Amphipathic alpha-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4B - Wikidata - wikimedia - TriplyDB

Amphipathic alpha-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4B

Amphipathic alpha-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4B

http://www.wikidata.org/entity/Q34416649

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Mechanisms of Cellular Membrane Reorganization to Support Hepatitis C Virus Replication Host-Targeting Agents to Prevent and Cure Hepatitis C Virus Infection Architecture and biogenesis of plus-strand RNA virus replication factories Membranous replication factories induced by plus-strand RNA viruses Sequential biogenesis of host cell membrane rearrangements induced by hepatitis C virus infection.Early dengue virus protein synthesis induces extensive rearrangement of the endoplasmic reticulum independent of the UPR and SREBP-2 pathway Dengue Virus Non-structural Protein 1 Modulates Infectious Particle Production via Interaction with the Structural Proteins Membrane interacting regions of Dengue virus NS2A protein.Aminoterminal amphipathic α-helix AH1 of hepatitis C virus nonstructural protein 4B possesses a dual role in RNA replication and virus production.Stearoyl coenzyme A desaturase 1 is associated with hepatitis C virus replication complex and regulates viral replication.Equilibrium and folding simulations of NS4B H2 in pure water and water/2,2,2-trifluoroethanol mixed solvent: examination of solvation models.Genetic complementation of hepatitis C virus nonstructural protein functions associated with replication exhibits requirements that differ from those for virion assembly.NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes.Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.Charged residues in hepatitis C virus NS4B are critical for multiple NS4B functions in RNA replication.Encoded library technology screening of hepatitis C virus NS4B yields a small-molecule compound series with in vitro replicon activity.The interaction between the hepatitis C proteins NS4B and NS5A is involved in viral replication Lipid Binding of the Amphipathic Helix Serving as Membrane Anchor of Pestivirus Glycoprotein Erns The emerging role of the first 17 amino acids of huntingtin in Huntington's disease Highly efficient full-length hepatitis C virus genotype 1 (strain TN) infectious culture system.Analysis of hepatitis C virus resistance to silibinin in vitro and in vivo points to a novel mechanism involving nonstructural protein 4B.Hepatitis C virus NS4B targets lipid droplets through hydrophobic residues in the amphipathic helices Post-translational modifications of hepatitis C viral proteins and their biological significance.Membrane-mediated aggregation of curvature-inducing nematogens and membrane tubulation.Hepatitis C virus RNA replication and virus particle assembly require specific dimerization of the NS4A protein transmembrane domain.Multifaceted roles for lipids in viral infection.Interaction networks of hepatitis C virus NS4B: implications for antiviral therapy.The molecular and structural basis of advanced antiviral therapy for hepatitis C virus infection.Interaction between Nonstructural Proteins NS4B and NS5A Is Essential for Proper NS5A Localization and Hepatitis C Virus RNA Replication.Preclinical Characterization and In Vivo Efficacy of GSK8853, a Small-Molecule Inhibitor of the Hepatitis C Virus NS4B Protein Entangled in a membranous web: ER and lipid droplet reorganization during hepatitis C virus infection.NS5A Domain 1 and Polyprotein Cleavage Kinetics Are Critical for Induction of Double-Membrane Vesicles Associated with Hepatitis C Virus Replication.The predominant species of nonstructural protein 4B in hepatitis C virus-replicating cells is not palmitoylated.A hepatitis C virus NS4B inhibitor suppresses viral genome replication by disrupting NS4B's dimerization/multimerization as well as its interaction with NS5A.Polyprotein-Driven Formation of Two Interdependent Sets of Complexes Supporting Hepatitis C Virus Genome Replication.An N-terminal amphipathic helix in dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication.Morphological and biochemical characterization of the membranous hepatitis C virus replication compartment.Reticulon 3 interacts with NS4B of the hepatitis C virus and negatively regulates viral replication by disrupting NS4B self-interaction.Glycine-zipper motifs in hepatitis C virus nonstructural protein 4B are required for the establishment of viral replication organelles.Current and future targets of antiviral therapy in the hepatitis C virus life cycle

P2860

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P2860

Amphipathic alpha-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4B

http://www.wikidata.org/entity/Q34416649

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Amphipathic alpha-helix AH2 is ...... virus nonstructural protein 4B

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Amphipathic alpha-helix AH2 is ...... virus nonstructural protein 4B

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Amphipathic alpha-helix AH2 is ...... virus nonstructural protein 4B

@nl

type

label

Amphipathic alpha-helix AH2 is ...... virus nonstructural protein 4B

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Amphipathic alpha-helix AH2 is ...... virus nonstructural protein 4B

@en

Amphipathic alpha-helix AH2 is ...... virus nonstructural protein 4B

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prefLabel

Amphipathic alpha-helix AH2 is ...... virus nonstructural protein 4B

@ast

Amphipathic alpha-helix AH2 is ...... virus nonstructural protein 4B

@en

Amphipathic alpha-helix AH2 is ...... virus nonstructural protein 4B

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Journal of Virology

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Amphipathic alpha-helix AH2 is ...... virus nonstructural protein 4B

@en

P2093

François Penin

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Philippe Roingeard

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P2860

Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex

Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle

Oligomerization and Cooperative RNA Synthesis Activity of Hepatitis C Virus RNA-Dependent RNA Polymerase

Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase

Palmitoylation and Polymerization of Hepatitis C Virus NS4B Protein

Topology of the Membrane-Associated Hepatitis C Virus Protein NS4B

Identification of the Hepatitis C Virus RNA Replication Complex in Huh-7 Cells Harboring Subgenomic Replicons

Structural determinants for membrane association and dynamic organization of the hepatitis C virus NS3-4A complex.

NS3 Helicase from the Hepatitis C Virus Can Function as a Monomer or Oligomer Depending on Enzyme and Substrate Concentrations

The Hepatitis C Virus NS4B Protein Can trans-Complement Viral RNA Replication and Modulates Production of Infectious Virus

P304

12529-12537

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scholarly article

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10.1128/JVI.01798-10

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24

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P478

84

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Darius Moradpour

Jérôme Gouttenoire

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2010-10-06T00:00:00Z

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20926561

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3004355

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