{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,4]],"date-time":"2025-11-04T08:38:28Z","timestamp":1762245508082,"version":"build-2065373602"},"reference-count":67,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31802335"],"award-info":[{"award-number":["31802335"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Developmental &amp; Comparative Immunology"],"published-print":{"date-parts":[[2025,5]]},"DOI":"10.1016\/j.dci.2025.105387","type":"journal-article","created":{"date-parts":[[2025,5,6]],"date-time":"2025-05-06T02:43:35Z","timestamp":1746499415000},"page":"105387","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Characterization, expression profiling, and immunological role of Cathepsin D in Sebastes schlegelii during bacterial infection"],"prefix":"10.1016","volume":"167","author":[{"given":"Xuan","family":"Xu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yiying","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xingchun","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pei","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fengjun","family":"Lin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chonghui","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiaoxu","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chao","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9094-5168","authenticated-orcid":false,"given":"Qiang","family":"Fu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib1","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1186\/s40425-019-0498-z","article-title":"Immunotherapy of triple-negative breast cancer with cathepsin D-targeting antibodies","volume":"7","author":"Ashraf","year":"2019","journal-title":"J. Immunother. Cancer"},{"issue":"9","key":"10.1016\/j.dci.2025.105387_bib2","doi-asserted-by":"crossref","first-page":"5406","DOI":"10.1074\/jbc.M504670200","article-title":"Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L","volume":"281","author":"Baechle","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"13","key":"10.1016\/j.dci.2025.105387_bib3","doi-asserted-by":"crossref","first-page":"1967","DOI":"10.1038\/sj.onc.1209221","article-title":"Overexpression of both catalytically active and -inactive cathepsin D by cancer cells enhances apoptosis-dependent chemo-sensitivity","volume":"25","author":"Beaujouin","year":"2006","journal-title":"Oncogene"},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib66","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.critrevonc.2008.02.008","article-title":"Cathepsin D--many functions of one aspartic protease","volume":"68","author":"Benes","year":"2008","journal-title":"Critical reviews in oncology\/hematology"},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib4","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.ibmb.2005.10.003","article-title":"Molecular cloning and functional characterization of an aspartic protease from the hard tick Haemaphysalis longicornis","volume":"36","author":"Boldbaatar","year":"2006","journal-title":"Insect Biochem. Mol. Biol."},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib5","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.bi.56.070187.002001","article-title":"Intracellular proteases","volume":"56","author":"Bond","year":"1987","journal-title":"Annu. Rev. Biochem."},{"issue":"2","key":"10.1016\/j.dci.2025.105387_bib6","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.exppara.2005.09.008","article-title":"Trypanosoma cruzi: effects of infection on cathepsin D activity in the midgut of Rhodnius prolixus","volume":"112","author":"Borges","year":"2006","journal-title":"Exp. Parasitol."},{"key":"10.1016\/j.dci.2025.105387_bib7","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1016\/j.fsi.2018.10.046","article-title":"Characterization, expression profiling and functional characterization of cathepsin Z (CTSZ) in turbot (Scophthalmus maximus L.)","volume":"84","author":"Cai","year":"2018","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.dci.2025.105387_bib8","doi-asserted-by":"crossref","first-page":"1078","DOI":"10.1016\/j.fsi.2020.09.015","article-title":"Full length transcriptome profiling reveals novel immune-related genes in black rockfish (Sebastes schlegelii)","volume":"106","author":"Cao","year":"2020","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.dci.2025.105387_bib9","article-title":"Characterization of the immune roles of cathepsin L in turbot (Scophthalmus maximus L.) mucosal immunity","volume":"97","author":"Chen","year":"2019","journal-title":"Fish Shellfish Immunol."},{"issue":"6","key":"10.1016\/j.dci.2025.105387_bib10","doi-asserted-by":"crossref","first-page":"1270","DOI":"10.1016\/j.fsi.2011.09.012","article-title":"Identification and expressional analysis of two cathepsins from half-smooth tongue sole (Cynoglossus semilaevis)","volume":"31","author":"Chen","year":"2011","journal-title":"Fish Shellfish Immunol."},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib11","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.fsi.2014.07.013","article-title":"Cloning, characterisation, and expression analysis of the cathepsin D gene from rock bream (Oplegnathus fasciatus)","volume":"40","author":"Choi","year":"2014","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.dci.2025.105387_bib12","article-title":"Diverse regulatory roles for lysosomal proteases in the immune response","volume":"11","author":"Colbert","year":"2009","journal-title":"Eur. J. Immunol."},{"key":"10.1016\/j.dci.2025.105387_bib13","doi-asserted-by":"crossref","DOI":"10.4414\/smw.2010.12734","article-title":"Cathepsins and their involvement in immune responses","volume":"140","author":"Conus","year":"2010","journal-title":"Swiss Med. Wkly."},{"issue":"1\u20132","key":"10.1016\/j.dci.2025.105387_bib14","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.vetmic.2013.06.025","article-title":"Virulence, genomic features, and plasticity of Aeromonas salmonicida subsp. salmonicida, the causative agent of fish furunculosis","volume":"169","author":"Dallaire-Dufresne","year":"2014","journal-title":"Vet. Microbiol."},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib15","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.margen.2009.03.001","article-title":"Aspartic proteinases in Antarctic fish","volume":"2","author":"De Luca","year":"2009","journal-title":"Mar Genom."},{"issue":"12","key":"10.1016\/j.dci.2025.105387_bib16","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1080\/14728222.2016.1252334","article-title":"Cathepsin D as a therapeutic target in Alzheimer's disease","volume":"20","author":"Di Domenico","year":"2016","journal-title":"Expert Opin. Ther. Targets"},{"key":"10.1016\/j.dci.2025.105387_bib17","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.vetpar.2008.03.017","article-title":"Immunodiagnostic\/ protective role of Cathepsin L cysteine proteinase secreted by Fasciola species","volume":"154","author":"Dixit","year":"2008","journal-title":"Veterinary Parasitology"},{"key":"10.1016\/j.dci.2025.105387_bib18","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/j.fsi.2016.11.013","article-title":"The expression signatures of neuronal nitric oxide synthase (NOS1) in turbot (Scophthalmus maximus L.) mucosal surfaces against bacterial challenge","author":"Dong","year":"2016","journal-title":"Fish Shellfish Immunol."},{"issue":"5","key":"10.1016\/j.dci.2025.105387_bib67","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1016\/j.fsi.2012.09.012","article-title":"Molecular cloning, characterization and expression of cathepsin D from grass carp (Ctenopharyngodon idella)","volume":"33","author":"Dong","year":"2012","journal-title":"Fish & shellfish immunology"},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib19","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.fsi.2011.04.006","article-title":"Molecular characterization and expression analysis of the channel catfish cathepsin D genes","volume":"31","author":"Feng","year":"2011","journal-title":"Fish Shellfish Immunol."},{"issue":"2","key":"10.1016\/j.dci.2025.105387_bib20","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/j.abb.2005.01.005","article-title":"Cathepsin D-mediated yolk protein degradation is blocked by acid phosphatase inhibitors","volume":"436","author":"Fialho","year":"2005","journal-title":"Arch. Biochem. Biophys."},{"issue":"2","key":"10.1016\/j.dci.2025.105387_bib21","doi-asserted-by":"crossref","DOI":"10.1042\/BSR20120100","article-title":"Knockdown of cathepsin D in zebrafish fertilized eggs determines congenital myopathy","volume":"33","author":"Follo","year":"2013","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.dci.2025.105387_bib22","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1186\/1756-3305-3-119","article-title":"Dynamics of digestive proteolytic system during blood feeding of the hard tick Ixodes ricinus","volume":"3","author":"Franta","year":"2010","journal-title":"Parasites Vectors"},{"key":"10.1016\/j.dci.2025.105387_bib23","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.fsi.2018.07.002","article-title":"Characterization, expression signatures and microbial binding analysis of cathepsin A in turbot, Scophthalmus maximus L.(SmCTSA)","volume":"81","author":"Fu","year":"2018","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.dci.2025.105387_bib24","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.fsi.2020.04.028","article-title":"Genome-wide identification, expression signature and immune functional analysis of two cathepsin S (CTSS) genes in turbot (Scophthalmus maximus L.)","volume":"102","author":"Fu","year":"2020","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.dci.2025.105387_bib25","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.fsi.2020.04.028","article-title":"Genome-wide identification, expression signature and immune functional analysis of two cathepsin S (CTSS) genes in turbot (Scophthalmus maximus L.) - ScienceDirect","volume":"102","author":"Fu","year":"2020","journal-title":"Fish Shellfish Immunol."},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib26","doi-asserted-by":"crossref","first-page":"43","DOI":"10.5507\/bp.2005.003","article-title":"Dual role of cathepsin D: ligand and protease","volume":"149","author":"Fusek","year":"2005","journal-title":"Biomed. Pap. Med. Fac. Palacky Univ. Olomouc Czech Repub."},{"key":"10.1016\/j.dci.2025.105387_bib27","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1016\/j.fsi.2016.05.015","article-title":"The mucosal expression signatures of g-type lysozyme in turbot (Scophthalmus maximus) following bacterial challenge","volume":"54","author":"Gao","year":"2016","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.dci.2025.105387_bib28","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/j.fsi.2017.03.019","article-title":"Characterization and expression analysis of chitinase genes (CHIT1, CHIT2 and CHIT3) in turbot (Scophthalmus maximus L.) following bacterial challenge","volume":"64","author":"Gao","year":"2017","journal-title":"Fish Shellfish Immunol."},{"issue":"2","key":"10.1016\/j.dci.2025.105387_bib29","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/j.molbiopara.2004.03.015","article-title":"A gene family of cathepsin L-like proteases of filarial nematodes are associated with larval molting and cuticle and eggshell remodeling","volume":"136","author":"Guiliano","year":"2004","journal-title":"Mol. Biochem. Parasitol."},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib30","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1111\/j.1365-2249.2004.02420.x","article-title":"Cathepsin D is up-regulated in inflammatory bowel disease macrophages","volume":"136","author":"Hausmann","year":"2004","journal-title":"Clin. Exp. Immunol."},{"key":"10.1016\/j.dci.2025.105387_bib31","doi-asserted-by":"crossref","DOI":"10.1016\/j.fsi.2020.01.050","article-title":"Identification and characterization of a cathepsin K homologue that interacts with pathogen bacteria in black rockfish, Sebastes schlegelii","volume":"98","author":"He","year":"2020","journal-title":"Fish Shellfish Immunol."},{"issue":"6","key":"10.1016\/j.dci.2025.105387_bib32","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1515\/BC.2004.055","article-title":"Cathepsin L and Arg\/Lys aminopeptidase: a distinct prohormone processing pathway for the biosynthesis of peptide neurotransmitters and hormones","volume":"385","author":"Hook","year":"2004","journal-title":"Biol. Chem."},{"issue":"10","key":"10.1016\/j.dci.2025.105387_bib33","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1016\/j.chembiol.2009.09.009","article-title":"Hemoglobin digestion in blood-feeding ticks: mapping a multipeptidase pathway by functional proteomics","volume":"16","author":"Horn","year":"2009","journal-title":"Chem. Biol."},{"key":"10.1016\/j.dci.2025.105387_bib34","doi-asserted-by":"crossref","DOI":"10.1111\/j.0105-2896.2005.00310.x","article-title":"The lysosomal cysteine proteases in MHC class II antigen presentation","volume":"207","author":"Hsing","year":"2005","journal-title":"Immunol. Rev."},{"issue":"2","key":"10.1016\/j.dci.2025.105387_bib35","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/j.jinsphys.2007.10.009","article-title":"The movement of proteins across the insect and tick digestive system","volume":"54","author":"Jeffers","year":"2008","journal-title":"J. Insect Physiol."},{"issue":"4","key":"10.1016\/j.dci.2025.105387_bib36","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1016\/j.fsi.2008.09.011","article-title":"Molecular cloning, characterization and expression analysis of cathepsin D gene from turbot Scophthalmus maximus","volume":"26","author":"Jia","year":"2009","journal-title":"Fish Shellfish Immunol."},{"issue":"6","key":"10.1016\/j.dci.2025.105387_bib37","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1038\/nprot.2015.053","article-title":"The Phyre2 web portal for protein modeling, prediction and analysis","volume":"10","author":"Kelley","year":"2015","journal-title":"Nat. Protoc."},{"issue":"3","key":"10.1016\/j.dci.2025.105387_bib38","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1007\/s00705-005-0661-3","article-title":"A new genotype of lymphocystivirus, LCDV-RF, from lymphocystis diseased rockfish","volume":"151","author":"Kitamura","year":"2006","journal-title":"Arch. Virol."},{"issue":"3","key":"10.1016\/j.dci.2025.105387_bib39","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1016\/j.cbpc.2004.01.006","article-title":"Todarepsin, a new cathepsin D from hepatopancreas of Japanese common squid (Todarodes pacificus)","volume":"137","author":"Komai","year":"2004","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"issue":"4","key":"10.1016\/j.dci.2025.105387_bib40","doi-asserted-by":"crossref","DOI":"10.1002\/psc.3154","article-title":"Design, synthesis, and bioactivities of tasiamide B derivatives as cathepsin D inhibitors","volume":"25","author":"Li","year":"2019","journal-title":"J. Pept. Sci."},{"issue":"9","key":"10.1016\/j.dci.2025.105387_bib41","doi-asserted-by":"crossref","first-page":"1963","DOI":"10.1016\/j.bmc.2015.03.034","article-title":"Design, synthesis and biological evaluation of tasiamide B derivatives as BACE1 inhibitors","volume":"23","author":"Liu","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.dci.2025.105387_bib42","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1016\/j.fsi.2020.03.034","article-title":"The red swamp crayfish, Procambarus clarkii cathepsin C, participates in the innate immune response to the viral and bacterial pathogens","volume":"100","author":"Liu","year":"2020","journal-title":"Fish Shellfish Immunol."},{"year":"2015","series-title":"Clonal Identification of tilapia Histone D and Matrix Metalloproteinase 2 Genes and Their Functional Analysis","author":"Liu","key":"10.1016\/j.dci.2025.105387_bib43"},{"issue":"23","key":"10.1016\/j.dci.2025.105387_bib44","doi-asserted-by":"crossref","first-page":"10749","DOI":"10.1021\/jm301630s","article-title":"Cyanobacterial peptides as a prototype for the design of potent \u03b2-secretase inhibitors and the development of selective chemical probes for other aspartic proteases","volume":"55","author":"Liu","year":"2012","journal-title":"J. Med. Chem."},{"issue":"22","key":"10.1016\/j.dci.2025.105387_bib45","doi-asserted-by":"crossref","first-page":"7088","DOI":"10.1016\/S0021-9258(17)32945-9","article-title":"Mode of inhibition of acid proteases by pepstatin","volume":"251","author":"Marciniszyn","year":"1976","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib46","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1248\/bpb.33.22","article-title":"Translocation of lysosomal cathepsin D caused by oxidative stress or proteasome inhibition in primary cultured neurons and astrocytes","volume":"33","author":"Miura","year":"2010","journal-title":"Biol. Pharm. Bull."},{"issue":"5","key":"10.1016\/j.dci.2025.105387_bib47","doi-asserted-by":"crossref","first-page":"1566","DOI":"10.1016\/j.fsi.2013.08.027","article-title":"Comparative transcriptional analysis reveals distinct expression patterns of channel catfish genes after the first infection and re-infection with Aeromonas hydrophila","volume":"35","author":"Mu","year":"2013","journal-title":"Fish Shellfish Immunol."},{"key":"10.1016\/j.dci.2025.105387_bib48","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/0076-6879(94)44004-2","article-title":"Families of serine peptidases","volume":"244","author":"Rawlings","year":"1994","journal-title":"Methods Enzymol."},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib49","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.bbapap.2011.08.016","article-title":"Lysosomes and lysosomal cathepsins in cell death","volume":"1824","author":"Repnik","year":"2012","journal-title":"BBA - Proteins and Proteomics"},{"issue":"2\u20133","key":"10.1016\/j.dci.2025.105387_bib50","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0165-2478(93)90018-W","article-title":"Role of cathepsin D in the degradation of human serum albumin by peritoneal macrophages and veiled cells in antigen presentation","volume":"37","author":"Rhodes","year":"1993","journal-title":"Immunol. Lett."},{"issue":"7","key":"10.1016\/j.dci.2025.105387_bib51","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1002\/psc.1254","article-title":"Total synthesis and stereochemical reassignment of tasiamide B","volume":"16","author":"Sun","year":"2010","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.dci.2025.105387_bib52","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.dci.2017.09.019","article-title":"Cathepsin L-like protease can regulate the process of metamorphosis and fat body dissociation in Antheraea pernyi","volume":"78","author":"Sun","year":"2018","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.dci.2025.105387_bib53","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.fsi.2019.07.038","article-title":"Characterization and initial functional analysis of cathepsin K in turbot (Scophthalmus maximus L)","volume":"93","author":"Tian","year":"2019","journal-title":"Fish Shellfish Immunol."},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib54","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.bbapap.2011.10.002","article-title":"Cysteine cathepsins: from structure, function and regulation to new frontiers","volume":"1824","author":"Turk","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"issue":"4","key":"10.1016\/j.dci.2025.105387_bib55","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1046\/j.1365-3083.2003.01322.x","article-title":"Phylogeny of antigen-processing enzymes: cathepsins of a cephalochordate, an agnathan and a bony fish","volume":"58","author":"Uinuk-Ool","year":"2010","journal-title":"Scand. J. Immunol."},{"issue":"5","key":"10.1016\/j.dci.2025.105387_bib56","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1002\/med.21394","article-title":"The role of cathepsin D in the pathogenesis of human Neurodegenerative disorders","volume":"36","author":"Vidoni","year":"2016","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.dci.2025.105387_bib57","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/j.fsi.2019.08.012","article-title":"Characterization, expression, enzymatic activity, and functional identification of cathepsin S from black rockfish Sebastes schlegelii","volume":"93","author":"Wang","year":"2019","journal-title":"Fish Shellfish Immunol."},{"issue":"8","key":"10.1016\/j.dci.2025.105387_bib58","doi-asserted-by":"crossref","DOI":"10.3390\/v14081680","article-title":"Functional analysis of the cathepsin D gene response to SGIV infection in the orange-spotted grouper, Epinephelus coioides","volume":"14","author":"Wang","year":"2022","journal-title":"Viruses"},{"key":"10.1016\/j.dci.2025.105387_bib59","first-page":"531","article-title":"Protein identification and analysis tools in the ExPASy server","volume":"112","author":"Wilkins","year":"1999","journal-title":"Methods Mol. Biol."},{"issue":"Pt 2","key":"10.1016\/j.dci.2025.105387_bib60","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1017\/S0031182002002706","article-title":"Hookworm cathepsin D aspartic proteases: contributing roles in the host-specific degradation of serum proteins and skin macromolecules","volume":"126","author":"Williamson","year":"2003","journal-title":"Parasitology"},{"issue":"1","key":"10.1016\/j.dci.2025.105387_bib61","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.dci.2014.10.014","article-title":"Identification and characterization of a cathepsin D homologue from lampreys (Lampetra japonica)","volume":"49","author":"Xiao","year":"2015","journal-title":"Dev. Comp. Immunol."},{"issue":"9","key":"10.1016\/j.dci.2025.105387_bib62","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1002\/psc.3014","article-title":"Cyanobacterial peptides as a prototype for the design of cathepsin D inhibitors","volume":"23","author":"Xu","year":"2017","journal-title":"J. Pept. Sci."},{"issue":"3","key":"10.1016\/j.dci.2025.105387_bib63","doi-asserted-by":"crossref","first-page":"2075","DOI":"10.3892\/ol.2016.4160","article-title":"AGR2 is associated with gastric cancer progression and poor survival","volume":"11","author":"Zhang","year":"2016","journal-title":"Oncol. Lett."},{"issue":"10","key":"10.1016\/j.dci.2025.105387_bib64","article-title":"Identification of antimicrobial peptide genes in black rockfish Sebastes schlegelii and their responsive mechanisms to Edwardsiella tarda infection","volume":"10","author":"Zhang","year":"2021","journal-title":"Biology (Basel)"},{"issue":"4","key":"10.1016\/j.dci.2025.105387_bib65","first-page":"163","article-title":"The function of cathepsins B, D, and X in atherosclerosis","volume":"6","author":"Zhao","year":"2016","journal-title":"Am. J. Cardiovasc. Dis."}],"container-title":["Developmental &amp; Comparative Immunology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0145305X2500076X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0145305X2500076X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,4]],"date-time":"2025-11-04T08:35:41Z","timestamp":1762245341000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0145305X2500076X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,5]]},"references-count":67,"alternative-id":["S0145305X2500076X"],"URL":"https:\/\/doi.org\/10.1016\/j.dci.2025.105387","relation":{},"ISSN":["0145-305X"],"issn-type":[{"type":"print","value":"0145-305X"}],"subject":[],"published":{"date-parts":[[2025,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Characterization, expression profiling, and immunological role of Cathepsin D in Sebastes schlegelii during bacterial infection","name":"articletitle","label":"Article Title"},{"value":"Developmental & Comparative Immunology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.dci.2025.105387","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"105387"}}