| pubmed-article:6184609 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6184609 | lifeskim:mentions | umls-concept:C0032556 | lld:lifeskim |
| pubmed-article:6184609 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
| pubmed-article:6184609 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:6184609 | lifeskim:mentions | umls-concept:C0444598 | lld:lifeskim |
| pubmed-article:6184609 | lifeskim:mentions | umls-concept:C0003343 | lld:lifeskim |
| pubmed-article:6184609 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:6184609 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:6184609 | pubmed:dateCreated | 1983-2-25 | lld:pubmed |
| pubmed-article:6184609 | pubmed:abstractText | Middle T antigen of polyoma virus is associated principally with the plasma membrane. Comparison of the trypsin sensitivity of middle T in intact cells and "inside out" membrane preparations showed that middle T is oriented towards the inside of the cell. This was confirmed by labeling of middle T in permeabilized cells, but not in intact cells, using [gamma-32P]ATP. Middle T molecules active in the in vitro kinase reaction could be differentiated from the bulk (metabolically labeled) middle T based on resistance to trypsin treatment. The active fraction also behaved differently from the bulk when cell frameworks were prepared with Triton-containing buffers; whereas the bulk middle T was evenly distributed in the soluble and cell framework fractions, the kinase-active forms were largely associated with the framework. Middle T molecules labeled in vivo with 32PO4 were found largely in the framework fraction, like the molecules that show kinase activity in vitro. Experiments with ATP affinity reagents 8-azido-ATP and 2,3-dialdehyde ATP have failed to label the middle T antigen. However, 2,3-dialdehyde ATP could be used to inhibit the kinase reaction. This raises the question of whether middle T antigen possesses intrinsic kinase activity or, rather, associates with a cellular tyrosine kinase. | lld:pubmed |
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| pubmed-article:6184609 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6184609 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6184609 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6184609 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6184609 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6184609 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:6184609 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:6184609 | pubmed:author | pubmed-author:BenjaminT LTL | lld:pubmed |
| pubmed-article:6184609 | pubmed:author | pubmed-author:SchaffhausenB... | lld:pubmed |
| pubmed-article:6184609 | pubmed:author | pubmed-author:DoraiHH | lld:pubmed |
| pubmed-article:6184609 | pubmed:author | pubmed-author:ArakereGG | lld:pubmed |
| pubmed-article:6184609 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6184609 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:6184609 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6184609 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6184609 | pubmed:pagination | 1187-98 | lld:pubmed |
| pubmed-article:6184609 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:6184609 | pubmed:meshHeading | pubmed-meshheading:6184609-... | lld:pubmed |
| pubmed-article:6184609 | pubmed:meshHeading | pubmed-meshheading:6184609-... | lld:pubmed |
