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http://purl.uniprot.org/citations/8946947http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8946947http://www.w3.org/2000/01/rdf-schema#comment"Three lines of evidence indicate that the 14-3-3 proteins that inactivate the phosphorylated form of spinach leaf NADH:nitrate reductase (NR) bind to the enzyme at the regulatory phosphorylation site (Ser-543). First, a phosphorylated synthetic peptide based on the regulatory site can prevent and also reverse the inactivation of phospho-NR caused by 14-3-3 proteins. Second, sequence-specific and phosphorylation-dependent binding of the aforementioned synthetic peptide to the 14-3-3 proteins was demonstrated in vitro. Third, 14-3-3 proteins were required for the ATP-dependent phosphorylation of NR (as assessed by activity measurements) in the presence of NR-kinase and leaf protein phosphatases. Lastly, we demonstrate specificity of recombinant Arabidopsis 14-3-3 isoforms in the interaction with phospho-NR: omega> chi> upsilon>>> phi, psi."xsd:string
http://purl.uniprot.org/citations/8946947http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(96)01188-x"xsd:string
http://purl.uniprot.org/citations/8946947http://purl.uniprot.org/core/author"Ferl R.J."xsd:string
http://purl.uniprot.org/citations/8946947http://purl.uniprot.org/core/author"Wu K."xsd:string
http://purl.uniprot.org/citations/8946947http://purl.uniprot.org/core/author"Bachmann M."xsd:string
http://purl.uniprot.org/citations/8946947http://purl.uniprot.org/core/author"Huber S.C."xsd:string
http://purl.uniprot.org/citations/8946947http://purl.uniprot.org/core/author"Huber J.L."xsd:string
http://purl.uniprot.org/citations/8946947http://purl.uniprot.org/core/author"Athwal G.S."xsd:string
http://purl.uniprot.org/citations/8946947http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8946947http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/8946947http://purl.uniprot.org/core/pages"26-30"xsd:string
http://purl.uniprot.org/citations/8946947http://purl.uniprot.org/core/title"14-3-3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduce dephosphorylation of Ser-543 by endogenous protein phosphatases."xsd:string
http://purl.uniprot.org/citations/8946947http://purl.uniprot.org/core/volume"398"xsd:string
http://purl.uniprot.org/citations/8946947http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8946947
http://purl.uniprot.org/citations/8946947http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8946947
http://purl.uniprot.org/uniprot/#_P42645-mappedCitation-8946947http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/8946947
http://purl.uniprot.org/uniprot/#_Q01525-mappedCitation-8946947http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/8946947
http://purl.uniprot.org/uniprot/Q01525http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/8946947
http://purl.uniprot.org/uniprot/P42645http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/8946947