| pubmed-article:12504570 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C0029347 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C0029348 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C0028326 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C0033618 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C0305052 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C1706044 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C0872079 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C1522138 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:12504570 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:12504570 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12504570 | pubmed:dateCreated | 2002-12-30 | lld:pubmed |
| pubmed-article:12504570 | pubmed:abstractText | The N-terminal domains of the NS1 protein of influenza B virus (NS1B protein) and the NS1 protein of influenza A virus (NS1A protein) share one function: binding double-stranded RNA (dsRNA). Here we show that the N-terminal domain of the NS1B protein possesses an additional function that is not shared by its NS1A counterpart: binding the ubiquitin-like ISG15 protein that is induced by influenza B virus infection. Homology modeling predicts that the dimeric six-helical N-terminal domain of the NS1B protein differs from its NS1A protein counterpart in containing large loops between helices 1 and 2 (loops 1 and 1') and between helices 2 and 3 (loops 2 and 2'). Mutagenesis establishes that residues located in loop 1/1' together with residues located in polypeptide segment 94-103 form the ISG15 protein-binding site of NS1B protein. Loop 1/1' is not required for dsRNA binding, which instead requires arginine residues R50, R53, R50', and R53' located in antiparallel helices 1 and 1'. Further, we demonstrate that the binding sites for RNA and protein are independent of each other. In particular, ISG15 and dsRNA can bind simultaneously; the binding of the ISG15 protein does not have a detectable effect on the binding of dsRNA, and vice versa. | lld:pubmed |
| pubmed-article:12504570 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12504570 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12504570 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12504570 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12504570 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12504570 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12504570 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12504570 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12504570 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12504570 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12504570 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12504570 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12504570 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:12504570 | pubmed:issn | 0042-6822 | lld:pubmed |
| pubmed-article:12504570 | pubmed:author | pubmed-author:MontelioneGae... | lld:pubmed |
| pubmed-article:12504570 | pubmed:author | pubmed-author:KrugRobert... | lld:pubmed |
| pubmed-article:12504570 | pubmed:author | pubmed-author:YuanWeimingW | lld:pubmed |
| pubmed-article:12504570 | pubmed:author | pubmed-author:AraminiJames... | lld:pubmed |
| pubmed-article:12504570 | pubmed:copyrightInfo | Copyright 2002 Elsevier Science (USA) | lld:pubmed |
| pubmed-article:12504570 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12504570 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:12504570 | pubmed:volume | 304 | lld:pubmed |
| pubmed-article:12504570 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12504570 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12504570 | pubmed:pagination | 291-301 | lld:pubmed |
| pubmed-article:12504570 | pubmed:dateRevised | 2008-5-6 | lld:pubmed |
| pubmed-article:12504570 | pubmed:meshHeading | pubmed-meshheading:12504570... | lld:pubmed |
| pubmed-article:12504570 | pubmed:meshHeading | pubmed-meshheading:12504570... | lld:pubmed |
| pubmed-article:12504570 | pubmed:meshHeading | pubmed-meshheading:12504570... | lld:pubmed |
| pubmed-article:12504570 | pubmed:meshHeading | pubmed-meshheading:12504570... | lld:pubmed |
| pubmed-article:12504570 | pubmed:meshHeading | pubmed-meshheading:12504570... | lld:pubmed |
| pubmed-article:12504570 | pubmed:meshHeading | pubmed-meshheading:12504570... | lld:pubmed |
| pubmed-article:12504570 | pubmed:meshHeading | pubmed-meshheading:12504570... | lld:pubmed |
| pubmed-article:12504570 | pubmed:meshHeading | pubmed-meshheading:12504570... | lld:pubmed |
| pubmed-article:12504570 | pubmed:meshHeading | pubmed-meshheading:12504570... | lld:pubmed |
| pubmed-article:12504570 | pubmed:meshHeading | pubmed-meshheading:12504570... | lld:pubmed |
| pubmed-article:12504570 | pubmed:meshHeading | pubmed-meshheading:12504570... | lld:pubmed |
| pubmed-article:12504570 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12504570 | pubmed:articleTitle | Structural basis for ubiquitin-like ISG 15 protein binding to the NS1 protein of influenza B virus: a protein-protein interaction function that is not shared by the corresponding N-terminal domain of the NS1 protein of influenza A virus. | lld:pubmed |
| pubmed-article:12504570 | pubmed:affiliation | Institute for Cellular and Molecular Biology, Section of Molecular Genetics and Microbiology, University of Texas at Austin, 78712, USA. | lld:pubmed |
| pubmed-article:12504570 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12504570 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12504570 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12504570 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12504570 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12504570 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12504570 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12504570 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12504570 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12504570 | lld:pubmed |
