| http://purl.uniprot.org/citations/19264777 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19264777 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19264777 | http://www.w3.org/2000/01/rdf-schema#comment | "The adenovirus type 5 (Ad5) late region 4 (L4) 100-kDa nonstructural protein (L4-100K) mediates inhibition of cellular protein synthesis and selective translation of tripartite leader (TL)-containing viral late mRNAs via ribosome shunting. In addition, L4-100K has been implicated in the trimerization and nuclear localization of hexon protein. We previously proved that L4-100K is a substrate of the protein arginine methylation machinery, an emergent posttranslational modification system involved in a growing list of cellular processes, including transcriptional regulation, cell signaling, RNA processing, and DNA repair. As understood at present, L4-100K arginine methylation involves protein arginine methyltransferase 1 (PRMT1), which asymmetrically dimethylates arginines embedded in arginine-glycine-glycine (RGG) or glycine-arginine-rich (GAR) domains. To identify the methylated arginine residues and assess the role of L4-100K arginine methylation, we generated amino acid substitution mutations in the RGG and GAR motifs to examine their effects in Ad-infected and plasmid-transfected cells. Arginine-to-glycine exchanges in the RGG boxes significantly diminished L4-100K methylation in the course of an infection and substantially reduced virus growth, demonstrating that L4-100K methylation in RGG motifs is an important host cell function required for efficient Ad replication. Our data further indicate that PRMT1-catalyzed arginine methylation in the RGG boxes regulates the binding of L4-100K to hexon and promotes the capsid assembly of the structural protein as well as modulating TL-mRNA interaction. Furthermore, substitutions in GAR, but not RGG, regions affected L4-100K nuclear import, implying that the nuclear localization signal of L4-100K is located within the GAR sequence."xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.02493-08"xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.02493-08"xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/author | "Dobner T."xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/author | "Dobner T."xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/author | "Koyuncu O.O."xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/author | "Koyuncu O.O."xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/name | "J. Virol."xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/name | "J. Virol."xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/pages | "4778-4790"xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/pages | "4778-4790"xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/title | "Arginine methylation of human adenovirus type 5 L4 100-kilodalton protein is required for efficient virus production."xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/title | "Arginine methylation of human adenovirus type 5 L4 100-kilodalton protein is required for efficient virus production."xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/volume | "83"xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://purl.uniprot.org/core/volume | "83"xsd:string |
| http://purl.uniprot.org/citations/19264777 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19264777 |
| http://purl.uniprot.org/citations/19264777 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19264777 |
| http://purl.uniprot.org/citations/19264777 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19264777 |
| http://purl.uniprot.org/citations/19264777 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19264777 |
| http://purl.uniprot.org/uniprot/P24932 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/19264777 |
| http://purl.uniprot.org/uniprot/P24933 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/19264777 |