http://purl.uniprot.org/citations/2546678 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2546678 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2546678 | http://www.w3.org/2000/01/rdf-schema#comment | "The association between the retinoblastoma protein (p105-RB) and either the large T antigen of SV40 or the E1A proteins of adenovirus is thought to be an important step in transformation by these viral oncogenes. E1A and large T antigen share a small region of amino acid homology that is necessary for high affinity binding with p105-RB. Mutations of this homology region were shown to reduce drastically the frequency of transformation mediated by the E1A or large T oncogenes. Previously, this small region in E1A was shown to be sufficient for interaction with a second cellular protein of 107,000 daltons (107K). Here we show that in human cells, the large T antigens of SV40 or JC virus also form complexes with 107K. Demonstration of complexes between 107K and the large T antigens of SV40 and JC virus suggests that these associations may represent another component of a common mechanism for transformation between adenoviruses and polyoma viruses."xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.org/dc/terms/identifier | "doi:10.1016/0092-8674(89)90839-8"xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.org/dc/terms/identifier | "doi:10.1016/0092-8674(89)90839-8"xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/author | "Harlow E."xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/author | "Harlow E."xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/author | "Buchkovich K."xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/author | "Buchkovich K."xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/author | "Dyson N."xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/author | "Dyson N."xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/author | "Whyte P."xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/author | "Whyte P."xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/date | "1989"xsd:gYear |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/date | "1989"xsd:gYear |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/pages | "249-255"xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/pages | "249-255"xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/title | "The cellular 107K protein that binds to adenovirus E1A also associates with the large T antigens of SV40 and JC virus."xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/title | "The cellular 107K protein that binds to adenovirus E1A also associates with the large T antigens of SV40 and JC virus."xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/volume | "58"xsd:string |
http://purl.uniprot.org/citations/2546678 | http://purl.uniprot.org/core/volume | "58"xsd:string |
http://purl.uniprot.org/citations/2546678 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2546678 |
http://purl.uniprot.org/citations/2546678 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2546678 |