NS3 is a serine protease required for processing of hepatitis C virus polyprotein - sprookjes - yvandenbroek - TriplyDB

NS3 is a serine protease required for processing of hepatitis C virus polyprotein

NS3 is a serine protease required for processing of hepatitis C virus polyprotein

http://www.wikidata.org/entity/Q27486059

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NS4A protein as a marker of HCV history suggests that different HCV genotypes originally evolved from genotype 1b Nonstructural protein 5A of hepatitis C virus inhibits the function of karyopherin beta3 Hepatitis C virus non-structural protein NS3 interacts with LMP7, a component of the immunoproteasome, and affects its proteasome activity Human VAP-C negatively regulates hepatitis C virus propagation Kinetic and structural analyses of hepatitis C virus polyprotein processing Direct interaction of hepatitis C virus core protein with the cellular lymphotoxin-beta receptor modulates the signal pathway of the lymphotoxin-beta receptor The New Era of Interferon-Free Treatment of Chronic Hepatitis C Selection of functional variants of the NS3-NS4A protease of hepatitis C virus by using chimeric sindbis viruses Modulation of hepatitis C virus NS5A hyperphosphorylation by nonstructural proteins NS3, NS4A, and NS4B Development of cell-based assays for in vitro characterization of hepatitis C virus NS3/4A protease inhibitors Hepatitis G virus encodes protease activities which can effect processing of the virus putative nonstructural proteins.Characterization of an autonomous subgenomic pestivirus RNA replicon Multiple enzymatic activities associated with recombinant NS3 protein of hepatitis C virus The native form and maturation process of hepatitis C virus core protein Cell fusion activity of hepatitis C virus envelope proteins In vivo selection of protease cleavage sites by using chimeric Sindbis virus libraries De novo initiation of RNA synthesis by the RNA-dependent RNA polymerase (NS5B) of hepatitis C virus Subcellular localization, stability, and trans-cleavage competence of the hepatitis C virus NS3-NS4A complex expressed in tetracycline-regulated cell lines.Isolation and characterization of monoclonal antibodies that inhibit hepatitis C virus NS3 protease Roles of the AX(4)GKS and arginine-rich motifs of hepatitis C virus RNA helicase in ATP- and viral RNA-binding activity.Hyperphosphorylation of the hepatitis C virus NS5A protein requires an active NS3 protease, NS4A, NS4B, and NS5A encoded on the same polyprotein Mutations in Hepatitis C Virus RNAs Conferring Cell Culture Adaptation Specific Interaction of Hepatitis C Virus Protease/Helicase NS3 with the 3'-Terminal Sequences of Viral Positive- and Negative-Strand RNA Enhancement of hepatitis C virus RNA replication by cell culture-adaptive mutations.Stealth and cunning: hepatitis B and hepatitis C viruses.Persistent and transient replication of full-length hepatitis C virus genomes in cell culture Generation of hepatitis C virus-like particles by use of a recombinant vesicular stomatitis virus vector Isolation of specific and high-affinity RNA aptamers against NS3 helicase domain of hepatitis C virus.Hepatitis C Virus RNA Synthesis in a Cell-Free System Isolated from Replicon-Containing Hepatoma Cells SCH 503034, a mechanism-based inhibitor of hepatitis C virus NS3 protease, suppresses polyprotein maturation and enhances the antiviral activity of alpha interferon in replicon cells.VX-950, a Novel Hepatitis C Virus (HCV) NS3-4A Protease Inhibitor, Exhibits Potent Antiviral Activities in HCV Replicon Cells Antigenic structure of the hepatitis C virus envelope 2 protein Role of Divalent Metal Cations in ATP Hydrolysis Catalyzed by the Hepatitis C Virus NS3 Helicase: Magnesium Provides a Bridge for ATP to Fuel Unwinding Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing Pestivirus NS3 (p80) protein possesses RNA helicase activity An amino-terminal domain of the hepatitis C virus NS3 protease is essential for interaction with NS4A NS3-4A of hepatitis C virus is a chymotrypsin-like protease Hepatitis C virus nonstructural protein NS3 transforms NIH 3T3 cells Phosphorylation of hepatitis C virus-encoded nonstructural protein NS5A

P2860

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P2860

NS3 is a serine protease required for processing of hepatitis C virus polyprotein

http://www.wikidata.org/entity/Q27486059

description

1993 nî lūn-bûn

@nan

1993 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1993 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

1993年の論文

@ja

1993年論文

@yue

1993年論文

@zh-hant

1993年論文

@zh-hk

1993年論文

@zh-mo

1993年論文

@zh-tw

1993年论文

@wuu

name

NS3 is a serine protease required for processing of hepatitis C virus polyprotein

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NS3 is a serine protease required for processing of hepatitis C virus polyprotein

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NS3 is a serine protease required for processing of hepatitis C virus polyprotein

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type

label

NS3 is a serine protease required for processing of hepatitis C virus polyprotein

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NS3 is a serine protease required for processing of hepatitis C virus polyprotein

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NS3 is a serine protease required for processing of hepatitis C virus polyprotein

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prefLabel

NS3 is a serine protease required for processing of hepatitis C virus polyprotein

@ast

NS3 is a serine protease required for processing of hepatitis C virus polyprotein

@en

NS3 is a serine protease required for processing of hepatitis C virus polyprotein

@nl

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P1433

Journal of Virology

P1476

NS3 is a serine protease required for processing of hepatitis C virus polyprotein

@en

P2093

Failla C

http://www.w3.org/2001/XMLSchema#string

La Monica N

http://www.w3.org/2001/XMLSchema#string

Santolini E

http://www.w3.org/2001/XMLSchema#string

Tomei L

http://www.w3.org/2001/XMLSchema#string

P2860

A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions

Structure and organization of the hepatitis C virus genome isolated from human carriers

Processing and localization of Dengue virus type 2 polyprotein precursor NS3-NS4A-NS4B-NS5

Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins

Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease

Expression of processed core protein of hepatitis C virus in mammalian cells

Cleavage of dengue virus NS1-NS2A requires an octapeptide sequence at the C terminus of NS1

Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer

Proper processing of dengue virus nonstructural glycoprotein NS1 requires the N-terminal hydrophobic signal sequence and the downstream nonstructural protein NS2a

Genetic organization and diversity of the hepatitis C virus

P304

4017-4026

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P31

scholarly article

P433

7

http://www.w3.org/2001/XMLSchema#string

P478

67

http://www.w3.org/2001/XMLSchema#string

P50

Raffaele De Francesco

P577

1993-07-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

7685406

http://www.w3.org/2001/XMLSchema#string

P932

237769

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