pubmed-article:9007060 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9007060 | lifeskim:mentions | umls-concept:C0042216 | lld:lifeskim |
pubmed-article:9007060 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:9007060 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
pubmed-article:9007060 | lifeskim:mentions | umls-concept:C0073240 | lld:lifeskim |
pubmed-article:9007060 | lifeskim:mentions | umls-concept:C1442161 | lld:lifeskim |
pubmed-article:9007060 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:9007060 | pubmed:dateCreated | 1997-2-21 | lld:pubmed |
pubmed-article:9007060 | pubmed:abstractText | This work investigated whether the Escherichia coli RNase III gene, rnc+, could complement vp1080, a mutant vaccinia virus that is deleted of its E3L gene. Like E3L, rnc+ codes for a dsRNA binding protein that contains an additional nucleolytic activity. Rnc genes were cloned into the eukaryotic expression vector pMTVa-, expressed in COS-1 cells, and shown to be functional. Transient rescue experiments in HeLa cells demonstrated that the cleavage function of the rnc+ gene was necessary for full rescue of vp1080. The rnc 70 gene, which encodes a product deficient in catalytic activity but still capable of binding to dsRNA, rescued vp1080 weakly. The rnc 105 gene, which encodes a product that cannot bind or cleave dsRNA, was unable to rescue vp1080. The rnc genes were also inserted into the E3L locus of vp1080. While recombinants containing the rnc+ gene or the rnc 70 gene regained the IFN resistance phenotype in RK13 cells, full host range of vaccinia virus was only restored in the recombinant containing the rnc+ gene. Thus, the ability of RNase III to process dsRNA appears to be necessary to restore the host range phenotype. The vp-rnc 105 recombinant behaved similarly to vp1080. | lld:pubmed |
pubmed-article:9007060 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:language | eng | lld:pubmed |
pubmed-article:9007060 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9007060 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9007060 | pubmed:month | Jan | lld:pubmed |
pubmed-article:9007060 | pubmed:issn | 0042-6822 | lld:pubmed |
pubmed-article:9007060 | pubmed:author | pubmed-author:JacobsB LBL | lld:pubmed |
pubmed-article:9007060 | pubmed:author | pubmed-author:ShoreBB | lld:pubmed |
pubmed-article:9007060 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9007060 | pubmed:day | 6 | lld:pubmed |
pubmed-article:9007060 | pubmed:volume | 227 | lld:pubmed |
pubmed-article:9007060 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9007060 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9007060 | pubmed:pagination | 77-87 | lld:pubmed |
pubmed-article:9007060 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:9007060 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9007060 | pubmed:articleTitle | Complementation of deletion of the vaccinia virus E3L gene by the Escherichia coli RNase III gene. | lld:pubmed |
pubmed-article:9007060 | pubmed:affiliation | Department of Microbiology and the Graduate Program in Molecular and Cellular Biology, Arizona State University, Tempe, Arizona, 85287-2701, USA. | lld:pubmed |
pubmed-article:9007060 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9007060 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9007060 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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