{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T23:17:55Z","timestamp":1773098275941,"version":"3.50.1"},"reference-count":62,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,5,1]],"date-time":"2019-05-01T00:00:00Z","timestamp":1556668800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"name":"Project of Screening of Sex-linked Markers and Sex Determination Gene for Acipenser dabryanus Based on Transcriptome Sequencing Technology","award":["2017QNJJ-013"],"award-info":[{"award-number":["2017QNJJ-013"]}]},{"DOI":"10.13039\/100012542","name":"Sichuan Science and Technology Program","doi-asserted-by":"publisher","award":["2018JY0636"],"award-info":[{"award-number":["2018JY0636"]}],"id":[{"id":"10.13039\/100012542","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012542","name":"Sichuan Science and Technology Program","doi-asserted-by":"publisher","award":["2017SZ0083"],"award-info":[{"award-number":["2017SZ0083"]}],"id":[{"id":"10.13039\/100012542","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012542","name":"Sichuan Science and Technology Program","doi-asserted-by":"publisher","award":["2016NYZ0047"],"award-info":[{"award-number":["2016NYZ0047"]}],"id":[{"id":"10.13039\/100012542","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Fish &amp; Shellfish Immunology"],"published-print":{"date-parts":[[2019,5]]},"DOI":"10.1016\/j.fsi.2019.02.050","type":"journal-article","created":{"date-parts":[[2019,2,25]],"date-time":"2019-02-25T08:10:29Z","timestamp":1551082229000},"page":"207-216","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":35,"special_numbering":"C","title":["Identification and characterization of three novel antimicrobial peptides from Acipenser dabryanus"],"prefix":"10.1016","volume":"88","author":[{"given":"Yeyu","family":"Chen","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Quan","family":"Gong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mingjiang","family":"Song","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jiansheng","family":"Lai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jiahua","family":"Sun","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ya","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.fsi.2019.02.050_bib1","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/415389a","article-title":"Antimicrobial peptides of multicellular organisms","volume":"415","author":"Zasloff","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.fsi.2019.02.050_bib2","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/j.peptides.2010.11.005","article-title":"Applications of antimicrobial peptides from fish and perspectives for the future","volume":"32","author":"Rajanbabu","year":"2011","journal-title":"Peptides"},{"key":"10.1016\/j.fsi.2019.02.050_bib3","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1038\/nri1180","article-title":"Defensins: antimicrobial peptides of innate immunity","volume":"3","author":"Ganz","year":"2003","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib4","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1038\/nrmicro1441","article-title":"The co-evolution of host cationic antimicrobial peptides and microbial resistance","volume":"4","author":"Peschel","year":"2006","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.fsi.2019.02.050_bib5","doi-asserted-by":"crossref","first-page":"265","DOI":"10.3390\/ph7030265","article-title":"Antimicrobial peptides from fish","volume":"7","author":"Massosilva","year":"2014","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.fsi.2019.02.050_bib6","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1189\/jlb.69.5.691","article-title":"Participation of mammalian defensins and cathelicidins in anti-microbial immunity: receptors and activities of human defensins and cathelicidin (LL-37)","volume":"69","author":"Yang","year":"2001","journal-title":"J. Leukoc. Biol."},{"key":"10.1016\/j.fsi.2019.02.050_bib7","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0045-2068(03)00080-4","article-title":"Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance","volume":"31","author":"Shinnar","year":"2003","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.fsi.2019.02.050_bib8","doi-asserted-by":"crossref","first-page":"10957","DOI":"10.1007\/s11033-012-1997-x","article-title":"Cathelicidins: family of antimicrobial peptides. A review","volume":"39","author":"Ko\u015bciuczuk","year":"2012","journal-title":"Mol. Biol. Rep."},{"key":"10.1016\/j.fsi.2019.02.050_bib9","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1097\/MOH.0b013e32831ac517","article-title":"The roles of cathelicidin LL-37 in immune defences and novel clinical applications","volume":"16","author":"Nijnik","year":"2009","journal-title":"Curr. Opin. Hematol."},{"key":"10.1016\/j.fsi.2019.02.050_bib10","doi-asserted-by":"crossref","first-page":"1665","DOI":"10.1172\/JCI17545","article-title":"An angiogenic role for the human peptide antibiotic LL-37\/hCAP-18","volume":"111","author":"Koczulla","year":"2003","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.fsi.2019.02.050_bib11","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1046\/j.1523-1747.2003.12069.x","article-title":"The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium","volume":"120","author":"Heilborn","year":"2003","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.fsi.2019.02.050_bib12","series-title":"Chapter 17-Cathelicidins: an Ancient Family of Fish Antimicrobial Peptides, Lessons in Immunity","first-page":"225","author":"Scocchi","year":"2016"},{"key":"10.1016\/j.fsi.2019.02.050_bib13","doi-asserted-by":"crossref","first-page":"3723","DOI":"10.1016\/j.molimm.2008.06.002","article-title":"Characterisation of cathelicidin gene family members in divergent fish species","volume":"45","author":"Maier","year":"2008","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib14","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.fsi.2011.03.005","article-title":"Identification and characterization of a novel cathelicidin from ayu, Plecoglossus altivelis","volume":"31","author":"Lu","year":"2011","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib15","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1128\/AAC.50.1.185-195.2006","article-title":"Two cathelicidin genes are present in both Rainbow Trout (Oncorhynchus mykiss) and Atlantic Salmon (Salmo salar)","volume":"50","author":"Chang","year":"2006","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.fsi.2019.02.050_bib16","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0014-5793(00)01920-7","article-title":"LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity","volume":"480","author":"Krause","year":"2000","journal-title":"FEBS Lett."},{"key":"10.1016\/j.fsi.2019.02.050_bib17","doi-asserted-by":"crossref","first-page":"7806","DOI":"10.1074\/jbc.M008922200","article-title":"Hepcidin, a urinary antimicrobial peptide synthesized in the liver","volume":"276","author":"Park","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.fsi.2019.02.050_bib18","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1016\/j.dci.2003.11.009","article-title":"Organization and expression analysis of the zebrafish hepcidin gene, an antimicrobial peptide gene conserved among vertebrates","volume":"28","author":"Shike","year":"2004","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib19","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1007\/3-540-29916-5_7","article-title":"Hepcidin-A peptide hormone at the interface of innate immunity and iron metabolism","volume":"306","author":"Ganz","year":"2006","journal-title":"Curr. Top. Microbiol."},{"key":"10.1016\/j.fsi.2019.02.050_bib20","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1182\/blood-2003-03-0672","article-title":"Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation","volume":"102","author":"Ganz","year":"2003","journal-title":"Blood"},{"key":"10.1016\/j.fsi.2019.02.050_bib21","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/bip.20900","article-title":"Structure-activity relationships in \u03b2-defensin peptides","volume":"90","author":"Taylor","year":"2010","journal-title":"Biopolymers"},{"key":"10.1016\/j.fsi.2019.02.050_bib22","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1016\/j.peptides.2005.08.018","article-title":"Recent advances in the research and development of human defensins","volume":"27","author":"Chen","year":"2006","journal-title":"Peptides"},{"key":"10.1016\/j.fsi.2019.02.050_bib23","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/S0952-7915(01)00303-X","article-title":"Defensins of vertebrate animals","volume":"14","author":"Lehrer","year":"2002","journal-title":"Curr. Opin. Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib24","doi-asserted-by":"crossref","first-page":"3131","DOI":"10.2174\/138161207782110453","article-title":"Defensin participation in innate and adaptive immunity","volume":"13","author":"Yang","year":"2007","journal-title":"Curr. Pharmaceut. Des."},{"key":"10.1016\/j.fsi.2019.02.050_bib25","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1111\/j.1365-3083.2009.02319.x","article-title":"Mucosal immunity: induction, dissemination, and effector functions","volume":"70","author":"Brandtzaeg","year":"2010","journal-title":"Scand. J. Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib26","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.fsi.2014.04.015","article-title":"Mucosal immunity and probiotics in fish","volume":"39","author":"Lazado","year":"2014","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib27","doi-asserted-by":"crossref","first-page":"525","DOI":"10.3390\/biology4030525","article-title":"The mucosal immune system of teleost fish","volume":"4","author":"Salinas","year":"2015","journal-title":"Biology"},{"key":"10.1016\/j.fsi.2019.02.050_bib28","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1016\/j.fsi.2013.09.032","article-title":"The mucosal immune system of fish: the evolution of tolerating commensals while fighting pathogens","volume":"35","author":"Gomez","year":"2013","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib29","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1038\/nature11551","article-title":"Reciprocal interactions of the intestinal microbiota and immune system","volume":"489","author":"Maynard","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.fsi.2019.02.050_bib30","doi-asserted-by":"crossref","first-page":"1768","DOI":"10.1126\/science.1195568","article-title":"Has the microbiota played a critical role in the evolution of the adaptive immune system?","volume":"330","author":"Yun","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.fsi.2019.02.050_bib31","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1006\/fsim.1998.0181","article-title":"The morphology of the immune system in teleost fishes","volume":"9","author":"Press","year":"1999","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib32","doi-asserted-by":"crossref","first-page":"1893","DOI":"10.1111\/are.12136","article-title":"Transcriptional regulation of antimicrobial peptides in mucosal tissues of Atlantic cod Gadus morhua L. in response to different stimuli","volume":"45","author":"Ruangsri","year":"2015","journal-title":"Aquacult. Res."},{"key":"10.1016\/j.fsi.2019.02.050_bib33","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1023\/A:1007399729080","article-title":"Biology and life history of Dabry's sturgeon, Acipenser dabryanus, in the Yangtze River","volume":"48","author":"Zhuang","year":"1997","journal-title":"Environ. Biol. Fish."},{"key":"10.1016\/j.fsi.2019.02.050_bib34","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1002\/ar.10080","article-title":"Structure of the conus arteriosus of the sturgeon (Acipenser naccarii) heart. I: the conus valves and the subendocardium","volume":"267","author":"Icardo","year":"2010","journal-title":"Anat. Rec."},{"key":"10.1016\/j.fsi.2019.02.050_bib35","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1007\/s10750-015-2511-y","article-title":"Discriminating Dabry's sturgeon (Acipenser dabryanus) and Chinese sturgeon (A. sinensis) based on DNA barcode and six nuclear markers","volume":"762","author":"Li","year":"2015","journal-title":"Hydrobiologia"},{"key":"10.1016\/j.fsi.2019.02.050_bib36","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1111\/jai.12597","article-title":"Initial evaluation of the release programme for Dabry's sturgeon (Acipenser dabryanus Dum\u00e9ril, 1868) in the upper Yangtze River","volume":"30","author":"Wu","year":"2015","journal-title":"J. Appl. Ichthyol."},{"key":"10.1016\/j.fsi.2019.02.050_bib37","series-title":"China Red Data Book of Endangered Animals: Pisces","first-page":"204","author":"Wang","year":"1998"},{"key":"10.1016\/j.fsi.2019.02.050_bib38","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/j.aquaculture.2018.04.010","article-title":"Pathogenesis and pathological analysis of Edwardsiella tarda from Dabry's sturgeon (Acipenser dabryanus) in China","volume":"495","author":"Yang","year":"2018","journal-title":"Aquaculture"},{"key":"10.1016\/j.fsi.2019.02.050_bib39","doi-asserted-by":"crossref","first-page":"e5389","DOI":"10.7717\/peerj.5389","article-title":"Gonadal transcriptome sequencing of the critically endangered Acipenser dabryanus to discover candidate sex-related genes","volume":"6","author":"Chen","year":"2018","journal-title":"Peerj"},{"key":"10.1016\/j.fsi.2019.02.050_bib40","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression data using real time quantitative PCR and the 2\u2013\u0394\u0394CT method","volume":"25","author":"Livak","year":"2001","journal-title":"Methods"},{"key":"10.1016\/j.fsi.2019.02.050_bib41","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0045-2068(03)00080-4","article-title":"Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance","volume":"31","author":"Shinnar","year":"2003","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.fsi.2019.02.050_bib42","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1093\/protein\/gzh013","article-title":"Prediction of proprotein convertase cleavage sites","volume":"17","author":"Duckert","year":"2004","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.fsi.2019.02.050_bib43","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1016\/S0145-305X(03)00036-3","article-title":"Identification and expression analysis of hepcidin-like antimicrobial peptides in bony fish","volume":"27","author":"Liebscher","year":"2003","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib44","first-page":"2232","article-title":"Bass hepcidin is a novel antimicrobial peptide induced by bacterial challenge","volume":"269","author":"Westerman","year":"2010","journal-title":"FEBS J."},{"key":"10.1016\/j.fsi.2019.02.050_bib45","doi-asserted-by":"crossref","first-page":"2333","DOI":"10.1016\/j.molimm.2007.11.007","article-title":"The antimicrobial peptide hepcidin exerts an important role in the innate immunity against bacteria in the bony fish gilthead seabream","volume":"45","author":"Cuesta","year":"2008","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib46","doi-asserted-by":"crossref","first-page":"3358","DOI":"10.1016\/j.molimm.2009.07.018","article-title":"Characterization of three novel beta-defensin antimicrobial peptides in rainbow trout (Oncorhynchus mykiss)","volume":"46","author":"Casadei","year":"2009","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib47","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/j.fsi.2013.04.049","article-title":"Identification, expression and bioactivity of Paramisgurnus dabryanus \u03b2-defensin that might be involved in immune defense against bacterial infection","volume":"35","author":"Chen","year":"2013","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib48","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/j.fsi.2012.04.011","article-title":"Identification and characterization of a hepcidin from half-smooth tongue sole Cynoglossus semilaevis","volume":"33","author":"Wang","year":"2012","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib49","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1016\/j.fsi.2013.07.001","article-title":"Molecular characterization of hepcidin gene in common carp (Cyprinus carpio L.) and its expression pattern responding to bacterial challenge","volume":"35","author":"Li","year":"2013","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib50","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.fsi.2006.04.004","article-title":"Molecular cloning and expression analysis of a hepcidin antimicrobial peptide gene from turbot (Scophthalmus maximus)","volume":"22","author":"Chen","year":"2007","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib51","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1002\/jmor.10385","article-title":"Cytomorphological alterations of the thymus, spleen, head-kidney, and liver in cardinal fish (Apogonidae, Teleostei) as bioindicators of stress","volume":"267","author":"Fishelson","year":"2010","journal-title":"J. Morphol."},{"key":"10.1016\/j.fsi.2019.02.050_bib52","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/j.molimm.2017.03.009","article-title":"Identification and characterization of a \u03b2-defensin gene involved in the immune defense response of channel catfish, Ictalurus punctatus","volume":"85","author":"Zhu","year":"2017","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib53","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1034\/j.1600-0714.2001.300305.x","article-title":"Expression profile of human defensins and antimicrobial proteins in oral tissues","volume":"30","author":"Dunsche","year":"2010","journal-title":"J. Oral Pathol. Med."},{"key":"10.1016\/j.fsi.2019.02.050_bib54","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1136\/bjo.83.6.737","article-title":"Antimicrobial defensin peptides of the human ocular surface","volume":"83","author":"Haynes","year":"1999","journal-title":"Br. J. Ophthalmol."},{"key":"10.1016\/j.fsi.2019.02.050_bib55","doi-asserted-by":"crossref","first-page":"1750","DOI":"10.1016\/S0140-6736(05)63574-X","article-title":"Expression of natural peptide antibiotics in human skin","volume":"350","author":"Fulton","year":"1997","journal-title":"Lancet"},{"key":"10.1016\/j.fsi.2019.02.050_bib56","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1016\/j.dci.2008.11.006","article-title":"Antimicrobial activity-specific to Gram-negative bacteria and immune modulation-mediated NF-kappaB and Sp1 of a medaka beta-defensin","volume":"33","author":"Zhao","year":"2009","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib57","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.aanat.2010.01.006","article-title":"Functional relationship between cationic amino acid transporters and beta-defensins: implications for dry skin diseases and the dry eye","volume":"192","author":"J\u00e4ger","year":"2010","journal-title":"Ann. Anat."},{"key":"10.1016\/j.fsi.2019.02.050_bib58","doi-asserted-by":"crossref","first-page":"8054","DOI":"10.4049\/jimmunol.0902140","article-title":"Beta-defensins 2 and 3 together promote resistance to Pseudomonas aeruginosa keratitis","volume":"183","author":"Wu","year":"2009","journal-title":"J. Immunol."},{"key":"10.1016\/j.fsi.2019.02.050_bib59","doi-asserted-by":"crossref","first-page":"16430","DOI":"10.1074\/jbc.271.27.16430","article-title":"Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils","volume":"271","author":"Selsted","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.fsi.2019.02.050_bib60","doi-asserted-by":"crossref","first-page":"26249","DOI":"10.1074\/jbc.274.37.26249","article-title":"Cloning and expression of bovine neutrophil beta-defensins. Biosynthetic profile during neutrophilic maturation and localization of mature peptide to novel cytoplasmic dense granules","volume":"274","author":"Yount","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.fsi.2019.02.050_bib61","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.gene.2015.04.025","article-title":"\u03b2-defensin in Nile tilapia (Oreochromis niloticus): sequence, tissue expression, and anti-bacterial activity of synthetic peptides","volume":"566","author":"Dong","year":"2015","journal-title":"Gene"},{"key":"10.1016\/j.fsi.2019.02.050_bib62","first-page":"430","article-title":"Characterization and expression pattern of a novel \u03b2-defensin in common carp (Cyprinus carpio L.): implications for its role in mucosal immunity","volume":"78","author":"Li","year":"2014","journal-title":"J. Agr. Chem. Soc. Jap."}],"container-title":["Fish &amp; Shellfish Immunology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S105046481930124X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S105046481930124X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,9,13]],"date-time":"2023-09-13T22:32:57Z","timestamp":1694644377000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S105046481930124X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,5]]},"references-count":62,"alternative-id":["S105046481930124X"],"URL":"https:\/\/doi.org\/10.1016\/j.fsi.2019.02.050","relation":{},"ISSN":["1050-4648"],"issn-type":[{"value":"1050-4648","type":"print"}],"subject":[],"published":{"date-parts":[[2019,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Identification and characterization of three novel antimicrobial peptides from Acipenser dabryanus","name":"articletitle","label":"Article Title"},{"value":"Fish & Shellfish Immunology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.fsi.2019.02.050","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}