| pubmed-article:2168961 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2168961 | lifeskim:mentions | umls-concept:C0040682 | lld:lifeskim |
| pubmed-article:2168961 | lifeskim:mentions | umls-concept:C0071655 | lld:lifeskim |
| pubmed-article:2168961 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
| pubmed-article:2168961 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:2168961 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:2168961 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:2168961 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:2168961 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:2168961 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:2168961 | lifeskim:mentions | umls-concept:C0032552 | lld:lifeskim |
| pubmed-article:2168961 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:2168961 | pubmed:dateCreated | 1990-10-17 | lld:pubmed |
| pubmed-article:2168961 | pubmed:abstractText | Phosphatidylinositol 3-kinase associates with the polyomavirus middle T antigen (PyMTAg)-pp60c-src complex in polyomavirus-transformed cells. Here we show that anti-PyMTAg immunoprecipitates from PyMTAg-transformed NIH 3T3 cells have lipid kinase activities that phosphorylate phosphatidylinositol, phosphatidylinositol-4-bisphosphate, and phosphatidylinositol-4,5-bisphosphate at the D-3 position of the inositol ring to produce three new polyphosphoinositides: phosphatidylinositol-3-phosphate (PI-3-P), phosphatidylinositol-3,4-bisphosphate (PI-3,4-P2), and phosphatidylinositol trisphosphate (PIP3), respectively. PI-3-P was detected in intact parental and PyMTAg-transformed NIH 3T3 fibroblasts at both low and high cell densities. However, parental NIH 3T3 fibroblasts produced no detectable PI-3,4-P2 or PIP3 at high density. In contrast, growing, subconfluent cells and wild-type PyMTAg-transformed cells at high density had greatly enhanced incorporation of [3H]-inositol into these highly phosphorylated lipids. Cells transfected with a transformation-defective mutant of PyMTAg had undetectable levels of PI-3,4-P2 and PIP3 at high density. Thus, the synthesis of novel polyphosphoinositides by lipid kinase activity associated with PyMTAg correlates with cell growth and transformation. | lld:pubmed |
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| pubmed-article:2168961 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2168961 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2168961 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2168961 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2168961 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2168961 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:2168961 | pubmed:author | pubmed-author:RobertsT MTM | lld:pubmed |
| pubmed-article:2168961 | pubmed:author | pubmed-author:SerunianL ALA | lld:pubmed |
| pubmed-article:2168961 | pubmed:author | pubmed-author:CantleyL CLC | lld:pubmed |
| pubmed-article:2168961 | pubmed:author | pubmed-author:AugerK RKR | lld:pubmed |
| pubmed-article:2168961 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2168961 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:2168961 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2168961 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2168961 | pubmed:pagination | 4718-25 | lld:pubmed |
| pubmed-article:2168961 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:2168961 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2168961 | pubmed:articleTitle | Production of novel polyphosphoinositides in vivo is linked to cell transformation by polyomavirus middle T antigen. | lld:pubmed |
| pubmed-article:2168961 | pubmed:affiliation | Department of Physiology, Tufts University School of Medicine, Boston, Massachusetts 02111. | lld:pubmed |
| pubmed-article:2168961 | pubmed:publicationType | Journal Article | lld:pubmed |
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