pubmed-article:9151887 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9151887 | lifeskim:mentions | umls-concept:C0042760 | lld:lifeskim |
pubmed-article:9151887 | lifeskim:mentions | umls-concept:C0206267 | lld:lifeskim |
pubmed-article:9151887 | lifeskim:mentions | umls-concept:C0026649 | lld:lifeskim |
pubmed-article:9151887 | lifeskim:mentions | umls-concept:C1136102 | lld:lifeskim |
pubmed-article:9151887 | lifeskim:mentions | umls-concept:C0183683 | lld:lifeskim |
pubmed-article:9151887 | lifeskim:mentions | umls-concept:C1550518 | lld:lifeskim |
pubmed-article:9151887 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
pubmed-article:9151887 | lifeskim:mentions | umls-concept:C0205373 | lld:lifeskim |
pubmed-article:9151887 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:9151887 | pubmed:dateCreated | 1997-6-9 | lld:pubmed |
pubmed-article:9151887 | pubmed:abstractText | Previous investigations into recombination in cowpea chlorotic mottle bromovirus (CCMV) resulted in the recovery of an unusual recombinant virus, 3-57, which caused a symptomless infection of cowpeas but formed no detectable virions. Sequence analysis of cDNA clones derived from 3-57 determined that mutations near the 5' terminus of the capsid protein gene introduced an early translational termination codon. Further mutations introduced a new in-frame start codon that allowed translation of the 3' two-thirds of the capsid protein gene. Based on the mutations observed in 3-57, wild-type CCMV clones were modified to determine if the carboxyl two-thirds of the capsid protein functions independently of the complete protein in long-distance movement. Analysis of these mutants determined that while virion formation is not required for systemic infection, the carboxy-terminal two-thirds of the capsid protein is both required and sufficient for systemic movement of viral RNA. This indicates that the CCMV capsid protein is multifunctional, with a distinct long-distance movement function in addition to its role in virion formation. | lld:pubmed |
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pubmed-article:9151887 | pubmed:language | eng | lld:pubmed |
pubmed-article:9151887 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9151887 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9151887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9151887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9151887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9151887 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9151887 | pubmed:month | Jun | lld:pubmed |
pubmed-article:9151887 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:9151887 | pubmed:author | pubmed-author:GreeneA EAE | lld:pubmed |
pubmed-article:9151887 | pubmed:author | pubmed-author:AllisonR FRF | lld:pubmed |
pubmed-article:9151887 | pubmed:author | pubmed-author:SchneiderW... | lld:pubmed |
pubmed-article:9151887 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9151887 | pubmed:volume | 71 | lld:pubmed |
pubmed-article:9151887 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9151887 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9151887 | pubmed:pagination | 4862-5 | lld:pubmed |
pubmed-article:9151887 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:9151887 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9151887 | pubmed:articleTitle | The carboxy-terminal two-thirds of the cowpea chlorotic mottle bromovirus capsid protein is incapable of virion formation yet supports systemic movement. | lld:pubmed |
pubmed-article:9151887 | pubmed:affiliation | Genetics Program, Michigan State University, East Lansing 48824, USA. | lld:pubmed |
pubmed-article:9151887 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9151887 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9151887 | lld:pubmed |