pubmed-article:10590262 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10590262 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:10590262 | lifeskim:mentions | umls-concept:C0123771 | lld:lifeskim |
pubmed-article:10590262 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
pubmed-article:10590262 | lifeskim:mentions | umls-concept:C0002345 | lld:lifeskim |
pubmed-article:10590262 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
pubmed-article:10590262 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
pubmed-article:10590262 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:10590262 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:10590262 | pubmed:dateCreated | 2000-1-24 | lld:pubmed |
pubmed-article:10590262 | pubmed:abstractText | IL-4 plays a major role in IgE production. Its signal is conferred to effector cells through binding to the alpha chain of the membrane-bound human IL-4 receptor (huIL-4Ralpha). Here we present the genomic structure and organization of huIL-4Ralpha. The promotor region shows binding sites for several transcription factors involved in inflammatory processes. HuIL-4Ralpha has been shown to be organized differently to that of mouse IL-4Ralpha. A soluble form of huIL-4Ralpha is produced by alternative splicing of the huIL-4Ralpha gene (shuIL-4Ralpha/splice). Expression of the corresponding mRNA coding for the extracellular part of the receptor and an additional three amino acids is also shown. A second form of huIL-4Ralpha, i.e. shuIL-4Ralpha/prot, is produced by limited proteolysis of the receptor (shedding) and is already known. These results reveal a complex pattern for the regulation of the IL-4 pathway at the receptor level. The patterns of expression of all three receptor proteins as well as their individual meaning in the context of inflammation still have to be elucidated. | lld:pubmed |
pubmed-article:10590262 | pubmed:language | eng | lld:pubmed |
pubmed-article:10590262 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10590262 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10590262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10590262 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10590262 | pubmed:month | Dec | lld:pubmed |
pubmed-article:10590262 | pubmed:issn | 0953-8178 | lld:pubmed |
pubmed-article:10590262 | pubmed:author | pubmed-author:ForsterJJ | lld:pubmed |
pubmed-article:10590262 | pubmed:author | pubmed-author:KuehnNN | lld:pubmed |
pubmed-article:10590262 | pubmed:author | pubmed-author:KruseSS | lld:pubmed |
pubmed-article:10590262 | pubmed:author | pubmed-author:DeichmannK... | lld:pubmed |
pubmed-article:10590262 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10590262 | pubmed:volume | 11 | lld:pubmed |
pubmed-article:10590262 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10590262 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10590262 | pubmed:pagination | 1965-70 | lld:pubmed |
pubmed-article:10590262 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:10590262 | pubmed:meshHeading | pubmed-meshheading:10590262... | lld:pubmed |
pubmed-article:10590262 | pubmed:meshHeading | pubmed-meshheading:10590262... | lld:pubmed |
pubmed-article:10590262 | pubmed:meshHeading | pubmed-meshheading:10590262... | lld:pubmed |
pubmed-article:10590262 | pubmed:meshHeading | pubmed-meshheading:10590262... | lld:pubmed |
pubmed-article:10590262 | pubmed:meshHeading | pubmed-meshheading:10590262... | lld:pubmed |
pubmed-article:10590262 | pubmed:meshHeading | pubmed-meshheading:10590262... | lld:pubmed |
pubmed-article:10590262 | pubmed:meshHeading | pubmed-meshheading:10590262... | lld:pubmed |
pubmed-article:10590262 | pubmed:meshHeading | pubmed-meshheading:10590262... | lld:pubmed |
pubmed-article:10590262 | pubmed:meshHeading | pubmed-meshheading:10590262... | lld:pubmed |
pubmed-article:10590262 | pubmed:meshHeading | pubmed-meshheading:10590262... | lld:pubmed |
pubmed-article:10590262 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10590262 | pubmed:articleTitle | Characterization of the membrane-bound and a soluble form of human IL-4 receptor alpha produced by alternative splicing. | lld:pubmed |
pubmed-article:10590262 | pubmed:affiliation | University Children's Hospital, University of Freiburg, Mathildenstrasse 1, 79106 Freiburg, Germany. | lld:pubmed |
pubmed-article:10590262 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10590262 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:3566 | entrezgene:pubmed | pubmed-article:10590262 | lld:entrezgene |
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