| pubmed-article:9889156 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9889156 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:9889156 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:9889156 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:9889156 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:9889156 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
| pubmed-article:9889156 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:9889156 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:9889156 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:9889156 | pubmed:dateCreated | 1999-4-7 | lld:pubmed |
| pubmed-article:9889156 | pubmed:abstractText | The proteinase domain of the hepatitis C virus NS3 protein is involved in the maturation of the viral polyprotein. A central hydrophobic domain of the NS4A protein is required as a cofactor for its proteolytic activity. The three-dimensional structure of the proteinase domain alone and complexed with an NS4A-derived peptide has been solved recently and revealed that the N terminus of the proteinase is in near proximity to the C terminus of the cofactor. To study the molecular basis of the enzyme activation by its cofactor and to overcome the difficulties of structural and functional investigation associated with a two-species complex, we rationally designed a link to bridge the two molecules in order to have a single polypeptide construct. | lld:pubmed |
| pubmed-article:9889156 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9889156 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9889156 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9889156 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9889156 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9889156 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9889156 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9889156 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9889156 | pubmed:issn | 1359-0278 | lld:pubmed |
| pubmed-article:9889156 | pubmed:author | pubmed-author:De... | lld:pubmed |
| pubmed-article:9889156 | pubmed:author | pubmed-author:TomerEE | lld:pubmed |
| pubmed-article:9889156 | pubmed:author | pubmed-author:TramontanoAA | lld:pubmed |
| pubmed-article:9889156 | pubmed:author | pubmed-author:SteinkühlerCC | lld:pubmed |
| pubmed-article:9889156 | pubmed:author | pubmed-author:DimaseJJ | lld:pubmed |
| pubmed-article:9889156 | pubmed:author | pubmed-author:DelmastroPP | lld:pubmed |
| pubmed-article:9889156 | pubmed:author | pubmed-author:PasquoAA | lld:pubmed |
| pubmed-article:9889156 | pubmed:author | pubmed-author:NardiM CMC | lld:pubmed |
| pubmed-article:9889156 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9889156 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:9889156 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9889156 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9889156 | pubmed:pagination | 433-41 | lld:pubmed |
| pubmed-article:9889156 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9889156 | pubmed:meshHeading | pubmed-meshheading:9889156-... | lld:pubmed |
| pubmed-article:9889156 | pubmed:meshHeading | pubmed-meshheading:9889156-... | lld:pubmed |
| pubmed-article:9889156 | pubmed:meshHeading | pubmed-meshheading:9889156-... | lld:pubmed |
| pubmed-article:9889156 | pubmed:meshHeading | pubmed-meshheading:9889156-... | lld:pubmed |
| pubmed-article:9889156 | pubmed:meshHeading | pubmed-meshheading:9889156-... | lld:pubmed |
| pubmed-article:9889156 | pubmed:meshHeading | pubmed-meshheading:9889156-... | lld:pubmed |
| pubmed-article:9889156 | pubmed:meshHeading | pubmed-meshheading:9889156-... | lld:pubmed |
| pubmed-article:9889156 | pubmed:meshHeading | pubmed-meshheading:9889156-... | lld:pubmed |
| pubmed-article:9889156 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9889156 | pubmed:articleTitle | Rational design and functional expression of a constitutively active single-chain NS4A-NS3 proteinase. | lld:pubmed |
| pubmed-article:9889156 | pubmed:affiliation | Istituto di Ricerche di Biologia Molecolare (IRBM), P. Angeletti, Pomezia (Rome), Italy. | lld:pubmed |
| pubmed-article:9889156 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9889156 | lld:pubmed |
