pubmed-article:19004948 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19004948 | lifeskim:mentions | umls-concept:C0222679 | lld:lifeskim |
pubmed-article:19004948 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:19004948 | lifeskim:mentions | umls-concept:C0006933 | lld:lifeskim |
pubmed-article:19004948 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:19004948 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:19004948 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:19004948 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:19004948 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:19004948 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:19004948 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
pubmed-article:19004948 | lifeskim:mentions | umls-concept:C1627932 | lld:lifeskim |
pubmed-article:19004948 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:19004948 | pubmed:dateCreated | 2008-12-30 | lld:pubmed |
pubmed-article:19004948 | pubmed:abstractText | Adenovirus serotype 5 protein IX (pIX) has two domains connected by a flexible linker. Three N-terminal domains form triskelions on the capsid facets that cement hexons together, and the C-terminal domains of four monomers form complexes toward the facet periphery. Here we present a cryoelectron microscopy structure of recombinant adenovirus with a peptide tag added to the C terminus of pIX. The structure, made up by several C termini of pIX, is longer at both ends than the wild-type protein, and Fabs directed against the tag bind to both ends of the oligomer, demonstrating that the pIX C termini associate in an antiparallel manner. | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:language | eng | lld:pubmed |
pubmed-article:19004948 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19004948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19004948 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19004948 | pubmed:month | Jan | lld:pubmed |
pubmed-article:19004948 | pubmed:issn | 1098-5514 | lld:pubmed |
pubmed-article:19004948 | pubmed:author | pubmed-author:BoulangerPier... | lld:pubmed |
pubmed-article:19004948 | pubmed:author | pubmed-author:SchoehnGuyG | lld:pubmed |
pubmed-article:19004948 | pubmed:author | pubmed-author:RuigrokRob... | lld:pubmed |
pubmed-article:19004948 | pubmed:author | pubmed-author:Rosa-Calatrav... | lld:pubmed |
pubmed-article:19004948 | pubmed:author | pubmed-author:MoriscotChris... | lld:pubmed |
pubmed-article:19004948 | pubmed:author | pubmed-author:FabryCéline... | lld:pubmed |
pubmed-article:19004948 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19004948 | pubmed:volume | 83 | lld:pubmed |
pubmed-article:19004948 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19004948 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19004948 | pubmed:pagination | 1135-9 | lld:pubmed |
pubmed-article:19004948 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:19004948 | pubmed:meshHeading | pubmed-meshheading:19004948... | lld:pubmed |
pubmed-article:19004948 | pubmed:meshHeading | pubmed-meshheading:19004948... | lld:pubmed |
pubmed-article:19004948 | pubmed:meshHeading | pubmed-meshheading:19004948... | lld:pubmed |
pubmed-article:19004948 | pubmed:meshHeading | pubmed-meshheading:19004948... | lld:pubmed |
pubmed-article:19004948 | pubmed:meshHeading | pubmed-meshheading:19004948... | lld:pubmed |
pubmed-article:19004948 | pubmed:meshHeading | pubmed-meshheading:19004948... | lld:pubmed |
pubmed-article:19004948 | pubmed:meshHeading | pubmed-meshheading:19004948... | lld:pubmed |
pubmed-article:19004948 | pubmed:meshHeading | pubmed-meshheading:19004948... | lld:pubmed |
pubmed-article:19004948 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19004948 | pubmed:articleTitle | The C-terminal domains of adenovirus serotype 5 protein IX assemble into an antiparallel structure on the facets of the capsid. | lld:pubmed |
pubmed-article:19004948 | pubmed:affiliation | Université Joseph Fourier, Unit for Virus Host Cell Interaction, UMR 5233 UJF-EMBL-CNRS, Grenoble cedex 9, France. | lld:pubmed |
pubmed-article:19004948 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19004948 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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