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http://purl.uniprot.org/citations/1733929http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1733929http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1733929http://www.w3.org/2000/01/rdf-schema#comment"We have isolated from seeds of Mirabilis jalapa L. two antimicrobial peptides, designated Mj-AMP1 and Mj-AMP2, respectively. These peptides are highly basic and consist of 37 and 36 residues for Mj-AMP1 and Mj-AMP2, respectively. Both peptides contain three disulfide bridges and differ from one another only by 4 amino acids. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the reduced and unreduced peptides suggests that the peptides associate into dimers in their native form. The Mj-AMPs exhibit a broad spectrum of antifungal activity since they are active against all 13 tested plant pathogenic fungi. Concentrations required for 50% inhibition of fungal growth vary from 6 to 300 micrograms/ml for Mj-AMP1 and from 0.5 to 20 micrograms/ml for Mj-AMP2. These peptides were also active on two tested Gram-positive bacteria but were apparently nontoxic for Gram-negative bacteria and cultured human cells. Although the Mj-AMPs show sequence similarity to mu-agatoxins, a class of insecticidal neurotoxic peptides isolated from the venom of spiders, they do not affect pulse transmission in insect nerves."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)45866-8"xsd:string
http://purl.uniprot.org/citations/1733929http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)45866-8"xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Cammue B.P.A."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Cammue B.P.A."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"van Damme J."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"van Damme J."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Vanderleyden J."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Vanderleyden J."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Proost P."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Proost P."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Broekaert W.F."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Broekaert W.F."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Rees S.B."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Rees S.B."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Terras F.R.G."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"Terras F.R.G."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"de Bolle M.F.C."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/author"de Bolle M.F.C."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1733929http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string