| pubmed-article:1710288 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1710288 | lifeskim:mentions | umls-concept:C0014644 | lld:lifeskim |
| pubmed-article:1710288 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
| pubmed-article:1710288 | lifeskim:mentions | umls-concept:C0007595 | lld:lifeskim |
| pubmed-article:1710288 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
| pubmed-article:1710288 | lifeskim:mentions | umls-concept:C0042736 | lld:lifeskim |
| pubmed-article:1710288 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:1710288 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:1710288 | pubmed:dateCreated | 1991-7-11 | lld:pubmed |
| pubmed-article:1710288 | pubmed:abstractText | Epstein-Barr virus (EBV) encodes two integral membrane proteins in latently infected growth-transformed cells. One of these, LMP1, can transform rodent fibroblasts and induce markers of B-lymphocyte activation. The second, LMP2, colocalizes with LMP1 in a constitutive patch in the EBV-transformed B-lymphocyte plasma membrane. The experiments reported here demonstrate that LMP2 may biochemically interact with LMP1 and that LMP2 closely associates with and is an important substrate for a B-lymphocyte tyrosine kinase in EBV-transformed B lymphocytes or in B-lymphoma cells in which LMP2 is expressed by gene transfer. LMP2 is also serine and threonine phosphorylated. LMP2 localizes to a peripheral membrane (presumably plasma membrane) patch in transfected B-lymphoma cells and colocalizes with much of the cellular tyrosine-phosphorylated proteins. LMP2 undergoes tyrosine phosphorylation in anti-LMP2 or antiphosphotyrosine immunoprecipitates from transfected B-lymphoma cells or EBV-transformed B lymphocytes. The first 167 of the 497 amino acids of LMP2 retain full ability to associate with and act as a substrate for a tyrosine kinase. A 70-kDa phosphotyrosine cell protein associates with LMP2 in transfected cells or in EBV-transformed B lymphocytes and could be a mediator of the effects of LMP2. | lld:pubmed |
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| pubmed-article:1710288 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1710288 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1710288 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1710288 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1710288 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1710288 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1710288 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:1710288 | pubmed:author | pubmed-author:RobertsT MTM | lld:pubmed |
| pubmed-article:1710288 | pubmed:author | pubmed-author:KieffEE | lld:pubmed |
| pubmed-article:1710288 | pubmed:author | pubmed-author:DrukerBB | lld:pubmed |
| pubmed-article:1710288 | pubmed:author | pubmed-author:LongneckerRR | lld:pubmed |
| pubmed-article:1710288 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1710288 | pubmed:volume | 65 | lld:pubmed |
| pubmed-article:1710288 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1710288 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1710288 | pubmed:pagination | 3681-92 | lld:pubmed |
| pubmed-article:1710288 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:1710288 | pubmed:meshHeading | pubmed-meshheading:1710288-... | lld:pubmed |
| pubmed-article:1710288 | pubmed:meshHeading | pubmed-meshheading:1710288-... | lld:pubmed |
