Biochemical and kinetic analyses of NS5B RNA-dependent RNA polymerase of the hepatitis C virus.
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TLDR
The profile of several inhibitors of RdRp activity and substrate analogs indicated that the enzyme has a strong preference for ribonucleoside 5'-triphosphates and that it closely resembles 3Dpol of picornaviruses.About:
This article is published in Virology.The article was published on 1998-09-15 and is currently open access. It has received 178 citations till now. The article focuses on the topics: RNA-dependent RNA polymerase & NS5B.read more
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Flaviviridae :T he Viruses and Their Replication
TL;DR: The present research attacked the Flavivirus infection through two mechanisms: Membrane Reorganization and the Compartmentalization and Assembly and Release of Particles from Flaviv virus-infected Cells and Host Resistance to Flaviviral Infection.
Journal ArticleDOI
Replication of the hepatitis C virus
TL;DR: This review summarizes the current knowledge about HCV replication and describes attempts pursued in the last few years to establish efficient and reliable cell culture systems.
Journal ArticleDOI
Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
Charles A. Lesburg,Michael B. Cable,Eric Ferrari,Zhi Hong,Anthony F. Mannarino,Patricia C. Weber +5 more
TL;DR: The HCV NS5B apoenzyme structure reported here can accommodate a template:primer duplex without global conformational changes, supporting the hypothesis that this structure is essentially preserved during the reaction pathway.
Book ChapterDOI
Overview of Hepatitis C Virus Genome Structure, Polyprotein Processing, and Protein Properties
K. E. Reed,Charles M. Rice +1 more
TL;DR: The genome of hepatitis C virus (HCV) was first cloned in 1989 by screening a λgt11 cDNA expression library, derived from the plasma of a persistently infected chimpanzee, with hepatitis C patient serum, and hybridization and nuclease digestion experiments indicated that the HCV genome consists of a single-stranded, positive-sense, RNA molecule.
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Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus.
Hideo Ago,Tsuyoshi Adachi,Atsuhito Yoshida,Masaki Yamamoto,Noriyuki Habuka,Kimio Yatsunami,Masashi Miyano +6 more
TL;DR: It is proposed that the unique alpha fingers might represent a common structural discriminator of the template-primer duplex that distinguishes between RNA and DNA during the replication of positive single-stranded RNA by viral RdRps.
References
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Journal ArticleDOI
A simplification of the protein assay method of Lowry et al. which is more generally applicable
TL;DR: A simple method based on a linear log-log protein standard curve is presented to permit rapid and totally objective protein analysis using small programmable calculators.
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Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome
TL;DR: A random-primed complementary DNA library was constructed from plasma containing the uncharacterized non-A, non-B hepatitis agent and screened with serum from a patient diagnosed with NANBH, showing consistent with the agent being similar to the togaviridae or flaviviridae.
Book ChapterDOI
The International Committee on Taxonomy of Viruses
Frederick A. Murphy,Claude M. Fauquet,David H. L. Bishop,Said A. Ghabrial,Audrey W. Jarvis,Giovanni P. Martelli,Michael Mayo,Max D. Summers +7 more
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Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus.
TL;DR: Experimental evidence that an RNA‐dependent RNA polymerase is encoded by HCV and that this enzymatic activity is the function of the 65 kDa non‐structural protein 5B (NS5B) is presented, representing a first important step towards a better understanding of the life cycle of the HCV.
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Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity.
TL;DR: The NS5B protein of the hepatitis C virus is an RNA-dependent RNA polymerase (RdRp) that is assumed to be required for replication of the viral genome and four amino acid sequence motifs crucial for RdRp activity were identified by using a mutational analysis.