{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,3]],"date-time":"2026-05-03T02:58:59Z","timestamp":1777777139830,"version":"3.51.4"},"reference-count":64,"publisher":"Elsevier BV","issue":"12","license":[{"start":{"date-parts":[[2007,1,1]],"date-time":"2007-01-01T00:00:00Z","timestamp":1167609600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2007,1,1]],"date-time":"2007-01-01T00:00:00Z","timestamp":1167609600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/100000097","name":"National Center for Research Resources","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000097","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["P20 RR017686"],"award-info":[{"award-number":["P20 RR017686"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["P20 RR016475"],"award-info":[{"award-number":["P20 RR016475"]}],"id":[{"id":"10.13039\/100000002","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":[[2007]]},"DOI":"10.1016\/j.dci.2007.03.007","type":"journal-article","created":{"date-parts":[[2007,4,17]],"date-time":"2007-04-17T07:16:56Z","timestamp":1176794216000},"page":"1278-1296","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":60,"title":["Canine cathelicidin (K9CATH): Gene cloning, expression, and biochemical activity of a novel pro-myeloid antimicrobial peptide"],"prefix":"10.1016","volume":"31","author":[{"given":"Yongming","family":"Sang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M.","family":"Teresa Ortega","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kristina","family":"Rune","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wang","family":"Xiau","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guolong","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jose L.","family":"Soulages","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gerald H.","family":"Lushington","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jianwen","family":"Fang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Todd D.","family":"Williams","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Frank","family":"Blecha","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tonatiuh","family":"Melgarejo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.dci.2007.03.007_bib1","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1189\/jlb.0403147","article-title":"Cathelicidins, multifunctional peptides of the innate immunity","volume":"75","author":"Zanetti","year":"2004","journal-title":"J Leukoc Biol"},{"key":"10.1016\/j.dci.2007.03.007_bib2","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1046\/j.1365-2796.2003.01228.x","article-title":"Antibacterial peptides: basic facts and emerging concepts","volume":"254","author":"Boman","year":"2003","journal-title":"J Intern Med"},{"key":"10.1016\/j.dci.2007.03.007_bib3","doi-asserted-by":"crossref","first-page":"23","DOI":"10.2174\/1389203053027520","article-title":"The cathelicidins\u2014structure, function and evolution","volume":"6","author":"Tomasinsig","year":"2005","journal-title":"Curr Protein Pept Sci"},{"key":"10.1016\/j.dci.2007.03.007_bib4","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1007\/s00109-002-0350-6","article-title":"Cathelicidins, essential gene-encoded mammalian antibiotics","volume":"80","author":"Zaiou","year":"2002","journal-title":"J Mol Med"},{"key":"10.1016\/j.dci.2007.03.007_bib5","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1007\/s00018-003-2186-9","article-title":"Cathelicidins\u2014a family of multifunctional antimicrobial peptides","volume":"60","author":"Bals","year":"2003","journal-title":"Cell Mol Life Sci"},{"key":"10.1016\/j.dci.2007.03.007_bib6","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1016\/S0021-9258(18)54182-X","article-title":"The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics","volume":"268","author":"Zanetti","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1016\/j.dci.2007.03.007_bib7","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1046\/j.1523-1747.2003.12132.x","article-title":"Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18\/LL-37) prosequence","volume":"120","author":"Zaiou","year":"2003","journal-title":"J Invest Dermatol"},{"key":"10.1016\/j.dci.2007.03.007_bib8","doi-asserted-by":"crossref","first-page":"3086","DOI":"10.1182\/blood.V96.9.3086","article-title":"The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations","volume":"96","author":"Agerberth","year":"2000","journal-title":"Blood"},{"key":"10.1016\/j.dci.2007.03.007_bib9","doi-asserted-by":"crossref","first-page":"231","DOI":"10.4049\/jimmunol.152.1.231","article-title":"A novel granulocyte-derived peptide with lipopolysaccharide-neutralizing activity","volume":"152","author":"Larrick","year":"1994","journal-title":"J Immunol"},{"key":"10.1016\/j.dci.2007.03.007_bib10","doi-asserted-by":"crossref","first-page":"224","DOI":"10.2174\/1568010033484115","article-title":"Epithelial cell-derived antibacterial peptides human beta-defensins and cathelicidin: multifunctional activities on mast cells","volume":"2","author":"Niyonsaba","year":"2003","journal-title":"Curr Drug Targets Inflamm Allergy"},{"key":"10.1016\/j.dci.2007.03.007_bib11","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1046\/j.1365-2567.2002.01398.x","article-title":"A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis","volume":"106","author":"Niyonsaba","year":"2002","journal-title":"Immunology"},{"key":"10.1016\/j.dci.2007.03.007_bib12","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1002\/1097-0282(2000)55:1<31::AID-BIP40>3.0.CO;2-9","article-title":"Structural features and biological activities of the cathelicidin-derived antimicrobial peptides","volume":"55","author":"Gennaro","year":"2000","journal-title":"Biopolymers"},{"key":"10.1016\/j.dci.2007.03.007_bib13","doi-asserted-by":"crossref","first-page":"2695","DOI":"10.1128\/AAC.45.10.2695-2702.2001","article-title":"RL-37, an alpha-helical antimicrobial peptide of the rhesus monkey","volume":"45","author":"Zhao","year":"2001","journal-title":"Antimicrob Agents Chemother"},{"key":"10.1016\/j.dci.2007.03.007_bib14","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1128\/CDLI.8.2.370-375.2001","article-title":"Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules","volume":"8","author":"Bals","year":"2001","journal-title":"Clin Diagn Lab Immunol"},{"key":"10.1016\/j.dci.2007.03.007_bib15","doi-asserted-by":"crossref","first-page":"9541","DOI":"10.1073\/pnas.95.16.9541","article-title":"The peptide antibiotic LL-37\/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface","volume":"95","author":"Bals","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.dci.2007.03.007_bib16","doi-asserted-by":"crossref","first-page":"28375","DOI":"10.1074\/jbc.271.45.28375","article-title":"Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities","volume":"271","author":"Skerlavaj","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/j.dci.2007.03.007_bib17","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/S0014-5793(97)01310-0","article-title":"Structural organization of the bovine cathelicidin gene family and identification of a novel member","volume":"417","author":"Scocchi","year":"1997","journal-title":"FEBS Lett"},{"key":"10.1016\/j.dci.2007.03.007_bib18","doi-asserted-by":"crossref","first-page":"4106","DOI":"10.1128\/IAI.67.8.4106-4111.1999","article-title":"Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytes","volume":"67","author":"Shamova","year":"1999","journal-title":"Infect Immun"},{"key":"10.1016\/j.dci.2007.03.007_bib19","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/0014-5793(95)01285-3","article-title":"cDNA sequences of three sheep myeloid cathelicidins","volume":"376","author":"Bagella","year":"1995","journal-title":"FEBS Lett"},{"key":"10.1016\/j.dci.2007.03.007_bib20","doi-asserted-by":"crossref","first-page":"7855","DOI":"10.1016\/S0021-9258(17)37128-4","article-title":"Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells","volume":"269","author":"Zanetti","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/j.dci.2007.03.007_bib21","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1111\/j.1399-3011.1997.tb01121.x","article-title":"Synthesis and antibacterial action of cecropin and proline\u2013arginine-rich peptides from pig intestine","volume":"49","author":"Vunnam","year":"1997","journal-title":"J Pept Res"},{"key":"10.1016\/j.dci.2007.03.007_bib22","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1016\/S0014-5793(99)01097-2","article-title":"Novel cathelicidins in horse leukocytes(1)","volume":"457","author":"Scocchi","year":"1999","journal-title":"FEBS Lett"},{"key":"10.1016\/j.dci.2007.03.007_bib23","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1128\/AAC.45.3.715-722.2001","article-title":"Structural and functional analysis of horse cathelicidin peptides","volume":"45","author":"Skerlavaj","year":"2001","journal-title":"Antimicrob Agents Chemother"},{"key":"10.1016\/j.dci.2007.03.007_bib24","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1016\/S0196-9781(01)00499-5","article-title":"Processing site and gene structure for the murine antimicrobial peptide CRAMP","volume":"22","author":"Pestonjamasp","year":"2001","journal-title":"Peptides"},{"key":"10.1016\/j.dci.2007.03.007_bib25","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1007\/s000180300045","article-title":"Phylogeny, processing and expression of the rat cathelicidin rCRAMP: a model for innate antimicrobial peptides","volume":"60","author":"Termen","year":"2003","journal-title":"Cell Mol Life Sci"},{"key":"10.1016\/j.dci.2007.03.007_bib26","doi-asserted-by":"crossref","first-page":"3329","DOI":"10.4049\/jimmunol.167.6.3329","article-title":"Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells","volume":"167","author":"Nagaoka","year":"2001","journal-title":"J Immunol"},{"key":"10.1016\/j.dci.2007.03.007_bib27","doi-asserted-by":"crossref","first-page":"6058","DOI":"10.1016\/S0021-9258(18)53425-6","article-title":"Antibacterial 15-kDa protein isoforms (p15s) are members of a novel family of leukocyte proteins","volume":"268","author":"Levy","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1016\/j.dci.2007.03.007_bib28","first-page":"179","article-title":"The role of cathelicidins in the innate host defenses of mammals","volume":"7","author":"Zanetti","year":"2005","journal-title":"Curr Issues Mol Biol"},{"key":"10.1016\/j.dci.2007.03.007_bib29","doi-asserted-by":"crossref","first-page":"5552","DOI":"10.1128\/IAI.68.10.5552-5558.2000","article-title":"Regulation of cathelicidin gene expression: induction by lipopolysaccharide, interleukin-6, retinoic acid, and Salmonella enterica serovar typhimurium infection","volume":"68","author":"Wu","year":"2000","journal-title":"Infect Immun"},{"key":"10.1016\/j.dci.2007.03.007_bib30","doi-asserted-by":"crossref","first-page":"2611","DOI":"10.1128\/IAI.73.5.2611-2620.2005","article-title":"Molecular cloning and characterization of three {beta}-defensins from canine testes","volume":"73","author":"Sang","year":"2005","journal-title":"Infect Immun"},{"key":"10.1016\/j.dci.2007.03.007_bib31","doi-asserted-by":"crossref","first-page":"1864","DOI":"10.4049\/jimmunol.177.3.1864","article-title":"Macrophages acquire neutrophil granules for antimicrobial activity against intracellular pathogens","volume":"177","author":"Tan","year":"2006","journal-title":"J Immunol"},{"key":"10.1016\/j.dci.2007.03.007_bib32","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/S0022-2836(05)80360-2","article-title":"Basic local alignment search tool","volume":"215","author":"Altschul","year":"1990","journal-title":"J Mol Biol"},{"key":"10.1016\/j.dci.2007.03.007_bib33","doi-asserted-by":"crossref","first-page":"34162","DOI":"10.1074\/jbc.M105836200","article-title":"Essential role of the conformational flexibility of helices 1 and 5 on the lipid binding activity of apolipophorin-III","volume":"276","author":"Soulages","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1016\/j.dci.2007.03.007_bib34","doi-asserted-by":"crossref","first-page":"3350","DOI":"10.1021\/bi00713a027","article-title":"Determination of the helix and beta form of proteins in aqueous solution by circular dichroism","volume":"13","author":"Chen","year":"1974","journal-title":"Biochemistry"},{"key":"10.1016\/j.dci.2007.03.007_bib35","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/0014-5793(95)00792-8","article-title":"The solution structure of the active domain of CAP18\u2014a lipopolysaccharide binding protein from rabbit leukocytes","volume":"370","author":"Chen","year":"1995","journal-title":"FEBS Lett"},{"key":"10.1016\/j.dci.2007.03.007_bib36","doi-asserted-by":"crossref","first-page":"4673","DOI":"10.1093\/nar\/22.22.4673","article-title":"CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice","volume":"22","author":"Thompson","year":"1994","journal-title":"Nucl Acids Res"},{"key":"10.1016\/j.dci.2007.03.007_bib37","first-page":"97","article-title":"Comparative protein structure modeling","volume":"143","author":"Sanchez","year":"2000","journal-title":"Introduction and practical examples with modeller. Methods Mol Biol"},{"key":"10.1016\/j.dci.2007.03.007_bib38","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1093\/bioinformatics\/16.4.404","article-title":"The PSIPRED protein structure prediction server","volume":"16","author":"McGuffin","year":"2000","journal-title":"Bioinformatics"},{"key":"10.1016\/j.dci.2007.03.007_bib39","unstructured":"Pfaller MA, Chaturvedi V, Espinel-Ingroff A, et al. Manual NCCLS. Reference method for broth dilution antifungal susceptibility testing of yeasts; approved standard-2nd ed. NCCLS document M27-A2 [ISBN 1-56238-469-4]. NCCLS, 940 West Valley Road, Suite 1400, Wayne, PA 19087\u20131898, USA. NCCLS 2002;22."},{"key":"10.1016\/j.dci.2007.03.007_bib40","unstructured":"Ferraro MJ, Wikler MA, Craig WA, et al. Manual NCCLS. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically; approved standard, 6th ed. NCCLS document M7-A6 [ISBN 1-56238-486-4]. NCCLS, 940 West Valley Road, Suite 1400, Wayne, PA 19087\u20131898 USA, 2003. NCCLS 2003;23."},{"key":"10.1016\/j.dci.2007.03.007_bib41","doi-asserted-by":"crossref","first-page":"2206","DOI":"10.1128\/AAC.42.9.2206","article-title":"Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils","volume":"42","author":"Turner","year":"1998","journal-title":"Antimicrob Agents Chemother"},{"key":"10.1016\/j.dci.2007.03.007_bib42","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1046\/j.0014-2956.2002.02751.x","article-title":"SMAP-29 has two LPS-binding sites and a central hinge","volume":"269","author":"Tack","year":"2002","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.dci.2007.03.007_bib43","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/S0014-5793(99)01600-2","article-title":"SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytes","volume":"463","author":"Skerlavaj","year":"1999","journal-title":"FEBS Lett"},{"key":"10.1016\/j.dci.2007.03.007_bib44","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1034\/j.1399-3011.2002.01968.x","article-title":"Solution structure of a cathelicidin-derived antimicrobial peptide, CRAMP as determined by NMR spectroscopy","volume":"60","author":"Yu","year":"2002","journal-title":"J Pept Res"},{"key":"10.1016\/j.dci.2007.03.007_bib45","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1006\/cimm.1998.1358","article-title":"Cytotoxicity and apoptosis mediated by two peptides of innate immunity","volume":"189","author":"Risso","year":"1998","journal-title":"Cell Immunol"},{"key":"10.1016\/j.dci.2007.03.007_bib46","doi-asserted-by":"crossref","first-page":"3883","DOI":"10.4049\/jimmunol.169.7.3883","article-title":"The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses","volume":"169","author":"Scott","year":"2002","journal-title":"J Immunol"},{"key":"10.1016\/j.dci.2007.03.007_bib47","first-page":"240","article-title":"Six antimicrobial peptide genes of the cathelicidin family map to bovine chromosome 22q24 by fluorescence in situ hybridization","volume":"75","author":"Castiglioni","year":"1996","journal-title":"Cytogenet Cell Genet"},{"key":"10.1016\/j.dci.2007.03.007_bib48","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1051\/vetres:2000121","article-title":"Porcine antimicrobial peptides: new prospects for ancient molecules of host defense","volume":"31","author":"Zhang","year":"2000","journal-title":"Vet Res"},{"key":"10.1016\/j.dci.2007.03.007_bib49","doi-asserted-by":"crossref","first-page":"3070","DOI":"10.4049\/jimmunol.172.5.3070","article-title":"Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense","volume":"172","author":"Murakami","year":"2004","journal-title":"J Immunol"},{"key":"10.1016\/j.dci.2007.03.007_bib50","doi-asserted-by":"crossref","first-page":"1046","DOI":"10.1006\/bbrc.2001.5280","article-title":"Structure-activity analysis of SMAP-29, a sheep leukocytes-derived antimicrobial peptide","volume":"285","author":"Shin","year":"2001","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.dci.2007.03.007_bib51","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1177\/154405910208101210","article-title":"Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva","volume":"81","author":"Murakami","year":"2002","journal-title":"J Dent Res"},{"key":"10.1016\/j.dci.2007.03.007_bib52","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.peptides.2004.09.020","article-title":"Protegrin structure-activity relationships: using homology models of synthetic sequences to determine structural characteristics important for activity","volume":"26","author":"Ostberg","year":"2005","journal-title":"Peptides"},{"key":"10.1016\/j.dci.2007.03.007_bib53","doi-asserted-by":"crossref","first-page":"779","DOI":"10.2174\/1381612023395457","article-title":"Cathelicidin peptides as candidates for a novel class of antimicrobials","volume":"8","author":"Zanetti","year":"2002","journal-title":"Curr Pharm Des"},{"key":"10.1016\/j.dci.2007.03.007_bib54","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/S1286-4579(02)01549-6","article-title":"Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity","volume":"4","author":"Ramanathan","year":"2002","journal-title":"Microbes Infect"},{"key":"10.1016\/j.dci.2007.03.007_bib55","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1002\/(SICI)1097-0282(1998)47:6<451::AID-BIP4>3.0.CO;2-F","article-title":"Mode of action of linear amphipathic alpha-helical antimicrobial peptides","volume":"47","author":"Oren","year":"1998","journal-title":"Biopolymers"},{"key":"10.1016\/j.dci.2007.03.007_bib56","first-page":"63","article-title":"Transmission of Brucella canis by contact exposure","volume":"78","author":"Carmichael","year":"1988","journal-title":"Cornell Vet"},{"key":"10.1016\/j.dci.2007.03.007_bib57","first-page":"233","article-title":"The genital Mycoplasma and Ureaplasma flora of healthy and diseased dogs","volume":"45","author":"Doig","year":"1981","journal-title":"Can J Comp Med"},{"key":"10.1016\/j.dci.2007.03.007_bib58","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1099\/00207713-43-4-640","article-title":"Ureaplasma canigenitalium spp. nov., isolated from dogs","volume":"43","author":"Harasawa","year":"1993","journal-title":"Int J Syst Bacteriol"},{"key":"10.1016\/j.dci.2007.03.007_bib59","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1111\/j.1462-5822.2005.00530.x","article-title":"Neisseria gonorrhoeae downregulates expression of the human antimicrobial peptide LL-37","volume":"7","author":"Bergman","year":"2005","journal-title":"Cell Microbiol"},{"key":"10.1016\/j.dci.2007.03.007_bib60","doi-asserted-by":"crossref","first-page":"5387","DOI":"10.1128\/JB.187.15.5387-5396.2005","article-title":"Cationic antimicrobial peptide resistance in Neisseria meningitidis","volume":"187","author":"Tzeng","year":"2005","journal-title":"J Bacteriol"},{"key":"10.1016\/j.dci.2007.03.007_bib61","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1016\/j.ijantimicag.2004.02.018","article-title":"Reduction in the bactericidal activity of selected cathelicidin peptides by bovine calf serum or exogenous endotoxin","volume":"23","author":"Bartlett","year":"2004","journal-title":"Int J Antimicrob Agents"},{"key":"10.1016\/j.dci.2007.03.007_bib62","doi-asserted-by":"crossref","first-page":"2845","DOI":"10.1128\/AAC.49.7.2845-2850.2005","article-title":"Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37","volume":"49","author":"Ciornei","year":"2005","journal-title":"Antimicrob Agents Chemother"},{"key":"10.1016\/j.dci.2007.03.007_bib63","doi-asserted-by":"crossref","first-page":"2748","DOI":"10.1128\/IAI.68.5.2748-2755.2000","article-title":"Bactericidal activity of mammalian cathelicidin-derived peptides","volume":"68","author":"Travis","year":"2000","journal-title":"Infect Immun"},{"key":"10.1016\/j.dci.2007.03.007_bib64","doi-asserted-by":"crossref","first-page":"904","DOI":"10.1006\/bbrc.2000.3269","article-title":"CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity","volume":"275","author":"Shin","year":"2000","journal-title":"Biochem Biophys Res Commun"}],"container-title":["Developmental &amp; Comparative Immunology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0145305X0700050X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0145305X0700050X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T18:46:40Z","timestamp":1777488400000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0145305X0700050X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007]]},"references-count":64,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2007]]}},"alternative-id":["S0145305X0700050X"],"URL":"https:\/\/doi.org\/10.1016\/j.dci.2007.03.007","relation":{},"ISSN":["0145-305X"],"issn-type":[{"value":"0145-305X","type":"print"}],"subject":[],"published":{"date-parts":[[2007]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Canine cathelicidin (K9CATH): Gene cloning, expression, and biochemical activity of a novel pro-myeloid antimicrobial peptide","name":"articletitle","label":"Article Title"},{"value":"Developmental & Comparative Immunology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.dci.2007.03.007","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2007 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}