| pubmed-article:19246376 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19246376 | lifeskim:mentions | umls-concept:C1005582 | lld:lifeskim |
| pubmed-article:19246376 | lifeskim:mentions | umls-concept:C0029246 | lld:lifeskim |
| pubmed-article:19246376 | lifeskim:mentions | umls-concept:C0006933 | lld:lifeskim |
| pubmed-article:19246376 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:19246376 | lifeskim:mentions | umls-concept:C1710548 | lld:lifeskim |
| pubmed-article:19246376 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:19246376 | pubmed:dateCreated | 2009-3-18 | lld:pubmed |
| pubmed-article:19246376 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19246376 | pubmed:abstractText | For most dsRNA viruses, the genome-enclosing capsid comprises 120 copies of a single capsid protein (CP) organized into 60 icosahedrally equivalent dimers, generally identified as 2 nonsymmetricallyinteracting CP molecules with extensive lateral contacts. The crystal structure of a partitivirus, Penicillium stoloniferum virus F (PsV-F), reveals a different organization, in which the CP dimer is related by almost-perfect local 2-fold symmetry, forms prominent surface arches, and includes extensive structure swapping between the 2 subunits. An electron cryomicroscopy map of PsV-F shows that the disordered N terminus of each CP molecule interacts with the dsRNA genome and probably participates in its packaging or transcription. Intact PsV-F particles mediate semiconservative transcription, and transcripts are likely to exit through negatively charged channels at the icosahedral 5-fold axes. Other findings suggest that the PsV-F capsid is assembled from dimers of CP dimers, with an arrangement similar to flavivirus E glycoproteins. | lld:pubmed |
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| pubmed-article:19246376 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19246376 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19246376 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19246376 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19246376 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:19246376 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:19246376 | pubmed:author | pubmed-author:JooFF | lld:pubmed |
| pubmed-article:19246376 | pubmed:author | pubmed-author:NibertMax LML | lld:pubmed |
| pubmed-article:19246376 | pubmed:author | pubmed-author:BakerTimothy... | lld:pubmed |
| pubmed-article:19246376 | pubmed:author | pubmed-author:OchoaWendy... | lld:pubmed |
| pubmed-article:19246376 | pubmed:author | pubmed-author:SinkovitsRobe... | lld:pubmed |
| pubmed-article:19246376 | pubmed:author | pubmed-author:GhabrialSaid... | lld:pubmed |
| pubmed-article:19246376 | pubmed:author | pubmed-author:TaoYizhi... | lld:pubmed |
| pubmed-article:19246376 | pubmed:author | pubmed-author:PanJunhuaJ | lld:pubmed |
| pubmed-article:19246376 | pubmed:author | pubmed-author:DongLipingL | lld:pubmed |
| pubmed-article:19246376 | pubmed:author | pubmed-author:HavensWendy... | lld:pubmed |
| pubmed-article:19246376 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19246376 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:19246376 | pubmed:volume | 106 | lld:pubmed |
| pubmed-article:19246376 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19246376 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19246376 | pubmed:pagination | 4225-30 | lld:pubmed |
| pubmed-article:19246376 | pubmed:dateRevised | 2011-2-14 | lld:pubmed |
| pubmed-article:19246376 | pubmed:meshHeading | pubmed-meshheading:19246376... | lld:pubmed |
| pubmed-article:19246376 | pubmed:meshHeading | pubmed-meshheading:19246376... | lld:pubmed |
| pubmed-article:19246376 | pubmed:meshHeading | pubmed-meshheading:19246376... | lld:pubmed |
| pubmed-article:19246376 | pubmed:meshHeading | pubmed-meshheading:19246376... | lld:pubmed |
| pubmed-article:19246376 | pubmed:meshHeading | pubmed-meshheading:19246376... | lld:pubmed |
| pubmed-article:19246376 | pubmed:meshHeading | pubmed-meshheading:19246376... | lld:pubmed |
| pubmed-article:19246376 | pubmed:meshHeading | pubmed-meshheading:19246376... | lld:pubmed |
| pubmed-article:19246376 | pubmed:meshHeading | pubmed-meshheading:19246376... | lld:pubmed |
| pubmed-article:19246376 | pubmed:meshHeading | pubmed-meshheading:19246376... | lld:pubmed |
| pubmed-article:19246376 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19246376 | pubmed:articleTitle | Atomic structure reveals the unique capsid organization of a dsRNA virus. | lld:pubmed |
| pubmed-article:19246376 | pubmed:affiliation | Department of Biochemistry and Cell Biology, Rice University, Houston, TX 77005, USA. | lld:pubmed |
| pubmed-article:19246376 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19246376 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:19246376 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19246376 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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