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http://purl.uniprot.org/citations/14688290http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14688290http://www.w3.org/2000/01/rdf-schema#comment"The NADPH-dependent protochlorophyllide (Pchlide) oxidoreductase (POR) is unique because it is a photoenzyme that requires light for its catalytic activity and uses Pchlide itself as a photoreceptor. In Arabidopsis, there are three structurally related PORs, denoted PORA, PORB, and PORC. The import of one of them, PORA, into plastids of cotyledons is substrate dependent. This substrate dependence is demonstrated in intact seedlings of wild-type Arabidopsis and two mutants, xantha2, which is devoid of Pchlide, and flu, which upon redarkening rapidly accumulates Pchlide. In true leaves, PORA uptake does not require the presence of Pchlide. The organ specificity of the substrate-dependent import of PORA reveals a means of controlling plastid protein translocation that is closely associated with a key step in plant development, the light-dependent transformation of cotyledons from a storage organ to a photosynthetically active leaf."xsd:string
http://purl.uniprot.org/citations/14688290http://purl.org/dc/terms/identifier"doi:10.1105/tpc.015008"xsd:string
http://purl.uniprot.org/citations/14688290http://purl.uniprot.org/core/author"Apel K."xsd:string
http://purl.uniprot.org/citations/14688290http://purl.uniprot.org/core/author"Kim C."xsd:string
http://purl.uniprot.org/citations/14688290http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14688290http://purl.uniprot.org/core/name"Plant Cell"xsd:string
http://purl.uniprot.org/citations/14688290http://purl.uniprot.org/core/pages"88-98"xsd:string
http://purl.uniprot.org/citations/14688290http://purl.uniprot.org/core/title"Substrate-dependent and organ-specific chloroplast protein import in planta."xsd:string
http://purl.uniprot.org/citations/14688290http://purl.uniprot.org/core/volume"16"xsd:string
http://purl.uniprot.org/citations/14688290http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14688290
http://purl.uniprot.org/citations/14688290http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14688290
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http://purl.uniprot.org/uniprot/#_F4JFR2-mappedCitation-14688290http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14688290
http://purl.uniprot.org/uniprot/#_F4I2F8-mappedCitation-14688290http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14688290
http://purl.uniprot.org/uniprot/#_Q0WVW0-mappedCitation-14688290http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14688290
http://purl.uniprot.org/uniprot/#_O48741-mappedCitation-14688290http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14688290
http://purl.uniprot.org/uniprot/#_P21218-mappedCitation-14688290http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14688290
http://purl.uniprot.org/uniprot/#_Q42536-mappedCitation-14688290http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14688290
http://purl.uniprot.org/uniprot/#_Q940U6-mappedCitation-14688290http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14688290
http://purl.uniprot.org/uniprot/F4JFR1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/14688290
http://purl.uniprot.org/uniprot/F4JFR2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/14688290
http://purl.uniprot.org/uniprot/P21218http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/14688290
http://purl.uniprot.org/uniprot/Q42536http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/14688290
http://purl.uniprot.org/uniprot/Q940U6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/14688290