| pubmed-article:11463384 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11463384 | lifeskim:mentions | umls-concept:C0702091 | lld:lifeskim |
| pubmed-article:11463384 | lifeskim:mentions | umls-concept:C0029246 | lld:lifeskim |
| pubmed-article:11463384 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:11463384 | lifeskim:mentions | umls-concept:C0597177 | lld:lifeskim |
| pubmed-article:11463384 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11463384 | pubmed:dateCreated | 2001-8-15 | lld:pubmed |
| pubmed-article:11463384 | pubmed:abstractText | The tick-borne encephalitis (TBE) flavivirus contains two transmembrane proteins, E and M. Coexpression of E and the M precursor (prM) leads to secretion of recombinant subviral particles (RSPs). In the most common form of these RSPs, analyzed at a 19 A resolution by cryo-electron microscopy (cryo-EM), 60 copies of E pack as dimers in a T = 1 icosahedral surface lattice (outer diameter, 315 A). Fitting the high-resolution structure of a soluble E fragment into the RSP density defines interaction sites between E dimers, positions M relative to E, and allows assignment of transmembrane regions of E and M. Lateral interactions among the glycoproteins stabilize this capsidless particle; similar interactions probably contribute to assembly of virions. The structure suggests a picture for trimer association under fusion-inducing conditions. | lld:pubmed |
| pubmed-article:11463384 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11463384 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11463384 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11463384 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11463384 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11463384 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:11463384 | pubmed:author | pubmed-author:HarrisonS CSC | lld:pubmed |
| pubmed-article:11463384 | pubmed:author | pubmed-author:ClarkeMM | lld:pubmed |
| pubmed-article:11463384 | pubmed:author | pubmed-author:FullerS DSD | lld:pubmed |
| pubmed-article:11463384 | pubmed:author | pubmed-author:HeinzF XFX | lld:pubmed |
| pubmed-article:11463384 | pubmed:author | pubmed-author:AllisonS LSL | lld:pubmed |
| pubmed-article:11463384 | pubmed:author | pubmed-author:ReyF AFA | lld:pubmed |
| pubmed-article:11463384 | pubmed:author | pubmed-author:SchalichJJ | lld:pubmed |
| pubmed-article:11463384 | pubmed:author | pubmed-author:FerlenghiII | lld:pubmed |
| pubmed-article:11463384 | pubmed:author | pubmed-author:RuttanTT | lld:pubmed |
| pubmed-article:11463384 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11463384 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:11463384 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11463384 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11463384 | pubmed:pagination | 593-602 | lld:pubmed |
| pubmed-article:11463384 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11463384 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11463384 | pubmed:articleTitle | Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus. | lld:pubmed |
| pubmed-article:11463384 | pubmed:affiliation | The Structural Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany. | lld:pubmed |
| pubmed-article:11463384 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11463384 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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