| http://purl.uniprot.org/citations/11119590 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11119590 | http://www.w3.org/2000/01/rdf-schema#comment | "Interaction between viral proteins is necessary for viral replication and viral particle assembly. We used the yeast two-hybrid assay to identify interactions among all the mature proteins of the hepatitis C virus. The interaction between NS3 and NS3 was one of the strongest viral protein-protein interactions detected. The minimal region required for this interaction was mapped to a specific subdomain of 174 amino acids in the N terminus of the helicase region. Random mutations in the minimal region were generated by PCR, and mutants that failed to interact with a wild-type minimal fragment were isolated using the yeast two-hybrid assay as a screen. Three of these mutations resulted in a reduction or a loss of interaction between helicases. Analytical gel filtration showed that in the presence of an oligonucleotide, wild-type helicases form dimers whereas the mutants remain mostly monomeric. All three mutants were partially or almost inactive when assayed for helicase activity in vitro. Mixing a mutant helicase (Y267S) with wild-type helicase did not dramatically affect helicase activity. These data indicate that dimerization of the helicase is important for helicase activity. The mutations that reduce self-association of the helicase may define the key residues involved in NS3-NS3 dimerization."xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.75.1.205-214.2001"xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/author | "Brenner S."xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/author | "Lim S.G."xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/author | "Tan Y.H."xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/author | "Koh E."xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/author | "Goh P.Y."xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/author | "Lim S.P."xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/author | "Hong W.J."xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/author | "Khu Y.L."xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/name | "J Virol"xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/pages | "205-214"xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/title | "Mutations that affect dimer formation and helicase activity of the hepatitis C virus helicase."xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://purl.uniprot.org/core/volume | "75"xsd:string |
| http://purl.uniprot.org/citations/11119590 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11119590 |
| http://purl.uniprot.org/citations/11119590 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11119590 |