{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T23:16:46Z","timestamp":1792883806909,"version":"4.5.0"},"reference-count":0,"publisher":"Walter de Gruyter GmbH","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,6,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    We report the identification, cloning, heterologous expression and functional characterization of a novel antifungal peptide named lucimycin from the common green bottle fly\n                    <jats:italic>Lucilia sericata<\/jats:italic>\n                    . The lucimycin cDNA was isolated from a library of genes induced during the innate immune response in\n                    <jats:italic>L. sericata<\/jats:italic>\n                    larvae, which are used as therapeutic maggots. The peptide comprises 77 amino acid residues with a molecular mass of 8.2 kDa and a p\n                    <jats:italic>I<\/jats:italic>\n                    of 6.6. It is predicted to contain a zinc-binding motif and to form a random coil, lacking \u03b2-sheets or other secondary structures. Lucimycin was active against fungi from the phyla Ascomycota, Basidiomycota and Zygomycota, in addition to the oomycete\n                    <jats:italic>Phytophtora parasitica<\/jats:italic>\n                    , but it was inactive against bacteria. A mutant version of lucimycin, lacking the four C-terminal amino acid residues, displayed 40-fold lower activity. The activity of lucimycin against a number of highly-destructive plant pathogens could be exploited to produce transgenic crops that are resistant against fungal diseases.\n                  <\/jats:p>","DOI":"10.1515\/hsz-2013-0263","type":"journal-article","created":{"date-parts":[[2014,3,12]],"date-time":"2014-03-12T16:10:37Z","timestamp":1394640637000},"page":"649-656","source":"Crossref","is-referenced-by-count":56,"title":["Lucimycin, an antifungal peptide from the therapeutic maggot of the common green bottle fly\n                    <i>Lucilia sericata<\/i>"],"prefix":"10.1515","volume":"395","author":[{"given":"Anne-Kathrin","family":"P\u00f6ppel","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aline","family":"Koch","sequence":"additional","affiliation":[{"name":"Institute for Phytopathology and Applied Zoology, Justus-Liebig-University of Giessen, Heinrich-Buff-Ring 26-32, D-35392 Giessen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karl-Heinz","family":"Kogel","sequence":"additional","affiliation":[{"name":"Institute for Phytopathology and Applied Zoology, Justus-Liebig-University of Giessen, Heinrich-Buff-Ring 26-32, D-35392 Giessen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heiko","family":"Vogel","sequence":"additional","affiliation":[{"name":"Max-Planck-Institute for Chemical Ecology, Department of Entomology, Hans-Knoell-Strasse 8, D-07745 Jena, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Kollewe","sequence":"additional","affiliation":[{"name":"Fraunhofer Institute for Molecular Biology and Applied Ecology, Department of Bioresources, Winchester Strasse, D-35394 Giessen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jochen","family":"Wiesner","sequence":"additional","affiliation":[{"name":"Fraunhofer Institute for Molecular Biology and Applied Ecology, Department of Bioresources, Winchester Strasse, D-35394 Giessen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andreas","family":"Vilcinskas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","published-online":{"date-parts":[[2014,3,12]]},"container-title":["Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.degruyter.com\/view\/j\/bchm.2014.395.issue-6\/hsz-2013-0263\/hsz-2013-0263.xml","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/hsz-2013-0263\/xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/hsz-2013-0263\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,14]],"date-time":"2022-03-14T11:19:22Z","timestamp":1647256762000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/hsz-2013-0263\/html"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,3,12]]},"references-count":0,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2014,2,14]]},"published-print":{"date-parts":[[2014,6,1]]}},"alternative-id":["10.1515\/hsz-2013-0263"],"URL":"https:\/\/doi.org\/10.1515\/hsz-2013-0263","relation":{},"ISSN":["1437-4315","1431-6730"],"issn-type":[{"value":"1437-4315","type":"electronic"},{"value":"1431-6730","type":"print"}],"subject":[],"published":{"date-parts":[[2014,3,12]]}}}