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http://purl.uniprot.org/citations/21418358http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21418358http://www.w3.org/2000/01/rdf-schema#comment"Plant secondary metabolites are known to facilitate interactions with a variety of beneficial and detrimental organisms, yet the contribution of specific metabolites to interactions with fungal pathogens is poorly understood. Here we show that, with respect to aliphatic glucosinolate-derived isothiocyanates, toxicity against the pathogenic ascomycete Sclerotinia sclerotiorum depends on side chain structure. Genes associated with the formation of the secondary metabolites camalexin and glucosinolate were induced in Arabidopsis thaliana leaves challenged with the necrotrophic pathogen S. sclerotiorum. Unlike S. sclerotiorum, the closely related ascomycete Botrytis cinerea was not identified to induce genes associated with aliphatic glucosinolate biosynthesis in pathogen-challenged leaves. Mutant plant lines deficient in camalexin, indole, or aliphatic glucosinolate biosynthesis were hypersusceptible to S. sclerotiorum, among them the myb28 mutant, which has a regulatory defect resulting in decreased production of long-chained aliphatic glucosinolates. The antimicrobial activity of aliphatic glucosinolate-derived isothiocyanates was dependent on side chain elongation and modification, with 8-methylsulfinyloctyl isothiocyanate being most toxic to S. sclerotiorum. This information is important for microbial associations with cruciferous host plants and for metabolic engineering of pathogen defenses in cruciferous plants that produce short-chained aliphatic glucosinolates."xsd:string
http://purl.uniprot.org/citations/21418358http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-313x.2011.04578.x"xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/author"Kamiya Y."xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/author"Shimada Y."xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/author"Saito K."xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/author"Sawada Y."xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/author"Stotz H.U."xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/author"Hirai M.Y."xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/author"Sasaki E."xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/author"Brown P.D."xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/author"Krischke M."xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/name"Plant J"xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/pages"81-93"xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/title"Role of camalexin, indole glucosinolates, and side chain modification of glucosinolate-derived isothiocyanates in defense of Arabidopsis against Sclerotinia sclerotiorum."xsd:string
http://purl.uniprot.org/citations/21418358http://purl.uniprot.org/core/volume"67"xsd:string
http://purl.uniprot.org/citations/21418358http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21418358
http://purl.uniprot.org/citations/21418358http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21418358
http://purl.uniprot.org/uniprot/Q9FWW9#attribution-D864A9AF44D2C843C1F9969C94D3D7BChttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21418358
http://purl.uniprot.org/uniprot/Q9SPG5#attribution-8BF67164D8A86511398C03C5B0861F70http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21418358
http://purl.uniprot.org/uniprot/Q9FLR1#attribution-8BF67164D8A86511398C03C5B0861F70http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21418358
http://purl.uniprot.org/uniprot/Q9FLR1#attribution-A8CBC81BB68E0C3C7D84E26702B37A6Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21418358
http://purl.uniprot.org/uniprot/Q9SPG2#attribution-8BF67164D8A86511398C03C5B0861F70http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21418358
http://purl.uniprot.org/uniprot/#_A0A178UN88-mappedCitation-21418358http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21418358