| pubmed-article:19074433 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19074433 | lifeskim:mentions | umls-concept:C0015450 | lld:lifeskim |
| pubmed-article:19074433 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
| pubmed-article:19074433 | lifeskim:mentions | umls-concept:C0014239 | lld:lifeskim |
| pubmed-article:19074433 | lifeskim:mentions | umls-concept:C1159339 | lld:lifeskim |
| pubmed-article:19074433 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:19074433 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:19074433 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:19074433 | pubmed:dateCreated | 2009-2-9 | lld:pubmed |
| pubmed-article:19074433 | pubmed:abstractText | Viperin is an evolutionarily conserved interferon-inducible protein that localizes to the endoplasmic reticulum (ER) and inhibits a number of DNA and RNA viruses. In this study, we report that viperin specifically localizes to the cytoplasmic face of the ER and that an amphipathic alpha-helix at its N terminus is necessary for the ER localization of viperin and sufficient to promote ER localization of a reporter protein, dsRed. Overexpression of intact viperin but not the amphipathic alpha-helix fused to dsRed induced crystalloid ER. Consistent with other proteins that induce crystalloid ER, viperin self-associates, and it does so independently of the amphipathic alpha-helix. Viperin expression also affected the transport of soluble but not membrane-associated proteins. Expression of intact viperin or an N-terminal alpha-helix-dsRed fusion protein significantly reduced secretion of soluble alkaline phosphatase and reduced its rate of ER-to-Golgi trafficking. Similarly, viperin expression inhibited bulk protein secretion and secretion of endogenous alpha(1)-antitrypsin and serum albumin from HepG2 cells. Converting hydrophobic residues in the N-terminal alpha-helix to acidic residues partially or completely restored normal transport of soluble alkaline phosphatase, suggesting that the extended amphipathic nature of the N-terminal alpha-helical domain is essential for inhibiting protein secretion. | lld:pubmed |
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| pubmed-article:19074433 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19074433 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19074433 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19074433 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19074433 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:19074433 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:19074433 | pubmed:author | pubmed-author:CresswellPete... | lld:pubmed |
| pubmed-article:19074433 | pubmed:author | pubmed-author:HinsonElla... | lld:pubmed |
| pubmed-article:19074433 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19074433 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:19074433 | pubmed:volume | 284 | lld:pubmed |
| pubmed-article:19074433 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19074433 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19074433 | pubmed:pagination | 4705-12 | lld:pubmed |
| pubmed-article:19074433 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:19074433 | pubmed:meshHeading | pubmed-meshheading:19074433... | lld:pubmed |
| pubmed-article:19074433 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19074433 | pubmed:articleTitle | The N-terminal amphipathic alpha-helix of viperin mediates localization to the cytosolic face of the endoplasmic reticulum and inhibits protein secretion. | lld:pubmed |
| pubmed-article:19074433 | pubmed:affiliation | Section of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut 06520-8011, USA. | lld:pubmed |
| pubmed-article:19074433 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19074433 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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