Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus - Wikidata - wikimedia - TriplyDB

Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

http://www.wikidata.org/entity/Q27488306

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The lipid kinase phosphatidylinositol-4 kinase III alpha regulates the phosphorylation status of hepatitis C virus NS5A Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a "fuzzy complex" with VAPB-MSP domain which carries ALS-causing mutations Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A Virologic Tools for HCV Drug Resistance Testing The yin and yang of hepatitis C: synthesis and decay of hepatitis C virus RNA Architecture and biogenesis of plus-strand RNA virus replication factories Structures of hepatitis C virus nonstructural proteins required for replicase assembly and function Asymmetric binding to NS5A by daclatasvir (BMS-790052) and analogs suggests two novel modes of HCV inhibition.Human Choline Kinase-α Promotes Hepatitis C Virus RNA Replication through Modulation of Membranous Viral Replication Complex Formation Identification of Hepatitis C Virus NS5A Inhibitors Cyclosporine Inhibits a Direct Interaction between Cyclophilins and Hepatitis C NS5A The crystal structure of NS5A domain 1 from genotype 1a reveals new clues to the mechanism of action for dimeric HCV inhibitors Metabolism of phosphatidylinositol 4-kinase IIIα-dependent PI4P Is subverted by HCV and is targeted by a 4-anilino quinazoline with antiviral activity A quantitative high-resolution genetic profile rapidly identifies sequence determinants of hepatitis C viral fitness and drug sensitivity Coordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5A The Disordered Region of the HCV Protein NS5A: Conformational Dynamics, SH3 Binding, and Phosphorylation Hepatitis C virus NS5A protein blocks epidermal growth factor receptor degradation via a proline motif- dependent interaction Applications of computer-aided approaches in the development of hepatitis C antiviral agents.Common molecular mechanism of the hepatic lesion and the cardiac parasympathetic regulation in chronic hepatitis C infection: a critical role for the muscarinic receptor type 3.Hepatitis C virus nonstructural protein 5A: biochemical characterization of a novel structural class of RNA-binding proteins Small molecules targeting hepatitis C virus-encoded NS5A cause subcellular redistribution of their target: insights into compound modes of action.Chemical genetics.Resistance analysis of the hepatitis C virus NS5A inhibitor BMS-790052 in an in vitro replicon system.Expanding the proteome of an RNA virus by phosphorylation of an intrinsically disordered viral protein.All three domains of the hepatitis C virus nonstructural NS5A protein contribute to RNA binding.Discovery of potent hepatitis C virus NS5A inhibitors with dimeric structures.Distinct functions of NS5A in hepatitis C virus RNA replication uncovered by studies with the NS5A inhibitor BMS-790052 Analysis of functional differences between hepatitis C virus NS5A of genotypes 1-7 in infectious cell culture systems.Hepatitis C NS5A protein: two drug targets within the same protein with different mechanisms of resistance.Insights into the complexity and functionality of hepatitis C virus NS5A phosphorylation.Genetic history of hepatitis C virus in Venezuela: high diversity and long time of evolution of HCV genotype 2.Hepatitis C virus NS5A inhibitors and drug resistance mutations.Potent hepatitis C inhibitors bind directly to NS5A and reduce its affinity for RNA.The intraviral protein interaction network of hepatitis C virus.Structural and molecular basis of interaction of HCV non-structural protein 5A with human casein kinase 1α and PKR.Resistance patterns associated with HCV NS5A inhibitors provide limited insight into drug binding.Identification of a novel phosphorylation site in hepatitis C virus NS5A Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.Daclatasvir inhibits hepatitis C virus NS5A motility and hyper-accumulation of phosphoinositides.Regulation of the production of infectious genotype 1a hepatitis C virus by NS5A domain III.

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P2860

Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

http://www.wikidata.org/entity/Q27488306

description

2009 nî lūn-bûn

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2009 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2009 թվականի մայիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

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Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

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Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

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type

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Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

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Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

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Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

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Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

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Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

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Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

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Journal of Virology

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Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus

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P2093

Ciarán N Cronin

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Michael J Hickey

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Oleg Brodsky

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Peter A Wells

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Robert A Love

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P2860

Hepatitis C virus NS5A as a potential viral Bcl-2 homologue interacts with Bax and inhibits apoptosis in hepatocellular carcinoma

Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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

Protein-Protein Interactions between Hepatitis C Virus Nonstructural Proteins

Amphipathic Helix-Dependent Localization of NS5A Mediates Hepatitis C Virus RNA Replication

Binding Dynamics of Hepatitis C Virus' NS5A Amphipathic Peptide to Cell and Model Membranes

The N-terminal region of hepatitis C virus-encoded NS5A is important for NS4A-dependent phosphorylation

Cell Culture Adaptation of Hepatitis C Virus and In Vivo Viability of an Adapted Variant

Identification of Residues Required for RNA Replication in Domains II and III of the Hepatitis C Virus NS5A Protein

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4395-403

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10.1128/JVI.02352-08

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9

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83

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2009-05-01T00:00:00Z

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19244328

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protein structure

crystal structure

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2668466

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