| pubmed-article:11579226 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C0025663 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C0920472 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C0084378 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C0332255 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C2737044 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C0598002 | lld:lifeskim |
| pubmed-article:11579226 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:11579226 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:11579226 | pubmed:dateCreated | 2001-10-1 | lld:pubmed |
| pubmed-article:11579226 | pubmed:abstractText | RNA helicases represent a family of enzymes that unwind double-stranded (ds) RNA in a nucleoside triphosphate (NTP)-dependent fashion and which are required in all aspects of cellular RNA metabolism and processing. The hepatitis C virus (HCV) non-structural 3 (NS3) protein possesses a serine protease activity in the N-terminal one-third, whereas RNA-stimulated NTPase and helicase activities reside in the C-terminal portion of the 631 amino acid residue bifunctional enzyme. The HCV NS3 RNA helicase is of key importance in the life cycle of HCV, which makes it a target for the development of therapeutics. However, neither the precise mechanism nor the substrate structure has been defined for this enzyme. For nuclear magnetic resonance (NMR)-based drug discovery methods and for mechanistic studies we engineered, prepared and characterized various truncated constructs of the 451-residue HCV NS3 RNA helicase. Our goal was to produce smaller fragments of the enzyme, which would be amenable to solution NMR techniques while retaining their native NTP and/or nucleic acid binding sites. Solution conditions were optimized to obtain high-quality heteronuclear NMR spectra of nitrogen-15 isotope-labeled constructs, which are typical of well-folded monomeric proteins. Moreover, NMR binding studies and functional data directly support the correct folding of these fragments. | lld:pubmed |
| pubmed-article:11579226 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11579226 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11579226 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11579226 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11579226 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11579226 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11579226 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11579226 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11579226 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11579226 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11579226 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:11579226 | pubmed:issn | 0269-2139 | lld:pubmed |
| pubmed-article:11579226 | pubmed:author | pubmed-author:LieTT | lld:pubmed |
| pubmed-article:11579226 | pubmed:author | pubmed-author:WeberP CPC | lld:pubmed |
| pubmed-article:11579226 | pubmed:author | pubmed-author:WangY SYS | lld:pubmed |
| pubmed-article:11579226 | pubmed:author | pubmed-author:HessonTT | lld:pubmed |
| pubmed-article:11579226 | pubmed:author | pubmed-author:MadisonV SVS | lld:pubmed |
| pubmed-article:11579226 | pubmed:author | pubmed-author:WyssD FDF | lld:pubmed |
| pubmed-article:11579226 | pubmed:author | pubmed-author:GesellJ JJJ | lld:pubmed |
| pubmed-article:11579226 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11579226 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:11579226 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11579226 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11579226 | pubmed:pagination | 573-82 | lld:pubmed |
| pubmed-article:11579226 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:meshHeading | pubmed-meshheading:11579226... | lld:pubmed |
| pubmed-article:11579226 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11579226 | pubmed:articleTitle | Design, high-level expression, purification and characterization of soluble fragments of the hepatitis C virus NS3 RNA helicase suitable for NMR-based drug discovery methods and mechanistic studies. | lld:pubmed |
| pubmed-article:11579226 | pubmed:affiliation | These two authors contributed equally to this work. Department of Structural Chemistry, Schering-Plough Research Institute, 2015 Galloping Hill Road, Kenilworth, NJ 07033, USA. | lld:pubmed |
| pubmed-article:11579226 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11579226 | lld:pubmed |
