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http://purl.uniprot.org/citations/9257708http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9257708http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9257708http://www.w3.org/2000/01/rdf-schema#comment"We cloned precursors of three new antimicrobial peptides, Styelins C, D and E, from a pharyngeal cDNA library of a tunicate, Styela clava. Preprostyelins resembled dipteran preprocecropins, while the mature domain of Styelin C resembled Cecropin P1, an antimicrobial peptide purified from the porcine intestine. Beginning with the last 6 residues of their signal sequences, Styelin C and Cecropin 1 from Drosophila virilis had 8/11 identical amino acids (72.7%). Moreover, 4 of the last 6 residues of their mature peptide domains were also identical. Styelins were shorter, by 8 residues, than dipteran cecropins and preprostyelins contained a conserved, polyanionic C-terminal extension that was absent in preprocecropins. Delineation of cecropin-like antimicrobial peptides in a protochordate supports the antiquity of this family as effectors of innate immunity in animals and it increases the likelihood that additional cecropin-like peptides will be found among other evolutionary descendants of protochordates--vertebrates."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(97)00769-2"xsd:string
http://purl.uniprot.org/citations/9257708http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(97)00769-2"xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/author"Zhao C."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/author"Zhao C."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/author"Lee I.H."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/author"Lee I.H."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/author"Lehrer R.I."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/author"Lehrer R.I."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/author"Liaw L."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/author"Liaw L."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/pages"144-148"xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/pages"144-148"xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/title"cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate, Styela clava."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/title"cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate, Styela clava."xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/volume"412"xsd:string
http://purl.uniprot.org/citations/9257708http://purl.uniprot.org/core/volume"412"xsd:string
http://purl.uniprot.org/citations/9257708http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9257708
http://purl.uniprot.org/citations/9257708http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9257708