| pubmed-article:9195957 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9195957 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9195957 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:9195957 | lifeskim:mentions | umls-concept:C1425324 | lld:lifeskim |
| pubmed-article:9195957 | lifeskim:mentions | umls-concept:C1412687 | lld:lifeskim |
| pubmed-article:9195957 | lifeskim:mentions | umls-concept:C1826773 | lld:lifeskim |
| pubmed-article:9195957 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:9195957 | pubmed:dateCreated | 1997-7-16 | lld:pubmed |
| pubmed-article:9195957 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195957 | pubmed:abstractText | The hepatitis B virus X protein induces transcriptional activation of a wide variety of viral and cellular genes. In addition to its ability to interact directly with many nuclear transcription factors, several reports indicate that the X protein stimulates different cytoplasmic kinase signal cascades. Using the yeast two-hybrid screen, we have isolated a clone designated X-associated protein 3 (XAP3) that encodes a human homolog of the rat protein kinase C-binding protein. One of the activation domains of X (amino acids 90-122) is required for binding to XAP3, while the NH2-terminal part of XAP3 is necessary for binding to X. Both X and XAP3 bound specifically to the eta PKC isoenzyme synthesized in rabbit reticulocyte lysates. Overexpression of XAP3 enhanced X transactivation activity. These results support earlier findings that one of the mechanisms of transactivation by X is through involvement with the cellular protein kinase C pathway. | lld:pubmed |
| pubmed-article:9195957 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195957 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9195957 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195957 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9195957 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195957 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195957 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195957 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9195957 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9195957 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9195957 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9195957 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9195957 | pubmed:author | pubmed-author:BOOO | lld:pubmed |
| pubmed-article:9195957 | pubmed:author | pubmed-author:SetoEE | lld:pubmed |
| pubmed-article:9195957 | pubmed:author | pubmed-author:CongY SYS | lld:pubmed |
| pubmed-article:9195957 | pubmed:author | pubmed-author:Kuzhandaivelu... | lld:pubmed |
| pubmed-article:9195957 | pubmed:author | pubmed-author:YangW MWM | lld:pubmed |
| pubmed-article:9195957 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9195957 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:9195957 | pubmed:volume | 272 | lld:pubmed |
| pubmed-article:9195957 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9195957 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9195957 | pubmed:pagination | 16482-9 | lld:pubmed |
| pubmed-article:9195957 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:9195957 | pubmed:meshHeading | pubmed-meshheading:9195957-... | lld:pubmed |
| pubmed-article:9195957 | pubmed:meshHeading | pubmed-meshheading:9195957-... | lld:pubmed |
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| pubmed-article:9195957 | pubmed:meshHeading | pubmed-meshheading:9195957-... | lld:pubmed |
| pubmed-article:9195957 | pubmed:meshHeading | pubmed-meshheading:9195957-... | lld:pubmed |
| pubmed-article:9195957 | pubmed:meshHeading | pubmed-meshheading:9195957-... | lld:pubmed |
| pubmed-article:9195957 | pubmed:meshHeading | pubmed-meshheading:9195957-... | lld:pubmed |
| pubmed-article:9195957 | pubmed:meshHeading | pubmed-meshheading:9195957-... | lld:pubmed |
| pubmed-article:9195957 | pubmed:meshHeading | pubmed-meshheading:9195957-... | lld:pubmed |
| pubmed-article:9195957 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9195957 | pubmed:articleTitle | The hepatitis B virus X-associated protein, XAP3, is a protein kinase C-binding protein. | lld:pubmed |
| pubmed-article:9195957 | pubmed:affiliation | Moffitt Cancer Center & Research Institute, Department of Medical Microbiology/Immunology, College of Medicine, University of South Florida, Tampa, Florida 33612, USA. | lld:pubmed |
| pubmed-article:9195957 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9195957 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9195957 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:9195957 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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