{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,5]],"date-time":"2025-11-05T14:19:24Z","timestamp":1762352364549},"reference-count":76,"publisher":"Oxford University Press (OUP)","issue":"6","license":[{"start":{"date-parts":[[2016,10,2]],"date-time":"2016-10-02T00:00:00Z","timestamp":1475366400000},"content-version":"vor","delay-in-days":692,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,3,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Motivation: The increased prevalence of multi-drug resistant (MDR) pathogens heightens the need to design new antimicrobial agents. Antimicrobial peptides (AMPs) exhibit broad-spectrum potent activity against MDR pathogens and kills rapidly, thus giving rise to AMPs being recognized as a potential substitute for conventional antibiotics. Designing new AMPs using current in-silico approaches is, however, challenging due to the absence of suitable models, large number of design parameters, testing cycles, production time and cost. To date, AMPs have merely been categorized into families according to their primary sequences, structures and functions. The ability to computationally determine the properties that discriminate AMP families from each other could help in exploring the key characteristics of these families and facilitate the in-silico design of synthetic AMPs.<\/jats:p>\n               <jats:p>Results: Here we studied 14 AMP families and sub-families. We selected a specific description of AMP amino acid sequence and identified compositional and physicochemical properties of amino acids that accurately distinguish each AMP family from all other AMPs with an average sensitivity, specificity and precision of 92.88%, 99.86% and 95.96%, respectively. Many of our identified discriminative properties have been shown to be compositional or functional characteristics of the corresponding AMP family in literature. We suggest that these properties could serve as guides for in-silico methods in design of novel synthetic AMPs. The methodology we developed is generic and has a potential to be applied for characterization of any protein family.<\/jats:p>\n               <jats:p>Contact: \u00a0vladimir.bajic@kaust.edu.sa<\/jats:p>\n               <jats:p>Supplementary information: \u00a0Supplementary data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btu738","type":"journal-article","created":{"date-parts":[[2014,11,12]],"date-time":"2014-11-12T04:44:24Z","timestamp":1415767464000},"page":"849-856","source":"Crossref","is-referenced-by-count":30,"title":["Distinct profiling of antimicrobial peptide families"],"prefix":"10.1093","volume":"31","author":[{"given":"Abdullah M.","family":"Khamis","sequence":"first","affiliation":[{"name":"Computational Bioscience Research Center (CBRC), Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Magbubah","family":"Essack","sequence":"additional","affiliation":[{"name":"Computational Bioscience Research Center (CBRC), Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xin","family":"Gao","sequence":"additional","affiliation":[{"name":"Computational Bioscience Research Center (CBRC), Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vladimir B.","family":"Bajic","sequence":"additional","affiliation":[{"name":"Computational Bioscience Research Center (CBRC), Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2014,11,10]]},"reference":[{"key":"2023020116172102000_btu738-B1","doi-asserted-by":"crossref","first-page":"6475","DOI":"10.1073\/pnas.80.21.6475","article-title":"Solid-phase synthesis of cecropin A and related peptides","volume":"80","author":"Andreu","year":"1983","journal-title":"Proc. Natl Acad. Sci. U. S. A."},{"key":"2023020116172102000_btu738-B2","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1002\/(SICI)1097-0282(1998)47:6<415::AID-BIP2>3.0.CO;2-D","article-title":"Animal antimicrobial peptides: an overview","volume":"47","author":"Andreu","year":"1998","journal-title":"Biopolymers"},{"key":"2023020116172102000_btu738-B3","doi-asserted-by":"crossref","first-page":"D586","DOI":"10.1093\/nar\/gkh032","article-title":"ANTIMIC: a database of antimicrobial sequences","volume":"32","author":"Brahmachary","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"2023020116172102000_btu738-B4","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":"Brogden","year":"2005","journal-title":"Nat. Rev. Microbiol"},{"key":"2023020116172102000_btu738-B5","doi-asserted-by":"crossref","DOI":"10.1007\/978-3-540-68830-3","volume-title":"Advances in Differential Evolution","author":"Chakraborty","year":"2008"},{"key":"2023020116172102000_btu738-B6","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1046\/j.1523-1747.2001.01231.x","article-title":"Anti-microbial activity and cell binding are controlled by sequence determinants in the anti-microbial peptide PR-39","volume":"116","author":"Chan","year":"2001","journal-title":"J. Invest. Dermatol."},{"key":"2023020116172102000_btu738-B7","doi-asserted-by":"crossref","first-page":"6052","DOI":"10.1021\/bi900154f","article-title":"Structure, dynamics, and activity of an all-cysteine mutated human beta defensin-3 peptide analogue","volume":"48","author":"Chandrababu","year":"2009","journal-title":"Biochemistry"},{"key":"2023020116172102000_btu738-B8","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/0022-5193(83)90265-5","article-title":"The dependence of the Chou\u2013Fasman parameters on amino acid side chain structure","volume":"102","author":"Charton","year":"1983","journal-title":"J. Theor. Biol."},{"key":"2023020116172102000_btu738-B9","doi-asserted-by":"crossref","first-page":"709","DOI":"10.4208\/cicp.071210.240511a","article-title":"How the antimicrobial peptides kill bacteria: computational physics insights","volume":"11","author":"Chen","year":"2012","journal-title":"Commun. Comput. Phys."},{"key":"2023020116172102000_btu738-B10","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1186\/1471-2105-7-518","article-title":"Prediction of protein submitochondria locations by hybridizing pseudo-amino acid composition with various physicochemical features of segmented sequence","volume":"7","author":"Du","year":"2006","journal-title":"BMC Bioinformatics"},{"key":"2023020116172102000_btu738-B11","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/S0005-2736(99)00198-4","article-title":"Diversity of antimicrobial peptides and their mechanisms of action","volume":"1462","author":"Epand","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"2023020116172102000_btu738-B12","doi-asserted-by":"crossref","first-page":"6260","DOI":"10.1016\/S0021-9258(18)83342-7","article-title":"The chemical synthesis of cecropin D and an analog with enhanced antibacterial activity","volume":"264","author":"Fink","year":"1989","journal-title":"J. Biol. Chem."},{"key":"2023020116172102000_btu738-B13","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1038\/nrd3591","article-title":"Designing antimicrobial peptides: form follows function","volume":"11","author":"Fjell","year":"2012","journal-title":"Nat. Rev. Drug Discov."},{"key":"2023020116172102000_btu738-B14","doi-asserted-by":"crossref","first-page":"3349","DOI":"10.1128\/AAC.48.9.3349-3357.2004","article-title":"De novo design of potent antimicrobial peptides","volume":"48","author":"Frecer","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"2023020116172102000_btu738-B15","doi-asserted-by":"crossref","first-page":"972","DOI":"10.1126\/science.1136800","article-title":"Clustering by passing messages between data points","volume":"315","author":"Frey","year":"2007","journal-title":"Science"},{"key":"2023020116172102000_btu738-B16","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1093\/icb\/43.2.300","article-title":"The role of antimicrobial peptides in innate immunity","volume":"43","author":"Ganz","year":"2003","journal-title":"Integr. Comp. Biol."},{"key":"2023020116172102000_btu738-B17","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1093\/protein\/15.11.871","article-title":"An analysis of protein domain linkers: their classification and role in protein folding","volume":"15","author":"George","year":"2002","journal-title":"Protein Eng."},{"key":"2023020116172102000_btu738-B18","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1080\/02713680590968637","article-title":"A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs","volume":"30","author":"Gordon","year":"2005","journal-title":"Curr. Eye Res."},{"key":"2023020116172102000_btu738-B19","doi-asserted-by":"crossref","first-page":"e59305","DOI":"10.1371\/journal.pone.0059305","article-title":"From design to screening: a new antimicrobial peptide discovery pipeline","volume":"8","author":"Guralp","year":"2013","journal-title":"PLoS One"},{"key":"2023020116172102000_btu738-B20","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/S0966-842X(00)01823-0","article-title":"The role of cationic antimicrobial peptides in innate host defences","volume":"8","author":"Hancock","year":"2000","journal-title":"Trends Microbiol."},{"key":"2023020116172102000_btu738-B21","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/S0167-7799(97)01156-6","article-title":"Cationic peptides: a new source of antibiotics","volume":"16","author":"Hancock","year":"1998","journal-title":"Trends Biotechnol."},{"key":"2023020116172102000_btu738-B22","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.1038\/nbt1267","article-title":"Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies","volume":"24","author":"Hancock","year":"2006","journal-title":"Nat. Biotechnol."},{"key":"2023020116172102000_btu738-B23","doi-asserted-by":"crossref","first-page":"8856","DOI":"10.1073\/pnas.97.16.8856","article-title":"The role of antimicrobial peptides in animal defenses","volume":"97","author":"Hancock","year":"2000","journal-title":"Proc. Natl Acad. Sci. U. S. A."},{"key":"2023020116172102000_btu738-B24","doi-asserted-by":"crossref","first-page":"2260","DOI":"10.1128\/AEM.72.3.2260-2264.2006","article-title":"Casein-derived antimicrobial peptides generated by Lactobacillus acidophilus DPC6026","volume":"72","author":"Hayes","year":"2006","journal-title":"Appl. Environ. Microbiol."},{"key":"2023020116172102000_btu738-B25","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/s00018-005-5486-4","article-title":"Key role of glutamic acid for the cytotoxic activity of the cyclotide cycloviolacin O2","volume":"63","author":"Herrmann","year":"2006","journal-title":"Cell. Mol. Life Sci."},{"key":"2023020116172102000_btu738-B26","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1128\/CMR.00056-05","article-title":"Peptide antimicrobial agents","volume":"19","author":"Jenssen","year":"2006","journal-title":"Clin. Microbiol. Rev."},{"key":"2023020116172102000_btu738-B27","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1007\/s00249-011-0674-7","article-title":"Knowledge-based computational methods for identifying or designing novel, non-homologous antimicrobial peptides","volume":"40","author":"Juretic","year":"2011","journal-title":"Eur. Biophys. J."},{"key":"2023020116172102000_btu738-B28","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1189\/jlb.68.6.779","article-title":"Expression of mammalian defensin genes","volume":"68","author":"Kaiser","year":"2000","journal-title":"J. Leukoc. Biol."},{"key":"2023020116172102000_btu738-B29","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1093\/nar\/28.1.374","article-title":"AAindex: amino acid index database","volume":"28","author":"Kawashima","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"2023020116172102000_btu738-B30","first-page":"760","article-title":"Particle swarm optimization","volume-title":"Encyclopedia of Machine Learning","author":"Kennedy","year":"2010"},{"key":"2023020116172102000_btu738-B31","doi-asserted-by":"crossref","first-page":"21183","DOI":"10.1073\/pnas.1311183110","article-title":"Oxytocic plant cyclotides as templates for peptide G protein-coupled receptor ligand design","volume":"110","author":"Koehbach","year":"2013","journal-title":"Proc. Natl Acad. Sci. U. S. A."},{"key":"2023020116172102000_btu738-B32","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1016\/j.peptides.2008.03.018","article-title":"Correlation between simulated physicochemical properties and hemolycity of protegrin-like antimicrobial peptides: predicting experimental toxicity","volume":"29","author":"Langham","year":"2008","journal-title":"Peptides"},{"issue":"Suppl. 1","key":"2023020116172102000_btu738-B33","doi-asserted-by":"crossref","first-page":"S19","DOI":"10.1186\/1471-2105-11-S1-S19","article-title":"AntiBP2: improved version of antibacterial peptide prediction","volume":"11","author":"Lata","year":"2010","journal-title":"BMC Bioinformatics"},{"key":"2023020116172102000_btu738-B34","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1186\/1471-2105-8-263","article-title":"Analysis and prediction of antibacterial peptides","volume":"8","author":"Lata","year":"2007","journal-title":"BMC Bioinformatics"},{"key":"2023020116172102000_btu738-B35","doi-asserted-by":"crossref","first-page":"9159","DOI":"10.1073\/pnas.86.23.9159","article-title":"Antibacterial peptides from pig intestine: isolation of a mammalian cecropin","volume":"86","author":"Lee","year":"1989","journal-title":"Proc. Natl Acad. Sci. U. S. A."},{"key":"2023020116172102000_btu738-B36","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1097\/00062752-200701000-00005","article-title":"Multispecific myeloid defensins","volume":"14","author":"Lehrer","year":"2007","journal-title":"Curr. Opin. Hematol."},{"key":"2023020116172102000_btu738-B37","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/S0952-7915(99)80005-3","article-title":"Antimicrobial peptides in mammalian and insect host defence","volume":"11","author":"Lehrer","year":"1999","journal-title":"Curr. Opin. Immunol."},{"key":"2023020116172102000_btu738-B38","doi-asserted-by":"crossref","first-page":"4277","DOI":"10.1021\/bi00613a026","article-title":"Conformational preferences of amino acids in globular proteins","volume":"17","author":"Levitt","year":"1978","journal-title":"Biochemistry"},{"key":"2023020116172102000_btu738-B39","doi-asserted-by":"crossref","first-page":"1658","DOI":"10.1093\/bioinformatics\/btl158","article-title":"Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences","volume":"22","author":"Li","year":"2006","journal-title":"Bioinformatics"},{"key":"2023020116172102000_btu738-B40","doi-asserted-by":"crossref","first-page":"e46633","DOI":"10.1371\/journal.pone.0046633","article-title":"Using amino acid physicochemical distance transformation for fast protein remote homology detection","volume":"7","author":"Liu","year":"2012","journal-title":"PLoS One"},{"key":"2023020116172102000_btu738-B41","doi-asserted-by":"crossref","first-page":"e1003212","DOI":"10.1371\/journal.pcbi.1003212","article-title":"Antimicrobial peptides design by evolutionary multiobjective optimization","volume":"9","author":"Maccari","year":"2013","journal-title":"PLoS Comput. Biol."},{"key":"2023020116172102000_btu738-B42","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1146\/annurev.phyto.121307.094843","article-title":"Identification and rational design of novel antimicrobial peptides for plant protection","volume":"46","author":"Marcos","year":"2008","journal-title":"Annu. Rev. Phytopathol."},{"key":"2023020116172102000_btu738-B44","doi-asserted-by":"crossref","first-page":"2804","DOI":"10.1110\/ps.051597405","article-title":"A novel representation of protein sequences for prediction of subcellular location using support vector machines","volume":"14","author":"Matsuda","year":"2005","journal-title":"Protein Sci."},{"key":"2023020116172102000_btu738-B45","doi-asserted-by":"crossref","first-page":"3730","DOI":"10.1128\/IAI.71.7.3730-3739.2003","article-title":"Staphylococcus aureus susceptibility to innate antimicrobial peptides, beta-defensins and CAP18, expressed by human keratinocytes","volume":"71","author":"Midorikawa","year":"2003","journal-title":"Infect. Immun."},{"key":"2023020116172102000_btu738-B46","doi-asserted-by":"crossref","first-page":"5297","DOI":"10.1128\/AEM.69.9.5297-5305.2003","article-title":"Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species","volume":"69","author":"Minervini","year":"2003","journal-title":"Appl. Environ. Microbiol."},{"key":"2023020116172102000_btu738-B47","doi-asserted-by":"crossref","first-page":"1913","DOI":"10.1099\/mic.0.28812-0","article-title":"Broad-spectrum antibacterial activity by a novel abiogenic peptide mimic","volume":"152","author":"Nusslein","year":"2006","journal-title":"Microbiology"},{"key":"2023020116172102000_btu738-B48","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1111\/j.1399-3011.1982.tb02620.x","article-title":"Protein secondary structure. Studies on the limits of prediction accuracy","volume":"19","author":"Palau","year":"1982","journal-title":"Int. J. Pept. Protein Res."},{"key":"2023020116172102000_btu738-B49","doi-asserted-by":"crossref","first-page":"143","DOI":"10.3109\/07388551.2011.594423","article-title":"Antimicrobial peptides: key components of the innate immune system","volume":"32","author":"Pasupuleti","year":"2012","journal-title":"Crit. Rev. Biotechnol."},{"key":"2023020116172102000_btu738-B50","doi-asserted-by":"crossref","first-page":"e1001067","DOI":"10.1371\/journal.ppat.1001067","article-title":"Antimicrobial peptides: primeval molecules or future drugs?","volume":"6","author":"Peters","year":"2010","journal-title":"PLoS Pathog."},{"key":"2023020116172102000_btu738-B51","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/978-3-642-15060-9_6","article-title":"An SVM model based on physicochemical properties to predict antimicrobial activity from protein sequences with cysteine knot motifs","volume-title":"Advances in Bioinformatics and Computational Biology","author":"Porto","year":"2010"},{"key":"2023020116172102000_btu738-B52","doi-asserted-by":"crossref","first-page":"675391","DOI":"10.1155\/2013\/675391","article-title":"Antimicrobial peptides: versatile biological properties","volume":"2013","author":"Pushpanathan","year":"2013","journal-title":"Int. J. Pept."},{"key":"2023020116172102000_btu738-B53","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1007\/s00281-007-0064-5","article-title":"Antimicrobial peptides: natural effectors of the innate immune system","volume":"29","author":"Radek","year":"2007","journal-title":"Semin. Immunopathol."},{"key":"2023020116172102000_btu738-B54","doi-asserted-by":"crossref","first-page":"21509","DOI":"10.1074\/jbc.M801851200","article-title":"The conserved salt bridge in human alpha-defensin 5 is required for its precursor processing and proteolytic stability","volume":"283","author":"Rajabi","year":"2008","journal-title":"J. Biol. Chem."},{"key":"2023020116172102000_btu738-B55","doi-asserted-by":"crossref","first-page":"4525","DOI":"10.1021\/cr010168i","article-title":"Precursor processing by kex2\/furin proteases","volume":"102","author":"Rockwell","year":"2002","journal-title":"Chem. Rev."},{"key":"2023020116172102000_btu738-B56","doi-asserted-by":"crossref","first-page":"8606","DOI":"10.1074\/jbc.M211147200","article-title":"Twists, knots, and rings in proteins. Structural definition of the cyclotide framework","volume":"278","author":"Rosengren","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2023020116172102000_btu738-B57","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1017\/S1466252308001497","article-title":"Antimicrobial peptides and bacteriocins: alternatives to traditional antibiotics","volume":"9","author":"Sang","year":"2008","journal-title":"Anim. Health Res. Rev."},{"key":"2023020116172102000_btu738-B58","doi-asserted-by":"crossref","first-page":"13838","DOI":"10.1074\/jbc.M212115200","article-title":"Interactions of mouse Paneth cell alpha-defensins and alpha-defensin precursors with membranes. Prosegment inhibition of peptide association with biomimetic membranes","volume":"278","author":"Satchell","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2023020116172102000_btu738-B59","first-page":"12","article-title":"Surmounting antimicrobial resistance in the Millennium Superbug: Staphylococcus aureus","volume":"5","author":"Saxena","year":"2010","journal-title":"cent.eur.j.med"},{"key":"2023020116172102000_btu738-B60","doi-asserted-by":"crossref","first-page":"21866","DOI":"10.1074\/jbc.M112.358721","article-title":"Arginine in alpha-defensins: differential effects on bactericidal activity correspond to geometry of membrane curvature generation and peptide-lipid phase behavior","volume":"287","author":"Schmidt","year":"2012","journal-title":"J. Biol. Chem."},{"key":"2023020116172102000_btu738-B61","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0045-2068(03)00080-4","article-title":"Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance","volume":"31","author":"Shinnar","year":"2003","journal-title":"Bioorg. Chem."},{"key":"2023020116172102000_btu738-B62","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S1367-5931(98)80033-1","article-title":"The proprotein convertases","volume":"2","author":"Steiner","year":"1998","journal-title":"Curr. Opin. Chem. Biol."},{"key":"2023020116172102000_btu738-B63","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/0005-2736(88)90069-7","article-title":"Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects","volume":"939","author":"Steiner","year":"1988","journal-title":"Biochim. Biophys. Acta"},{"key":"2023020116172102000_btu738-B64","doi-asserted-by":"crossref","first-page":"D1108","DOI":"10.1093\/nar\/gkr1063","article-title":"DAMPD: a manually curated antimicrobial peptide database","volume":"40","author":"Sundararajan","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"2023020116172102000_btu738-B65","volume-title":"Introduction to Data Mining","author":"Tan","year":"2006"},{"key":"2023020116172102000_btu738-B66","doi-asserted-by":"crossref","first-page":"D774","DOI":"10.1093\/nar\/gkp1021","article-title":"CAMP: a useful resource for research on antimicrobial peptides","volume":"38","author":"Thomas","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"2023020116172102000_btu738-B67","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":"Nucleic Acids Res."},{"key":"2023020116172102000_btu738-B68","doi-asserted-by":"crossref","first-page":"e16968","DOI":"10.1371\/journal.pone.0016968","article-title":"Connecting peptide physicochemical and antimicrobial properties by a rational prediction model","volume":"6","author":"Torrent","year":"2011","journal-title":"PLoS One"},{"key":"2023020116172102000_btu738-B69","doi-asserted-by":"crossref","first-page":"D191","DOI":"10.1093\/nar\/gkt1140","article-title":"Activities at the Universal Protein Resource (UniProt)","volume":"42","author":"UniProt","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"2023020116172102000_btu738-B70","author":"Uzzell","year":"2002"},{"key":"2023020116172102000_btu738-B71","doi-asserted-by":"crossref","first-page":"D1154","DOI":"10.1093\/nar\/gkt1157","article-title":"CAMP: collection of sequences and structures of antimicrobial peptides","volume":"42","author":"Waghu","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"2023020116172102000_btu738-B72","doi-asserted-by":"crossref","first-page":"D933","DOI":"10.1093\/nar\/gkn823","article-title":"APD2: the updated antimicrobial peptide database and its application in peptide design","volume":"37","author":"Wang","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"2023020116172102000_btu738-B73","doi-asserted-by":"crossref","first-page":"e18476","DOI":"10.1371\/journal.pone.0018476","article-title":"Prediction of antimicrobial peptides based on sequence alignment and feature selection methods","volume":"6","author":"Wang","year":"2011","journal-title":"PLoS One"},{"key":"2023020116172102000_btu738-B74","doi-asserted-by":"crossref","first-page":"D590","DOI":"10.1093\/nar\/gkh025","article-title":"APD: the antimicrobial peptide database","volume":"32","author":"Wang","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"2023020116172102000_btu738-B75","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1124\/pr.55.1.2","article-title":"Mechanisms of antimicrobial peptide action and resistance","volume":"55","author":"Yeaman","year":"2003","journal-title":"Pharmacol. Rev."},{"key":"2023020116172102000_btu738-B76","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0014-5793(95)01050-O","article-title":"Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain","volume":"374","author":"Zanetti","year":"1995","journal-title":"FEBS Lett."},{"key":"2023020116172102000_btu738-B77","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/415389a","article-title":"Antimicrobial peptides of multicellular organisms","volume":"415","author":"Zasloff","year":"2002","journal-title":"Nature"}],"container-title":["Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article-pdf\/31\/6\/849\/49011187\/bioinformatics_31_6_849.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article-pdf\/31\/6\/849\/49011187\/bioinformatics_31_6_849.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,2,2]],"date-time":"2023-02-02T00:30:56Z","timestamp":1675297856000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article\/31\/6\/849\/214926"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,11,10]]},"references-count":76,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2015,3,15]]}},"URL":"https:\/\/doi.org\/10.1093\/bioinformatics\/btu738","relation":{},"ISSN":["1367-4811","1367-4803"],"issn-type":[{"value":"1367-4811","type":"electronic"},{"value":"1367-4803","type":"print"}],"subject":[],"published-other":{"date-parts":[[2015,3,15]]},"published":{"date-parts":[[2014,11,10]]}}}