http://purl.uniprot.org/citations/1567877 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/1567877 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/1567877 | http://www.w3.org/2000/01/rdf-schema#comment | "Two antimicrobial peptides (Ac-AMP1 and Ac-AMP2) were isolated from seeds of amaranth (Amaranthus caudatus), and their physicochemical and biological properties were characterized. On the basis of fast atom bombardment mass spectroscopy, Ac-AMP1 and Ac-AMP2 have monoisotopic molecular masses of 3025 and 3181, respectively. Both proteins have pI values above 10. The amino acid sequence of Ac-AMP1 (29 residues) is identical to that of Ac-AMP2 (30 residues), except that the latter has 1 additional residue at the carboxyl terminus. The sequences are highly homologous to the cysteine/glycine-rich domain occurring in many chitin-binding proteins. Both Ac-AMP1 and Ac-AMP2 bind to chitin in a reversible way. Ac-AMP1 and Ac-AMP2 inhibit the growth of different plant pathogenic fungi at much lower doses than other known antifungal chitin-binding proteins. In addition, they show some activity on Gram-positive bacteria. The antimicrobial effect of Ac-AMP1 and Ac-AMP2 is strongly antagonized by cations."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi00132a023"xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi00132a023"xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Claeys M."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Claeys M."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Cammue B.P.A."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Cammue B.P.A."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "van Damme J."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "van Damme J."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Vanderleyden J."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Vanderleyden J."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Proost P."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Proost P."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Broekaert W.F."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Broekaert W.F."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Dillen L."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Dillen L."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Marien W."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Marien W."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Rees S.B."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Rees S.B."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Terras F.R.G."xsd:string |
http://purl.uniprot.org/citations/1567877 | http://purl.uniprot.org/core/author | "Terras F.R.G."xsd:string |