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http://purl.uniprot.org/citations/8888618http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8888618http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8888618http://www.w3.org/2000/01/rdf-schema#comment"Short-term cultured suspension cells of rice (Oryza sativa L.) are capable of regeneration, but not in long-term culture. For clarification of the mechanism of regeneration, protein phosphorylation in short-term and long-term cultured suspension cells was compared by two dimensional-polyacrylamide gel electrophoresis. A 56 kDa protein having an isoelectric point of 4.5 was phosphorylated in vitro in short-term cultured suspension cells, but was not phosphorylated after regeneration. This protein in long-term cultured suspension cells remained phosphorylated after transfer to the regeneration medium. However, using an antibody raised against this protein from short-term cultured suspension cells, it was always detected in long-term and short-term cultured suspension cells after transfer to the regeneration medium. The partial amino acid sequence of the HPLC-purified protein showed homology to a calcium-binding protein from maize. The phosphorylation of the 56 kDa protein (pp56) appears to be associated with the regeneration of cultured rice cells."xsd:string
http://purl.uniprot.org/citations/8888618http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.pcp.a029009"xsd:string
http://purl.uniprot.org/citations/8888618http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.pcp.a029009"xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/author"Abe K."xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/author"Abe K."xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/author"Masuda T."xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/author"Masuda T."xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/author"Komatsu S."xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/author"Komatsu S."xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/name"Plant Cell Physiol."xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/name"Plant Cell Physiol."xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/pages"748-753"xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/pages"748-753"xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/title"Phosphorylation of a protein (pp56) is related to the regeneration of rice cultured suspension cells."xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/title"Phosphorylation of a protein (pp56) is related to the regeneration of rice cultured suspension cells."xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/8888618http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/8888618http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8888618
http://purl.uniprot.org/citations/8888618http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8888618
http://purl.uniprot.org/citations/8888618http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8888618
http://purl.uniprot.org/citations/8888618http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8888618