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http://purl.uniprot.org/citations/20418437http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20418437http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20418437http://www.w3.org/2000/01/rdf-schema#comment"Enterocin X, composed of two antibacterial peptides (Xalpha and Xbeta), is a novel class IIb bacteriocin from Enterococcus faecium KU-B5. When combined, Xalpha and Xbeta display variably enhanced or reduced antibacterial activity toward a panel of indicators compared to each peptide individually. In E. faecium strains that produce enterocins A and B, such as KU-B5, only one additional bacteriocin had previously been known."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.org/dc/terms/identifier"doi:10.1128/AEM.02264-09"xsd:string
http://purl.uniprot.org/citations/20418437http://purl.org/dc/terms/identifier"doi:10.1128/aem.02264-09"xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/author"Nakayama J."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/author"Nakayama J."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/author"Sonomoto K."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/author"Sonomoto K."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/author"Zendo T."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/author"Zendo T."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/author"Hu C.B."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/author"Hu C.-B."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/author"Malaphan W."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/author"Malaphan W."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/name"Appl. Environ. Microbiol."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/name"Appl Environ Microbiol"xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/pages"4542-4545"xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/pages"4542-4545"xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/title"Enterocin X, a novel two-peptide bacteriocin from Enterococcus faecium KU-B5, has an antibacterial spectrum entirely different from those of its component peptides."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/title"Enterocin X, a novel two-peptide bacteriocin from Enterococcus faecium KU-B5, has an antibacterial spectrum entirely different from those of its component peptides."xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/volume"76"xsd:string
http://purl.uniprot.org/citations/20418437http://purl.uniprot.org/core/volume"76"xsd:string