{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T12:39:14Z","timestamp":1788871154645,"version":"build-2803163510"},"reference-count":43,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"name":"Nation Nature Science Foundation of China","award":["31001120"],"award-info":[{"award-number":["31001120"]}]},{"name":"Zhejiang Provincial Natural Science Foundation of China","award":["Y3100013"],"award-info":[{"award-number":["Y3100013"]}]},{"name":"Important Science and Technology Specific Projects of Zhejiang Province"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Fish &amp; Shellfish Immunology"],"published-print":{"date-parts":[[2013,2]]},"DOI":"10.1016\/j.fsi.2012.11.042","type":"journal-article","created":{"date-parts":[[2012,12,16]],"date-time":"2012-12-16T11:16:50Z","timestamp":1355656610000},"page":"556-563","source":"Crossref","is-referenced-by-count":11,"title":["Miiuy croaker (Miichthys miiuy) Peroxiredoxin2: Molecular characterization, genomic structure and immune response against bacterial infection"],"prefix":"10.1016","volume":"34","author":[{"given":"Liping","family":"Ren","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tianjun","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rixin","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuena","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.fsi.2012.11.042_bib1","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1002\/biof.5520100218","article-title":"A\u00a0family of novel peroxidases, peroxiredoxins","volume":"10","author":"Rhee","year":"1999","journal-title":"BioFactors"},{"key":"10.1016\/j.fsi.2012.11.042_bib2","doi-asserted-by":"crossref","first-page":"1513","DOI":"10.1007\/s00018-003-3048-1","article-title":"Peroxiredoxin 2 (PRDX2), an antioxidant enzyme, is underexpressed in Down syndrome fetal brains","volume":"60","author":"S\u00e1nchez-Font","year":"2003","journal-title":"Cell Mol Life Sci"},{"key":"10.1016\/j.fsi.2012.11.042_bib3","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/S0969-2126(00)00147-7","article-title":"Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7\u00a0\u00c5 resolution","volume":"8","author":"Schr\u00f6der","year":"2000","journal-title":"Structure"},{"key":"10.1016\/j.fsi.2012.11.042_bib4","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/S0378-1119(99)00413-8","article-title":"Characterization of mouse peroxiredoxin I genomic DNA and its expression","volume":"239","author":"Lee","year":"1999","journal-title":"Gene"},{"key":"10.1016\/j.fsi.2012.11.042_bib5","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1089\/ars.2005.7.768","article-title":"Peroxiredoxins, oxidative stress, and cell proliferation","volume":"7","author":"Immenschuh","year":"2005","journal-title":"Antioxid Redox Signal"},{"key":"10.1016\/j.fsi.2012.11.042_bib6","doi-asserted-by":"crossref","first-page":"45419","DOI":"10.1074\/jbc.M307871200","article-title":"Phorbol ester-dependent activation of peroxiredoxin I gene expression via a protein kinase C, Ras, p38 mitogen-activated protein kinase signaling pathway","volume":"278","author":"Hess","year":"2003","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.fsi.2012.11.042_bib7","doi-asserted-by":"crossref","first-page":"30952","DOI":"10.1074\/jbc.272.49.30952","article-title":"Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation","volume":"272","author":"Jin","year":"1997","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.fsi.2012.11.042_bib8","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.fsi.2010.11.011","article-title":"Cloning, genomic structure, and expression analysis of peroxiredoxin V from bay scallop argopecten irradians","volume":"30","author":"Li","year":"2011","journal-title":"Fish Shellfish Immunol"},{"key":"10.1016\/j.fsi.2012.11.042_bib9","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1016\/j.fsi.2008.10.006","article-title":"Molecular cloning and characterization of peroxiredoxin 6 from Chinese mitten crab Eriocheir sinensis","volume":"26","author":"Mu","year":"2009","journal-title":"Fish Shellfish Immunol"},{"key":"10.1016\/j.fsi.2012.11.042_bib10","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1089\/ars.2008.2081","article-title":"Peroxiredoxin 2 and peroxide metabolism in the erythrocyte","volume":"10","author":"Low","year":"2008","journal-title":"Antioxid Redox Signal"},{"key":"10.1016\/j.fsi.2012.11.042_bib11","doi-asserted-by":"crossref","first-page":"2611","DOI":"10.1182\/blood-2006-09-048728","article-title":"Peroxiredoxin2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte","volume":"109","author":"Low","year":"2007","journal-title":"Blood"},{"key":"10.1016\/j.fsi.2012.11.042_bib12","doi-asserted-by":"crossref","first-page":"900","DOI":"10.1006\/bbrc.1995.2856","article-title":"Thioredoxin-linked peroxidase from human red blood cells: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell","volume":"217","author":"Cha","year":"1995","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.fsi.2012.11.042_bib13","doi-asserted-by":"crossref","first-page":"38029","DOI":"10.1074\/jbc.M206626200","article-title":"Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid","volume":"277","author":"Yang","year":"2002","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.fsi.2012.11.042_bib14","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1016\/j.fsi.2010.08.013","article-title":"Identification of immune genes of the miiuy croaker (Miichthys miiuy) by sequencing and bioinformatic analysis of ESTs","volume":"29","author":"Xu","year":"2010","journal-title":"Fish Shellfish Immunol"},{"key":"10.1016\/j.fsi.2012.11.042_bib15","series-title":"Molecular cloning: a laboratory manual","year":"2001"},{"key":"10.1016\/j.fsi.2012.11.042_bib16","doi-asserted-by":"crossref","first-page":"4876","DOI":"10.1093\/nar\/25.24.4876","article-title":"The CLUSTAL-X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools","volume":"25","author":"Thompson","year":"1997","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.fsi.2012.11.042_bib17","first-page":"406","article-title":"The neighbor-joining method, a new method for reconstructing phylogenetic trees","volume":"4","author":"Saitou","year":"1987","journal-title":"Mol Biol Evol"},{"key":"10.1016\/j.fsi.2012.11.042_bib18","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.cbpb.2010.02.011","article-title":"Cloning and functional characterization of a typical 2-Cys peroxiredoxin from southern bluefin tuna (Thunnus maccoyii)","volume":"156","author":"Sutton","year":"2010","journal-title":"Comp Biochem Physiol Part B: Biochem Mol Biol"},{"key":"10.1016\/j.fsi.2012.11.042_bib19","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/S0014-5793(98)01736-0","article-title":"Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member","volume":"443","author":"Matsumotoa","year":"1999","journal-title":"FEBS Lett"},{"key":"10.1016\/j.fsi.2012.11.042_bib20","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1002\/pmic.200390059","article-title":"Proteins from bovine tissues and biological fluids: defining a reference electrophoresis map for liver, kidney, muscle, plasma and red blood cells","volume":"3","author":"Talamo","year":"2003","journal-title":"Proteomics"},{"key":"10.1016\/j.fsi.2012.11.042_bib21","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1023\/A:1006271823973","article-title":"Molecular cloning, expression, and functional characterization of a 2Cys-peroxiredoxin in Chinese cabbage","volume":"40","author":"Cheong","year":"1999","journal-title":"Plant Mol Biol"},{"key":"10.1016\/j.fsi.2012.11.042_bib22","doi-asserted-by":"crossref","first-page":"4071","DOI":"10.1021\/bi00612a031","article-title":"Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay","volume":"17","author":"Holmgren","year":"1978","journal-title":"Biochemistry"},{"key":"10.1016\/j.fsi.2012.11.042_bib23","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.tox.2007.07.021","article-title":"Differential expression of peroxiredoxin 6 in fetal rat testis","volume":"240","author":"Zhang","year":"2007","journal-title":"Toxicology"},{"key":"10.1016\/j.fsi.2012.11.042_bib24","doi-asserted-by":"crossref","first-page":"2119","DOI":"10.1002\/eji.200424962","article-title":"Reactive oxygen species induced by the deletion of peroxiredoxin II (Prx II) increases the number of thymocytes resulting in the enlargement of PrxII-null thymus","volume":"34","author":"Moon","year":"2004","journal-title":"Eur J Immunol"},{"key":"10.1016\/j.fsi.2012.11.042_bib25","doi-asserted-by":"crossref","first-page":"3501","DOI":"10.1016\/j.molimm.2007.03.014","article-title":"Molecular cloning, expression of a peroxiredoxin gene in Chinese shrimp Fenneropenaeus chinensis and the antioxidant activity of its recombinant protein","volume":"44","author":"Zhang","year":"2007","journal-title":"Mol Immunol"},{"key":"10.1016\/j.fsi.2012.11.042_bib26","doi-asserted-by":"crossref","first-page":"6297","DOI":"10.1074\/jbc.273.11.6297","article-title":"Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha","volume":"273","author":"Kang","year":"1998","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.fsi.2012.11.042_bib27","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1046\/j.1432-1033.2001.01843.x","article-title":"Augmented expression of peroxiredoxin VI in rat lung and kidney after birth implies an antioxidative role","volume":"268","author":"Fujii","year":"2001","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.fsi.2012.11.042_bib28","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1016\/S0891-5849(00)00221-5","article-title":"Protein kinase C signaling and oxidative stress","volume":"28","author":"Gopalakrishna","year":"2000","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.fsi.2012.11.042_bib29","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\u00c9s","year":"1999","journal-title":"Clin Biochem"},{"key":"10.1016\/j.fsi.2012.11.042_bib30","doi-asserted-by":"crossref","first-page":"27670","DOI":"10.1016\/S0021-9258(18)47038-X","article-title":"Thioredoxin-dependent peroxide reductase from yeast","volume":"269","author":"Chae","year":"1994","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.fsi.2012.11.042_bib31","doi-asserted-by":"crossref","first-page":"980","DOI":"10.1038\/nature02075","article-title":"ATP-dependent reduction of cysteine-sulphinic acid by S.\u00a0cerevisiae sulphiredoxin","volume":"425","author":"Biteau","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.fsi.2012.11.042_bib32","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/j.molmed.2005.10.006","article-title":"2-Cys peroxiredoxin function in intracellular signal transduction: therapeutic implications","volume":"11","author":"Kang","year":"2005","journal-title":"Trends Mol Med"},{"key":"10.1016\/j.fsi.2012.11.042_bib33","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1016\/j.cell.2004.05.002","article-title":"Two enzymes in one: two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function","volume":"117","author":"Jang","year":"2004","journal-title":"Cell"},{"key":"10.1016\/j.fsi.2012.11.042_bib34","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1152\/ajplung.2000.279.6.L1029","article-title":"Heme oxygenase: colors of defense against cellular stress","volume":"279","author":"Otterbein","year":"2000","journal-title":"Am J Physiol Lung Cell Mol Physiol"},{"key":"10.1016\/j.fsi.2012.11.042_bib35","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/S1096-4959(03)00290-2","article-title":"Cloning of bovine peroxiredoxins\u2013gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins","volume":"136","author":"Leyens","year":"2003","journal-title":"Comp Biochem Physiol B: Biochem Mol Biol"},{"key":"10.1016\/j.fsi.2012.11.042_bib36","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/j.dci.2010.12.003","article-title":"Genomic sequences comparison and differential expression of miiuy croaker MHC class I gene, after infection by Vibrio anguillarum","volume":"35","author":"Xu","year":"2011","journal-title":"Dev Comp Immunol"},{"key":"10.1016\/j.fsi.2012.11.042_bib37","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/j.fsi.2011.06.016","article-title":"Molecular cloning, characterization and expression analysis of a miiuy croaker (Miichthys miiuy) CXC chemokine gene resembling the CXCL9\/CXCL10\/CXCL11","volume":"31","author":"Cheng","year":"2011","journal-title":"Fish Shellfish Immunol"},{"key":"10.1016\/j.fsi.2012.11.042_bib38","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.fsi.2011.02.024","article-title":"Molecular characterization of miiuy croaker CC chemokine gene and its expression following Vibrio anguillarum injection","volume":"31","author":"Cheng","year":"2011","journal-title":"Fish Shellfish Immunol"},{"key":"10.1016\/j.fsi.2012.11.042_bib39","first-page":"e23832","article-title":"Characterization of the major histocompatibility complex class II genes in Miiuy Croaker","volume":"6","author":"Xu","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1016\/j.fsi.2012.11.042_bib40","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.fsi.2011.11.033","article-title":"Molecular cloning and comprehensive characterization of cathepsin D in the Miiuy croaker Miichthys miiuy","volume":"32","author":"Liu","year":"2012","journal-title":"Fish Shellfish Immunol"},{"key":"10.1016\/j.fsi.2012.11.042_bib41","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1016\/j.fsi.2012.02.010","article-title":"An unexpected loss of domains in the conservative evolution ninth complement component in a higher teleost, Miichthys miiuy","volume":"32","author":"Meng","year":"2012","journal-title":"Fish Shellfish Immunol"},{"key":"10.1016\/j.fsi.2012.11.042_bib42","doi-asserted-by":"crossref","first-page":"e35449","DOI":"10.1371\/journal.pone.0035449","article-title":"Miiuy Croaker Hepcidin Gene and Comparative Analyses Reveal Evidence for Positive Selection","volume":"7","author":"Xu","year":"2012","journal-title":"PLoS ONE"},{"key":"10.1016\/j.fsi.2012.11.042_bib43","doi-asserted-by":"crossref","first-page":"e43936","DOI":"10.1371\/journal.pone.0043936","article-title":"Miiuy croaker transferrin gene and evidence for positive selection events reveals different evolutionary patterns","volume":"7","author":"Sun","year":"2012","journal-title":"PLoS ONE"}],"container-title":["Fish &amp; Shellfish Immunology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1050464812004457?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1050464812004457?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,2,3]],"date-time":"2022-02-03T08:44:57Z","timestamp":1643877897000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1050464812004457"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,2]]},"references-count":43,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2013,2]]}},"alternative-id":["S1050464812004457"],"URL":"https:\/\/doi.org\/10.1016\/j.fsi.2012.11.042","relation":{},"ISSN":["1050-4648"],"issn-type":[{"value":"1050-4648","type":"print"}],"subject":[],"published":{"date-parts":[[2013,2]]}}}