Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus. - Wikidata - awgldk - TriplyDB

Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus.

Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus.

http://www.wikidata.org/entity/Q40484115

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Molecular targets for flavivirus drug discovery The role of viral persistence in flavivirus biology Structure and functionality in flavivirus NS-proteins: perspectives for drug design Structural proteomics of dengue virus Crystal structure of Zika virus NS2B-NS3 protease in complex with a boronate inhibitor Mechanisms of activation and inhibition of Zika virus NS2B-NS3 protease Anti-dengue drug: viral polyprotein, a potential target Cleavage preference distinguishes the two-component NS2B–NS3 serine proteinases of Dengue and West Nile viruses Expression and purification of a two-component flaviviral proteinase resistant to autocleavage at the NS2B–NS3 junction region Switching the Substrate Specificity of the Two-Component NS2B-NS3 Flavivirus Proteinase by Structure-Based Mutagenesis Crystal Structure of the Dengue Virus RNA-Dependent RNA Polymerase Catalytic Domain at 1.85-Angstrom Resolution The C Terminus of Hepatitis C Virus NS4A Encodes an Electrostatic Switch That Regulates NS5A Hyperphosphorylation and Viral Replication Structural evidence for regulation and specificity of flaviviral proteases and evolution of theFlaviviridaefold Crystal Structure of the NS3 Protease-Helicase from Dengue Virus Functional Analysis of Potential Carboxy-Terminal Cleavage Sites of Tick-Borne Encephalitis Virus Capsid Protein Yellow Fever Virus NS3 Plays an Essential Role in Virus Assembly Independent of Its Known Enzymatic Functions The Two-component NS2B-NS3 Proteinase Represses DNA Unwinding Activity of the West Nile Virus NS3 Helicase Identification and Biochemical Characterization of Small-Molecule Inhibitors of West Nile Virus Serine Protease by a High-Throughput Screen Mechanism of NS2B-Mediated Activation of NS3pro in Dengue Virus: Molecular Dynamics Simulations and Bioassays Discovery of a Non-Peptidic Inhibitor of West Nile Virus NS3 Protease by High-Throughput Docking Conservation and Variability of West Nile Virus Proteins Structure-based discovery of dengue virus protease inhibitors Activation of the West Nile virus NS3 protease: Molecular dynamics evidence for a conformational selection mechanism 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 Focus on flaviviruses: current and future drug targets Serotype-Specific Structural Differences in the Protease-Cofactor Complexes of the Dengue Virus Family Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications Ligand-Bound Structures of the Dengue Virus Protease Reveal the Active Conformation Allosteric Inhibition of the NS2B-NS3 Protease from Dengue Virus Development and characterization of new peptidomimetic inhibitors of the West Nile virus NS2B-NS3 protease Structure of the NS2B-NS3 protease from Zika virus after self-cleavage Intrinsically Disordered Side of the Zika Virus Proteome Crystal structure of unlinked NS2B-NS3 protease from Zika virus Enzymatic analysis of recombinant Japanese encephalitis virus NS2B(H)-NS3pro protease with fluorogenic model peptide substrates 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 A brief review on dengue molecular virology, diagnosis, treatment and prevalence in Pakistan 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.

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Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus.

http://www.wikidata.org/entity/Q40484115

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Structural basis for the activ ...... om dengue and West Nile virus.

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Nature Structural & Molecular Biology

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Structural basis for the activ ...... rom dengue and West Nile virus

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Allan D'Arcy

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Markus Kroemer

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Martin Renatus

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Nikolaus Schiering

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Paul Erbel

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Subhash G Vasudevan

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Ulrich Hommel

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Zheng Yin

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P2860

Flavivirus genome organization, expression, and replication

The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site

Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide

An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virus

Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro.

Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors.

Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects.

Peptide inhibitors of dengue virus NS3 protease. Part 2: SAR study of tetrapeptide aldehyde inhibitors.

Site-directed mutagenesis and kinetic studies of the West Nile Virus NS3 protease identify key enzyme-substrate interactions.

Enzymatic characterization and homology model of a catalytically active recombinant West Nile virus NS3 protease.

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372-373

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10.1038/NSMB1073

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4

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13

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Thomas H. Keller

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2006-03-12T00:00:00Z

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7246513

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16532006

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West Nile virus