pubmed-article:19370068 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19370068 | lifeskim:mentions | umls-concept:C1175743 | lld:lifeskim |
pubmed-article:19370068 | lifeskim:mentions | umls-concept:C0042774 | lld:lifeskim |
pubmed-article:19370068 | lifeskim:mentions | umls-concept:C0524816 | lld:lifeskim |
pubmed-article:19370068 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:19370068 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:19370068 | pubmed:dateCreated | 2009-4-16 | lld:pubmed |
pubmed-article:19370068 | pubmed:abstractText | The multimerization/self-interaction of viral proteins is an important step in the process of viral assembly and maturation. Our previous study indicated that the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) nucleocapsid protein forms self-multimers through a serine-arginine (SR)-rich motif (SSRSSSRSRGNSR) by using a mammalian two-hybrid system. To determine the biological relevance of this motif, we constructed a SARS-CoV reverse genetic construct by using a bacterial artificial chromosome (BAC)-based vector controlled by a T7 promoter; and subsequently deleted the SR-rich motif from the N gene. The mutated infectious clone showed reduced level of genome transcription and significantly reduced levels of the infectious virions. These results strongly suggest that the SR-rich motif is critical for effective virus replication. | lld:pubmed |
pubmed-article:19370068 | pubmed:language | eng | lld:pubmed |
pubmed-article:19370068 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19370068 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19370068 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19370068 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19370068 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19370068 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19370068 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19370068 | pubmed:month | Mar | lld:pubmed |
pubmed-article:19370068 | pubmed:issn | 0008-4166 | lld:pubmed |
pubmed-article:19370068 | pubmed:author | pubmed-author:CaoJingxinJ | lld:pubmed |
pubmed-article:19370068 | pubmed:author | pubmed-author:LiXuguangX | lld:pubmed |
pubmed-article:19370068 | pubmed:author | pubmed-author:AndonovAntonA | lld:pubmed |
pubmed-article:19370068 | pubmed:author | pubmed-author:HeRuntaoR | lld:pubmed |
pubmed-article:19370068 | pubmed:author | pubmed-author:CuttsToddT | lld:pubmed |
pubmed-article:19370068 | pubmed:author | pubmed-author:Van... | lld:pubmed |
pubmed-article:19370068 | pubmed:author | pubmed-author:TylorShaunS | lld:pubmed |
pubmed-article:19370068 | pubmed:author | pubmed-author:GrudeskyElsey... | lld:pubmed |
pubmed-article:19370068 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:19370068 | pubmed:volume | 55 | lld:pubmed |
pubmed-article:19370068 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19370068 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19370068 | pubmed:pagination | 254-60 | lld:pubmed |
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pubmed-article:19370068 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19370068 | pubmed:articleTitle | The SR-rich motif in SARS-CoV nucleocapsid protein is important for virus replication. | lld:pubmed |
pubmed-article:19370068 | pubmed:affiliation | National Microbiology Laboratory, Health Canada, 1015 Arlington St, Winnipeg, MB R3E3R2, Canada. | lld:pubmed |
pubmed-article:19370068 | pubmed:publicationType | Journal Article | lld:pubmed |
literatureCitation:6899_193... | literatureCitation:pubmed | pubmed-article:19370068 | lld:drugbank |
entrez-gene:1489678 | entrezgene:pubmed | pubmed-article:19370068 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19370068 | lld:entrezgene |