{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T04:04:57Z","timestamp":1791173097880,"version":"4.1.0"},"reference-count":0,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[1993,12,1]],"date-time":"1993-12-01T00:00:00Z","timestamp":754704000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[1993,12]]},"abstract":"<jats:p>A cationic antimicrobial protein of 18 kDa (CAP18) was originally isolated from rabbit granulocytes by using as an assay the agglutination of Re-lipopolysaccharide-coated erythrocytes. The C-terminal 37 amino acids of CAP18 (CAP18(106-142)) make up the lipopolysaccharide-binding domain. Synthetic CAP18(106-142) has broad antimicrobial activity against both gram-positive (50% inhibitory concentration, 130 to 200 nM) and gram-negative (50% inhibitory concentration, 20 to 100 nM) bacteria. Susceptible strains include Staphylococcus aureus, Streptococcus pneumoniae, Escherichia coli, Pseudomonas aeruginosa, and Salmonella typhimurium. Antimicrobial activity is highly dependent on peptide structure. Although a 32-amino-acid peptide resulting from the truncation of 5 amino acids from the C terminus of CAP18(106-142) is highly active, other fragments of CAP18(106-142), including CAP18(106-142) with a truncated N terminus, do not exhibit antimicrobial activity. Unlike previously characterized antimicrobial peptides derived from granulocyte proteins, CAP18(106-142) is active in serum. CAP18(106-142) or a derivative peptide may have therapeutic potential for bacterial sepsis.<\/jats:p>","DOI":"10.1128\/aac.37.12.2534","type":"journal-article","created":{"date-parts":[[2012,6,28]],"date-time":"2012-06-28T00:05:50Z","timestamp":1340841950000},"page":"2534-2539","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":82,"title":["Antimicrobial activity of rabbit CAP18-derived peptides"],"prefix":"10.1128","volume":"37","author":[{"given":"J W","family":"Larrick","sequence":"first","affiliation":[{"name":"Palo Alto Institute of Molecular Medicine, Mountain View, California 94043."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M","family":"Hirata","sequence":"additional","affiliation":[{"name":"Palo Alto Institute of Molecular Medicine, Mountain View, California 94043."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Y","family":"Shimomoura","sequence":"additional","affiliation":[{"name":"Palo Alto Institute of Molecular Medicine, Mountain View, California 94043."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M","family":"Yoshida","sequence":"additional","affiliation":[{"name":"Palo Alto Institute of Molecular Medicine, Mountain View, California 94043."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"H","family":"Zheng","sequence":"additional","affiliation":[{"name":"Palo Alto Institute of Molecular Medicine, Mountain View, California 94043."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J","family":"Zhong","sequence":"additional","affiliation":[{"name":"Palo Alto Institute of Molecular Medicine, Mountain View, California 94043."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S C","family":"Wright","sequence":"additional","affiliation":[{"name":"Palo Alto Institute of Molecular Medicine, Mountain View, California 94043."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","container-title":["Antimicrobial Agents and Chemotherapy"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.37.12.2534","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.37.12.2534","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,21]],"date-time":"2022-02-21T15:31:40Z","timestamp":1645457500000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/AAC.37.12.2534"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1993,12]]},"references-count":0,"journal-issue":{"issue":"12","published-print":{"date-parts":[[1993,12]]}},"alternative-id":["10.1128\/AAC.37.12.2534"],"URL":"https:\/\/doi.org\/10.1128\/aac.37.12.2534","relation":{},"ISSN":["0066-4804","1098-6596"],"issn-type":[{"value":"0066-4804","type":"print"},{"value":"1098-6596","type":"electronic"}],"subject":[],"published":{"date-parts":[[1993,12]]},"assertion":[{"value":"1993-12-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}