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http://purl.uniprot.org/citations/1894596http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1894596http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1894596http://www.w3.org/2000/01/rdf-schema#comment"Amino acid deprivation of rat hepatoma cells induced the levels of a 612-base pair mRNA termed ASI (Shay, N. F., Nick, H. S., and Kilberg, M. S. (1990) J. Biol. Chem. 265, 17844-17848). The ASI mRNA was present at levels equal to or greater than actin in every rat tissue tested. The corresponding full-length cDNA was cloned, and the present report demonstrates that the deduced 184-residue amino acid sequence shares greater than 30% identity to a number of bacterial and chloroplast L22 ribosomal proteins, including those from Escherichia coli and Halobacterium halobium. A monospecific anti-peptide antibody was produced that upon immunochemical analysis of subcellular fractions of rat liver recognized a band in the microsomal fraction and, more specifically, reacted with a single polypeptide in the ribosomal large subunit fraction. The antibody did not react with any proteins of the mitochondrial large subunit, but did recognize a protein in human liver homogenate at the same relative mobility (23 kDa) as that observed for rat liver."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)47324-9"xsd:string
http://purl.uniprot.org/citations/1894596http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)47324-9"xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/author"Kilberg M.S."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/author"Kilberg M.S."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/author"Laipis P.J."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/author"Laipis P.J."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/author"Shay N.F."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/author"Shay N.F."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/author"Laine R.O."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/author"Laine R.O."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/pages"16969-16972"xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/pages"16969-16972"xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/title"Identification of an amino acid-regulated mRNA from rat liver as the mammalian equivalent of bacterial ribosomal protein L22."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/title"Identification of an amino acid-regulated mRNA from rat liver as the mammalian equivalent of bacterial ribosomal protein L22."xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/volume"266"xsd:string
http://purl.uniprot.org/citations/1894596http://purl.uniprot.org/core/volume"266"xsd:string
http://purl.uniprot.org/citations/1894596http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1894596
http://purl.uniprot.org/citations/1894596http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1894596