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http://purl.uniprot.org/citations/15361857http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15361857http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15361857http://www.w3.org/2000/01/rdf-schema#comment"Nonsense-mediated mRNA decay (NMD) in mammalian cells targets cap-binding protein 80 (CBP80)-bound mRNA during or after a pioneer round of translation. It is unknown whether eukaryotic translation initiation factor 4G (eIF4G) functions in the pioneer round. We show that baculovirus-produced CBP80 and CBP20 independently interact with eIF4GI. The interactions between eIF4G and the heterodimer CBP80/20 suggest that eIF4G has a function in the pioneer initiation complex rather than merely a presence during remodeling to the steady-state complex. First, NMD is inhibited upon eIF4G cleavage by HIV-2 or poliovirus 2A protease. Second, eIF4GI coimmunopurifies with pre-mRNA, indicating that it associates with transcripts before the pioneer round. Third, eIF4G immunopurifies with Upf NMD factors and eIF4AIII, which are constituents of the pioneer translation initiation complex. We propose a model in which eIF4G serves to connect CBP80/20 with other initiation factors during the pioneer round of translation."xsd:string
http://purl.uniprot.org/citations/15361857http://purl.org/dc/terms/identifier"doi:10.1038/nsmb824"xsd:string
http://purl.uniprot.org/citations/15361857http://purl.org/dc/terms/identifier"doi:10.1038/nsmb824"xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/author"Maquat L.E."xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/author"Maquat L.E."xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/author"Lejeune F."xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/author"Lejeune F."xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/author"Ranganathan A.C."xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/author"Ranganathan A.C."xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/pages"992-1000"xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/pages"992-1000"xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/title"eIF4G is required for the pioneer round of translation in mammalian cells."xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/title"eIF4G is required for the pioneer round of translation in mammalian cells."xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/15361857http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/15361857http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15361857
http://purl.uniprot.org/citations/15361857http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15361857
http://purl.uniprot.org/citations/15361857http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15361857
http://purl.uniprot.org/citations/15361857http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15361857