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- W2145469333 endingPage "5580" @default.
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- W2145469333 abstract "The mosquito-borne dengue viruses are widespread human pathogens causing dengue fever, dengue hemorrhagic fever, and dengue shock syndrome, placing 40% of the world's population at risk with no effective treatment. The viral genome is a positive strand RNA that encodes a single polyprotein precursor. Processing of the polyprotein precursor into mature proteins is carried out by the host signal peptidase and by NS3 serine protease, which requires NS2B as a cofactor. We report here the crystal structure of the NS3 serine protease domain at 2.1 A resolution. This structure of the protease combined with modeling of peptide substrates into the active site suggests identities of residues involved in substrate recognition as well as providing a structural basis for several mutational effects on enzyme activity. This structure will be useful for development of specific inhibitors as therapeutics against dengue and other flaviviral proteases." @default.
- W2145469333 created "2016-06-24" @default.
- W2145469333 creator A5001363452 @default.
- W2145469333 creator A5045725292 @default.
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- W2145469333 date "1999-02-01" @default.
- W2145469333 modified "2023-10-04" @default.
- W2145469333 title "Dengue Virus NS3 Serine Protease" @default.
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- W2145469333 doi "https://doi.org/10.1074/jbc.274.9.5573" @default.
- W2145469333 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2797214" @default.
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