{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T16:40:08Z","timestamp":1789749608723,"version":"4.0.1"},"reference-count":70,"publisher":"The Endocrine Society","issue":"7","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2004,7,1]]},"DOI":"10.1210\/en.2003-1698","type":"journal-article","created":{"date-parts":[[2004,3,23]],"date-time":"2004-03-23T01:44:16Z","timestamp":1080006256000},"page":"3165-3173","source":"Crossref","is-referenced-by-count":92,"title":["The Androgen-Regulated Epididymal Sperm-Binding Protein, Human \u03b2-Defensin 118 (DEFB118) (Formerly ESC42), Is an Antimicrobial \u03b2-Defensin"],"prefix":"10.1210","volume":"145","author":[{"given":"Suresh","family":"Yenugu","sequence":"first","affiliation":[{"name":"Laboratories for Reproductive Biology, Department of Pediatrics, University of North Carolina, Chapel Hill, North Carolina 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katherine G.","family":"Hamil","sequence":"additional","affiliation":[{"name":"Laboratories for Reproductive Biology, Department of Pediatrics, University of North Carolina, Chapel Hill, North Carolina 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yashwanth","family":"Radhakrishnan","sequence":"additional","affiliation":[{"name":"Laboratories for Reproductive Biology, Department of Pediatrics, University of North Carolina, Chapel Hill, North Carolina 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frank S.","family":"French","sequence":"additional","affiliation":[{"name":"Laboratories for Reproductive Biology, Department of Pediatrics, University of North Carolina, Chapel Hill, North Carolina 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susan H.","family":"Hall","sequence":"additional","affiliation":[{"name":"Laboratories for Reproductive Biology, Department of Pediatrics, University of North Carolina, Chapel Hill, North Carolina 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"80","reference":[{"key":"2019041123321139600_R1","first-page":"99","article-title":"Role of epididymal secretory proteins in sperm maturation with particular reference to the boar.","volume":"53","author":"Dacheux","year":"1998","journal-title":"J Reprod Fertil Suppl"},{"key":"2019041123321139600_R2","first-page":"119","article-title":"Interactions between epididymal secretions and spermatozoa.","volume":"53","author":"Cooper","year":"1998","journal-title":"J Reprod Fertil Suppl"},{"key":"2019041123321139600_R3","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1002\/jemt.10312","article-title":"Contribution of epididymal secretory proteins for spermatozoa maturation.","volume":"61","author":"Dacheux","year":"2003","journal-title":"Microsc Res Tech"},{"key":"2019041123321139600_R4","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1042\/bj20030225","article-title":"Antibacterial properties of the sperm-binding proteins and peptides of human epididymis 2 (HE2) family; salt sensitivity, structural dependence and their interaction with outer and cytoplasmic membranes of Escherichia coli.","volume":"372","author":"Yenugu","year":"2003","journal-title":"Biochem J"},{"key":"2019041123321139600_R5","doi-asserted-by":"crossref","first-page":"2787","DOI":"10.1210\/endo.143.7.8925","article-title":"Cystatin 11: a new member of the cystatin type 2 family.","volume":"143","author":"Hamil","year":"2002","journal-title":"Endocrinology"},{"key":"2019041123321139600_R6","first-page":"1371","article-title":"Cystatin and cystatin-derived peptides have antibacterial activity against the pathogen Porphyromonas gingivalis.","volume":"379","author":"Blankenvoorde","year":"1998","journal-title":"Biol Chem"},{"key":"2019041123321139600_R7","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1002\/(SICI)1098-2795(199708)47:4<490::AID-MRD16>3.0.CO;2-#","article-title":"Direct evidence for the secretion of lactoferrin and its binding to sperm in the porcine epididymis.","volume":"47","author":"Jin","year":"1997","journal-title":"Mol Reprod Dev"},{"key":"2019041123321139600_R8","doi-asserted-by":"crossref","first-page":"4297","DOI":"10.1128\/IAI.68.7.4297-4302.2000","article-title":"The human cationic antimicrobial protein (hCAP18) is expressed in the epithelium of human epididymis, is present in seminal plasma at high concentrations and is attached to spermatozoa.","volume":"68","author":"Malm","year":"2000","journal-title":"Infect Immun"},{"key":"2019041123321139600_R9","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1038\/279725a0","article-title":"Seminal plasmin\u2014an antimicrobial protein from bovine seminal plasma which acts in E. coli by specific inhibition of rRNA synthesis.","volume":"279","author":"Reddy","year":"1979","journal-title":"Nature"},{"key":"2019041123321139600_R10","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":"2019041123321139600_R11","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1126\/science.1056545","article-title":"An antimicrobial peptide gene found in the male reproductive system of rats.","volume":"291","author":"Li","year":"2001","journal-title":"Science"},{"key":"2019041123321139600_R12","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/0014-5793(96)01123-4","article-title":"Widespread expression of \u03b2-defensin hBD-1 in human secretory glands and epithelial cells.","volume":"396","author":"Zhao","year":"1996","journal-title":"FEBS Lett"},{"key":"2019041123321139600_R13","doi-asserted-by":"crossref","first-page":"1819","DOI":"10.1096\/fj.00-0865fje","article-title":"Human \u03b2-defensin 4: a novel inducible peptide with a specific salt-sensitive spectrum of antimicrobial activity.","volume":"15","author":"Garcia","year":"2001","journal-title":"FASEB J"},{"key":"2019041123321139600_R14","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1095\/biolreprod.102.008953","article-title":"Messenger RNA (mRNA) expression for the antimicrobial peptides \u03b2-defensin-1 and \u03b2-defensin-2 in the male rat reproductive tract: \u03b2-defensin-1 mRNA in initial segment and caput epididymis is regulated by androgens and not bacterial lipopolysaccharides.","volume":"68","author":"Palladino","year":"2003","journal-title":"Biol Reprod"},{"key":"2019041123321139600_R15","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1095\/biolreprod.102.005389","article-title":"Expression of antimicrobial defensins in the male reproductive tract of rats, mice, and humans.","volume":"68","author":"Com","year":"2003","journal-title":"Biol Reprod"},{"key":"2019041123321139600_R16","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1016\/S1357-4310(99)01490-2","article-title":"Antibiotic peptides from higher eukaryotes: biology and applications.","volume":"5","author":"Ganz","year":"1999","journal-title":"Mol Med Today"},{"key":"2019041123321139600_R17","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S0304-4157(98)00014-8","article-title":"Magainins as paradigm for the mode of action of pore forming polypeptides.","volume":"1376","author":"Matsuzaki","year":"1998","journal-title":"Biochim Biophys Acta"},{"key":"2019041123321139600_R18","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1021\/bi991892m","article-title":"Membrane thinning effect of the \u03b2-sheet antimicrobial protegrin.","volume":"39","author":"Heller","year":"2000","journal-title":"Biochemistry"},{"key":"2019041123321139600_R19","doi-asserted-by":"crossref","first-page":"3152","DOI":"10.1016\/S0006-3495(99)77145-6","article-title":"Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy.","volume":"77","author":"Marassi","year":"1999","journal-title":"Biophys J"},{"key":"2019041123321139600_R20","doi-asserted-by":"crossref","first-page":"14150","DOI":"10.1021\/bi0012843","article-title":"Interaction between heat shock proteins and antimicrobial peptides.","volume":"39","author":"Otvos Jr","year":"2000","journal-title":"Biochemistry"},{"key":"2019041123321139600_R21","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1172\/JCI114198","article-title":"Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity.","volume":"84","author":"Lehrer","year":"1989","journal-title":"J Clin Invest"},{"key":"2019041123321139600_R22","doi-asserted-by":"crossref","first-page":"4529","DOI":"10.1210\/endo.142.10.8422","article-title":"Primate epididymis-specific proteins: characterization of ESC42, a novel protein containing a trefoil-like motif in monkey and human.","volume":"142","author":"Liu","year":"2001","journal-title":"Endocrinology"},{"key":"2019041123321139600_R23","doi-asserted-by":"crossref","first-page":"2129","DOI":"10.1073\/pnas.042692699","article-title":"Discovery of five conserved \u03b2-defensin gene clusters using a computational search strategy.","volume":"99","author":"Schutte","year":"2002","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041123321139600_R24","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1186\/1477-7827-1-112","article-title":"LCN6, a novel human epididymal lipocalin.","volume":"1","author":"Hamil","year":"2003","journal-title":"Reprod Biol Endocrinol"},{"key":"2019041123321139600_R25","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1128\/AAC.26.4.546","article-title":"Use of the fluorescent probe 1-N-phenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa.","volume":"26","author":"Loh","year":"1984","journal-title":"Antimicrob Agents Chemother"},{"key":"2019041123321139600_R26","doi-asserted-by":"crossref","first-page":"7235","DOI":"10.1021\/bi9826299","article-title":"Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli.","volume":"38","author":"Wu","year":"1999","journal-title":"Biochemistry"},{"key":"2019041123321139600_R27","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1002\/elps.11501401163","article-title":"The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences.","volume":"14","author":"Bjellqvist","year":"1993","journal-title":"Electrophoresis"},{"key":"2019041123321139600_R28","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/S0196-9781(01)00628-3","article-title":"Antibacterial activities and conformations of bovine \u03b2-defensin BNBD-12 and analogs: structural and disulfide bridge requirements for activity.","volume":"23","author":"Mandal","year":"2002","journal-title":"Peptides"},{"key":"2019041123321139600_R29","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/S0092-8674(00)81895-4","article-title":"Human \u03b2-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis.","volume":"88","author":"Goldman","year":"1997","journal-title":"Cell"},{"key":"2019041123321139600_R30","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":"2019041123321139600_R31","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/0014-5793(96)00236-0","article-title":"Change in membrane permeability induced by protegrin 1: implication of disulfide bridges for pore formation.","volume":"383","author":"Mangoni","year":"1996","journal-title":"FEBS Lett"},{"key":"2019041123321139600_R32","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1093\/oxfordjournals.jbchem.a123077","article-title":"Determination of the disulfide array in sapecin, an antibacterial peptide of Sarcophaga peregrina (flesh fly).","volume":"107","author":"Kuzuhara","year":"1990","journal-title":"J Biochem (Tokyo)"},{"key":"2019041123321139600_R33","doi-asserted-by":"crossref","first-page":"11704","DOI":"10.1021\/bi00094a029","article-title":"Role of disulfide linkages in tachyplesin-lipid interactions.","volume":"32","author":"Matsuzaki","year":"1993","journal-title":"Biochemistry"},{"key":"2019041123321139600_R34","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1006\/bbrc.1994.2757","article-title":"Antimicrobial peptides from the skin of a Korean frog, Rana rugosa.","volume":"205","author":"Park","year":"1994","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041123321139600_R35","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1002\/(SICI)1097-0282(20000405)53:4<281::AID-BIP1>3.0.CO;2-2","article-title":"Synthesis, microbicidal activity, and solution structure of the dodecapeptide from bovine neutrophils.","volume":"53","author":"Raj","year":"1999","journal-title":"Biopolymers"},{"key":"2019041123321139600_R36","doi-asserted-by":"crossref","first-page":"32911","DOI":"10.1074\/jbc.M006098200","article-title":"The structure of human \u03b2-defensin-2 shows evidence of higher order oligomerization.","volume":"275","author":"Hoover","year":"2000","journal-title":"J Biol Chem"},{"key":"2019041123321139600_R37","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/S0888-7543(02)00034-4","article-title":"Distribution of new human \u03b2-defensin genes clustered on chromosome 20 in functionally different segments of epididymis.","volume":"81","author":"Rodriguez-Jimenez","year":"2003","journal-title":"Genomics"},{"key":"2019041123321139600_R38","doi-asserted-by":"crossref","first-page":"1624","DOI":"10.1172\/JCI118588","article-title":"Intramolecular inhibition of human defensin HNP-1 by its propiece.","volume":"97","author":"Valore","year":"1996","journal-title":"J Clin Invest"},{"key":"2019041123321139600_R39","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1126\/science.286.5437.113","article-title":"Regulation of intestinal \u03b1-defensin activation by the metalloproteinase matrilysin in innate host defense.","volume":"286","author":"Wilson","year":"1999","journal-title":"Science"},{"key":"2019041123321139600_R40","first-page":"954","article-title":"Electrolyte content of human seminal fluid at different states of fertility.","volume":"16","author":"Nag","year":"1978","journal-title":"Indian J Exp Biol"},{"key":"2019041123321139600_R41","doi-asserted-by":"crossref","first-page":"842","DOI":"10.1136\/oem.52.12.842","article-title":"Some altered concentrations of elements in semen of workers exposed to trinitrotoluene.","volume":"52","author":"Liu","year":"1995","journal-title":"Occup Environ"},{"key":"2019041123321139600_R42","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1111\/j.1439-0272.1986.tb01767.x","article-title":"Change in sodium and potassium concentration in human seminal plasma infected experimentally with Ureaplasma urealyticum.","volume":"18","author":"Mehl","year":"1986","journal-title":"Andrologia"},{"key":"2019041123321139600_R43","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1530\/jrf.0.0750035","article-title":"Sodium, potassium, calcium, magnesium, zinc, citrate and chloride content of human prostatic and seminal fluid.","volume":"75","author":"Kavanagh","year":"1985","journal-title":"J Reprod Fertil"},{"key":"2019041123321139600_R44","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/S0022-5347(17)38251-4","article-title":"Biochemical analysis of electroejaculates in spinal cord injured men: comparison to normal ejaculates.","volume":"145","author":"Hirsch","year":"1991","journal-title":"J Urol"},{"key":"2019041123321139600_R45","doi-asserted-by":"crossref","first-page":"14961","DOI":"10.1073\/pnas.95.25.14961","article-title":"Production of \u03b2-defensins by human airway epithelia.","volume":"95","author":"Singh","year":"1998","journal-title":"Proc Nat Acad Sci USA"},{"key":"2019041123321139600_R46","doi-asserted-by":"crossref","first-page":"1225","DOI":"10.1128\/IAI.66.3.1225-1232.1998","article-title":"Mouse \u03b2-defensin 1 is a salt-sensitive antimicrobial peptide present in epithelia of the lung and urogenital tract.","volume":"66","author":"Bals","year":"1998","journal-title":"Infect Immun"},{"key":"2019041123321139600_R47","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/S0924-8579(99)00095-3","article-title":"Anionic antimicrobial peptide-lysozyme interactions in innate pulmonary immunity.","volume":"13","author":"Kalfa","year":"1999","journal-title":"Int J Antimicrob Agents"},{"key":"2019041123321139600_R48","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1006\/bbrc.2001.6234","article-title":"Salt resistance and synergistic effect with vancomycin of \u03b1-helical antimicrobial peptide p18.","volume":"290","author":"Shin","year":"2002","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041123321139600_R49","first-page":"287","article-title":"Antibacterial properties and partial cDNA sequences of cecropin-like antibacterial peptides from the common cutworm, Spodoptera litura.","volume":"125","author":"Choi","year":"2000","journal-title":"Comp Biochem Physiol C Toxicol Pharmacol"},{"key":"2019041123321139600_R50","doi-asserted-by":"crossref","first-page":"1542","DOI":"10.1128\/AAC.43.7.1542","article-title":"Salt-resistant \u03b1-helical cationic antimicrobial peptides.","volume":"43","author":"Friedrich","year":"1999","journal-title":"Antimicrob Agents Chemother"},{"key":"2019041123321139600_R51","doi-asserted-by":"crossref","first-page":"5030","DOI":"10.1074\/jbc.M109173200","article-title":"Discovery and characterization of two isoforms of moronecidin, a novel antimicrobial peptide from hybrid striped bass.","volume":"277","author":"Lauth","year":"2002","journal-title":"J Biol Chem"},{"key":"2019041123321139600_R52","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":"2019041123321139600_R53","doi-asserted-by":"crossref","first-page":"19298","DOI":"10.1074\/jbc.271.32.19298","article-title":"Mode of action of the antimicrobial peptide indolicidin.","volume":"271","author":"Falla","year":"1996","journal-title":"J Biol Chem"},{"key":"2019041123321139600_R54","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/0014-5793(96)00996-9","article-title":"Requirements for antibacterial and hemolytic activities in the bovine neutrophil derived 13-residue peptide indolicidin.","volume":"395","author":"Subbalakshmi","year":"1996","journal-title":"FEBS Lett"},{"key":"2019041123321139600_R55","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1074\/jbc.274.1.29","article-title":"Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane.","volume":"274","author":"Wu","year":"1999","journal-title":"J Biol Chem"},{"key":"2019041123321139600_R56","doi-asserted-by":"crossref","first-page":"5451","DOI":"10.1128\/AEM.65.12.5451-5458.1999","article-title":"Permeabilization of fungal membranes by plant defensins inhibits fungal growth.","volume":"65","author":"Thevissen","year":"1999","journal-title":"Appl Environ Microbiol"},{"key":"2019041123321139600_R57","doi-asserted-by":"crossref","first-page":"2086","DOI":"10.1128\/AAC.44.8.2086-2092.2000","article-title":"Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria.","volume":"44","author":"Friedrich","year":"2000","journal-title":"Antimicrob Agents Chemother"},{"key":"2019041123321139600_R58","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":"2019041123321139600_R59","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1006\/bbrc.2001.5020","article-title":"Histone H1: an antimicrobial protein of Atlantic salmon (Salmo salar).","volume":"284","author":"Richards","year":"2001","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041123321139600_R60","doi-asserted-by":"crossref","first-page":"2279","DOI":"10.1128\/AAC.46.7.2279-2283.2002","article-title":"Structure-function relationship studies on the frog skin antimicrobial peptide tigerinin 1: design of analogs with improved activity and their action on clinical bacterial isolates.","volume":"46","author":"Sitaram","year":"2002","journal-title":"Antimicrob Agents Chemother"},{"key":"2019041123321139600_R61","doi-asserted-by":"crossref","first-page":"2886","DOI":"10.1128\/IAI.63.8.2886-2891.1995","article-title":"Morphology of defensin-treated Staphylococcus aureus.","volume":"63","author":"Shimoda","year":"1995","journal-title":"Infect Immun"},{"key":"2019041123321139600_R62","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1038\/35086601","article-title":"Antibacterial agents based on the cyclic D, L-\u03b1-peptide architecture.","volume":"412","author":"Fernandez-Lopez","year":"2001","journal-title":"Nature"},{"key":"2019041123321139600_R63","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0005-2736(99)00197-2","article-title":"Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes.","volume":"1462","author":"Matsuzaki","year":"1999","journal-title":"Biochim Biophys Acta"},{"key":"2019041123321139600_R64","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1095\/biolreprod.103.016105","article-title":"ESP13.2, a member of the \u03b2-defensin family, is a macaque sperm surface-coating protein involved in the capacitation process.","volume":"69","author":"Yudin","year":"2003","journal-title":"Biol Reprod"},{"key":"2019041123321139600_R65","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1095\/biolreprod.102.005983","article-title":"Cloning and characterization of a novel sperm-associated isoantigen (e-3) with defensin- and lectin-like motifs expressed in rat epididymis.","volume":"68","author":"Rao","year":"2003","journal-title":"Biol Reprod"},{"key":"2019041123321139600_R66","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1210\/endo.141.3.7389","article-title":"HE2\u03b2 and HE2\u03b3, new members of an epididymis-specific family of androgen-regulated proteins in the human.","volume":"141","author":"Hamil","year":"2000","journal-title":"Endocrinology"},{"key":"2019041123321139600_R67","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1095\/biolreprod.102.004564","article-title":"Novel antimicrobial peptide of human epididymal duct origin.","volume":"67","author":"von Horsten","year":"2002","journal-title":"Biol Reprod"},{"key":"2019041123321139600_R68","doi-asserted-by":"crossref","first-page":"3724","DOI":"10.1128\/IAI.58.11.3724-3730.1990","article-title":"Rapid membrane permeabilization and inhibition of vital functions of gram-negative bacteria by bactenecins.","volume":"58","author":"Skerlavaj","year":"1990","journal-title":"Infect Immun"},{"key":"2019041123321139600_R69","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1007\/s002840010263","article-title":"DNA as the intracellular secondary target for antibacterial action of human neutrophil peptide-I against Mycobacterium tuberculosis H37Ra.","volume":"42","author":"Sharma","year":"2001","journal-title":"Curr Microbiol"},{"key":"2019041123321139600_R70","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1128\/AAC.46.3.605-614.2002","article-title":"Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in E. coli.","volume":"46","author":"Patrzykat","year":"2002","journal-title":"Antimicrob Agents Chemother"}],"container-title":["Endocrinology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/endo\/article-pdf\/145\/7\/3165\/10379912\/endo3165.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,3,31]],"date-time":"2020-03-31T19:16:40Z","timestamp":1585682200000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/endo\/article\/145\/7\/3165\/2499794"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,7,1]]},"references-count":70,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2004,7,1]]}},"URL":"https:\/\/doi.org\/10.1210\/en.2003-1698","relation":{},"ISSN":["0013-7227","1945-7170"],"issn-type":[{"value":"0013-7227","type":"print"},{"value":"1945-7170","type":"electronic"}],"subject":[],"published":{"date-parts":[[2004,7,1]]}}}