pubmed-article:12604805 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12604805 | lifeskim:mentions | umls-concept:C0682323 | lld:lifeskim |
pubmed-article:12604805 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:12604805 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
pubmed-article:12604805 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:12604805 | lifeskim:mentions | umls-concept:C1332412 | lld:lifeskim |
pubmed-article:12604805 | lifeskim:mentions | umls-concept:C0529765 | lld:lifeskim |
pubmed-article:12604805 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:12604805 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:12604805 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:12604805 | lifeskim:mentions | umls-concept:C1569072 | lld:lifeskim |
pubmed-article:12604805 | pubmed:issue | Pt 3 | lld:pubmed |
pubmed-article:12604805 | pubmed:dateCreated | 2003-2-26 | lld:pubmed |
pubmed-article:12604805 | pubmed:abstractText | The hepatitis C virus (HCV) NS5A protein is highly phosphorylated by cellular protein kinases. To study how NS5A might be integrated in cellular kinase signalling, we isolated phosphoproteins from HuH-7 hepatoma cells that specifically interacted with recombinant NS5A protein. Subsequent mass spectrometry identified the adaptor protein amphiphysin II as a novel interaction partner of NS5A. Mutational analysis revealed that complex formation is primarily mediated by a proline-rich region in the C-terminal part of NS5A, which interacts with the amphiphysin II Src homology 3 domain. Importantly, we could further demonstrate specific co-precipitation and cellular co-localization of endogenous amphiphysin II with NS5A in HuH-7 cells carrying a persistently replicating subgenomic HCV replicon. Although the NS5A-amphiphysin II interaction appeared to be dispensable for replication of these HCV RNAs in cell culture, our results indicate that NS5A-amphiphysin II complex formation might be of physiological relevance for the HCV life cycle. | lld:pubmed |
pubmed-article:12604805 | pubmed:language | eng | lld:pubmed |
pubmed-article:12604805 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12604805 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12604805 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12604805 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12604805 | pubmed:month | Mar | lld:pubmed |
pubmed-article:12604805 | pubmed:issn | 0022-1317 | lld:pubmed |
pubmed-article:12604805 | pubmed:author | pubmed-author:Bartenschlage... | lld:pubmed |
pubmed-article:12604805 | pubmed:author | pubmed-author:KriegerNicole... | lld:pubmed |
pubmed-article:12604805 | pubmed:author | pubmed-author:StrandDennisD | lld:pubmed |
pubmed-article:12604805 | pubmed:author | pubmed-author:CottenMattM | lld:pubmed |
pubmed-article:12604805 | pubmed:author | pubmed-author:HergetThomasT | lld:pubmed |
pubmed-article:12604805 | pubmed:author | pubmed-author:DaubHenrikH | lld:pubmed |
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pubmed-article:12604805 | pubmed:author | pubmed-author:WissingJosefJ | lld:pubmed |
pubmed-article:12604805 | pubmed:author | pubmed-author:ZechBirgitB | lld:pubmed |
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pubmed-article:12604805 | pubmed:author | pubmed-author:ObertSabineS | lld:pubmed |
pubmed-article:12604805 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12604805 | pubmed:volume | 84 | lld:pubmed |
pubmed-article:12604805 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12604805 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12604805 | pubmed:pagination | 555-60 | lld:pubmed |
pubmed-article:12604805 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:12604805 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12604805 | pubmed:articleTitle | Identification and characterization of amphiphysin II as a novel cellular interaction partner of the hepatitis C virus NS5A protein. | lld:pubmed |
pubmed-article:12604805 | pubmed:affiliation | Axxima Pharmaceuticals AG, Am Klopferspitz 19, 82152 Martinsried, Germany. | lld:pubmed |
pubmed-article:12604805 | pubmed:publicationType | Journal Article | lld:pubmed |
entrez-gene:274 | entrezgene:pubmed | pubmed-article:12604805 | lld:entrezgene |
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