| pubmed-article:11013211 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11013211 | lifeskim:mentions | umls-concept:C0042776 | lld:lifeskim |
| pubmed-article:11013211 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
| pubmed-article:11013211 | lifeskim:mentions | umls-concept:C0332516 | lld:lifeskim |
| pubmed-article:11013211 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:11013211 | pubmed:dateCreated | 2000-12-8 | lld:pubmed |
| pubmed-article:11013211 | pubmed:abstractText | Alphaviruses are enveloped icosahedral viruses that mature by budding at the plasma membrane. According to a prevailing model maturation is driven by binding of membrane protein spikes to a preformed nucleocapsid (NC). The T = 4 geometry of the membrane is thought to be imposed by the NC through one-to-one interactions between spike protomers and capsid proteins (CPs). This model is challenged here by a Semliki Forest virus capsid gene mutant. Its CPs cannot assemble into NCs, or its intermediate structures, due to defective CP-CP interactions. Nevertheless, it can use its horizontal spike-spike interactions on membrane surface and vertical spike-CP interactions to make a particle with correct geometry and protein stoichiometry. Thus, our results highlight the direct role of membrane proteins in organizing the icosahedral conformation of alphaviruses. | lld:pubmed |
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| pubmed-article:11013211 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11013211 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11013211 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11013211 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11013211 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:11013211 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11013211 | pubmed:author | pubmed-author:GaroffHH | lld:pubmed |
| pubmed-article:11013211 | pubmed:author | pubmed-author:XingLL | lld:pubmed |
| pubmed-article:11013211 | pubmed:author | pubmed-author:ChengR HRH | lld:pubmed |
| pubmed-article:11013211 | pubmed:author | pubmed-author:ForsellKK | lld:pubmed |
| pubmed-article:11013211 | pubmed:author | pubmed-author:KozlovskaTT | lld:pubmed |
| pubmed-article:11013211 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11013211 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:11013211 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:11013211 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11013211 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11013211 | pubmed:pagination | 5081-91 | lld:pubmed |
| pubmed-article:11013211 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11013211 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11013211 | pubmed:articleTitle | Membrane proteins organize a symmetrical virus. | lld:pubmed |
| pubmed-article:11013211 | pubmed:affiliation | Karolinska Institute, Department of Biosciences at Novum, S-141 57 Huddinge, Sweden. | lld:pubmed |
| pubmed-article:11013211 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11013211 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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