QSAR studies on hepatitis C virus NS5A protein tetracyclic inhibitors in wild type and mutants by CoMFA and CoMSIA
Author:
Affiliation:
1. State Key Laboratory of Chemical Resource Engineering, Department of Pharmaceutical Engineering, Beijing University of Chemical Technology, Beijing, PR China
Publisher
Informa UK Limited
Subject
Drug Discovery,Molecular Medicine,General Medicine,Bioengineering
Link
https://www.tandfonline.com/doi/pdf/10.1080/1062936X.2020.1740889
Reference38 articles.
1. Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites
2. New Merck and Vertex drugs raise standard of care in hepatitis C
3. Understanding the hepatitis C virus life cycle paves the way for highly effective therapies
4. Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase
5. Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus
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4. In silico design and pharmacokinetics investigation of some novel hepatitis C virus NS5B inhibitors: pharmacoinformatics approach;Bulletin of the National Research Centre;2022-04-15
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