| pubmed-article:19226622 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19226622 | lifeskim:mentions | umls-concept:C1047945 | lld:lifeskim |
| pubmed-article:19226622 | lifeskim:mentions | umls-concept:C0282629 | lld:lifeskim |
| pubmed-article:19226622 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:19226622 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:19226622 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:19226622 | pubmed:dateCreated | 2009-5-4 | lld:pubmed |
| pubmed-article:19226622 | pubmed:abstractText | We present the first all-atom model for the structure of a T = 3 virus, pariacoto virus (PaV), which is a nonenveloped, icosahedral RNA virus and a member of the Nodaviridae family. The model is an extension of the crystal structure, which reveals about 88% of the protein structure but only about 35% of the RNA structure. New modeling methods, combining coarse-grained and all-atom approaches, were required for developing the model. Evaluation of alternative models confirms our earlier observation that the polycationic N- and C-terminal tails of the capsid proteins must penetrate deeply into the core of the virus, where they stabilize the structure by neutralizing a substantial fraction of the RNA charge. This leads us to propose a model for the assembly of small icosahedral RNA viruses: nonspecific binding of the protein tails to the RNA leads to a collapse of the complex, in a fashion reminiscent of DNA condensation. The globular protein domains are excluded from the condensed phase but are tethered to it, so they accumulate in a shell around the condensed phase, where their concentration is high enough to trigger oligomerization and formation of the mature virus. | lld:pubmed |
| pubmed-article:19226622 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19226622 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19226622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19226622 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19226622 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:19226622 | pubmed:issn | 0006-3525 | lld:pubmed |
| pubmed-article:19226622 | pubmed:author | pubmed-author:TangLiangL | lld:pubmed |
| pubmed-article:19226622 | pubmed:author | pubmed-author:JohnsonJohn... | lld:pubmed |
| pubmed-article:19226622 | pubmed:author | pubmed-author:SchneemannAne... | lld:pubmed |
| pubmed-article:19226622 | pubmed:author | pubmed-author:HarveyStephen... | lld:pubmed |
| pubmed-article:19226622 | pubmed:author | pubmed-author:LemieuxSébast... | lld:pubmed |
| pubmed-article:19226622 | pubmed:author | pubmed-author:PetrovAnton... | lld:pubmed |
| pubmed-article:19226622 | pubmed:author | pubmed-author:BozMustafa... | lld:pubmed |
| pubmed-article:19226622 | pubmed:author | pubmed-author:DevkotaBatsal... | lld:pubmed |
| pubmed-article:19226622 | pubmed:copyrightInfo | (c) 2009 Wiley Periodicals, Inc. | lld:pubmed |
| pubmed-article:19226622 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19226622 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:19226622 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19226622 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19226622 | pubmed:pagination | 530-8 | lld:pubmed |
| pubmed-article:19226622 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:19226622 | pubmed:meshHeading | pubmed-meshheading:19226622... | lld:pubmed |
| pubmed-article:19226622 | pubmed:meshHeading | pubmed-meshheading:19226622... | lld:pubmed |
| pubmed-article:19226622 | pubmed:meshHeading | pubmed-meshheading:19226622... | lld:pubmed |
| pubmed-article:19226622 | pubmed:meshHeading | pubmed-meshheading:19226622... | lld:pubmed |
| pubmed-article:19226622 | pubmed:meshHeading | pubmed-meshheading:19226622... | lld:pubmed |
| pubmed-article:19226622 | pubmed:meshHeading | pubmed-meshheading:19226622... | lld:pubmed |
| pubmed-article:19226622 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19226622 | pubmed:articleTitle | Structural and electrostatic characterization of pariacoto virus: implications for viral assembly. | lld:pubmed |
| pubmed-article:19226622 | pubmed:affiliation | School of Biology, Georgia Institute of Technology, Atlanta, GA 30332-0230, USA. | lld:pubmed |
| pubmed-article:19226622 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19226622 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19226622 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19226622 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19226622 | lld:pubmed |
