Analysis of the nucleoside triphosphatase, RNA triphosphatase, and unwinding activities of the helicase domain of dengue virus NS3 protein. - Wikidata - awgldk - TriplyDB

Analysis of the nucleoside triphosphatase, RNA triphosphatase, and unwinding activities of the helicase domain of dengue virus NS3 protein.

Analysis of the nucleoside triphosphatase, RNA triphosphatase, and unwinding activities of the helicase domain of dengue virus NS3 protein.

http://www.wikidata.org/entity/Q40398956

about

Expression of dengue virus NS3 protein in Drosophila alters its susceptibility to infection Flaviviral Replication Complex: Coordination between RNA Synthesis and 5'-RNA Capping Flavivirus NS3 and NS5 proteins interaction network: a high-throughput yeast two-hybrid screen Steady-state NTPase activity of Dengue virus NS3: number of catalytic sites, nucleotide specificity and activation by ssRNA.X-ray structure of the pestivirus NS3 helicase and its conformation in solution.Novel ATP-independent RNA annealing activity of the dengue virus NS3 helicase Monomeric nature of dengue virus NS3 helicase and thermodynamic analysis of the interaction with single-stranded RNA.A novel dengue virus inhibitor, BP13944, discovered by high-throughput screening with dengue virus replicon cells selects for resistance in the viral NS2B/NS3 protease Models of the impact of dengue vaccines: a review of current research and potential approaches Superfamily 2 helicases Melting of Duplex DNA in the Absence of ATP by the NS3 Helicase Domain through Specific Interaction with a Single-Strand/Double-Strand Junction Identification and biochemical characterization of halisulfate 3 and suvanine as novel inhibitors of hepatitis C virus NS3 helicase from a marine sponge.Replication cycle and molecular biology of the West Nile virus.Organization of the Flavivirus RNA replicase complex.Uncoupling of Protease trans-Cleavage and Helicase Activities in Pestivirus NS3.Single point mutations in the helicase domain of the NS3 protein enhance dengue virus replicative capacity in human monocyte-derived dendritic cells and circumvent the type I interferon response.RNA binding property and RNA chaperone activity of dengue virus core protein and other viral RNA-interacting proteins.NS2B/NS3 protease: allosteric effect of mutations associated with the pathogenicity of tick-borne encephalitis virus.The role of surface basic amino acids of dengue virus NS3 helicase in viral RNA replication and enzyme activities.HCV NS3 protein helicase domain assists RNA structure conversion.Targeting Dengue Virus NS-3 Helicase by Ligand based Pharmacophore Modeling and Structure based Virtual Screening.Allostery in the dengue virus NS3 helicase: Insights into the NTPase cycle from molecular simulations.Interferon-stimulated TRIM69 interrupts dengue virus replication by ubiquitinating viral nonstructural protein 3

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P2860

Analysis of the nucleoside triphosphatase, RNA triphosphatase, and unwinding activities of the helicase domain of dengue virus NS3 protein.

http://www.wikidata.org/entity/Q40398956

description

2009 nî lūn-bûn

@nan

2009年の論文

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2009年論文

@yue

2009年論文

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2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

2009年论文

@zh

2009年论文

@zh-cn

name

Analysis of the nucleoside tri ...... n of dengue virus NS3 protein.

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type

label

Analysis of the nucleoside tri ...... n of dengue virus NS3 protein.

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prefLabel

Analysis of the nucleoside tri ...... n of dengue virus NS3 protein.

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P356

J.FEBSLET.2009.01.008

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P1476

Analysis of the nucleoside tri ...... n of dengue virus NS3 protein.

@en

P2093

Chien-Tsun Chen

http://www.w3.org/2001/XMLSchema#string

Chun-Chung Wang

http://www.w3.org/2001/XMLSchema#string

Huey-Nan Wu

http://www.w3.org/2001/XMLSchema#string

Pei-Ling Chiang

http://www.w3.org/2001/XMLSchema#string

Zhi-Shun Huang

http://www.w3.org/2001/XMLSchema#string

P2860

Mfold web server for nucleic acid folding and hybridization prediction

Mutagenesis of the Dengue virus type 2 NS3 protein within and outside helicase motifs: effects on enzyme activity and virus replication.

Structure of the Dengue Virus Helicase/Nucleoside Triphosphatase Catalytic Domain at a Resolution of 2.4 A

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

The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding.

Structure-Based Mutational Analysis of the NS3 Helicase from Dengue Virus

Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein

Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding

ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1.

DExD/H box RNA helicases: from generic motors to specific dissociation functions

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691-696

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10.1016/J.FEBSLET.2009.01.008

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