| pubmed-article:8083235 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8083235 | lifeskim:mentions | umls-concept:C0021760 | lld:lifeskim |
| pubmed-article:8083235 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:8083235 | lifeskim:mentions | umls-concept:C0063717 | lld:lifeskim |
| pubmed-article:8083235 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:8083235 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:8083235 | lifeskim:mentions | umls-concept:C0061829 | lld:lifeskim |
| pubmed-article:8083235 | pubmed:issue | 37 | lld:pubmed |
| pubmed-article:8083235 | pubmed:dateCreated | 1994-10-11 | lld:pubmed |
| pubmed-article:8083235 | pubmed:abstractText | The high affinity human interleukin-6 (IL-6) receptor complex consists of IL-6 and two membrane-associated receptor components, the IL-6 receptor (alpha-subunit) and the high affinity converter and signal transducing molecule, gp-130 (beta-subunit). Recombinant IL-6 and the extracellular ("soluble") components of the IL-6 receptor (sIL-6R) and gp-130 (sgp-130) have been prepared in order to investigate the stoichiometry and binding of these components in the low affinity (IL-6.sIL-6R) and high affinity (IL-6.sIL-6R.sgp-130) IL-6 receptor complexes. Using a combination of size-exclusion chromatography and analytical ultracentrifugation analysis, in the low affinity receptor complex, IL-6 was shown to bind sIL-6R in a stoichiometric ratio of 1:1, whereas the high affinity ternary complex is hexameric consisting of two molecules each of IL-6, sIL-6R, and sgp-130. This is the first direct demonstration of a higher order arrangement for receptor cytokine interactions that exhibit both high and low affinity complexes. | lld:pubmed |
| pubmed-article:8083235 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8083235 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8083235 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8083235 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8083235 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8083235 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8083235 | pubmed:author | pubmed-author:SimpsonR JRJ | lld:pubmed |
| pubmed-article:8083235 | pubmed:author | pubmed-author:YasukawaKK | lld:pubmed |
| pubmed-article:8083235 | pubmed:author | pubmed-author:HowlettG JGJ | lld:pubmed |
| pubmed-article:8083235 | pubmed:author | pubmed-author:HammacherAA | lld:pubmed |
| pubmed-article:8083235 | pubmed:author | pubmed-author:WardL DLD | lld:pubmed |
| pubmed-article:8083235 | pubmed:author | pubmed-author:MoritzR LRL | lld:pubmed |
| pubmed-article:8083235 | pubmed:author | pubmed-author:DiscoloGG | lld:pubmed |
| pubmed-article:8083235 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8083235 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:8083235 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:8083235 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8083235 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8083235 | pubmed:pagination | 23286-9 | lld:pubmed |
| pubmed-article:8083235 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8083235 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8083235 | pubmed:articleTitle | High affinity interleukin-6 receptor is a hexameric complex consisting of two molecules each of interleukin-6, interleukin-6 receptor, and gp-130. | lld:pubmed |
| pubmed-article:8083235 | pubmed:affiliation | Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research (Melbourne), Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Parkville, Victoria, Australia. | lld:pubmed |
| pubmed-article:8083235 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8083235 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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