| pubmed-article:2342462 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2342462 | lifeskim:mentions | umls-concept:C0013935 | lld:lifeskim |
| pubmed-article:2342462 | lifeskim:mentions | umls-concept:C0008051 | lld:lifeskim |
| pubmed-article:2342462 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:2342462 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
| pubmed-article:2342462 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:2342462 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:2342462 | lifeskim:mentions | umls-concept:C0205184 | lld:lifeskim |
| pubmed-article:2342462 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:2342462 | pubmed:dateCreated | 1990-6-25 | lld:pubmed |
| pubmed-article:2342462 | pubmed:abstractText | Serum stimulation of quiescent chicken embryo fibroblasts resulted in a time-dependent, biphasic activation of S6 kinase activity. Chromatographic fractionation of serum-stimulated cell lysates resolved two distinct S6 kinase activities. Anti-Xenopus S6 kinase II antiserum immunoprecipitated a 90,000-Mr S6 kinase but did not cross-react with a smaller, 65,000-Mr S6 kinase. Phosphopeptide analysis confirmed that the 90,000- and 65,000-Mr proteins were structurally unrelated and established that the 65,000-Mr protein isolated by the current protocol was the same serum-stimulated chicken embryo fibroblast S6 kinase as that previously characterized (J. Blenis, C. J. Kuo, and R. L. Erikson, J. Biol. Chem. 262:14373-14376, 1987). These results demonstrate the contribution of two distinct S6 kinases to total serum-stimulated ribosomal protein S6 phosphorylation. | lld:pubmed |
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| pubmed-article:2342462 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2342462 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2342462 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2342462 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2342462 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:2342462 | pubmed:author | pubmed-author:EriksonR LRL | lld:pubmed |
| pubmed-article:2342462 | pubmed:author | pubmed-author:AlcortaD ADA | lld:pubmed |
| pubmed-article:2342462 | pubmed:author | pubmed-author:SweetL JLJ | lld:pubmed |
| pubmed-article:2342462 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2342462 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:2342462 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2342462 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2342462 | pubmed:pagination | 2787-92 | lld:pubmed |
| pubmed-article:2342462 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:2342462 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2342462 | pubmed:articleTitle | Two distinct enzymes contribute to biphasic S6 phosphorylation in serum-stimulated chicken embryo fibroblasts. | lld:pubmed |
| pubmed-article:2342462 | pubmed:affiliation | Department of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138. | lld:pubmed |
| pubmed-article:2342462 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2342462 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2342462 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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