| pubmed-article:3285343 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C0521026 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C1000323 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C0032583 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C0450240 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C1706210 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C2347567 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:3285343 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:3285343 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:3285343 | pubmed:dateCreated | 1988-6-22 | lld:pubmed |
| pubmed-article:3285343 | pubmed:abstractText | Mature viral-encoded proteins of tobacco etch virus (TEV) arise by proteolytic processing of a large precursor. The proteinase responsible for most of these cleavages is a viral-encoded 49-kDa protein. All known or predicted cleavage sites in the TEV polyprotein are flanked by the conserved sequence motif Glu-Xaa-Xaa-Tyr-Xaa-Gln-Ser or Gly, with the scissile bond located between the Gln-Ser or Gly dipeptide. By using cell-free systems to manipulate and express cloned cDNA sequences, a 25-amino acid segment containing a putative proteolytic cleavage site of the TEV polyprotein has been introduced into the TEV capsid protein sequence. This recombinant protein is cleaved by the 49-kDa proteinase at the introduced cleavage site, thus demonstrating portability of a functional cleavage site. The role of the conserved amino acid sequence in determining substrate activity was tested by construction of engineered proteins that contained part or all of this motif. A protein that harbored an insertion of the conserved 7-amino acid segment was cleaved by the 49-kDa TEV proteinase. Cleavage of the synthetic precursor was shown to occur accurately between the expected Gln-Ser dipeptide by microsequence analysis. Proteins containing insertions that generated only the Gln-Ser, or only the serine moiety of the conserved sequence, were insensitive to the 49-kDa proteinase. | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3285343 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3285343 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3285343 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3285343 | pubmed:month | May | lld:pubmed |
| pubmed-article:3285343 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:3285343 | pubmed:author | pubmed-author:CarringtonJ... | lld:pubmed |
| pubmed-article:3285343 | pubmed:author | pubmed-author:DoughertyW... | lld:pubmed |
| pubmed-article:3285343 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3285343 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:3285343 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3285343 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3285343 | pubmed:pagination | 3391-5 | lld:pubmed |
| pubmed-article:3285343 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:meshHeading | pubmed-meshheading:3285343-... | lld:pubmed |
| pubmed-article:3285343 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3285343 | pubmed:articleTitle | A viral cleavage site cassette: identification of amino acid sequences required for tobacco etch virus polyprotein processing. | lld:pubmed |
| pubmed-article:3285343 | pubmed:affiliation | Department of Microbiology, Oregon State University, Corvallis 97331. | lld:pubmed |
| pubmed-article:3285343 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3285343 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3285343 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3285343 | lld:pubmed |
