West Nile Virus Methyltransferase Catalyzes Two Methylations of the Viral RNA Cap through a Substrate-Repositioning Mechanism - Test2 - elhamkhani - TriplyDB

West Nile Virus Methyltransferase Catalyzes Two Methylations of the Viral RNA Cap through a Substrate-Repositioning Mechanism

West Nile Virus Methyltransferase Catalyzes Two Methylations of the Viral RNA Cap through a Substrate-Repositioning Mechanism

http://www.wikidata.org/entity/Q27485750

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Analysis of RNA binding by the dengue virus NS5 RNA capping enzyme Structure and functionality in flavivirus NS-proteins: perspectives for drug design Structural and Functional Analyses of a Conserved Hydrophobic Pocket of Flavivirus Methyltransferase Potent Allosteric Dengue Virus NS5 Polymerase Inhibitors: Mechanism of Action and Resistance Profiling Identification and Characterization of Novel Broad-Spectrum Inhibitors of the Flavivirus Methyltransferase Flaviviral Replication Complex: Coordination between RNA Synthesis and 5'-RNA Capping A crystal structure of the Dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replication mRNA capping: biological functions and applications Genetic Interactions among the West Nile Virus Methyltransferase, the RNA-Dependent RNA Polymerase, and the 5' Stem-Loop of Genomic RNA Separate molecules of West Nile virus methyltransferase can independently catalyze the N7 and 2′-O methylations of viral RNA cap Phosphorylation of yellow fever virus NS5 alters methyltransferase activity Analysis of a structural homology model of the 2'-O-ribose methyltransferase domain within the vesicular stomatitis virus L protein.The flaviviral methyltransferase is a substrate of Casein Kinase 1 Focus on flaviviruses: current and future drug targets Crystal Structure of the Dengue Virus Methyltransferase Bound to a 5′-Capped Octameric RNA 2'-O methylation of internal adenosine by flavivirus NS5 methyltransferase Secondary metabolism and development is mediated by LlmF control of VeA subcellular localization in Aspergillus nidulans Murine Efficacy and Pharmacokinetic Evaluation of the Flaviviral NS5 Capping Enzyme 2-Thioxothiazolidin-4-One Inhibitor BG-323 Novel Broad Spectrum Inhibitors Targeting the Flavivirus Methyltransferase Broad-spectrum agents for flaviviral infections: dengue, Zika and beyond Dengue Virus Non-Structural Protein 5 A fluorescence-based alkaline phosphatase-coupled polymerase assay for identification of inhibitors of dengue virus RNA-dependent RNA polymerase.Small molecule drug discovery for Dengue and West Nile viruses: applying experience from hepatitis C virus.Trimethylguanosine capping selectively promotes expression of Rev-dependent HIV-1 RNAs.Rational design of human metapneumovirus live attenuated vaccine candidates by inhibiting viral mRNA cap methyltransferase Capturing the essence of organic synthesis: from bioactive natural products to designed molecules in today's medicine.Construction of a dengue virus type 4 reporter replicon and analysis of temperature-sensitive mutations in non-structural proteins 3 and 5.Functional analysis of two cavities in flavivirus NS5 polymerase S-adenosyl-homocysteine is a weakly bound inhibitor for a flaviviral methyltransferase Flavivirus RNA cap methyltransferase: structure, function, and inhibition.Flexibility of NS5 Methyltransferase-Polymerase Linker Region Is Essential for Dengue Virus Replication.Molecular basis for specific viral RNA recognition and 2'-O-ribose methylation by the dengue virus nonstructural protein 5 (NS5)A high-throughput screening assay for the identification of flavivirus NS5 capping enzyme GTP-binding inhibitors: implications for antiviral drug development.Selective inhibition of the West Nile virus methyltransferase by nucleoside analogs.Flavivirus methyltransferase: a novel antiviral target The essential, nonredundant roles of RIG-I and MDA5 in detecting and controlling West Nile virus infection.mRNA cap methylation influences pathogenesis of vesicular stomatitis virus in vivo.A Brief Review of West Nile Virus Biology.Refolding of a fully functional flavivirus methyltransferase revealed that S-adenosyl methionine but not S-adenosyl homocysteine is copurified with flavivirus methyltransferase.Molecular evolution of lineage 2 West Nile virus.

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P2860

West Nile Virus Methyltransferase Catalyzes Two Methylations of the Viral RNA Cap through a Substrate-Repositioning Mechanism

http://www.wikidata.org/entity/Q27485750

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2008 nî lūn-bûn

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2008 թվականի մայիսին հրատարակված գիտական հոդված

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2008年の論文

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2008年学术文章

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West Nile Virus Methyltransfer ...... strate-Repositioning Mechanism

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West Nile Virus Methyltransfer ...... strate-Repositioning Mechanism

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West Nile Virus Methyltransfer ...... strate-Repositioning Mechanism

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West Nile Virus Methyltransfer ...... strate-Repositioning Mechanism

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Journal of Virology

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West Nile Virus Methyltransfer ...... strate-Repositioning Mechanism

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Francesc Puig-Basagoiti

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Hongping Dong

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Suping Ren

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Yangsheng Zhou

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P2860

Flavivirus genome organization, expression, and replication

Inhibition of interferon signaling by dengue virus

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

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

High-throughput assays using a luciferase-expressing replicon, virus-like particles, and full-length virus for West Nile virus drug discovery.

Mutations in the Yellow Fever Virus Nonstructural Protein NS2A Selectively Block Production of Infectious Particles

Infectious cDNA clone of the epidemic west nile virus from New York City

West Nile Virus 5'-Cap Structure Is Formed by Sequential Guanine N-7 and Ribose 2'-O Methylations by Nonstructural Protein 5

Molecular and Functional Analyses of Kunjin Virus Infectious cDNA Clones Demonstrate the Essential Roles for NS2A in Virus Assembly and for a Nonconservative Residue in NS3 in RNA Replication

Structure and Function of Flavivirus NS5 Methyltransferase

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10.1128/JVI.02202-07

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9

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82

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18305027

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West Nile virus

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2293060

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