Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation - Wikidata - awgldk - TriplyDB

Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation

Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation

http://www.wikidata.org/entity/Q27675251

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Crystal structure of Zika virus NS2B-NS3 protease in complex with a boronate inhibitor The Potential Use of Natural and Structural Analogues of Antimicrobial Peptides in the Fight against Neglected Tropical Diseases Anti-dengue drug: viral polyprotein, a potential target Structure of the NS2B-NS3 protease from Zika virus after self-cleavage Crystal structure of unlinked NS2B-NS3 protease from Zika virus NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics Identification of novel small molecule inhibitors against NS2B/NS3 serine protease from Zika virus Broad-spectrum agents for flaviviral infections: dengue, Zika and beyond A conformational switch high-throughput screening assay and allosteric inhibition of the flavivirus NS2B-NS3 protease.Transplantation of a hydrogen bonding network from West Nile virus protease onto Dengue-2 protease improves catalytic efficiency and sheds light on substrate specificity.Capturing conformational States in proteins using sparse paramagnetic NMR data.New binding site conformations of the dengue virus NS3 protease accessed by molecular dynamics simulation.Solution conformations of Zika NS2B-NS3pro and its inhibition by natural products from edible plants C-terminal residue optimization and fragment merging: discovery of a potent Peptide-hybrid inhibitor of dengue protease.The flavivirus protease as a target for drug discovery.Novel dengue virus NS2B/NS3 protease inhibitors.Identification of natural antimicrobial agents to treat dengue infection: In vitro analysis of latarcin peptide activity against dengue virus.Policresulen, a novel NS2B/NS3 protease inhibitor, effectively inhibits the replication of DENV2 virus in BHK-21 cells.Identification of covalent active site inhibitors of dengue virus protease.Context-Dependent Cleavage of the Capsid Protein by the West Nile Virus Protease Modulates the Efficiency of Virus Assembly An In-Silico Investigation of Phytochemicals as Antiviral Agents Against Dengue Fever.Inhibitors of Dengue virus and West Nile virus proteases based on the aminobenzamide scaffold Design, synthesis and characterization of novel 1,2-benzisothiazol-3(2H)-one and 1,3,4-oxadiazole hybrid derivatives: potent inhibitors of Dengue and West Nile virus NS2B/NS3 proteases Characterization of 8-hydroxyquinoline derivatives containing aminobenzothiazole as inhibitors of dengue virus type 2 protease in vitro Increasing Clinical Severity during a Dengue Virus Type 3 Cuban Epidemic: Deep Sequencing of Evolving Viral Populations.Product release is rate-limiting for catalytic processing by the Dengue virus protease West Nile virus drug discovery.Existing drugs as broad-spectrum and potent inhibitors for Zika virus by targeting NS2B-NS3 interaction.Structural characterization of the linked NS2B-NS3 protease of Zika virus.Functional interplay among the flavivirus NS3 protease, helicase, and cofactors.A Brief Review of West Nile Virus Biology.Secondary Structure and Membrane Topology of the Full-Length Dengue Virus NS4B in Micelles.Dengue Virus NS2B/NS3 Protease Inhibitors Exploiting the Prime Side.Dengue Protease Substrate Recognition: Binding of the Prime Side.High-throughput screening for the identification of small-molecule inhibitors of the flaviviral protease.Reaction mechanism of the dengue virus serine protease: a QM/MM study.Ethyl 4-(4-methylphenyl)-4-pentenoate from Vetiveria zizanioides Inhibits Dengue NS2B-NS3 Protease and Prevents Viral Assembly: A Computational Molecular Dynamics and Docking Study.Conformational flexibility of DENV NS2B/NS3pro: from the inhibitor effect to the serotype influence.An inhibition model of BPTI to unlinked dengue virus NS2B-NS3 protease.The dengue virus NS2B-NS3 protease retains the closed conformation in the complex with BPTI.

P2860

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P2860

Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation

http://www.wikidata.org/entity/Q27675251

description

2012 nî lūn-bûn

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2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2012 թվականի հունվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation

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Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation

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Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation

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Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation

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Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation

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Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation

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Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation

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P2093

Alexander T Chao

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

Cheah Chen Seh

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Christian G Noble

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Pei Yong Shi

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P2860

Probing the substrate specificity of the dengue virus type 2 NS3 serine protease by using internally quenched fluorescent peptides

Cleavage preference distinguishes the two-component NS2B–NS3 serine proteinases of Dengue and West Nile viruses

Switching the Substrate Specificity of the Two-Component NS2B-NS3 Flavivirus Proteinase by Structure-Based Mutagenesis

Proteolytic activation of tick-borne encephalitis virus by furin

Structural evidence for regulation and specificity of flaviviral proteases and evolution of theFlaviviridaefold

Crystal Structure of the NS3 Protease-Helicase from Dengue Virus

Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins

Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease

NMR Analysis of the Dynamic Exchange of the NS2B Cofactor between Open and Closed Conformations of the West Nile Virus NS2B-NS3 Protease

Crystal Structure of a Novel Conformational State of the Flavivirus NS3 Protein: Implications for Polyprotein Processing and Viral Replication

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438-46

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scholarly article

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518233

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P356

10.1128/JVI.06225-11

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1

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86

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2012-01-01T00:00:00Z

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22031935

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P932

3255909

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