pubmed-article:8972861 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8972861 | lifeskim:mentions | umls-concept:C0040624 | lld:lifeskim |
pubmed-article:8972861 | lifeskim:mentions | umls-concept:C1425324 | lld:lifeskim |
pubmed-article:8972861 | lifeskim:mentions | umls-concept:C1412302 | lld:lifeskim |
pubmed-article:8972861 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:8972861 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:8972861 | pubmed:issue | 23 | lld:pubmed |
pubmed-article:8972861 | pubmed:dateCreated | 1997-1-30 | lld:pubmed |
pubmed-article:8972861 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8972861 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8972861 | pubmed:abstractText | The hepatitis B virus X protein is a promiscuous transcriptional transactivator. Transactivation by the X protein is most likely mediated through binding to different cellular factors. Using the yeast two-hybrid method, we have isolated a clone that encodes a novel X-associated cellular protein: XAP2. X and XAP2 interactions also occur in vitro. Antiserum raised against XAP2 recognizes a cytoplasmic protein with an apparent molecular mass of 36 kDa. The interaction between X and XAP2 requires a small region on X containing amino acids 13-26. From Northern blot analyses, XAP2 is ubiquitously expressed in both liver-derived and non-liver-derived cell lines as well as in normal non-liver tissues. In contrast, XAP2 is expressed in very low level in the normal human liver. In transfection assays, overexpression of XAP2 abolishes transactivation by the X protein. Based on these results, we suggest that XAP2 is an important cellular negative regulator of the X protein, and that X-XAP2 interaction may play a role in HBV pathology. | lld:pubmed |
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