| http://purl.uniprot.org/citations/12717439 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12717439 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12717439 | http://www.w3.org/2000/01/rdf-schema#comment | "The E2F-1 transcription factor is regulated during cell cycle progression and induced by cellular stress, such as DNA damage. We report that checkpoint kinase 2 (Chk2) regulates E2F-1 activity in response to the DNA-damaging agent etoposide. A Chk2 consensus phosphorylation site in E2F-1 is phosphorylated in response to DNA damage, resulting in protein stabilization, increased half-life, transcriptional activation and localization of phosphorylated E2F-1 to discrete nuclear structures. Expression of a dominant-negative Chk2 mutant blocks induction of E2F-1 and prevents E2F-1-dependent apoptosis. Moreover, E2F-1 is resistant to induction by etoposide in tumour cells expressing mutant chk2. Therefore, Chk2 phosphorylates and activates E2F-1 in response to DNA damage, resulting in apoptosis. These results suggest a role for E2F-1 in checkpoint control and provide a plausible explanation for the tumour suppressor activity of E2F-1."xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb974"xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb974"xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/author | "Stevens C."xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/author | "Stevens C."xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/author | "La Thangue N.B."xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/author | "La Thangue N.B."xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/author | "Smith L."xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/author | "Smith L."xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/pages | "401-409"xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/pages | "401-409"xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/title | "Chk2 activates E2F-1 in response to DNA damage."xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/title | "Chk2 activates E2F-1 in response to DNA damage."xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/volume | "5"xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://purl.uniprot.org/core/volume | "5"xsd:string |
| http://purl.uniprot.org/citations/12717439 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12717439 |
| http://purl.uniprot.org/citations/12717439 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12717439 |
| http://purl.uniprot.org/citations/12717439 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12717439 |
| http://purl.uniprot.org/citations/12717439 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12717439 |