| pubmed-article:11046044 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11046044 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:11046044 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:11046044 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:11046044 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11046044 | lifeskim:mentions | umls-concept:C0021747 | lld:lifeskim |
| pubmed-article:11046044 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:11046044 | lifeskim:mentions | umls-concept:C1415900 | lld:lifeskim |
| pubmed-article:11046044 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:11046044 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:11046044 | pubmed:dateCreated | 2000-11-3 | lld:pubmed |
| pubmed-article:11046044 | pubmed:abstractText | The cytoplasmic domain of the human type I IFN receptor chain 2 (IFNAR2c or IFN-alphaRbetaL) was used as bait in a yeast two-hybrid system to identify novel proteins interacting with this region of the receptor. We report here a specific interaction between the cytoplasmic domain of IFN-alphaRbetaL and a previously identified protein, RACK-1 (receptor for activated C kinase). Using GST fusion proteins encoding different regions of the cytoplasmic domain of IFN-alphaRbetaL, the minimum site for RACK-1 binding was mapped to aa 300-346. RACK-1 binding to IFN-alphaRbetaL did not require the first 91 aa of RACK-1, which includes two WD domains, WD1 and WD2. The interaction between RACK-1 and IFN-alphaRbetaL, but not the human IFN receptor chain 1 (IFNAR1 or IFN-alphaRalpha), was also detected in human Daudi cells by coimmunoprecipitation. RACK-1 was shown to be constitutively associated with IFN-alphaRbetaL, and this association was not effected by stimulation of Daudi cells with type I IFNs (IFN-beta1b). RACK-1 itself did not become tyrosine phosphorylated upon stimulation of Daudi cells with IFN-beta1b. However, stimulation of cells with either IFN-beta1b or PMA did result in an increase in detectable immunofluorescence and intracellular redistribution of RACK-1. | lld:pubmed |
| pubmed-article:11046044 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11046044 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11046044 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11046044 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11046044 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:11046044 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11046044 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11046044 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11046044 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11046044 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11046044 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11046044 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11046044 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11046044 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11046044 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11046044 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:11046044 | pubmed:author | pubmed-author:CrozeEE | lld:pubmed |
| pubmed-article:11046044 | pubmed:author | pubmed-author:PerezH DHD | lld:pubmed |
| pubmed-article:11046044 | pubmed:author | pubmed-author:ColamoniciOO | lld:pubmed |
| pubmed-article:11046044 | pubmed:author | pubmed-author:MinshallR DRD | lld:pubmed |
| pubmed-article:11046044 | pubmed:author | pubmed-author:AsarnowDD | lld:pubmed |
| pubmed-article:11046044 | pubmed:author | pubmed-author:UsachevaAA | lld:pubmed |
| pubmed-article:11046044 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11046044 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11046044 | pubmed:volume | 165 | lld:pubmed |
| pubmed-article:11046044 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11046044 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11046044 | pubmed:pagination | 5127-32 | lld:pubmed |
| pubmed-article:11046044 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:11046044 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11046044 | pubmed:articleTitle | Receptor for activated C-kinase (RACK-1), a WD motif-containing protein, specifically associates with the human type I IFN receptor. | lld:pubmed |
| pubmed-article:11046044 | pubmed:affiliation | Department of Immunology, Berlex Biosciences, Richmond CA 94804, USA. ed_croze@berlex.com | lld:pubmed |
| pubmed-article:11046044 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11046044 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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