. Sci."},{"issue":"11","key":"10.1016\/j.fsi.2024.110043_bib33","doi-asserted-by":"crossref","first-page":"4809","DOI":"10.1172\/JCI64578","article-title":"Extracellular hemin crisis triggers acute chest syndrome in sickle mice","volume":"123","author":"Ghosh","year":"2013","journal-title":"The Journal of clinical investigation"},{"issue":"8","key":"10.1016\/j.fsi.2024.110043_bib34","first-page":"1276","article-title":"Hemolysis and free hemoglobin revisited: exploring hemoglobin and hemin scavengers as a novel class of therapeutic proteins","volume":"121","author":"Schaer","year":"2013","journal-title":"Blood, The Journal of the American Society of Hematology"},{"issue":"37","key":"10.1016\/j.fsi.2024.110043_bib35","doi-asserted-by":"crossref","first-page":"13612","DOI":"10.1073\/pnas.0606424103","article-title":"Zip14 (Slc39a14) mediates non-transferrin-bound iron uptake into cells","volume":"103","author":"Liuzzi","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"5","key":"10.1016\/j.fsi.2024.110043_bib36","doi-asserted-by":"crossref","first-page":"1867","DOI":"10.1182\/blood-2004-10-3856","article-title":"Iron trafficking in the mitochondrion: novel pathways revealed by disease","volume":"105","author":"Napier","year":"2005","journal-title":"Blood"},{"issue":"12","key":"10.1016\/j.fsi.2024.110043_bib37","doi-asserted-by":"crossref","first-page":"3003","DOI":"10.1089\/ars.2011.3921","article-title":"Mitochondrial mayhem: the mitochondrion as a modulator of iron metabolism and its role in disease","volume":"15","author":"Huang","year":"2011","journal-title":"Antioxidants Redox Signal."},{"issue":"39","key":"10.1016\/j.fsi.2024.110043_bib38","doi-asserted-by":"crossref","first-page":"E4110","DOI":"10.1073\/pnas.1405023111","article-title":"Hemolysis-induced lethality involves inflammasome activation by heme","volume":"111","author":"Dutra","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"9","key":"10.1016\/j.fsi.2024.110043_bib39","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1016\/j.bbagen.2019.06.010","article-title":"Iron homeostasis and iron-regulated ROS in cell death, senescence and human diseases","volume":"1863","author":"Nakamura","year":"2019","journal-title":"Biochimica et Biophysica Acta (BBA)-General Subjects"},{"key":"10.1016\/j.fsi.2024.110043_bib40","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/j.freeradbiomed.2019.01.052","article-title":"Ferritinophagy activation and sideroflexin1-dependent mitochondria iron overload is involved in apelin-13-induced cardiomyocytes hypertrophy","volume":"134","author":"Tang","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.fsi.2024.110043_bib41","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.freeradbiomed.2020.02.029","article-title":"Mitochondrial superoxide\/hydrogen peroxide: an emerging therapeutic target for metabolic diseases","volume":"152","author":"Yan","year":"2020","journal-title":"Free Radic. Biol. Med."},{"issue":"7483","key":"10.1016\/j.fsi.2024.110043_bib42","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1038\/nature12985","article-title":"Mitochondrial form and function","volume":"505","author":"Friedman","year":"2014","journal-title":"Nature"},{"issue":"1","key":"10.1016\/j.fsi.2024.110043_bib43","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1080\/17474086.2016.1268047","article-title":"Mitochondria and Iron: current questions","volume":"10","author":"Paul","year":"2017","journal-title":"Expert review of hematology"},{"issue":"3","key":"10.1016\/j.fsi.2024.110043_bib44","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1002\/cbic.200600311","article-title":"Assessment of chelatable mitochondrial iron by using mitochondrion\u2010selective fluorescent iron indicators with different iron\u2010binding affinities","volume":"8","author":"Rauen","year":"2007","journal-title":"Chembiochem"},{"issue":"5","key":"10.1016\/j.fsi.2024.110043_bib45","doi-asserted-by":"crossref","first-page":"2161","DOI":"10.1182\/blood-2004-07-2722","article-title":"Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis","volume":"105","author":"Nie","year":"2005","journal-title":"Blood"},{"key":"10.1016\/j.fsi.2024.110043_bib46","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/j.freeradbiomed.2019.07.008","article-title":"Redox states of hemoglobin determine left ventricle pressure recovery and activity of mitochondrial complex IV in hypoxic rat hearts","volume":"141","author":"Edmondson","year":"2019","journal-title":"Free Radic. Biol. Med."},{"issue":"46","key":"10.1016\/j.fsi.2024.110043_bib47","doi-asserted-by":"crossref","first-page":"27939","DOI":"10.1074\/jbc.M115.651257","article-title":"Sickle cell hemoglobin in the ferryl state promotes \u03b2Cys-93 oxidation and mitochondrial dysfunction in epithelial lung cells (E10)","volume":"290","author":"Kassa","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.fsi.2024.110043_bib48","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.trsl.2021.01.005","article-title":"Hemoglobin induces oxidative stress and mitochondrial dysfunction in oligodendrocyte progenitor cells","volume":"231","author":"Pandya","year":"2021","journal-title":"Transl. Res."},{"issue":"9","key":"10.1016\/j.fsi.2024.110043_bib49","article-title":"Mitochondrial regulation of ferroptosis","volume":"220","author":"Gan","year":"2021","journal-title":"JCB (J. Cell Biol.)"},{"issue":"1","key":"10.1016\/j.fsi.2024.110043_bib50","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BJ20081386","article-title":"How mitochondria produce reactive oxygen species","volume":"417","author":"Murphy","year":"2009","journal-title":"Biochemical journal"},{"issue":"6","key":"10.1016\/j.fsi.2024.110043_bib51","doi-asserted-by":"crossref","first-page":"920","DOI":"10.1016\/j.cmet.2020.10.011","article-title":"The metabolic underpinnings of ferroptosis","volume":"32","author":"Zheng","year":"2020","journal-title":"Cell Metabol."},{"issue":"2","key":"10.1016\/j.fsi.2024.110043_bib52","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1016\/j.molcel.2018.10.042","article-title":"Role of mitochondria in ferroptosis","volume":"73","author":"Gao","year":"2019","journal-title":"Molecular cell"}],"container-title":["Fish &amp; Shellfish Immunology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1050464824006892?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1050464824006892?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,1,23]],"date-time":"2025-01-23T10:36:22Z","timestamp":1737628582000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1050464824006892"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2]]},"references-count":52,"alternative-id":["S1050464824006892"],"URL":"https:\/\/doi.org\/10.1016\/j.fsi.2024.110043","relation":{},"ISSN":["1050-4648"],"issn-type":[{"value":"1050-4648","type":"print"}],"subject":[],"published":{"date-parts":[[2025,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Hemolysis-associated release of hemoglobin induces mitochondrial oxidative phosphorylation (OXPHOS) disturbance and aggravates cell oxidative damage in grass carp (Ctenopharyngodon idella)","name":"articletitle","label":"Article Title"},{"value":"Fish & Shellfish Immunology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.fsi.2024.110043","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"110043"}}