| pubmed-article:14528291 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14528291 | lifeskim:mentions | umls-concept:C0011315 | lld:lifeskim |
| pubmed-article:14528291 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
| pubmed-article:14528291 | lifeskim:mentions | umls-concept:C0175631 | lld:lifeskim |
| pubmed-article:14528291 | lifeskim:mentions | umls-concept:C0162808 | lld:lifeskim |
| pubmed-article:14528291 | lifeskim:mentions | umls-concept:C2827662 | lld:lifeskim |
| pubmed-article:14528291 | lifeskim:mentions | umls-concept:C0597705 | lld:lifeskim |
| pubmed-article:14528291 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:14528291 | pubmed:dateCreated | 2003-10-29 | lld:pubmed |
| pubmed-article:14528291 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14528291 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14528291 | pubmed:abstractText | Improved technology for reconstructing cryo-electron microscopy (cryo-EM) images has now made it possible to determine secondary structural features of membrane proteins in enveloped viruses. The structure of mature dengue virus particles was determined to a resolution of 9.5 A by cryo-EM and image reconstruction techniques, establishing the secondary structural disposition of the 180 envelope (E) and 180 membrane (M) proteins in the lipid envelope. The alpha-helical 'stem' regions of the E molecules, as well as part of the N-terminal section of the M proteins, are buried in the outer leaflet of the viral membrane. The 'anchor' regions of E and the M proteins each form antiparallel E-E and M-M transmembrane alpha-helices, leaving their C termini on the exterior of the viral membrane, consistent with the predicted topology of the unprocessed polyprotein. This is one of only a few determinations of the disposition of transmembrane proteins in situ and shows that the nucleocapsid core and envelope proteins do not have a direct interaction in the mature virus. | lld:pubmed |
| pubmed-article:14528291 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14528291 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14528291 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14528291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14528291 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14528291 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:14528291 | pubmed:issn | 1072-8368 | lld:pubmed |
| pubmed-article:14528291 | pubmed:author | pubmed-author:ZhangWeiW | lld:pubmed |
| pubmed-article:14528291 | pubmed:author | pubmed-author:MukhopadhyayS... | lld:pubmed |
| pubmed-article:14528291 | pubmed:author | pubmed-author:ZhangYingY | lld:pubmed |
| pubmed-article:14528291 | pubmed:author | pubmed-author:ChipmanPaul... | lld:pubmed |
| pubmed-article:14528291 | pubmed:author | pubmed-author:RossmannMicha... | lld:pubmed |
| pubmed-article:14528291 | pubmed:author | pubmed-author:BakerTimothy... | lld:pubmed |
| pubmed-article:14528291 | pubmed:author | pubmed-author:KuhnRichard... | lld:pubmed |
| pubmed-article:14528291 | pubmed:author | pubmed-author:CorverJeroenJ | lld:pubmed |
| pubmed-article:14528291 | pubmed:author | pubmed-author:StraussJames... | lld:pubmed |
| pubmed-article:14528291 | pubmed:author | pubmed-author:JohnsonPeter... | lld:pubmed |
| pubmed-article:14528291 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14528291 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:14528291 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14528291 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14528291 | pubmed:pagination | 907-12 | lld:pubmed |
| pubmed-article:14528291 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:14528291 | pubmed:meshHeading | pubmed-meshheading:14528291... | lld:pubmed |
| pubmed-article:14528291 | pubmed:meshHeading | pubmed-meshheading:14528291... | lld:pubmed |
| pubmed-article:14528291 | pubmed:meshHeading | pubmed-meshheading:14528291... | lld:pubmed |
| pubmed-article:14528291 | pubmed:meshHeading | pubmed-meshheading:14528291... | lld:pubmed |
| pubmed-article:14528291 | pubmed:meshHeading | pubmed-meshheading:14528291... | lld:pubmed |
| pubmed-article:14528291 | pubmed:meshHeading | pubmed-meshheading:14528291... | lld:pubmed |
| pubmed-article:14528291 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14528291 | pubmed:articleTitle | Visualization of membrane protein domains by cryo-electron microscopy of dengue virus. | lld:pubmed |
| pubmed-article:14528291 | pubmed:affiliation | Department of Biological Sciences, Lilly Hall, 915 W. State Street, Purdue University, West Lafayette, Indiana 47907, USA. | lld:pubmed |
| pubmed-article:14528291 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14528291 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14528291 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:14528291 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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