Literature DB >> 10726059

Helicase, a target for novel inhibitors of hepatitis C virus.

N Yao1, P C Weber.   

Abstract

Virus-encoded enzymes of hepatitis C virus (HCV) were identified from its genome sequence. This allows application of drug discovery strategies which rely on inhibition of enzymes unique to HCV. Discovery of high-affinity inhibitors is facilitated by knowledge of the target enzyme's three-dimensional structure. For development of inhibitors of the HCV helicase, which belongs to a class of enzymes for which little structural information is available, the impact of structural information on the drug discovery process is greater than for targets belonging to well-characterized classes of enzyme. Here the structure of the HCV helicase is described. Regions required for enzymatic activity, which are also the preferred sites of drug interaction, are highlighted.

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Year:  1998        PMID: 10726059

Source DB:  PubMed          Journal:  Antivir Ther        ISSN: 1359-6535


  3 in total

1.  Host cell factor requirement for hepatitis C virus enzyme maturation.

Authors:  L Waxman; M Whitney; B A Pollok; L C Kuo; P L Darke
Journal:  Proc Natl Acad Sci U S A       Date:  2001-11-13       Impact factor: 11.205

2.  Comparative characterization of two DEAD-box RNA helicases in superfamily II: human translation-initiation factor 4A and hepatitis C virus non-structural protein 3 (NS3) helicase.

Authors:  Mark X Du; Robert B Johnson; Xin-Lai Sun; Kirk A Staschke; Joseph Colacino; Q May Wang
Journal:  Biochem J       Date:  2002-04-01       Impact factor: 3.857

Review 3.  Viral and cellular RNA helicases as antiviral targets.

Authors:  Ann D Kwong; B Govinda Rao; Kuan-Teh Jeang
Journal:  Nat Rev Drug Discov       Date:  2005-10       Impact factor: 84.694

  3 in total

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