| http://purl.uniprot.org/citations/15572026 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15572026 | http://www.w3.org/2000/01/rdf-schema#comment | "Epstein-Barr virus (EBV) transforms resting human B cells into immortalized immunoblasts. EBV-encoded nuclear antigens EBNA-5 (also called EBNA-LP) is one of the earliest viral proteins expressed in freshly infected B cells. We have recently shown that EBNA-5 binds p14ARF, a nucleolar protein that regulates the p53 pathway. Here, we report the identification of another protein with partially nucleolar localization, the v-fos transformation effector Fte-1 (Fte-1/S3a), as an EBNA-5 binding partner. In transfected cells, Fte-1/S3a and EBNA-5 proteins showed high levels of colocalization in extranucleolar inclusions. Fte-1/S3a has multiple biological functions. It enhances v-fos-mediated cellular transformation and is part of the small ribosomal subunit. It also interacts with the transcriptional factor CHOP and apoptosis regulator poly(ADP-ribose) polymerase (PARP). Fte-1/S3a is regularly expressed at high levels in both tumors and cancer cell lines. Its high expression favors the maintenance of malignant phenotype and undifferentiated state, whereas its down-regulation is associated with cellular differentiation and growth arrest. Here, we show that EBV-induced B cell transformation leads to the up-regulation of Fte-1/S3a. We suggest that EBNA-5 through binding may influence the growth promoting, differentiation inhibiting, or apoptosis regulating functions of Fte-1/S3a."xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.yexcr.2004.08.025"xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://purl.uniprot.org/core/author | "Klein G."xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://purl.uniprot.org/core/author | "Kashuba E."xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://purl.uniprot.org/core/author | "Szekely L."xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://purl.uniprot.org/core/author | "Stahl J."xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://purl.uniprot.org/core/author | "Szirak K."xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://purl.uniprot.org/core/author | "Yurchenko M."xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15572026 | http://purl.uniprot.org/core/name | "Exp Cell Res"xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://purl.uniprot.org/core/pages | "47-55"xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://purl.uniprot.org/core/title | "Epstein-Barr virus-encoded EBNA-5 binds to Epstein-Barr virus-induced Fte1/S3a protein."xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://purl.uniprot.org/core/volume | "303"xsd:string |
| http://purl.uniprot.org/citations/15572026 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15572026 |
| http://purl.uniprot.org/citations/15572026 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15572026 |
| http://purl.uniprot.org/uniprot/P61247#attribution-7239A8EDB9AC04DCD195FDA26338D1C0 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15572026 |