pubmed-article:3029410 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3029410 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:3029410 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
pubmed-article:3029410 | lifeskim:mentions | umls-concept:C0032551 | lld:lifeskim |
pubmed-article:3029410 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:3029410 | pubmed:dateCreated | 1987-4-22 | lld:pubmed |
pubmed-article:3029410 | pubmed:abstractText | Polyomavirus large T antigen is phosphorylated on both serine and threonine residues at a ratio of approximately 6 to 1. This phosphorylation could be resolved into a series of nine Staphylococcus aureus V8 phosphopeptides. All of these were found in an N-terminal chymotryptic fragment with a molecular weight of 57,000. A C-terminal formic acid fragment of 50,000-molecular-weight lacked phosphate. Therefore, unlike simian virus 40 large T antigen, polyomavirus large T antigen has no significant C-terminal phosphorylation. Limited V8 and hydroxylamine cleavage showed that the phosphorylations can be localized to two different portions of the molecule. A significant fraction of the phosphate was localized in the N-terminal portion of the molecule before residue 183. Within this region V8 peptides 4, 8, and 9 represented phosphorylations that were more proximal, while peptides 1, 2, and 3 included more distal phosphorylations. None of these phosphorylations appeared analogous to those of simian virus 40 large T antigen. V8 phosphopeptides 5 and 7 were more distal and could be distinguished in biological experiments from the N-terminal phosphorylations. Formic acid mapping suggested that much, if not all, of this phosphorylation is located between residues 257 and 285. | lld:pubmed |
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pubmed-article:3029410 | pubmed:language | eng | lld:pubmed |
pubmed-article:3029410 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3029410 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:3029410 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3029410 | pubmed:month | Apr | lld:pubmed |
pubmed-article:3029410 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:3029410 | pubmed:author | pubmed-author:SchaffhausenB... | lld:pubmed |
pubmed-article:3029410 | pubmed:author | pubmed-author:BockusB JBJ | lld:pubmed |
pubmed-article:3029410 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3029410 | pubmed:volume | 61 | lld:pubmed |
pubmed-article:3029410 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3029410 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3029410 | pubmed:pagination | 1155-63 | lld:pubmed |
pubmed-article:3029410 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:3029410 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3029410 | pubmed:articleTitle | Localization of the phosphorylations of polyomavirus large T antigen. | lld:pubmed |
pubmed-article:3029410 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3029410 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:3029410 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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