| pubmed-article:19467155 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19467155 | lifeskim:mentions | umls-concept:C0220847 | lld:lifeskim |
| pubmed-article:19467155 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:19467155 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:19467155 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:19467155 | lifeskim:mentions | umls-concept:C0596260 | lld:lifeskim |
| pubmed-article:19467155 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:19467155 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:19467155 | lifeskim:mentions | umls-concept:C0205088 | lld:lifeskim |
| pubmed-article:19467155 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:19467155 | pubmed:dateCreated | 2009-6-22 | lld:pubmed |
| pubmed-article:19467155 | pubmed:abstractText | Hepatitis C virus (HCV) induces membrane rearrangements during replication. All HCV proteins are associated to membranes, pointing out the importance of membranes for HCV. Non structural protein 4B (NS4B) has been reported to induce cellular membrane alterations like the membranous web. Four transmembrane segments in the middle of the protein anchor NS4B to membranes. An amphipatic helix at the amino-terminus attaches to membranes as well. The carboxy-terminal domain (CTD) of NS4B is highly conserved in Hepaciviruses, though its function remains unknown. | lld:pubmed |
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| pubmed-article:19467155 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19467155 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19467155 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19467155 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19467155 | pubmed:issn | 1743-422X | lld:pubmed |
| pubmed-article:19467155 | pubmed:author | pubmed-author:SpaanWilly... | lld:pubmed |
| pubmed-article:19467155 | pubmed:author | pubmed-author:BrandtBernd... | lld:pubmed |
| pubmed-article:19467155 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:19467155 | pubmed:author | pubmed-author:LiefhebberJol... | lld:pubmed |
| pubmed-article:19467155 | pubmed:author | pubmed-author:BroerReneR | lld:pubmed |
| pubmed-article:19467155 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19467155 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:19467155 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19467155 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19467155 | pubmed:pagination | 62 | lld:pubmed |
| pubmed-article:19467155 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
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| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:meshHeading | pubmed-meshheading:19467155... | lld:pubmed |
| pubmed-article:19467155 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19467155 | pubmed:articleTitle | Hepatitis C virus NS4B carboxy terminal domain is a membrane binding domain. | lld:pubmed |
| pubmed-article:19467155 | pubmed:affiliation | Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, 2300 RC Leiden, The Netherlands. J.M.P.Liefhebber@lumc.nl | lld:pubmed |
| pubmed-article:19467155 | pubmed:publicationType | Journal Article | lld:pubmed |
