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http://purl.uniprot.org/citations/8524242http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8524242http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8524242http://www.w3.org/2000/01/rdf-schema#comment"The poly(A)-binding protein (PABP) binds to the poly(A) tail present at the 3' ends of most eukaryotic mRNAs. PABP is thought to play a role in both translation and mRNA stability. Here we describe the molecular cloning and characterization of an inducible PABP, iPABP, from a cDNA library prepared from activated T cells. iPABP shows 79% sequence identity to PABP at the amino acid level. The RNA binding domains of iPABP and PABP are nearly identical, while their C termini are more divergent. Like PABP, iPABP is primarily localized to the cytoplasm. iPABP is expressed at low levels in resting normal human T cells; following T-cell activation, however, iPABP mRNA levels are rapidly up-regulated. In contrast, PABP is constitutively expressed in both resting and activated T cells. iPABP mRNA was also expressed at much higher levels than PABP mRNA in heart and skeletal muscle tissue. These data suggest that the regulation of cytoplasmic poly(A)-binding activity is more complex than previously believed. In most tissues, poly(A)-binding activity is likely to be the result of the combined effects of constitutively expressed PABP and iPABP, whose expression is subject to more complex regulation."xsd:string
http://purl.uniprot.org/citations/8524242http://purl.org/dc/terms/identifier"doi:10.1128/mcb.15.12.6770"xsd:string
http://purl.uniprot.org/citations/8524242http://purl.org/dc/terms/identifier"doi:10.1128/mcb.15.12.6770"xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/author"Yang H."xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/author"Yang H."xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/author"Lindsten T."xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/author"Lindsten T."xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/author"Duckett C.S."xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/author"Duckett C.S."xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/pages"6770-6776"xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/pages"6770-6776"xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/title"iPABP, an inducible poly(A)-binding protein detected in activated human T cells."xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/title"iPABP, an inducible poly(A)-binding protein detected in activated human T cells."xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/8524242http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/8524242http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8524242
http://purl.uniprot.org/citations/8524242http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8524242
http://purl.uniprot.org/citations/8524242http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8524242
http://purl.uniprot.org/citations/8524242http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8524242