{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T22:45:27Z","timestamp":1792709127251,"version":"4.5.0"},"reference-count":53,"publisher":"Public Library of Science (PLoS)","issue":"9","license":[{"start":{"date-parts":[[2008,9,16]],"date-time":"2008-09-16T00:00:00Z","timestamp":1221523200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0003217","type":"journal-article","created":{"date-parts":[[2008,9,15]],"date-time":"2008-09-15T19:20:24Z","timestamp":1221506424000},"page":"e3217","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":212,"title":["Snake Cathelicidin from Bungarus fasciatus Is a Potent Peptide Antibiotics"],"prefix":"10.1371","volume":"3","author":[{"given":"Yipeng","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jing","family":"Hong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiuhong","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hailong","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rui","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jing","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aili","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Donghai","family":"Lin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ren","family":"Lai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2008,9,16]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/415389a","article-title":"Antimicrobial peptides of multicellular organisms.","volume":"415","author":"M Zasloff","year":"2002","journal-title":"Nature"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/nrmicro1098","article-title":"Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?","volume":"3","author":"KA Borgden","year":"2005","journal-title":"Nat Rev Microbiol"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1189\/jlb.0403147","article-title":"Cathelicidins, multifunctional peptides of the innate immunity.","volume":"75","author":"M Zanetti","year":"2004","journal-title":"J Leukoc Biol"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1038\/nrmicro976","article-title":"Primate defensins.","volume":"2","author":"RI Lehrer","year":"2004","journal-title":"Nature Rev Microbiol"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1038\/nri1180","article-title":"Defensins: antimicrobial peptides of innate immunity.","volume":"3","author":"T Ganz","year":"2003","journal-title":"Nature Rev Immunol"},{"key":"ref6","first-page":"183","article-title":"Hepcidin\u2013a peptide hormone at the interface of innate immunity and iron metabolism.","volume":"306","author":"T Ganz","year":"2006","journal-title":"Curr Top Microbiol Immunol"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1211\/0022357022971","article-title":"Histatins: antimicrobial peptides with therapeutic potential.","volume":"56","author":"K Kavanagh","year":"2004","journal-title":"J Pharm Pharmacol"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"1408","DOI":"10.1016\/j.bbamem.2006.03.030","article-title":"LL-37, the only human member of the cathelicidin family of antimicrobial peptides.","volume":"1758","author":"UH D\u00fcrr","year":"2006","journal-title":"Biochim Biophys Acta"},{"key":"ref9","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":"R Bals","year":"2003","journal-title":"Cell Mol Life Sci"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"3142","DOI":"10.1128\/IAI.57.10.3142-3146.1989","article-title":"Purification, composition, and activity of two Bactenectins, antibacterial peptides of bovine neutrophils.","volume":"57","author":"R Gennaro","year":"1989","journal-title":"Infect Immun"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1083\/jcb.111.4.1363","article-title":"Bactenecins, defense polypeptides of bovine neutrophils, are generated from precursor molecules stored in the large granules.","volume":"111","author":"M Zanetti","year":"1990","journal-title":"J Cell Biol"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"18871","DOI":"10.1016\/S0021-9258(17)30595-1","article-title":"Amino acid sequences of two proline-rich bactenectins.","volume":"265","author":"RW Frank","year":"1990","journal-title":"J Biol Chem"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1016\/S0021-9258(18)54182-X","article-title":"The cDNAof the neutrophil antibioticBac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics.","volume":"268","author":"M Zanetti","year":"1993","journal-title":"J Biol Chem"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1128\/CDLI.8.2.370-375.2001","article-title":"Rhesus monkey (<italic>Macaca mulatta<\/italic>) mucosal antimicrobial peptides are close homologues of human molecules.","volume":"8","author":"R Bals","year":"2001","journal-title":"Clin Diagn Lab Immunol"},{"key":"ref15","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":"C Zhao","year":"2001","journal-title":"Antimicrob Agents Chemother"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"13088","DOI":"10.1074\/jbc.272.20.13088","article-title":"Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse.","volume":"272","author":"RL Gallo","year":"1997","journal-title":"J Biol Chem"},{"key":"ref17","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":"S Term\u00e9n","year":"2003","journal-title":"Cell Mol Life Sci"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"22742","DOI":"10.1074\/jbc.272.36.22742","article-title":"Isolation of cDNA encoding guinea pig neutrophil cationic antibacterial polypeptide of 11 kDa (CAP11) and evaluation of CAP11 mRNA expression during neutrophil maturation.","volume":"272","author":"I Nagaoka","year":"1997","journal-title":"J Biol Chem"},{"key":"ref19","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":"R Gennaro","year":"2000","journal-title":"Biopolymers"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/0014-5793(89)81093-2","article-title":"Primary structure of a new cysteine proteinase inhibitor from pig leukocytes.","volume":"255","author":"A Ritonja","year":"1989","journal-title":"FEBS Lett"},{"key":"ref21","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":"M Zaiou","year":"2002","journal-title":"J Mol Med"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1111\/j.1432-1033.1992.tb17324.x","article-title":"Proteolytic cleavage by neutrophil elastase converts inactive storage proforms to antibacterial bactenecins.","volume":"209","author":"M Scocchi","year":"1992","journal-title":"Eur J Biochem"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1128\/IAI.65.3.978-985.1997","article-title":"Porcine polymorphonuclear leukocytes generate extracellular microbicidal activity by elastasemediated activation of secreted proprotegrins.","volume":"65","author":"A Panyutich","year":"1997","journal-title":"Infect Immun"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"3951","DOI":"10.1182\/blood.V97.12.3951","article-title":"Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3.","volume":"97","author":"OE Sorensen","year":"2001","journal-title":"Blood"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"28540","DOI":"10.1074\/jbc.M301608200","article-title":"Processing of seminal plasma hCAP-18 to ALL-38 by Gastricsin.","volume":"278","author":"OE Sorensen","year":"2003","journal-title":"J Biol Chem"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"070","DOI":"10.4049\/jimmunol.172.5.3070","article-title":"Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense.","volume":"172","author":"M Murakami","year":"2004","journal-title":"J Immunol"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1016\/j.peptides.2003.08.024","article-title":"Hagfish intestinal antimicrobial peptides are ancient cathelicidins.","volume":"24","author":"T Uzzell","year":"2003","journal-title":"Peptides"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"5053","DOI":"10.1128\/IAI.73.8.5053-5064.2005","article-title":"Identification of a novel cathelicidin gene in the rainbow trout, <italic>Oncorhynchus mykiss<\/italic>.","volume":"73","author":"CI Chang","year":"2005","journal-title":"Infect Immun"},{"key":"ref29","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 (<italic>Oncorhynchus mykiss<\/italic>) and atlantic salmon (<italic>Salmo salar<\/italic>).","volume":"50","author":"CI Chang","year":"2006","journal-title":"Antimicrob Agents Chemother"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"2858","DOI":"10.1074\/jbc.M507180200","article-title":"Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity.","volume":"281","author":"Y Xiao","year":"2006","journal-title":"J Biol Chem"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"15063","DOI":"10.1073\/pnas.0707037104","article-title":"Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway.","volume":"104","author":"R Goitsuka","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref32","first-page":"334","article-title":"The hagfish immune system,","author":"RL Raison","year":"1998"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/j.peptides.2007.11.013","article-title":"A novel serine protease inhibitor from <italic>Bungarus fasciatus<\/italic> venom.","volume":"29","author":"J Lu","year":"2008","journal-title":"Peptides"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.peptides.2007.02.008","article-title":"A bactericidal homodimeric phospholipases A2 from <italic>Bungarus fasciatus<\/italic> venom.","volume":"28","author":"C Xu","year":"2007","journal-title":"Peptides"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/0003-2697(78)90812-6","article-title":"Circular dichroic analysis of protein conformation: inclusion of the beta-turns.","volume":"91","author":"CT Chang","year":"1978","journal-title":"Anal Biochem"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a Multidimensional Spectral Processing System Based on UNIX Pipes.","volume":"6","author":"F Delaglio","year":"1995","journal-title":"J Biomol NMR"},{"key":"ref37","article-title":"SPARKY 3,","author":"TD Goddard"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1007\/BF00211777","article-title":"1H, 13C and 15N chemical shift referencing in biomolecular NMR.","volume":"6","author":"DS Wishart","year":"1995","journal-title":"J Biomol NMR"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"2466","DOI":"10.1096\/fj.06-7966com","article-title":"Trypsin inhibitory loop is an excellent lead structure to design serine protease inhibitors and antimicrobial peptides.","volume":"21","author":"J Li","year":"2007","journal-title":"FASEB J"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1074\/mcp.M600334-MCP200","article-title":"Anti-infection peptidomics of amphibian skin.","volume":"6","author":"J Li","year":"2007","journal-title":"Mol Cell Proteomics"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1016\/j.molimm.2007.07.004","article-title":"The first antimicrobial peptide from sea amphibian.","volume":"45","author":"Y Lu","year":"2008","journal-title":"Mol Immunol"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"2069","DOI":"10.1016\/j.peptides.2007.07.020","article-title":"A new family of antimicrobial peptides from skin secretions of <italic>Rana pleuraden<\/italic>.","volume":"28","author":"X Wang","year":"2007","journal-title":"Peptides"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1038\/nature04051","article-title":"Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus.","volume":"437","author":"PH Mygind","year":"2005","journal-title":"Nature"},{"key":"ref44","article-title":"Defensins and the convergent evolution of platypus and reptile venom genes.","author":"CM Whittington","year":"2008","journal-title":"Genome Res [Epub ahead of print]"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1093\/jb\/mvg160","article-title":"Structural elucidation of the protein- and membrane-binding properties of the N-terminal tail domain of human annexin II.","volume":"134","author":"YH Hong","year":"2003","journal-title":"J Biochem"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1002\/bip.20370","article-title":"Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an alpha-helical conformation.","volume":"81","author":"C Landon","year":"2006","journal-title":"Biopolymers"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"4660","DOI":"10.1021\/ja075659k","article-title":"Structure, self-assembly, and dual role of a beta-defensin-like peptide from the Chinese soft-shelled turtle eggshell matrix.","volume":"130","author":"R Lakshminarayanan","year":"2008","journal-title":"J Am Chem Soc"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1002\/prot.20963","article-title":"Small cationic protein from a marine turtle has beta-defensin-like fold and antibacterial and antiviral activity.","volume":"64","author":"S Chattopadhyay","year":"2006","journal-title":"Proteins"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bbapap.2003.09.004","article-title":"Antimicrobial peptides from ranid frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents.","volume":"1696","author":"JM Conlon","year":"2004","journal-title":"Biochim Biophys Acta"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.1128\/AAC.49.4.1340-1345.2005","article-title":"Bactericidal and antiendotoxic properties of short cationic peptides derived from a snake venom Lys49 phospholipase A2.","volume":"49","author":"C Santamar\u00eda","year":"2005","journal-title":"Antimicrob Agents Chemother"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/j.toxicon.2004.09.012","article-title":"Antimicrobial activity of myotoxic phospholipases A2 from crotalid snake venoms and synthetic peptide variants derived from their C-terminal region.","volume":"45","author":"C Santamar\u00eda","year":"2005","journal-title":"Toxicon"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1042\/BJ20060318","article-title":"Antimicrobial activity of omwaprin, a new member of the waprin family of snake venom proteins.","volume":"402","author":"DG Nair","year":"2007","journal-title":"Biochem J"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1016\/0041-0101(91)90210-I","article-title":"Antibacterial effects of different snake venoms: purification and characterization of antibacterial proteins from <italic>Pseudechis australis<\/italic> (Australian king brown or mulga snake) venom.","volume":"29","author":"BG Stiles","year":"1991","journal-title":"Toxicon"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0003217","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,9,16]],"date-time":"2021-09-16T13:40:27Z","timestamp":1631799627000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0003217"}},"subtitle":[],"editor":[{"given":"Joseph","family":"El Khoury","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2008,9,16]]},"references-count":53,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2008,9,16]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0003217","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2008,9,16]]}}}