| pubmed-article:16731950 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16731950 | lifeskim:mentions | umls-concept:C0036636 | lld:lifeskim |
| pubmed-article:16731950 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:16731950 | lifeskim:mentions | umls-concept:C1564357 | lld:lifeskim |
| pubmed-article:16731950 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:16731950 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:16731950 | pubmed:dateCreated | 2006-5-29 | lld:pubmed |
| pubmed-article:16731950 | pubmed:abstractText | The alphavirus Semliki Forest virus (SFV) infects cells through low-pH-induced membrane fusion mediated by the E1 protein, a class II virus membrane fusion protein. During fusion, E1 inserts into target membranes via its hydrophobic fusion loop and refolds to form a stable E1 homotrimer. Mutation of a highly conserved histidine (the H230A mutation) within a loop adjacent to the fusion loop was previously shown to block SFV fusion and infection, although the mutant E1 protein still inserts into target membranes and forms a homotrimer. Here we report on second-site mutations in E1 that rescue the H230A mutant. These mutations were located in a cluster within the hinge region, at the membrane-interacting tip, and within the groove where the E1 stem is believed to pack. Together the revertants reveal specific and interconnected aspects of the fusion protein refolding reaction. | lld:pubmed |
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| pubmed-article:16731950 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16731950 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16731950 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16731950 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16731950 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:16731950 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:16731950 | pubmed:author | pubmed-author:KielianMargar... | lld:pubmed |
| pubmed-article:16731950 | pubmed:author | pubmed-author:Chanel-VosCha... | lld:pubmed |
| pubmed-article:16731950 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16731950 | pubmed:volume | 80 | lld:pubmed |
| pubmed-article:16731950 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16731950 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16731950 | pubmed:pagination | 6115-22 | lld:pubmed |
| pubmed-article:16731950 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:16731950 | pubmed:meshHeading | pubmed-meshheading:16731950... | lld:pubmed |
| pubmed-article:16731950 | pubmed:meshHeading | pubmed-meshheading:16731950... | lld:pubmed |
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| pubmed-article:16731950 | pubmed:meshHeading | pubmed-meshheading:16731950... | lld:pubmed |
| pubmed-article:16731950 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16731950 | pubmed:articleTitle | Second-site revertants of a Semliki Forest virus fusion-block mutation reveal the dynamics of a class II membrane fusion protein. | lld:pubmed |
| pubmed-article:16731950 | pubmed:affiliation | Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. | lld:pubmed |
| pubmed-article:16731950 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16731950 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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