| pubmed-article:3286889 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3286889 | lifeskim:mentions | umls-concept:C1000323 | lld:lifeskim |
| pubmed-article:3286889 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:3286889 | lifeskim:mentions | umls-concept:C0032583 | lld:lifeskim |
| pubmed-article:3286889 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:3286889 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:3286889 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:3286889 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:3286889 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:3286889 | lifeskim:mentions | umls-concept:C1504308 | lld:lifeskim |
| pubmed-article:3286889 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:3286889 | pubmed:dateCreated | 1988-7-12 | lld:pubmed |
| pubmed-article:3286889 | pubmed:abstractText | The genome of tobacco etch virus contains a single open reading frame with the potential to encode a 346-kilodalton (kDa) polyprotein. The large polyprotein is cleaved at several positions by a tobacco etch virus genome-encoded, 49-kDa proteinase. The locations of the 49-kDa proteinase-mediated cleavage sites flanking the 71-kDa cytoplasmic pinwheel inclusion protein, 6-kDa protein, 49-kDa proteinase, and 58-kDa putative polymerase have been determined by using cell-free expression, proteolytic processing, and site-directed mutagenesis systems. Each of these sites is characterized by the conserved sequence motif Glu-Xaa-Xaa-Tyr-Xaa-Gln-Ser or Gly (in which cleavage occurs after the Gln residue). The amino acid residue (Gln) predicted to occupy the -1 position relative to the scissile bond has been substituted, by mutagenesis of cloned cDNA, at each of four cleavage sites. The altered sites were not cleaved by the 49-kDa proteinase. A series of synthetic polyproteins that contained the 49-kDa proteinase linked to adjoining proteins via defective cleavage sites were expressed, and their proteolytic activities were analyzed. As part of a polyprotein, the proteinase was found to exhibit cis (intramolecular) and trans (intermolecular) activity. | lld:pubmed |
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| pubmed-article:3286889 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3286889 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3286889 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3286889 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3286889 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:3286889 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:3286889 | pubmed:author | pubmed-author:CarrS HSH | lld:pubmed |
| pubmed-article:3286889 | pubmed:author | pubmed-author:CarringtonJ... | lld:pubmed |
| pubmed-article:3286889 | pubmed:author | pubmed-author:DoughertyW... | lld:pubmed |
| pubmed-article:3286889 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3286889 | pubmed:volume | 62 | lld:pubmed |
| pubmed-article:3286889 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3286889 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3286889 | pubmed:pagination | 2313-20 | lld:pubmed |
| pubmed-article:3286889 | pubmed:dateRevised | 2010-9-9 | lld:pubmed |
| pubmed-article:3286889 | pubmed:meshHeading | pubmed-meshheading:3286889-... | lld:pubmed |
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| pubmed-article:3286889 | pubmed:meshHeading | pubmed-meshheading:3286889-... | lld:pubmed |
| pubmed-article:3286889 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3286889 | pubmed:articleTitle | Mutational analysis of tobacco etch virus polyprotein processing: cis and trans proteolytic activities of polyproteins containing the 49-kilodalton proteinase. | lld:pubmed |
| pubmed-article:3286889 | pubmed:affiliation | Department of Microbiology, Oregon State University, Corvallis 97331-3804. | lld:pubmed |
| pubmed-article:3286889 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3286889 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3286889 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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