| pubmed-article:8659132 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8659132 | lifeskim:mentions | umls-concept:C0014644 | lld:lifeskim |
| pubmed-article:8659132 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
| pubmed-article:8659132 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8659132 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
| pubmed-article:8659132 | lifeskim:mentions | umls-concept:C0018850 | lld:lifeskim |
| pubmed-article:8659132 | lifeskim:mentions | umls-concept:C0872079 | lld:lifeskim |
| pubmed-article:8659132 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8659132 | lifeskim:mentions | umls-concept:C1704222 | lld:lifeskim |
| pubmed-article:8659132 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8659132 | pubmed:dateCreated | 1996-8-1 | lld:pubmed |
| pubmed-article:8659132 | pubmed:abstractText | The EBNA-LP protein encoded by the open reading frame in the leader exons of the Epstein-Barr nuclear antigen messages is essential for efficient immortalization of B lymphocytes. Protein-protein interaction studies using affinity precipitation of proteins from [35S]methionine-labeled cell lysates and bacterially expressed maltose binding protein EBNA-LP fusions were performed. A cellular 68/72-kDa doublet protein was detected. This banding pattern was shown to be identical to that obtained in affinity precipitations with fusions of glutathione-S-transferase and Sp1 (a basal transcription factor). For both EBNA-LP and Sp1 the specific interacting cellular proteins have been identified as heat shock proteins (HSP) 72/73. Affinity precipitation of HSP 72/73 with deletion mutants of EBNA-LP maps the interaction domain on EBNA-LP to exon Y2 which is required for immortalization. Immunoprecipitation of EBNA-LP from EBV-positive lymphoblastoid cell lines coprecipitated the HSP 72/73 proteins, indicating that the interaction occurs in vivo as well as in vitro. The association of HSPs with a widening range of nuclear proteins involved in gene expression and proliferation control now includes Sp1 and EBNA-LP and suggests that there is a central role for molecular chaperones in these processes. | lld:pubmed |
| pubmed-article:8659132 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8659132 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8659132 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8659132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8659132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8659132 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8659132 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8659132 | pubmed:issn | 0042-6822 | lld:pubmed |
| pubmed-article:8659132 | pubmed:author | pubmed-author:RoweD TDT | lld:pubmed |
| pubmed-article:8659132 | pubmed:author | pubmed-author:KitayM KMK | lld:pubmed |
| pubmed-article:8659132 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8659132 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8659132 | pubmed:volume | 220 | lld:pubmed |
| pubmed-article:8659132 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8659132 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8659132 | pubmed:pagination | 91-9 | lld:pubmed |
| pubmed-article:8659132 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8659132 | pubmed:meshHeading | pubmed-meshheading:8659132-... | lld:pubmed |
| pubmed-article:8659132 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8659132 | pubmed:articleTitle | Protein-protein interactions between Epstein-Barr virus nuclear antigen-LP and cellular gene products: binding of 70-kilodalton heat shock proteins. | lld:pubmed |
| pubmed-article:8659132 | pubmed:affiliation | Department of Infectious Diseases and Microbiology, Graduate School of Public Health, University of Pittsburgh, Pennsylvania 15261, USA. | lld:pubmed |
| pubmed-article:8659132 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8659132 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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