The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form the RNA cap structure - Test2 - elhamkhani - TriplyDB

The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form the RNA cap structure

The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form the RNA cap structure

http://www.wikidata.org/entity/Q27490412

about

Analysis of RNA binding by the dengue virus NS5 RNA capping enzyme Identification of a novel antiviral inhibitor of the flavivirus guanylyltransferase enzyme Structural and Functional Analyses of a Conserved Hydrophobic Pocket of Flavivirus Methyltransferase Innate immunity evasion by Dengue virus Potent Allosteric Dengue Virus NS5 Polymerase Inhibitors: Mechanism of Action and Resistance Profiling Functions of the 3' and 5' genome RNA regions of members of the genus Flavivirus Flaviviral Replication Complex: Coordination between RNA Synthesis and 5'-RNA Capping The RNA capping machinery as an anti-infective target Common and unique features of viral RNA-dependent polymerases Japanese encephalitis: the virus and vaccines STAT2 signaling and dengue virus infection Viral RNA switch mediates the dynamic control of flavivirus replicase recruitment by genome cyclization Live Cell Analysis and Mathematical Modeling Identify Determinants of Attenuation of Dengue Virus 2'-O-Methylation Mutant A crystal structure of the Dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replication The C-terminal 18 Amino Acid Region of Dengue Virus NS5 Regulates its Subcellular Localization and Contains a Conserved Arginine Residue Essential for Infectious Virus Production Crystal Structure of the Dengue Virus Methyltransferase Bound to a 5′-Capped Octameric RNA Membrane Topology and Function of Dengue Virus NS2A Protein Crystal Structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface The FDA-approved drug sofosbuvir inhibits Zika virus infection Looking for inhibitors of the dengue virus NS5 RNA-dependent RNA-polymerase using a molecular docking approach Virtual high-throughput screening identifies mycophenolic acid as a novel RNA capping inhibitor The interface between methyltransferase and polymerase of NS5 is essential for flavivirus replication Murine Efficacy and Pharmacokinetic Evaluation of the Flaviviral NS5 Capping Enzyme 2-Thioxothiazolidin-4-One Inhibitor BG-323 Perturbation in the conserved methyltransferase-polymerase interface of flavivirus NS5 differentially affects polymerase initiation and elongation Novel cis-acting element within the capsid-coding region enhances flavivirus viral-RNA replication by regulating genome cyclization Structure and function of the Zika virus full-length NS5 protein Broad-spectrum agents for flaviviral infections: dengue, Zika and beyond Dengue Virus Non-Structural Protein 5 Flaviviruses, an expanding threat in public health: focus on dengue, West Nile, and Japanese encephalitis virus.Antiviral and neuroprotective role of octaguanidinium dendrimer-conjugated morpholino oligomers in Japanese encephalitis.Substitution of NS5 N-terminal domain of dengue virus type 2 RNA with type 4 domain caused impaired replication and emergence of adaptive mutants with enhanced fitness.Yellow fever: a reemerging threat Novel approaches to flavivirus drug discovery.The interferon signaling antagonist function of yellow fever virus NS5 protein is activated by type I interferon Molecular basis for nucleotide conservation at the ends of the dengue virus genome.Flaviviral RNAs: weapons and targets in the war between virus and host.Dengue virus co-opts UBR4 to degrade STAT2 and antagonize type I interferon signaling The flavivirus protease as a target for drug discovery.Two distinct sets of NS2A molecules are responsible for dengue virus RNA synthesis and virion assembly Oxidative stress influences positive strand RNA virus genome synthesis and capping.

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P2860

The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form the RNA cap structure

http://www.wikidata.org/entity/Q27490412

description

2009 nî lūn-bûn

@nan

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

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2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

The flavivirus NS5 protein is ...... to form the RNA cap structure

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The flavivirus NS5 protein is ...... to form the RNA cap structure

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The flavivirus NS5 protein is ...... to form the RNA cap structure

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The flavivirus NS5 protein is ...... to form the RNA cap structure

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The flavivirus NS5 protein is ...... to form the RNA cap structure

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The flavivirus NS5 protein is ...... to form the RNA cap structure

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Frédéric Picard-Jean

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Isabelle Bougie

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Joannie Mayette

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Martin Bisaillon

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Moheshwarnath Issur

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Sarah E Hobdey

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Simon Despins

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P2860

A recombinant hepatitis C virus RNA-dependent RNA polymerase capable of copying the full-length viral RNA.

An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization

Structure and Function of Flavivirus NS5 Methyltransferase

Crystal Structure of the Dengue Virus RNA-Dependent RNA Polymerase Catalytic Domain at 1.85-Angstrom Resolution

Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus

Analysis of Flavivirus NS5 Methyltransferase Cap Binding

Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site

Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus.

Crystal structure of NAD+-dependent DNA ligase: modular architecture and functional implications

Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining

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2340-50

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3038616

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P356

10.1261/RNA.1609709

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12

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15

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38030481

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19850911

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protein structure

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2779676

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