Proteolytic processing and membrane association of putative nonstructural proteins of hepatitis C virus - Wikidata - awgldk - TriplyDB

Proteolytic processing and membrane association of putative nonstructural proteins of hepatitis C virus

Proteolytic processing and membrane association of putative nonstructural proteins of hepatitis C virus

http://www.wikidata.org/entity/Q29620964

about

NS4A protein as a marker of HCV history suggests that different HCV genotypes originally evolved from genotype 1b Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a "fuzzy complex" with VAPB-MSP domain which carries ALS-causing mutations Raf-1 kinase associates with Hepatitis C virus NS5A and regulates viral replication Hepatitis C virus non-structural protein NS3 interacts with LMP7, a component of the immunoproteasome, and affects its proteasome activity Association of hepatitis C virus replication complexes with microtubules and actin filaments is dependent on the interaction of NS3 and NS5A Identification of a lactoferrin-derived peptide possessing binding activity to hepatitis C virus E2 envelope protein Caspase-mediated cleavage of eukaryotic translation initiation factor subunit 2alpha Hepatitis C virus subgenomic replicons induce endoplasmic reticulum stress activating an intracellular signaling pathway Interactions between viral nonstructural proteins and host protein hVAP-33 mediate the formation of hepatitis C virus RNA replication complex on lipid raft Kinetic and structural analyses of hepatitis C virus polyprotein processing Human Choline Kinase-α Promotes Hepatitis C Virus RNA Replication through Modulation of Membranous Viral Replication Complex Formation 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 Characterization of an autonomous subgenomic pestivirus RNA replicon Interferon resistance of hepatitis C virus genotype 1b: relationship to nonstructural 5A gene quasispecies mutations Multiple enzymatic activities associated with recombinant NS3 protein of hepatitis C virus The native form and maturation process of hepatitis C virus core protein Complete translation of the hepatitis C virus genome in vitro: membranes play a critical role in the maturation of all virus proteins except for NS3.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 Characterization of cell lines carrying self-replicating hepatitis C virus RNAs.Activation of the interferon-inducible 2'-5'-oligoadenylate synthetase gene by hepatitis C virus core protein Persistence of bovine viral diarrhea virus is determined by a cellular cofactor of a viral autoprotease VX-950, a Novel Hepatitis C Virus (HCV) NS3-4A Protease Inhibitor, Exhibits Potent Antiviral Activities in HCV Replicon Cells Protein-Protein Interactions between Hepatitis C Virus Nonstructural Proteins Topology of the Membrane-Associated Hepatitis C Virus Protein NS4B Amphipathic Helix-Dependent Localization of NS5A Mediates Hepatitis C Virus RNA Replication Comparison of full-length sequences of interferon-sensitive and resistant hepatitis C virus 1b. Sensitivity to interferon is conferred by amino acid substitutions in the NS5A region Hepatitis C virus core protein promotes proliferation of human hepatoma cells through enhancement of transforming growth factor expression via activation of nuclear factor- B 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 Hepatitis C virus nonstructural protein NS3 transforms NIH 3T3 cells Phosphorylation of hepatitis C virus-encoded nonstructural protein NS5A Hepatitis C virus-encoded NS2-3 protease: cleavage-site mutagenesis and requirements for bimolecular cleavage The N-terminal region of hepatitis C virus nonstructural protein 3 (NS3) is essential for stable complex formation with NS4A A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro The NS2 protein of hepatitis C virus is a transmembrane polypeptide Complex formation between the NS3 serine-type proteinase of the hepatitis C virus and NS4A and its importance for polyprotein maturation Identification of the sequence on NS4A required for enhanced cleavage of the NS5A/5B site by hepatitis C virus NS3 protease Use of recombinant protein to identify a motif-negative human cytotoxic T-cell epitope presented by HLA-A2 in the hepatitis C virus NS3 region

P2860

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P2860

Proteolytic processing and membrane association of putative nonstructural proteins of hepatitis C virus

http://www.wikidata.org/entity/Q29620964

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1993 nî lūn-bûn

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1993 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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1993 թվականի նոյեմբերին հրատարակված գիտական հոդված

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1993年の論文

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1993年論文

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1993年論文

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1993年論文

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1993年論文

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1993年論文

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1993年论文

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Proteolytic processing and mem ...... proteins of hepatitis C virus

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Proteolytic processing and mem ...... proteins of hepatitis C virus

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PNAS.90.22.10773

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Proceedings of the National Academy of Sciences of the United States of America

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Proteolytic processing and mem ...... proteins of hepatitis C virus

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H Mizushima

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K Kimura

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P2860

Molecular cloning and characterization of a cDNA for a novel phorbol-12-myristate-13-acetate-responsive gene that is highly expressed in an adult T-cell leukemia cell line

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Expression and identification of hepatitis C virus polyprotein cleavage products

Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites

Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions

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

Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus

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

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

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