| pubmed-article:7727425 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7727425 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:7727425 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:7727425 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:7727425 | lifeskim:mentions | umls-concept:C0035668 | lld:lifeskim |
| pubmed-article:7727425 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:7727425 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7727425 | lifeskim:mentions | umls-concept:C0678257 | lld:lifeskim |
| pubmed-article:7727425 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:7727425 | lifeskim:mentions | umls-concept:C1627358 | lld:lifeskim |
| pubmed-article:7727425 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:7727425 | pubmed:dateCreated | 1995-6-1 | lld:pubmed |
| pubmed-article:7727425 | pubmed:abstractText | The K protein was first identified in the heterogeneous ribonucleoprotein particle (hnRNP). Subsequently, K protein was shown to bind sequence-specific single-and double-stranded DNA, stimulate transcription, and bind Src, Fyn, Lyn, and Vav via SH3 interactions. The K protein also binds to the kappa B enhancer motif which stimulates its phosphorylation in vitro by an associated serine/threonine kinase. To gain more insight into this unique nucleic acid-dependent phosphorylation process, we set out to examine the regulation of this kinase. We demonstrate that the K protein exists in a complex with an IL-1-responsive kinase and that phosphorylation of the K protein by this kinase is augmented by either cognate DNA or RNA sequences. The IL-1-responsive kinase activity associated with the K protein is reduced by phosphatase treatment, suggesting that the K protein kinase activity is regulated by phosphorylation. The observation that phosphorylation of the K protein is DNA- or RNA-dependent and IL-1-responsive suggests that the function of the K protein is tightly regulated. | lld:pubmed |
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| pubmed-article:7727425 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7727425 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7727425 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7727425 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7727425 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:7727425 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:7727425 | pubmed:author | pubmed-author:OstrowskiJJ | lld:pubmed |
| pubmed-article:7727425 | pubmed:author | pubmed-author:BomsztykKK | lld:pubmed |
| pubmed-article:7727425 | pubmed:author | pubmed-author:Van... | lld:pubmed |
| pubmed-article:7727425 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7727425 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:7727425 | pubmed:volume | 34 | lld:pubmed |
| pubmed-article:7727425 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7727425 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7727425 | pubmed:pagination | 5644-50 | lld:pubmed |
| pubmed-article:7727425 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:7727425 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7727425 | pubmed:articleTitle | Description of an IL-1-responsive kinase that phosphorylates the K protein. Enhancement of phosphorylation by selective DNA and RNA motifs. | lld:pubmed |
| pubmed-article:7727425 | pubmed:affiliation | Department of Medicine, University of Washington, Seattle 98195, USA. | lld:pubmed |
| pubmed-article:7727425 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7727425 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7727425 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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