pubmed-article:7673234 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C0021764 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C0021755 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C0243192 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C0063710 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C0231491 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C0441587 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:7673234 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:7673234 | pubmed:issue | 38 | lld:pubmed |
pubmed-article:7673234 | pubmed:dateCreated | 1995-10-17 | lld:pubmed |
pubmed-article:7673234 | pubmed:abstractText | We showed previously that replacement of Lys-145 in the IL-1 receptor antagonist (IL-1ra) with Asp resulted in an analog (IL-1ra K145D) with partial agonist activity. To identify additional amino acids that affect IL-1 bioactivity, we created second site mutations in IL-1ra K145D. Substitutions of single amino acids surrounding position 145 were made; none of these substitutions increased the bioactivity of IL-1ra K145D. However, the insertion of the beta-bulge (QGEESN) of IL-1 beta at the corresponding region of IL-1ra K145D resulted in a 3-4-fold augmentation of bioactivity. An additional increase in agonist activity was observed when the beta-bulge was co-expressed with a second substitution (His-54 --> Pro) in IL-1ra K145D. We also show that the bioactivity of both IL-1ra K145D and the triple mutant IL-1ra K145D/H54P/QGEESN is dependent on interaction with the newly cloned IL-1 receptor accessory protein. | lld:pubmed |
pubmed-article:7673234 | pubmed:language | eng | lld:pubmed |
pubmed-article:7673234 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7673234 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7673234 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7673234 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7673234 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7673234 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7673234 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7673234 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7673234 | pubmed:month | Sep | lld:pubmed |
pubmed-article:7673234 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:7673234 | pubmed:author | pubmed-author:LevinWW | lld:pubmed |
pubmed-article:7673234 | pubmed:author | pubmed-author:MadisonVV | lld:pubmed |
pubmed-article:7673234 | pubmed:author | pubmed-author:RyanD EDE | lld:pubmed |
pubmed-article:7673234 | pubmed:author | pubmed-author:KUFF | lld:pubmed |
pubmed-article:7673234 | pubmed:author | pubmed-author:McIntyreK WKW | lld:pubmed |
pubmed-article:7673234 | pubmed:author | pubmed-author:GreenfederS... | lld:pubmed |
pubmed-article:7673234 | pubmed:author | pubmed-author:PowersGG | lld:pubmed |
pubmed-article:7673234 | pubmed:author | pubmed-author:ShusterDD | lld:pubmed |
pubmed-article:7673234 | pubmed:author | pubmed-author:Lombard-Gillo... | lld:pubmed |
pubmed-article:7673234 | pubmed:author | pubmed-author:VarnellTT | lld:pubmed |
pubmed-article:7673234 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7673234 | pubmed:day | 22 | lld:pubmed |
pubmed-article:7673234 | pubmed:volume | 270 | lld:pubmed |
pubmed-article:7673234 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7673234 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7673234 | pubmed:pagination | 22460-6 | lld:pubmed |
pubmed-article:7673234 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:7673234 | pubmed:meshHeading | pubmed-meshheading:7673234-... | lld:pubmed |
pubmed-article:7673234 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7673234 | pubmed:articleTitle | Insertion of a structural domain of interleukin (IL)-1 beta confers agonist activity to the IL-1 receptor antagonist. Implications for IL-1 bioactivity. | lld:pubmed |
pubmed-article:7673234 | pubmed:affiliation | Department of Inflammation/Autoimmune Diseases, Hoffman-La Roche Inc., Nutley, New Jersey 07110, USA. | lld:pubmed |
pubmed-article:7673234 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7673234 | pubmed:publicationType | In Vitro | lld:pubmed |
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