pubmed-article:15890965 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15890965 | lifeskim:mentions | umls-concept:C0024267 | lld:lifeskim |
pubmed-article:15890965 | lifeskim:mentions | umls-concept:C0206497 | lld:lifeskim |
pubmed-article:15890965 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
pubmed-article:15890965 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:15890965 | lifeskim:mentions | umls-concept:C0314603 | lld:lifeskim |
pubmed-article:15890965 | lifeskim:mentions | umls-concept:C1335439 | lld:lifeskim |
pubmed-article:15890965 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:15890965 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
pubmed-article:15890965 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:15890965 | pubmed:dateCreated | 2005-5-13 | lld:pubmed |
pubmed-article:15890965 | pubmed:abstractText | The arenavirus L protein has the characteristic sequence motifs conserved among the RNA-dependent RNA polymerase L proteins of negative-strand (NS) RNA viruses. Studies based on the use of reverse-genetics approaches have provided direct experimental evidence of the key role played by the arenavirus L protein in viral-RNA synthesis. Sequence alignment shows six conserved domains among L proteins of NS RNA viruses. The proposed polymerase module of L is located within its domain III, which contains highly conserved amino acids within motifs designated A and C. We have examined the role of these conserved residues in the polymerase activity of the L protein of the prototypic arenavirus, lymphocytic choriomeningitis virus (LCMV), in vivo using a minigenome rescue assay. We show here that the presence of sequence SDD, a characteristic of motif C of segmented NS RNA viruses, as well as the presence of the highly conserved D residue within motif A of L proteins, is strictly required for the polymerase activity of the LCMV L protein. The strong dominant negative phenotype associated with many of the mutants examined and results from coimmunoprecipitation studies provided genetic and biochemical evidence, respectively, for the requirement of the L-L interaction for the polymerase activity of the LCMV L protein. | lld:pubmed |
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pubmed-article:15890965 | pubmed:language | eng | lld:pubmed |
pubmed-article:15890965 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15890965 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:15890965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15890965 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15890965 | pubmed:month | Jun | lld:pubmed |
pubmed-article:15890965 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:15890965 | pubmed:author | pubmed-author:de la... | lld:pubmed |
pubmed-article:15890965 | pubmed:author | pubmed-author:SánchezAna... | lld:pubmed |
pubmed-article:15890965 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15890965 | pubmed:volume | 79 | lld:pubmed |
pubmed-article:15890965 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15890965 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15890965 | pubmed:pagination | 7262-8 | lld:pubmed |
pubmed-article:15890965 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:15890965 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:15890965 | pubmed:articleTitle | Genetic and biochemical evidence for an oligomeric structure of the functional L polymerase of the prototypic arenavirus lymphocytic choriomeningitis virus. | lld:pubmed |
pubmed-article:15890965 | pubmed:affiliation | Department of Neuropharmacology IMM-6, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. | lld:pubmed |
pubmed-article:15890965 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15890965 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:15890965 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:15890965 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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