{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,17]],"date-time":"2026-07-17T11:27:49Z","timestamp":1784287669455,"version":"3.55.0"},"reference-count":54,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000165","name":"National Science Foundation Division of Chemistry","doi-asserted-by":"publisher","award":["CHE-1904895"],"award-info":[{"award-number":["CHE-1904895"]}],"id":[{"id":"10.13039\/100000165","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Inorganic Biochemistry"],"published-print":{"date-parts":[[2026,1]]},"DOI":"10.1016\/j.jinorgbio.2025.113053","type":"journal-article","created":{"date-parts":[[2025,9,2]],"date-time":"2025-09-02T15:10:39Z","timestamp":1756825839000},"page":"113053","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"special_numbering":"C","title":["Physical and functional effects of substituting coevolved residues from \u03a9-loop C of yeast Iso-1-cytochrome c into human cytochrome c"],"prefix":"10.1016","volume":"274","author":[{"given":"Ariel K.","family":"Frederick","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruce E.","family":"Bowler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jinorgbio.2025.113053_bb0005","doi-asserted-by":"crossref","first-page":"3101","DOI":"10.1002\/1873-3468.13655","article-title":"New moonlighting functions of mitochondrial cytochrome c in the cytoplasm and nucleus","volume":"593","author":"Gonz\u00e1lez-Arzola","year":"2019","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0010","doi-asserted-by":"crossref","first-page":"6111","DOI":"10.1021\/acs.biochem.7b00890","article-title":"Heightened dynamics of the oxidized Y48H variant of human cytochrome c increases its peroxidatic activity","volume":"56","author":"Deacon","year":"2017","journal-title":"Biochemistry"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0015","series-title":"The Enzymes","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/S1874-6047(08)60215-2","volume":"vol. 11","author":"Dickerson","year":"1975"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0020","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0092-8674(00)80085-9","article-title":"Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c","volume":"86","author":"Liu","year":"1996","journal-title":"Cell"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0025","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1021\/acs.biochem.5b01385","article-title":"Alternative conformations of cytochrome c: structure, function and detection","volume":"55","author":"Hannibal","year":"2016","journal-title":"Biochemistry"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0030","doi-asserted-by":"crossref","first-page":"2349","DOI":"10.1101\/gad.272278.115","article-title":"Atomic structure of the apoptosome: mechanism of cytochrome c- and dATP-mediated activation of Apaf-1","volume":"29","author":"Zhou","year":"2015","journal-title":"Genes Dev."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0035","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1038\/nchembio727","article-title":"Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors","volume":"1","author":"Kagan","year":"2005","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0040","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.chemphyslip.2013.11.010","article-title":"Cardiolipin asymmetry, oxidation and signaling","volume":"179","author":"Kagan","year":"2014","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0045","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1016\/j.freeradbiomed.2009.03.004","article-title":"Cytochrome c\/cardiolipin relations in mitochondria: a kiss of death","volume":"46","author":"Kagan","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0050","doi-asserted-by":"crossref","first-page":"1170","DOI":"10.3324\/haematol.2016.146316","article-title":"Whole exome sequencing identifies genetic variants in inherited thrombocytopenia with secondary qualitative function defects","volume":"101","author":"Johnson","year":"2016","journal-title":"Haematologica"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0055","first-page":"269","article-title":"Mutations of cytochrome c identified in patients with thrombocytopenia THC4 affect both apoptosis and cellular bioenergetics","volume":"2014","author":"De Rocco","year":"1842","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0060","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1038\/ng.103","article-title":"A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia","volume":"40","author":"Morison","year":"2008","journal-title":"Nat. Genet."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0065","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1080\/09537104.2018.1543866","article-title":"CYCS gene variants associated with thrombocytopenia","volume":"30","author":"Ledgerwood","year":"2019","journal-title":"Platelets"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0070","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1111\/bjh.19567","article-title":"Thrombocytopenia 4 (THC4): six novel families with mutations of the cytochrome c gene","volume":"205","author":"Marzollo","year":"2024","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0075","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1007\/s00775-012-0973-1","article-title":"Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination, JBIC","volume":"18","author":"Josephs","year":"2013","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0080","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1021\/ja106328k","article-title":"The proapoptotic G41S mutation to human cytochrome c alters the heme electronic structure and increases the electron self-exchange rate","volume":"133","author":"Liptak","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0085","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1042\/BJ20131386","article-title":"Enhancing the peroxidase activity of cytochrome c by mutation of residue 41: implications for the peroxidase mechanism and cytochrome c release","volume":"458","author":"Josephs","year":"2014","journal-title":"Biochem. J."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0090","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2019.110924","article-title":"Comparison of the structural dynamic and mitochondrial electron-transfer properties of the proapoptotic human cytochrome c variants, G41S, Y48H and A51V","volume":"203","author":"Deacon","year":"2020","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0095","doi-asserted-by":"crossref","first-page":"4276","DOI":"10.1021\/acs.biochem.8b00520","article-title":"Naturally occurring disease-related mutations in the 40\u221257 \u03a9-loop of human cytochrome c control triggering of the alkaline isomerization","volume":"57","author":"Deacon","year":"2018","journal-title":"Biochemistry"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0100","doi-asserted-by":"crossref","first-page":"30447","DOI":"10.1038\/srep30447","article-title":"Increased dynamics in the 40\u201357\u03a9-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation","volume":"6","author":"Karsisiotis","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0105","doi-asserted-by":"crossref","first-page":"8939","DOI":"10.1021\/acs.jpcb.9b05869","article-title":"The naturally occurring A51V variant of human cytochrome c destabilizes the native state and enhances peroxidase activity","volume":"123","author":"Lei","year":"2019","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0110","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0022-2836(03)00698-3","article-title":"Folding units govern the cytochrome c alkaline transition","volume":"331","author":"Hoang","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0115","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0022-2836(03)00697-1","article-title":"Cooperative omega loops in cytochrome c: role in folding and function","volume":"331","author":"Krishna","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0120","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1002\/pro.120","article-title":"Compressing the free energy range of substructure stabilities in iso-1-cytochrome c","volume":"18","author":"Duncan","year":"2009","journal-title":"Protein Sci."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0125","doi-asserted-by":"crossref","first-page":"3358","DOI":"10.1021\/acs.biochem.7b00342","article-title":"Effect of a K72A mutation on the structure, stability, dynamics and peroxidase activity of human cytochrome c","volume":"56","author":"Nold","year":"2017","journal-title":"Biochemistry"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0130","doi-asserted-by":"crossref","first-page":"6648","DOI":"10.1073\/pnas.1323828111","article-title":"Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity","volume":"111","author":"McClelland","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0135","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1073\/pnas.50.4.672","article-title":"Primary structure and evolution of cytochrome c","volume":"50","author":"Margoliash","year":"1963","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0140","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1007\/s007750050356","article-title":"Mitochondrial cytochromes c: a comparative analysis","volume":"4","author":"Banci","year":"1999","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0145","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1101\/gr.849004","article-title":"WebLogo: a sequence logo generator","volume":"14","author":"Crooks","year":"2004","journal-title":"Genome Res."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0150","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1038\/nbt.3769","article-title":"Mutation effects predicted from sequence co-variation","volume":"35","author":"Hopf","year":"2017","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0155","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2022.111819","article-title":"Effect on intrinsic peroxidase activity of substituting coevolved residues from \u03a9-loop C of human cytochrome c into yeast iso-1-cytochrome c","volume":"232","author":"Frederick","year":"2022","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0160","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1042\/BJ20130758","article-title":"The hydrogen-peroxide-induced radical behaviour in human cytochrome c\u2013phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant","volume":"456","author":"Rajagopal","year":"2013","journal-title":"Biochem. J."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0165","doi-asserted-by":"crossref","first-page":"2921","DOI":"10.1021\/acs.biochem.9b00295","article-title":"Effect of V83G and I81A substitutions to human cytochrome c on acid unfolding and peroxidase activity below neutral pH","volume":"58","author":"Lei","year":"2019","journal-title":"Biochemistry"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0170","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.jinorgbio.2018.02.022","article-title":"Humanlike substitutions to \u03a9-loop D of yeast iso-1-cytochrome c only modestly affect dynamics and peroxidase activity","volume":"183","author":"Lei","year":"2018","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0175","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.jinorgbio.2015.12.025","article-title":"Disruption of a hydrogen bond network in human versus spider monkey cytochrome c affects heme crevice stability","volume":"158","author":"Goldes","year":"2016","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0180","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1016\/j.bbrc.2003.10.182","article-title":"Stability and apoptotic activity of recombinant human cytochrome c","volume":"312","author":"Olteanu","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0185","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2024.112699","article-title":"Binding of yeast and human cytochrome c to cardiolipin nanodiscs at physiological ionic strength","volume":"260","author":"Frederick","year":"2024","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0190","doi-asserted-by":"crossref","first-page":"2624","DOI":"10.1016\/S0021-9258(19)42776-2","article-title":"Alkaline isomerization of oxidized cytochrome c. equilibrium and kinetic measurements","volume":"249","author":"Davis","year":"1974","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0195","doi-asserted-by":"crossref","first-page":"11234","DOI":"10.1021\/ja971756+","article-title":"Proton-linked protein conformational switching: definition of the alkaline conformational transition of yeast iso-1-ferricytochrome c","volume":"120","author":"Rosell","year":"1998","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0200","series-title":"Cytochrome c: A Multidisciplinary Approach","first-page":"611","author":"Wilson","year":"1996"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0205","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1002\/prot.20757","article-title":"Functional role of a protein foldon - an \u03a9-loop foldon controls the alkaline transition in ferricytochrome c","volume":"63","author":"Maity","year":"2006","journal-title":"Proteins Struct. Funct. Genet."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0210","doi-asserted-by":"crossref","first-page":"2349","DOI":"10.1021\/bi048141r","article-title":"Communication of stabilizing energy between substructures of a protein","volume":"44","author":"Kristinsson","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0215","series-title":"Pettigrew Cytochromes c: Evolutionary, Structural and Physicochemical Aspects","author":"Moore","year":"1990"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0220","doi-asserted-by":"crossref","first-page":"4207","DOI":"10.1046\/j.1432-1327.2001.02335.x","article-title":"The peroxidase activity of cytochrome c-550 from Paracoccus versutus","volume":"268","author":"Diederix","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0225","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1006\/abio.1997.2191","article-title":"Identification of the colored guaiacol oxidation product produced by peroxidases","volume":"250","author":"Doerge","year":"1997","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0230","doi-asserted-by":"crossref","first-page":"1410","DOI":"10.1016\/j.jmb.2006.04.035","article-title":"Order of steps in the cytochrome c folding pathway: evidence for a sequential stabilization mechanism","volume":"359","author":"Krishna","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0235","doi-asserted-by":"crossref","first-page":"4741","DOI":"10.1073\/pnas.0501043102","article-title":"Protein folding: the stepwise assembly of foldon units","volume":"102","author":"Maity","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0240","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/j.jmb.2004.08.005","article-title":"How cytochrome c folds, and why: submolecular foldon units and their stepwise sequential stabilization","volume":"343","author":"Maity","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0245","series-title":"Cytochrome c","first-page":"103","author":"Brayer","year":"1996"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0250","doi-asserted-by":"crossref","first-page":"7605","DOI":"10.1021\/bi00081a001","article-title":"Helix stop signals in proteins and peptides: the capping box","volume":"32","author":"Harper","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0255","doi-asserted-by":"crossref","first-page":"1741","DOI":"10.1002\/pro.5560031014","article-title":"Sequence determinants of the capping box, a stabilizing motif at the N-termini of \u03b1-helices","volume":"3","author":"Seale","year":"1994","journal-title":"Protein Sci."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0260","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1042\/BCJ20200793","article-title":"Altered structure and dynamics of pathogenic cytochrome c variants correlate with increased apoptotic activity","volume":"478","author":"Fellner","year":"2021","journal-title":"Biochem. J."},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0265","doi-asserted-by":"crossref","first-page":"9047","DOI":"10.1021\/bi001095k","article-title":"Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c","volume":"39","author":"Rosell","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jinorgbio.2025.113053_bb0270","doi-asserted-by":"crossref","first-page":"2950","DOI":"10.1021\/acs.biochem.6b01187","article-title":"Remote perturbations in tertiary contacts trigger ligation of lysine to the heme iron in cytochrome c","volume":"56","author":"Gu","year":"2017","journal-title":"Biochemistry"}],"container-title":["Journal of Inorganic Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013425002338?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013425002338?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,6,2]],"date-time":"2026-06-02T14:24:43Z","timestamp":1780410283000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0162013425002338"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,1]]},"references-count":54,"alternative-id":["S0162013425002338"],"URL":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2025.113053","relation":{},"ISSN":["0162-0134"],"issn-type":[{"value":"0162-0134","type":"print"}],"subject":[],"published":{"date-parts":[[2026,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Physical and functional effects of substituting coevolved residues from \u03a9-loop C of yeast Iso-1-cytochrome c into human cytochrome c","name":"articletitle","label":"Article Title"},{"value":"Journal of Inorganic Biochemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2025.113053","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"113053"}}