| pubmed-article:8589260 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8589260 | lifeskim:mentions | umls-concept:C0021758 | lld:lifeskim |
| pubmed-article:8589260 | lifeskim:mentions | umls-concept:C0334094 | lld:lifeskim |
| pubmed-article:8589260 | lifeskim:mentions | umls-concept:C2266866 | lld:lifeskim |
| pubmed-article:8589260 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8589260 | pubmed:dateCreated | 1996-3-25 | lld:pubmed |
| pubmed-article:8589260 | pubmed:abstractText | In human interleukin 4(IL-4), the carboxyl and amino termini of the 129 amino acid hormone are close to each other and this region is believed to be important for binding to the IL-4 receptor (IL-4r). We constructed plasmids encoding circularly permuted IL-4 mutants with the peptide Gly-Gly-Asn-Gly-Gly (GGNGG) joining the carboxyl to the amino terminus and with new amino and carboxyl termini elsewhere. Mutant IL-4(38-37) is composed of IL-4 residues 38-129 GGNGG and 1-37. Mutant IL-4(105-104) is composed of IL-4 residues 105-129, GGNGG and 1-104. IL-4(38-37) and IL-4(105-104) were purified from E. coli to near homogeneity and retained 50-100% of the binding and proliferative activity of IL-4, and in addition retained the ability to upregulate CD23 on Burkitt's lymphoma cells. Circular dichroism studies indicated that the tertiary structures of both IL-4(38-37) and IL-4(105-104) were retained, with the former molecule most similar to native IL-4. We conclude that while both native termini of IL-4 may be near its binding site, neither is required to be free for optimum activity. | lld:pubmed |
| pubmed-article:8589260 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8589260 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8589260 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8589260 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8589260 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8589260 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8589260 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8589260 | pubmed:month | May | lld:pubmed |
| pubmed-article:8589260 | pubmed:issn | 1043-4666 | lld:pubmed |
| pubmed-article:8589260 | pubmed:author | pubmed-author:McPhiePP | lld:pubmed |
| pubmed-article:8589260 | pubmed:author | pubmed-author:PastanII | lld:pubmed |
| pubmed-article:8589260 | pubmed:author | pubmed-author:PuriR KRK | lld:pubmed |
| pubmed-article:8589260 | pubmed:author | pubmed-author:KreitmanR JRJ | lld:pubmed |
| pubmed-article:8589260 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8589260 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:8589260 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8589260 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8589260 | pubmed:pagination | 311-8 | lld:pubmed |
| pubmed-article:8589260 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
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| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:meshHeading | pubmed-meshheading:8589260-... | lld:pubmed |
| pubmed-article:8589260 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8589260 | pubmed:articleTitle | Circularly permuted interleukin 4 retains proliferative and binding activity. | lld:pubmed |
| pubmed-article:8589260 | pubmed:affiliation | Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. | lld:pubmed |
| pubmed-article:8589260 | pubmed:publicationType | Journal Article | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8589260 | lld:pubmed |
