Literature DB >> 12369938

Peptidic inhibitors of the hepatitis C virus serine protease within non-structural protein 3.

T O Fischmann1, P C Weber.   

Abstract

New treatments for HCV (Hepatitis C virus) infections are likely to arise from inhibition of the essential, virally-encoded enzymes. These targets include the serine protease required for processing of the HCV polyprotein. The protease constitutes one functional domain of the bifunctional HCV NS3 (non-structural protein 3). Here, insights regarding the NS3 structure and recently synthesized NS3 inhibitors are reviewed. Interestingly, many NS3 protease inhibitors have taken advantage of an unusual product inhibition by N-terminal products of cleavage at the polyprotein processing sites.

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Year:  2002        PMID: 12369938     DOI: 10.2174/1381612023392595

Source DB:  PubMed          Journal:  Curr Pharm Des        ISSN: 1381-6128            Impact factor:   3.116


  1 in total

1.  Hepatitis C virus protease gene diversity in patients coinfected with human immunodeficiency virus.

Authors:  Mark A Winters; Seth L Welles; Mark Holodniy
Journal:  J Virol       Date:  2006-04       Impact factor: 5.103

  1 in total

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