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http://purl.uniprot.org/citations/11034343http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11034343http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11034343http://www.w3.org/2000/01/rdf-schema#comment"A study by two-dimensional electrophoresis showed that the soluble, lumenal fraction of Arabidopsis thaliana thylakoids can be resolved into 300 protein spots. After subtraction of low-intensity spots and accounting for low-level stromal contamination, the number of more abundant, lumenal proteins was estimated to be between 30 and 60. Two of these proteins have been identified: a novel plastocyanin that also was the predominant component of the total plastocyanin pool, and a putative ascorbate peroxidase. Import studies showed that these proteins are routed to the thylakoid lumen by the Sec- and delta pH-dependent translocation pathways, respectively. In addition, novel isoforms of PsbO and PsbQ were identified."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(00)01890-1"xsd:string
http://purl.uniprot.org/citations/11034343http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(00)01890-1"xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/author"Schroeder W.P."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/author"Schroeder W.P."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/author"Robinson C."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/author"Robinson C."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/author"Kieselbach T."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/author"Kieselbach T."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/author"Bystedt M."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/author"Bystedt M."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/author"Hynds P."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/author"Hynds P."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/pages"271-276"xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/pages"271-276"xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/title"A peroxidase homologue and novel plastocyanin located by proteomics to the Arabidopsis chloroplast thylakoid lumen."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/title"A peroxidase homologue and novel plastocyanin located by proteomics to the Arabidopsis chloroplast thylakoid lumen."xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/volume"480"xsd:string
http://purl.uniprot.org/citations/11034343http://purl.uniprot.org/core/volume"480"xsd:string