{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T10:52:33Z","timestamp":1784717553510,"version":"3.55.0"},"reference-count":60,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,6,1]],"date-time":"2018-06-01T00:00:00Z","timestamp":1527811200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Fish & Shellfish Immunology"],"published-print":{"date-parts":[[2018,6]]},"DOI":"10.1016\/j.fsi.2018.03.045","type":"journal-article","created":{"date-parts":[[2018,3,28]],"date-time":"2018-03-28T08:08:17Z","timestamp":1522224497000},"page":"385-391","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"special_numbering":"C","title":["Cloning and functional characterization of thioredoxin genes from large yellow croaker Larimichthys crocea"],"prefix":"10.1016","volume":"77","author":[{"given":"Mengnan","family":"Chen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jianshe","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8411-4360","authenticated-orcid":false,"given":"Xiaoze","family":"Xie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6871-3320","authenticated-orcid":false,"given":"Changwen","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.fsi.2018.03.045_bib1","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1126\/science.291.5504.643","article-title":"Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster","volume":"291","author":"Kanzok","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.fsi.2018.03.045_bib2","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/S0009-9120(99)00075-2","article-title":"Antioxidant enzymes and human diseases","volume":"32","author":"Mat\u00e9s","year":"1999","journal-title":"Clin. Biochem."},{"key":"10.1016\/j.fsi.2018.03.045_bib3","doi-asserted-by":"crossref","first-page":"1368","DOI":"10.1016\/j.bbagen.2007.12.008","article-title":"Emerging potential of thioredoxin and thioredoxin interacting proteins in various disease conditions","volume":"1780","author":"Maulik","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.fsi.2018.03.045_bib4","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1146\/annurev.nutr.25.050304.092633","article-title":"Redox regulation by intrinsic species and extrinsic nutrients in normal and cancer cells","volume":"25","author":"Mceligot","year":"2005","journal-title":"Annu. Rev. Nutr."},{"key":"10.1016\/j.fsi.2018.03.045_bib5","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.cbpc.2008.03.013","article-title":"Shrimp thioredoxin is a potent antioxidant protein","volume":"148","author":"Aispuro-Hernandez","year":"2008","journal-title":"Comp. Biochem. Physiol. Toxicol. Pharmacol. Cbp."},{"key":"10.1016\/j.fsi.2018.03.045_bib6","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1146\/annurev.nutr.24.012003.132208","article-title":"Extracellular thiols and thiol\/disulfide redox in metabolism","volume":"24","author":"Moriartycraige","year":"2004","journal-title":"Annu. Rev. Nutr."},{"key":"10.1016\/j.fsi.2018.03.045_bib7","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1016\/j.jmb.2004.11.004","article-title":"Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster","volume":"345","author":"Wahl","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.fsi.2018.03.045_bib8","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1016\/S0006-2952(02)01176-0","article-title":"Cell signalling and the glutathione redox system","volume":"64","author":"G","year":"2002","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.fsi.2018.03.045_bib9","article-title":"Research advances in biological effects of glutaredoxin and thioredoxin on antioxidative stress of animals","author":"Huang","year":"2010","journal-title":"Chin. J. Anim. Nutr."},{"key":"10.1016\/j.fsi.2018.03.045_bib10","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/j.bbagen.2009.01.014","article-title":"Focus on mammalian thioredoxin reductases\u2013important selenoproteins with versatile functions","volume":"1790","author":"Arn\u00e9r","year":"2009","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.fsi.2018.03.045_bib11","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.bbrc.2010.03.083","article-title":"Thioredoxin and thioredoxin reductase: current research with special reference to human disease","volume":"396","author":"Holmgren","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.fsi.2018.03.045_bib12","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.cytogfr.2013.01.001","article-title":"Extracellular thioredoxin: a therapeutic tool to combat inflammation","volume":"24","author":"Matsuo","year":"2013","journal-title":"Cytokine Growth Factor Rev."},{"key":"10.1016\/j.fsi.2018.03.045_bib13","doi-asserted-by":"crossref","first-page":"13963","DOI":"10.1016\/S0021-9258(18)71625-6","article-title":"Thioredoxin and glutaredoxin systems (review). J biol chem","volume":"264","author":"Holmgren","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.fsi.2018.03.045_bib14","doi-asserted-by":"crossref","first-page":"6102","DOI":"10.1046\/j.1432-1327.2000.01701.x","article-title":"Physiological functions of thioredoxin and thioredoxin reductase","volume":"267","author":"Arn\u00e9r","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.fsi.2018.03.045_bib15","doi-asserted-by":"crossref","first-page":"3436","DOI":"10.1016\/S0021-9258(18)97742-2","article-title":"Enzymatic synthesis of deoxyribonucleotides. Iv. Isolation and characterization of thioredoxin, the hydrogen donor from escherichia coli B","volume":"239","author":"Laurent","year":"1964","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.fsi.2018.03.045_bib16","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1146\/annurev.pharmtox.41.1.261","article-title":"Properties and biological activities of thioredoxins","volume":"41","author":"Powis","year":"2003","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.fsi.2018.03.045_bib17","first-page":"59","article-title":"Significance of the antioxidant factor, thioredoxin, in heart failure","volume":"40","author":"Shioji","year":"2002","journal-title":"J. Cardiol."},{"key":"10.1016\/j.fsi.2018.03.045_bib18","first-page":"1470","article-title":"Protective effect of adult T-cell leukemia-derived factor on retinal ischemia-reperfusion injury in the rat","volume":"39","author":"Shibuki","year":"1998","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.fsi.2018.03.045_bib19","first-page":"1518","article-title":"Role of oxidative stress and thioredoxin in gastric cancer","volume":"31","author":"Tu","year":"2011","journal-title":"Nan Fang Yi Ke Da Xue Xue Bao"},{"key":"10.1016\/j.fsi.2018.03.045_bib20","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.freeradbiomed.2011.04.030","article-title":"Depletion of cytosolic or mitochondrial thioredoxin increases CYP2E1-induced oxidative stress via an ASK-1-JNK1 pathway in HepG2 cells","volume":"51","author":"Yang","year":"2011","journal-title":"Free Radical Biol. Med."},{"key":"10.1016\/j.fsi.2018.03.045_bib21","doi-asserted-by":"crossref","first-page":"2688","DOI":"10.1073\/pnas.041624998","article-title":"Chronic elevation of plasma thioredoxin: inhibition of chemotaxis and curtailment of life expectancy in AIDS","volume":"98","author":"Nakamura","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.fsi.2018.03.045_bib22","doi-asserted-by":"crossref","first-page":"351","DOI":"10.4049\/jimmunol.163.1.351","article-title":"Involvement of thioredoxin in rheumatoid arthritis: its costimulatory roles in the TNF-alpha-induced production of IL-6 and IL-8 from cultured synovial fibroblasts","volume":"163","author":"Yoshida","year":"1999","journal-title":"J. Immunol."},{"key":"10.1016\/j.fsi.2018.03.045_bib23","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1161\/01.ATV.0000251006.54632.bb","article-title":"Thiol-related genes in diabetic complications: a novel protective role for endogenous thioredoxin 2","volume":"27","author":"Liang","year":"2007","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.fsi.2018.03.045_bib24","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.dci.2013.09.013","article-title":"Insights into the fish thioredoxin system: expression profile of thioredoxin and thioredoxin reductase in rainbow trout (Oncorhynchus mykiss) during infection and in vitro stimulation","volume":"42","author":"Pacitti","year":"2014","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.fsi.2018.03.045_bib25","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1016\/j.fsi.2012.02.002","article-title":"Molecular characterization, expression, and functional analysis of two thioredoxins in the black rockfish (Sebastes schlegelii)","volume":"32","author":"Park","year":"2012","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2018.03.045_bib26","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1016\/j.fsi.2012.11.029","article-title":"Multiplex immune-related genes expression analysis response to bacterial challenge in mud crab, Scylla paramamosain","volume":"34","author":"Zhang","year":"2013","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2018.03.045_bib27","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.fsi.2011.12.010","article-title":"Mitochondrial thioredoxin-2 from Manila clam ( Ruditapes philippinarum ) is a potent antioxidant enzyme involved in antibacterial response","volume":"32","author":"Umasuthan","year":"2012","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2018.03.045_bib28","first-page":"11","article-title":"Mercury exposure modulates antioxidant enzymes in gill tissue and hemocytes of Venerupis philippinarum","author":"Li","year":"2014","journal-title":"Invertebr. Surviv. J."},{"key":"10.1016\/j.fsi.2018.03.045_bib29","doi-asserted-by":"crossref","first-page":"5227","DOI":"10.1038\/ncomms6227","article-title":"The draft genome of the large yellow croaker reveals well-developed innate immunity","volume":"5","author":"Wu","year":"2014","journal-title":"Nat. Commun."},{"key":"10.1016\/j.fsi.2018.03.045_bib30","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.jmb.2007.04.044","article-title":"The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis","volume":"370","author":"Fritz-Wolf","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.fsi.2018.03.045_bib31","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.fsi.2013.04.040","article-title":"The link between selenium binding protein from Sinonovacula constricta and environmental pollution exposure","volume":"35","author":"Lu","year":"2013","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2018.03.045_bib32","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1042\/BST0331375","article-title":"Thiol redox control via thioredoxin and glutaredoxin systems","volume":"33","author":"Holmgren","year":"2005","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.fsi.2018.03.045_bib33","doi-asserted-by":"crossref","first-page":"2936","DOI":"10.1074\/jbc.272.5.2936","article-title":"Cloning and expression of a novel mammalian thioredoxin","volume":"272","author":"Spyrou","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.fsi.2018.03.045_bib34","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.tox.2008.01.017","article-title":"Hexavalent chromium causes the oxidation of thioredoxin in human bronchial epithelial cells","volume":"246","author":"Myers","year":"2008","journal-title":"Toxicology"},{"key":"10.1016\/j.fsi.2018.03.045_bib35","doi-asserted-by":"crossref","first-page":"40180","DOI":"10.1074\/jbc.M007633200","article-title":"The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited","volume":"275","author":"Kanzok","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.fsi.2018.03.045_bib36","doi-asserted-by":"crossref","first-page":"10241","DOI":"10.4238\/2014.December.4.19","article-title":"Molecular characterization of thioredoxin-1 and thioredoxin reductase activity in mud crab Scylla paramamosain","volume":"13","author":"Hu","year":"2014","journal-title":"Genetics & Molecular Research Gmr"},{"key":"10.1016\/j.fsi.2018.03.045_bib37","doi-asserted-by":"crossref","first-page":"1369","DOI":"10.1110\/ps.051916606","article-title":"Solution structure of HndAc: a thioredoxin-like domain involved in the NADP-reducing hydrogenase complex","volume":"15","author":"Nouailler","year":"2006","journal-title":"Protein Sci."},{"key":"10.1016\/j.fsi.2018.03.045_bib38","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1042\/BJ20110753","article-title":"Crystal structures and kinetic studies of human Kappa class glutathione transferase provide insights into the catalytic mechanism","volume":"439","author":"Wang","year":"2011","journal-title":"Biochem. J."},{"key":"10.1016\/j.fsi.2018.03.045_bib39","doi-asserted-by":"crossref","first-page":"2659","DOI":"10.1002\/j.1460-2075.1996.tb00626.x","article-title":"The CXXC motif: imperatives for the formation of native disulfide bonds in the cell","volume":"15","author":"Chivers","year":"1996","journal-title":"EMBO J."},{"key":"10.1016\/j.fsi.2018.03.045_bib40","first-page":"1533","article-title":"The CXXC motif: crystal structure of an active-site variant of Escherichia coli thioredoxin","volume":"55","author":"Schultz","year":"2010","journal-title":"Acta Crystallogr."},{"key":"10.1016\/j.fsi.2018.03.045_bib41","doi-asserted-by":"crossref","first-page":"2217","DOI":"10.1110\/ps.062268106","article-title":"The origami of thioredoxin-like folds","volume":"15","author":"Pan","year":"2006","journal-title":"Protein Science A Publication of the Protein Society"},{"key":"10.1016\/j.fsi.2018.03.045_bib42","first-page":"20","article-title":"Homology modeling and structure prediction of thioredoxin (TRX) protein in wheat (Triticum aestivum L.)","volume":"1","author":"Prabhavathi","year":"2011","journal-title":"Int. J. Biosci."},{"key":"10.1016\/j.fsi.2018.03.045_bib43","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.cbpb.2014.12.004","article-title":"Comparative study of two thioredoxins from common cutworm (Spodoptera litura): cloning, expression, and functional characterization","volume":"182","author":"Kang","year":"2015","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"10.1016\/j.fsi.2018.03.045_bib44","doi-asserted-by":"crossref","first-page":"19433","DOI":"10.3390\/ijms160819433","article-title":"Molecular and functional characterization of thioredoxin 1 from Korean rose bitterling (Rhodeus uyekii)","volume":"16","author":"Kim","year":"2015","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.fsi.2018.03.045_bib45","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1016\/j.fsi.2009.02.024","article-title":"A thioredoxin with antioxidant activity identified from Eriocheir sinensis","volume":"26","author":"Mu","year":"2009","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2018.03.045_bib46","doi-asserted-by":"crossref","first-page":"15506","DOI":"10.1016\/S0021-9258(19)37617-3","article-title":"Cloning and expression of a cDNA for human thioredoxin","volume":"263","author":"Wollman","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.fsi.2018.03.045_bib47","doi-asserted-by":"crossref","first-page":"63","DOI":"10.3390\/toxins8030063","article-title":"Characterization and recombinant expression of terebrid venom peptide fromTerebra guttata","volume":"8","author":"John","year":"2016","journal-title":"Toxins"},{"key":"10.1016\/j.fsi.2018.03.045_bib48","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.cbpb.2014.12.004","article-title":"Comparative study of two thioredoxins from common cutworm ( Spodoptera litura ): cloning, expression, and functional characterization","volume":"182","author":"Kang","year":"2015","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"10.1016\/j.fsi.2018.03.045_bib49","first-page":"65","article-title":"Construction of a recombinant Escherichia coli BL21\/pET-28a-lpgad and the optimization of transformation conditions for the efficient production of \u03b3-aminobutyric acid","volume":"28","author":"Tian","year":"2012","journal-title":"Chin. J. Biotechnol."},{"key":"10.1016\/j.fsi.2018.03.045_bib50","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1146\/annurev.immunol.23.021704.115653","article-title":"How neutrophils kill microbes","volume":"23","author":"Segal","year":"2005","journal-title":"Annu. Rev. Immunol."},{"key":"10.1016\/j.fsi.2018.03.045_bib51","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1016\/j.micinf.2003.09.009","article-title":"Oxidative killing of microbes by neutrophils","volume":"5","author":"Roos","year":"2003","journal-title":"Microb. Infect."},{"key":"10.1016\/j.fsi.2018.03.045_bib52","doi-asserted-by":"crossref","first-page":"7017","DOI":"10.1073\/pnas.91.15.7017","article-title":"Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes","volume":"91","author":"Chae","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.fsi.2018.03.045_bib53","doi-asserted-by":"crossref","first-page":"16815","DOI":"10.1016\/S0021-9258(19)85489-3","article-title":"Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae","volume":"268","author":"HZ","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.fsi.2018.03.045_bib54","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1111\/j.1432-1033.1993.tb18025.x","article-title":"Strategies of antioxidant defense","volume":"215","author":"Sies","year":"1993","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.fsi.2018.03.045_bib55","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1126\/science.210504","article-title":"The biology of oxygen radicals","volume":"201","author":"Fridovich","year":"1978","journal-title":"Science"},{"key":"10.1016\/j.fsi.2018.03.045_bib56","first-page":"5","article-title":"Studies on pathogen of ulcer disease of cultured large yellow croakers,Pseudosciaena crocea and its control medicines","volume":"2","author":"Zheng","year":"2006","journal-title":"South China Fish. Sci."},{"key":"10.1016\/j.fsi.2018.03.045_bib57","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.dci.2017.03.004","article-title":"Fish skeletal muscle tissue is an important focus of immune reactions during pathogen infection","volume":"73","author":"Valenzuela","year":"2017","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.fsi.2018.03.045_bib58","first-page":"174","article-title":"Histopathological and ultrapathological study on ulcer disease of Pseudosciaena crocea","volume":"29","author":"Dai","year":"2010","journal-title":"J. Trop. Oceanogr."},{"key":"10.1016\/j.fsi.2018.03.045_bib59","doi-asserted-by":"crossref","first-page":"G1352","DOI":"10.1152\/ajpgi.00183.2002","article-title":"Glutathione and thioredoxin redox during differentiation in human colon epithelial (Caco-2) cells","volume":"283","author":"Nkabyo","year":"2002","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"10.1016\/j.fsi.2018.03.045_bib60","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1038\/sj.embor.embor729","article-title":"Non-reciprocal regulation of the redox state of the glutathione-glutaredoxin and thioredoxin systems","volume":"4","author":"Trotter","year":"2003","journal-title":"EMBO Rep."}],"container-title":["Fish & Shellfish Immunology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1050464818301621?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1050464818301621?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T20:40:50Z","timestamp":1693600850000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1050464818301621"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,6]]},"references-count":60,"alternative-id":["S1050464818301621"],"URL":"https:\/\/doi.org\/10.1016\/j.fsi.2018.03.045","relation":{},"ISSN":["1050-4648"],"issn-type":[{"value":"1050-4648","type":"print"}],"subject":[],"published":{"date-parts":[[2018,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Cloning and functional characterization of thioredoxin genes from large yellow croaker Larimichthys crocea","name":"articletitle","label":"Article Title"},{"value":"Fish & Shellfish Immunology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.fsi.2018.03.045","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}]}}