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Kinetic, thermodynamic and structural analysis of tamiphosphor binding to neuraminidase of H1N1 (2009) pandemic influenza.

Eur J Med Chem. 2016; 
AlbiñanaCarlos Berenguer,MacharaAleš,ŘezáčováPavlína,PachlPetr,KonvalinkaJan,KožíšekM
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Recombinant Antibody Services Cloning, expression and purification of recombinant NA2009wt DNA encoding the ectodomain of neuraminidase (residues 82 to 469) from the A/California/07/2009 (H1N1) influenza virus was prepared by GenScript USA Inc. Get A Quote

摘要

Influenza virus causes severe respiratory infections that are responsible for up to half a million deaths worldwide each year. Two inhibitors targeting viral neuraminidase have been approved to date (oseltamivir, zanamivir). However, the rapid development of antiviral drug resistance and the efficient transmission of resistant viruses among humans represent serious threats to public health. The approved influenza neuraminidase inhibitors have (oxa)cyclohexene scaffolds designed to mimic the oxonium transition state during enzymatic cleavage of sialic acid. Their active forms contain a carboxylate that interacts with three arginine residues in the enzyme active site. Recently, the phosphonate group was suc... More

关键词

Crystal structure,Influenza neuraminidase,Isothermal titration calorimetry,Lattice-translocation defect,Oseltamivir,Tamiphos