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http://purl.uniprot.org/citations/9011084http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9011084http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9011084http://www.w3.org/2000/01/rdf-schema#comment"In Arabidopsis thaliana, 1-aminocyclopropane-1-carboxylate synthase (ACS) is encoded by a multigene family consisting of at least five members whose expression is induced by hormones, developmental signals, and protein synthesis inhibition. Li+, known to interfere with the phosphoinositide (PI) second messenger system by inhibiting the activity of inositol-phosphate phosphatases, is one of the strongest inducers of ACC synthase activity in plants. Treatment of etiolated Arabidopsis seedlings with LiCl results in a rapid induction of the ACS5 gene. Also, LiCl represses the cycloheximide (CHX)-induced accumulation of the ACS2 mRNA. The effects of Li+ on the expression of ACS5 and ACS2 are specific, dose-dependent, and can be reversed by Ca2+ and mimicked by the protein kinase inhibitor K-252a. The results suggest that the regulation of some ACS genes by various inducers may involve protein kinase activity, which in turn may be controlled through an inositol 1,4,5-triphosphate (IP3)-mediated Ca2+ mobilization. Since plants contain no Li+, the cation appears to unmask pre-existing biochemical capacity that may be utilized by various unknown transducers during plant growth and development."xsd:string
http://purl.uniprot.org/citations/9011084http://purl.org/dc/terms/identifier"doi:10.1046/j.1365-313x.1996.10061027.x"xsd:string
http://purl.uniprot.org/citations/9011084http://purl.org/dc/terms/identifier"doi:10.1046/j.1365-313x.1996.10061027.x"xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/author"Liang X.-W."xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/author"Liang X.-W."xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/author"Theologis A."xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/author"Theologis A."xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/author"Shen N.F."xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/author"Shen N.F."xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/name"Plant J."xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/name"Plant J."xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/pages"1027-1036"xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/pages"1027-1036"xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/title"Li(+)-regulated 1-aminocyclopropane-1-carboxylate synthase gene expression in Arabidopsis thaliana."xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/title"Li(+)-regulated 1-aminocyclopropane-1-carboxylate synthase gene expression in Arabidopsis thaliana."xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/9011084http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/9011084http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9011084
http://purl.uniprot.org/citations/9011084http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9011084
http://purl.uniprot.org/citations/9011084http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9011084
http://purl.uniprot.org/citations/9011084http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9011084