{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,8]],"date-time":"2026-05-08T11:14:55Z","timestamp":1778238895586,"version":"3.51.4"},"reference-count":46,"publisher":"Springer Science and Business Media LLC","issue":"4","license":[{"start":{"date-parts":[[2018,5,16]],"date-time":"2018-05-16T00:00:00Z","timestamp":1526428800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Biol Rep"],"published-print":{"date-parts":[[2018,8]]},"DOI":"10.1007\/s11033-018-4177-9","type":"journal-article","created":{"date-parts":[[2018,5,16]],"date-time":"2018-05-16T08:01:30Z","timestamp":1526457690000},"page":"419-432","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Characterization of xanthine dehydrogenase and aldehyde oxidase of Marsupenaeus japonicus and their response to microbial pathogen"],"prefix":"10.1007","volume":"45","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9388-8202","authenticated-orcid":false,"given":"Yo","family":"Okamura","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6969-5558","authenticated-orcid":false,"given":"Mari","family":"Inada","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2924-9670","authenticated-orcid":false,"given":"Gehad Elsaid","family":"Elshopakey","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Toshiaki","family":"Itami","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2018,5,16]]},"reference":[{"issue":"1","key":"4177_CR1","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1016\/j.biocel.2006.07.001","volume":"39","author":"M Valko","year":"2007","unstructured":"Valko M, Leibfritz D, Moncol J, Cronin MT, Mazur M, Telser J (2007) Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol 39(1):44\u201384. https:\/\/doi.org\/10.1016\/j.biocel.2006.07.001","journal-title":"Int J Biochem Cell Biol"},{"issue":"3","key":"4177_CR2","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1186\/1467-4866-6-47","volume":"6","author":"CA Cohn","year":"2005","unstructured":"Cohn CA (2005) Quantifying hydrogen peroxide in iron-containing solutions using leuco crystal violet. Geochem Trans 6(3):47. https:\/\/doi.org\/10.1063\/1.1935449","journal-title":"Geochem Trans"},{"issue":"10","key":"4177_CR3","doi-asserted-by":"publisher","first-page":"6520","DOI":"10.1074\/jbc.M807564200","volume":"284","author":"JA Graves","year":"2008","unstructured":"Graves JA, Metukuri M, Scott D, Rothermund K, Prochownik EV (2008) Regulation of reactive oxygen species homeostasis by peroxiredoxins and c-Myc. J Biol Chem 284(10):6520\u20136529. https:\/\/doi.org\/10.1074\/jbc.m807564200","journal-title":"J Biol Chem"},{"issue":"2","key":"4177_CR4","doi-asserted-by":"publisher","first-page":"192","DOI":"10.1007\/s00018-003-3206-5","volume":"61","author":"P Chelikani","year":"2004","unstructured":"Chelikani P, Fita I, Loewen PC (2004) Diversity of structures and properties among catalases. Cell Mol Life Sci 61(2):192\u2013208. https:\/\/doi.org\/10.1007\/s00018-003-3206-5","journal-title":"Cell Mol Life Sci"},{"key":"4177_CR5","doi-asserted-by":"publisher","first-page":"1287","DOI":"10.1016\/S0891-5849(01)00724-9","volume":"31","author":"J Nordberg","year":"2001","unstructured":"Nordberg J, Arn\u00e9r ESJ (2001) Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 31:1287\u20131312","journal-title":"Free Radic Biol Med"},{"key":"4177_CR6","first-page":"158","volume":"70","author":"DE Paglia","year":"1967","unstructured":"Paglia DE, Valentine WN (1967) Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70:158\u2013169","journal-title":"J Lab Clin Med"},{"issue":"11","key":"4177_CR7","doi-asserted-by":"publisher","first-page":"1233","DOI":"10.4315\/0362-028X-59.11.1233","volume":"59","author":"BJ Juven","year":"1996","unstructured":"Juven BJ, Pierson MD (1996) Antibacterial effects of hydrogen peroxide and methods for its detection and quantitation. J Food Prot 59(11):1233\u20131241. https:\/\/doi.org\/10.4315\/0362-028x-59.11.1233","journal-title":"J Food Prot"},{"key":"4177_CR8","first-page":"1438","volume":"63","author":"VP Skulachev","year":"1998","unstructured":"Skulachev VP (1998) Possible role of reactive oxygen species in antiviral defense. Biochem 63:1438\u20131440","journal-title":"Biochem"},{"issue":"2","key":"4177_CR9","doi-asserted-by":"publisher","first-page":"128","DOI":"10.5483\/BMBRep.2005.38.2.128","volume":"38","author":"S Iwanaga","year":"2005","unstructured":"Iwanaga S, Lee B (2005) Recent advances in the innate immunity of invertebrate animals. BMB Rep 38(2):128\u2013150. https:\/\/doi.org\/10.5483\/bmbrep.2005.38.2.128","journal-title":"BMB Rep"},{"issue":"10","key":"4177_CR10","doi-asserted-by":"publisher","first-page":"1295","DOI":"10.1016\/S0965-1748(02)00092-9","volume":"32","author":"M Lavine","year":"2002","unstructured":"Lavine M, Strand M (2002) Insect hemocytes and their role in immunity. Insect Biochem Mol Biol 32(10):1295\u20131309. https:\/\/doi.org\/10.1016\/s0965-1748(02)00092-9","journal-title":"Insect Biochem Mol Biol"},{"issue":"12","key":"4177_CR11","doi-asserted-by":"publisher","first-page":"2049","DOI":"10.1124\/dmd.114.060368","volume":"42","author":"N Manevski","year":"2014","unstructured":"Manevski N, Balavenkatraman KK, Bertschi B, Swart P, Walles M, Camenisch G, Litherland K (2014) Aldehyde oxidase activity in fresh human skin. Drug Metab Dispos 42(12):2049\u20132057. https:\/\/doi.org\/10.1124\/dmd.114.060368","journal-title":"Drug Metab Dispos"},{"issue":"3","key":"4177_CR12","doi-asserted-by":"publisher","first-page":"1006","DOI":"10.1128\/JB.01281-08","volume":"191","author":"SD Pope","year":"2008","unstructured":"Pope SD, Chen L, Stewart V (2008) Purine utilization by Klebsiella oxytoca M5al: genes for ring-oxidizing and -opening enzymes. J Bacteriol 191(3):1006\u20131017. https:\/\/doi.org\/10.1128\/jb.01281-08","journal-title":"J Bacteriol"},{"issue":"1","key":"4177_CR13","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1042\/bj20030121","volume":"372","author":"E Garattini","year":"2003","unstructured":"Garattini E, Mendel R, Rom\u00e3o MJ, Wright R, Terao M (2003) Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology. Biochem J 372(1):15\u201332. https:\/\/doi.org\/10.1042\/bj20030121","journal-title":"Biochem J"},{"issue":"4","key":"4177_CR14","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1002\/biof.1362","volume":"43","author":"A Llamas","year":"2017","unstructured":"Llamas A, Chamizo-Ampudia A, Tejada-Jimenez M, Galvan A, Fernandez E (2017) The molybdenum cofactor enzyme mARC: moonlighting or promiscuous enzyme? BioFactors 43(4):486\u2013494. https:\/\/doi.org\/10.1002\/biof.1362","journal-title":"BioFactors"},{"key":"4177_CR15","doi-asserted-by":"publisher","DOI":"10.1016\/s1874-6047(08)60229-2","author":"R Bray","year":"1975","unstructured":"Bray R (1975) 6 Molybdenum iron-sulfur flauin hydroxylases and related enzymes. Enzymes. https:\/\/doi.org\/10.1016\/s1874-6047(08)60229-2","journal-title":"Enzymes"},{"issue":"3","key":"4177_CR16","doi-asserted-by":"publisher","first-page":"589","DOI":"10.1113\/jphysiol.2003.055913","volume":"555","author":"CE Berry","year":"2004","unstructured":"Berry CE, Hare JM (2004) Xanthine oxidoreductase and cardiovascular disease: molecular mechanisms and pathophysiological implications. J Physiol 555(3):589\u2013606. https:\/\/doi.org\/10.1113\/jphysiol.2003.055913","journal-title":"J Physiol"},{"issue":"13","key":"4177_CR17","doi-asserted-by":"publisher","first-page":"3278","DOI":"10.1111\/j.1742-4658.2008.06489.x","volume":"275","author":"T Nishino","year":"2008","unstructured":"Nishino T, Okamoto K, Eger BT, Pai EF, Nishino T (2008) Mammalian xanthine oxidoreductase\u2014mechanism of transition from xanthine dehydrogenase to xanthine oxidase. FEBS J 275(13):3278\u20133289. https:\/\/doi.org\/10.1111\/j.1742-4658.2008.06489.x","journal-title":"FEBS J"},{"issue":"1","key":"4177_CR18","doi-asserted-by":"publisher","first-page":"754","DOI":"10.1186\/1471-2164-15-754","volume":"15","author":"E Ng\u2019oma","year":"2014","unstructured":"Ng\u2019oma E, Groth M, Ripa R, Platzer M, Cellerino A (2014) Transcriptome profiling of natural dichromatism in the annual fishes Nothobranchius furzeri and Nothobranchius kadleci. BMC Genomics 15(1):754. https:\/\/doi.org\/10.1186\/1471-2164-15-754","journal-title":"BMC Genomics"},{"issue":"1","key":"4177_CR19","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1534\/genetics.107.080754","volume":"178","author":"X Zhou","year":"2008","unstructured":"Zhou X, Riddiford LM (2008) rosy function is required for juvenile hormone effects in Drosophila melanogaster. Genetics 178(1):273\u2013281. https:\/\/doi.org\/10.1534\/genetics.107.080754","journal-title":"Genetics"},{"issue":"4","key":"4177_CR20","doi-asserted-by":"publisher","first-page":"753","DOI":"10.1007\/s00204-016-1683-1","volume":"90","author":"M Terao","year":"2016","unstructured":"Terao M, Rom\u00e3o MJ, Leimk\u00fchler S, Bolis M, Fratelli M, Coelho C, Garattini E (2016) Structure and function of mammalian aldehyde oxidases. Arch Toxicol 90(4):753\u2013780. https:\/\/doi.org\/10.1007\/s00204-016-1683-1","journal-title":"Arch Toxicol"},{"issue":"10","key":"4177_CR21","doi-asserted-by":"publisher","first-page":"1807","DOI":"10.1007\/s00018-012-1229-5","volume":"70","author":"M Kurosaki","year":"2012","unstructured":"Kurosaki M, Bolis M, Fratelli M, Barzago MM, Pattini L, Perretta G, Garattini E (2012) Structure and evolution of vertebrate aldehyde oxidases: from gene duplication to gene suppression. Cell Mol Life Sci 70(10):1807\u20131830. https:\/\/doi.org\/10.1007\/s00018-012-1229-5","journal-title":"Cell Mol Life Sci"},{"issue":"12","key":"4177_CR22","doi-asserted-by":"publisher","first-page":"2201","DOI":"10.1242\/jeb.102129","volume":"217","author":"Z Marelja","year":"2014","unstructured":"Marelja Z, Dambowsky M, Bolis M, Georgiou ML, Garattini E, Missirlis F, Leimkuhler S (2014) The four aldehyde oxidases of Drosophila melanogaster have different gene expression patterns and enzyme substrate specificities. J Exp Biol 217(12):2201\u20132211. https:\/\/doi.org\/10.1242\/jeb.102129","journal-title":"J Exp Biol"},{"issue":"10","key":"4177_CR23","doi-asserted-by":"publisher","first-page":"893","DOI":"10.1016\/j.dci.2006.01.002","volume":"30","author":"G Gomezanduro","year":"2006","unstructured":"Gomezanduro G, Barillasmury C, Peregrinouriarte A, Gupta L, Gollasgalvan T, Hernandezlopez J, Yepizplascencia G (2006) The cytosolic manganese superoxide dismutase from the shrimp Litopenaeus vannamei: molecular cloning and expression. Dev Comp Immunol 30(10):893\u2013900. https:\/\/doi.org\/10.1016\/j.dci.2006.01.002","journal-title":"Dev Comp Immunol"},{"issue":"1\u20133","key":"4177_CR24","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1016\/S0044-8486(00)00420-8","volume":"191","author":"M Mu\u00f1oz","year":"2000","unstructured":"Mu\u00f1oz M, Cede\u00f1o R, Rodr\u00edguez J, Van der Knaap WP, Mialhe E, Bach\u00e8re E (2000) Measurement of reactive oxygen intermediate production in haemocytes of the penaeid shrimp, Penaeus vannamei. Aquaculture 191(1\u20133):89\u2013107. https:\/\/doi.org\/10.1016\/s0044-8486(00)00420-8","journal-title":"Aquaculture"},{"issue":"3","key":"4177_CR25","doi-asserted-by":"publisher","first-page":"381","DOI":"10.1111\/jwas.12406","volume":"48","author":"AG Tacon","year":"2017","unstructured":"Tacon AG (2017) Biosecure shrimp feeds and feeding practices: guidelines for future development. J World Aquac Soc 48(3):381\u2013392. https:\/\/doi.org\/10.1111\/jwas.12406","journal-title":"J World Aquac Soc"},{"key":"4177_CR26","doi-asserted-by":"publisher","first-page":"194","DOI":"10.1016\/j.aquaculture.2015.10.036","volume":"452","author":"MG Bulbul","year":"2016","unstructured":"Bulbul MG, Kader MA, Asaduzzaman M, Ambak MA, Chowdhury AJ, Hossain MS, Koshio S (2016) Can canola meal and soybean meal be used as major dietary protein sources for kuruma shrimp Marsupenaeus japonicus? Aquaculture 452:194\u2013199. https:\/\/doi.org\/10.1016\/j.aquaculture.2015.10.036","journal-title":"Aquaculture"},{"key":"4177_CR27","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1016\/j.aquaculture.2015.10.028","volume":"452","author":"S Thitamadee","year":"2016","unstructured":"Thitamadee S, Prachumwat A, Srisala J, Jaroenlak P, Salachan PV, Sritunyalucksana K, Itsathitphaisarn O (2016) Review of current disease threats for cultivated penaeid shrimp in Asia. Aquaculture 452:69\u201387. https:\/\/doi.org\/10.1016\/j.aquaculture.2015.10.028","journal-title":"Aquaculture"},{"key":"4177_CR28","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1016\/j.cbpa.2016.04.019","volume":"199","author":"A Garc\u00eda-Triana","year":"2016","unstructured":"Garc\u00eda-Triana A, Peregrino-Uriarte AB, Yepiz-Plascencia G (2016) Selenoprotein M gene expression, peroxidases activity and hydrogen peroxide concentration are differentially regulated in gill and hepatopancreas of the white shrimp Litopenaeus vannamei during hypoxia and reoxygenation. Comp Biochem Physiol Part A Mol Integr Physiol 199:14\u201320. https:\/\/doi.org\/10.1016\/j.cbpa.2016.04.019","journal-title":"Comp Biochem Physiol Part A Mol Integr Physiol"},{"issue":"1","key":"4177_CR29","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1007\/BF00037594","volume":"39","author":"B Messner","year":"1994","unstructured":"Messner B, Boll M (1994) Cell suspension cultures of spruce (Picea abies): inactivation of extracellular enzymes by fungal elicitor-induced transient release of hydrogen peroxide (oxidative burst). Plant Cell Tissue Organ Cult 39(1):69\u201378. https:\/\/doi.org\/10.1007\/bf00037594","journal-title":"Plant Cell Tissue Organ Cult"},{"key":"4177_CR30","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkr931","author":"I Letunic","year":"2011","unstructured":"Letunic I, Doerks T, Bork P (2011) SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res. https:\/\/doi.org\/10.1093\/nar\/gkr931","journal-title":"Nucleic Acids Res"},{"key":"4177_CR31","doi-asserted-by":"crossref","first-page":"24642","DOI":"10.1016\/S0021-9258(19)74514-1","volume":"268","author":"K Kobayashi","year":"1993","unstructured":"Kobayashi K, Miki M, Okamoto K, Nishino T (1993) Electron transfer process in milk xanthine dehydrogenase as studied by pulse radiolysis. J Biol Chem 268:24642\u201324646","journal-title":"J Biol Chem"},{"key":"4177_CR32","doi-asserted-by":"crossref","first-page":"4363","DOI":"10.1016\/S0021-9258(19)42428-9","volume":"249","author":"JS Olson","year":"1974","unstructured":"Olson JS, Ballou DP, Palmer G, Massey V (1974) The mechanism of action of xanthine oxidase. J Biol Chem 249:4363\u20134382","journal-title":"J Biol Chem"},{"key":"4177_CR33","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1016\/S0021-9258(19)45673-1","volume":"247","author":"M Kanda","year":"1972","unstructured":"Kanda M, Brady FO, Rajagopalan KV, Handler P (1972) Studies on the dissociation of flavin adenine dinucleotide from metalloflavoproteins. J Biol Chem 247:765\u2013 70","journal-title":"J Biol Chem"},{"key":"4177_CR34","doi-asserted-by":"crossref","first-page":"1692","DOI":"10.1016\/S0021-9258(18)91739-4","volume":"244","author":"H Komai","year":"1969","unstructured":"Komai H, Massey V, Palmer G (1969) The preparation and properties of deflavo xanthine oxidase. J Biol Chem 244:1692\u20131700","journal-title":"J Biol Chem"},{"issue":"6","key":"4177_CR35","doi-asserted-by":"publisher","first-page":"774","DOI":"10.1016\/S0891-5849(02)00956-5","volume":"33","author":"R Harrison","year":"2002","unstructured":"Harrison R (2002) Structure and function of xanthine oxidoreductase: where are we now? Free Radic Biol Med 33(6):774\u2013797. https:\/\/doi.org\/10.1016\/s0891-5849(02)00956-5","journal-title":"Free Radic Biol Med"},{"issue":"22","key":"4177_CR36","doi-asserted-by":"publisher","first-page":"10690","DOI":"10.1073\/pnas.90.22.10690","volume":"90","author":"RM Wright","year":"1993","unstructured":"Wright RM, Vaitaitis GM, Wilson CM, Repine TB, Terada LS, Repine JE (1993) cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase\/xanthine oxidase. Proc Natl Acad Sci USA 90(22):10690\u201310694. https:\/\/doi.org\/10.1073\/pnas.90.22.10690","journal-title":"Proc Natl Acad Sci USA"},{"issue":"4","key":"4177_CR37","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1007\/s11357-001-0020-6","volume":"24","author":"YS Kim","year":"2001","unstructured":"Kim YS, Nam HJ, Chung HY, Kim ND, Ryu JH, Lee WJ, Yoo MA (2001) Role of xanthine dehydrogenase and aging on the innate immune response of Drosophila. J Am Aging Assoc 24(4):187\u2013193. https:\/\/doi.org\/10.1007\/s11357-001-0020-6","journal-title":"J Am Aging Assoc"},{"issue":"13","key":"4177_CR38","doi-asserted-by":"publisher","first-page":"8545","DOI":"10.1074\/jbc.M507349200","volume":"281","author":"KJ Seymour","year":"2006","unstructured":"Seymour KJ, Roberts LE, Fini MA, Parmley LA, Oustitch TL, Wright RM (2006) Stress activation of mammary epithelial cell xanthine oxidoreductase is mediated by p38 MAPK and CCAAT\/enhancer-binding protein-\u03b2. J Biol Chem 281(13):8545\u20138558. https:\/\/doi.org\/10.1074\/jbc.m507349200","journal-title":"J Biol Chem"},{"issue":"3","key":"4177_CR39","doi-asserted-by":"publisher","first-page":"907","DOI":"10.1016\/j.aspen.2017.06.001","volume":"20","author":"Y Zhang","year":"2017","unstructured":"Zhang Y, Wang W, Li M, Li S, Liu S (2017) Identification of putative carboxylesterase and aldehyde oxidase genes from the antennae of the rice leaffolder, Cnaphalocrocis medinalis (Lepidoptera: Pyralidae). J Asia Pac Entomol 20(3):907\u2013913. https:\/\/doi.org\/10.1016\/j.aspen.2017.06.001","journal-title":"J Asia Pac Entomol"},{"issue":"5","key":"4177_CR40","doi-asserted-by":"publisher","first-page":"485","DOI":"10.1016\/j.fsi.2008.07.010","volume":"25","author":"S Pongsomboon","year":"2008","unstructured":"Pongsomboon S, Wongpanya R, Tang S, Chalorsrikul A, Tassanakajon A (2008) Abundantly expressed transcripts in the lymphoid organ of the black tiger shrimp, Penaeus monodon, and their implication in immune function. Fish Shellfish Immunol 25(5):485\u2013493. https:\/\/doi.org\/10.1016\/j.fsi.2008.07.010","journal-title":"Fish Shellfish Immunol"},{"issue":"4","key":"4177_CR41","doi-asserted-by":"publisher","first-page":"1291","DOI":"10.1016\/j.bbrc.2014.06.126","volume":"450","author":"MR Kamli","year":"2014","unstructured":"Kamli MR, Kim J, Pokharel S, Jan AT, Lee EJ, Choi I (2014) Expressional studies of the aldehyde oxidase (AOX1) gene during myogenic differentiation in C2C12 cells. Biochem Biophys Res Commun 450(4):1291\u20131296. https:\/\/doi.org\/10.1016\/j.bbrc.2014.06.126","journal-title":"Biochem Biophys Res Commun"},{"issue":"1","key":"4177_CR42","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1016\/j.abb.2006.12.032","volume":"460","author":"TK Kundu","year":"2007","unstructured":"Kundu TK, Hille R, Velayutham M, Zweier JL (2007) Characterization of superoxide production from aldehyde oxidase: an important source of oxidants in biological tissues. Arch Biochem Biophys 460(1):113\u2013121. https:\/\/doi.org\/10.1016\/j.abb.2006.12.032","journal-title":"Arch Biochem Biophys"},{"key":"4177_CR43","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1016\/j.plaphy.2016.09.001","volume":"109","author":"TM Yergaliyev","year":"2016","unstructured":"Yergaliyev TM, Nurbekova Z, Mukiyanova G, Akbassova A, Sutula M, Zhangazin S, Omarov RT (2016) The involvement of ROS producing aldehyde oxidase in plant response to Tombusvirus infection. Plant Physiol Biochem 109:36\u201344. https:\/\/doi.org\/10.1016\/j.plaphy.2016.09.001","journal-title":"Plant Physiol Biochem"},{"issue":"2","key":"4177_CR44","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1016\/j.fsi.2012.11.026","volume":"34","author":"M Inada","year":"2013","unstructured":"Inada M, Kihara K, Kono T, Sudhakaran R, Mekata T, Sakai M, Itami T (2013) Deciphering of the dual oxidase (Nox family) gene from kuruma shrimp, Marsupenaeus japonicus: full-length cDNA cloning and characterization. Fish Shellfish Immunol 34(2):471\u2013485. https:\/\/doi.org\/10.1016\/j.fsi.2012.11.026","journal-title":"Fish Shellfish Immunol"},{"issue":"2","key":"4177_CR45","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1093\/aob\/mcf118","volume":"91","author":"O Blokhina","year":"2003","unstructured":"Blokhina O (2003) Antioxidants, oxidative damage and oxygen deprivation stress: a review. Ann Bot 91(2):179\u2013194. https:\/\/doi.org\/10.1093\/aob\/mcf118","journal-title":"Ann Bot"},{"issue":"8","key":"4177_CR46","doi-asserted-by":"publisher","first-page":"865","DOI":"10.1016\/j.dci.2011.03.020","volume":"35","author":"M Arbi","year":"2011","unstructured":"Arbi M, Pouliliou S, Lampropoulou M, Marmaras VJ, Tsakas S (2011) Hydrogen peroxide is produced by E. coli challenged haemocytes and regulates phagocytosis, in the medfly Ceratitis capitata. The active role of superoxide dismutase. Dev Comp Immunol 35(8):865\u2013871. https:\/\/doi.org\/10.1016\/j.dci.2011.03.020","journal-title":"Dev Comp Immunol"}],"container-title":["Molecular Biology Reports"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s11033-018-4177-9\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11033-018-4177-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11033-018-4177-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,7,4]],"date-time":"2025-07-04T15:17:56Z","timestamp":1751642276000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s11033-018-4177-9"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,5,16]]},"references-count":46,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2018,8]]}},"alternative-id":["4177"],"URL":"https:\/\/doi.org\/10.1007\/s11033-018-4177-9","relation":{},"ISSN":["0301-4851","1573-4978"],"issn-type":[{"value":"0301-4851","type":"print"},{"value":"1573-4978","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,5,16]]},"assertion":[{"value":"9 December 2017","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"28 March 2018","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"16 May 2018","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Compliance with ethical standards"}},{"value":"No potential conflict of interest are disclosed.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}},{"value":"The kuruma shrimp that our target species in this study is edible shrimp in Japan. So, this study is not applicable study in this item. However, before dissecting, the kuruma shrimp was immersed into the iced water for around 5 mm into fall into suspended animation.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Research involving human participants and\/or animals"}},{"value":"We agree that the information in this study is disclosed.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Informed consent"}}]}}