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http://purl.uniprot.org/citations/15147898http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15147898http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15147898http://www.w3.org/2000/01/rdf-schema#comment"Copper transport across membranes plays an important role in plant growth and survival. P(1B)-type ATPases participate in transmembrane transport of copper in various organisms. A Brassica napus cDNA (BnRAN1) encoding a putative Cu(2+)-ATPase was cloned in this study. A complementation assay demonstrated that the protein encoded by this cDNA could functionally replace Ccc2p, a Saccharomyces cerevisiae Cu(2+)-ATPase, rescuing growth of ccc2 mutant under iron-limited conditions. Our results suggest that this rescue likely resulted from restoration of copper delivery, mediated by BnRAN1, to Fet3p. This study is amongst the first to demonstrate that a putative plant P(1B)-ATPase is functional and to examine its substrate specificity."xsd:string
http://purl.uniprot.org/citations/15147898http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2004.04.035"xsd:string
http://purl.uniprot.org/citations/15147898http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2004.04.035"xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/author"Basu U."xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/author"Basu U."xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/author"Southron J.L."xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/author"Southron J.L."xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/author"Taylor G.J."xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/author"Taylor G.J."xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/pages"218-222"xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/pages"218-222"xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/title"Complementation of Saccharomyces cerevisiae ccc2 mutant by a putative P1B-ATPase from Brassica napus supports a copper-transporting function."xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/title"Complementation of Saccharomyces cerevisiae ccc2 mutant by a putative P1B-ATPase from Brassica napus supports a copper-transporting function."xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/volume"566"xsd:string
http://purl.uniprot.org/citations/15147898http://purl.uniprot.org/core/volume"566"xsd:string
http://purl.uniprot.org/citations/15147898http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15147898
http://purl.uniprot.org/citations/15147898http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15147898
http://purl.uniprot.org/citations/15147898http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15147898
http://purl.uniprot.org/citations/15147898http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15147898