| pubmed-article:1645792 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1645792 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
| pubmed-article:1645792 | lifeskim:mentions | umls-concept:C0116397 | lld:lifeskim |
| pubmed-article:1645792 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:1645792 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:1645792 | pubmed:dateCreated | 1991-7-11 | lld:pubmed |
| pubmed-article:1645792 | pubmed:abstractText | The Epstein-Barr virus nuclear antigen 2A (EBNA-2A) was immunoprecipitated from latently Epstein-Barr virus-infected lymphocytes with a polyclonal serum raised against the EBNA-2A C terminus. The nucleus contained three subfractions of EBNA-2A which could be distinguished by their resistance to salt extraction: (i) a nucleoplasmatic fraction that was solubilized at 50 mM NaCl, (ii) a chromatin-associated fraction extractable at 1.5 M NaCl, and (iii) a nuclear matrix-associated fraction solubilized only by boiling with buffer containing 2% sodium dodecyl sulfate. The three subfractions were phosphorylated; it was demonstrated that the nucleoplasmatic and the chromatin-associated fractions were phosphorylated at serine and threonine residues. The half-life of the EBNA-2A protein was determined by cycloheximide treatment and by pulse-chase experiments and was found to be at least 24 h. The turnover of the phosphate residues bound to the two salt-soluble subfractions was determined to be approximately 6 to 9 h, suggesting a possible role of the phosphorylation in the regulation of the biological activity of EBNA-2A. Dephosphorylation of EBNA-2A resulted in an increased mobility of the protein during sodium dodecyl sulfate-polyacrylamide gel electrophoresis and indicated the presence of differentially phosphorylated subclasses of the protein. Analysis of EBNA-2A by sucrose gradient centrifugation revealed the existence of two subclasses of complexed molecules which exhibited sedimentation coefficients of approximately 13S and 34S. | lld:pubmed |
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| pubmed-article:1645792 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1645792 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1645792 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1645792 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1645792 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1645792 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:1645792 | pubmed:author | pubmed-author:Mueller-Lantz... | lld:pubmed |
| pubmed-article:1645792 | pubmed:author | pubmed-author:GrässerF AFA | lld:pubmed |
| pubmed-article:1645792 | pubmed:author | pubmed-author:HaissPP | lld:pubmed |
| pubmed-article:1645792 | pubmed:author | pubmed-author:GöttelSS | lld:pubmed |
| pubmed-article:1645792 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1645792 | pubmed:volume | 65 | lld:pubmed |
| pubmed-article:1645792 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1645792 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1645792 | pubmed:pagination | 3779-88 | lld:pubmed |
| pubmed-article:1645792 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1645792 | pubmed:meshHeading | pubmed-meshheading:1645792-... | lld:pubmed |
| pubmed-article:1645792 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1645792 | pubmed:articleTitle | Biochemical characterization of Epstein-Barr virus nuclear antigen 2A. | lld:pubmed |
| pubmed-article:1645792 | pubmed:affiliation | Abteilung Virologie, Universitätskliniken des Saarlandes, Homburg, Germany. | lld:pubmed |
| pubmed-article:1645792 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1645792 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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