articleTop 1% cited

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

Nature Structural & Molecular Biology · 2006 · Vol. 13(4) · pp. 372–373

P. Erbel✉Nikolaus Schiering(Novartis Institutes for BioMedical Research)A. D’Arcy(Novartis Institutes for BioMedical Research)Martin Renatus(Novartis (Switzerland))M. Kroemer(Novartis (Switzerland))Siew Pheng Lim(Novartis (Singapore))Zheng Yin(Novartis (Singapore))Thomas H. Keller(Novartis (Singapore))Subhash G. Vasudevan(Novartis (Singapore))Ulrich Hommel(Novartis Institutes for BioMedical Research)

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Mosquito-borne diseases and control Malaria Research and Control Viral Infections and VectorsNS3Dengue virusDengue feverProteaseWest Nile virusVirologyProteasesFlavivirusVirusChemistry

MeSH terms

Viral ProteasesBinding SitesDengue VirusEnzyme ActivationHydrogen BondingModels, MolecularOligopeptidesProtease InhibitorsSerine EndopeptidasesWest Nile virusViral Nonstructural ProteinsRNA HelicasesNucleoside-TriphosphataseMacromolecular SubstancesDEAD-box RNA Helicases

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