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Crystal structure of a new benzoic acid inhibitor of influenza neuraminidase bound with a new tilt induced by overpacking subsite C6.
A strategy for theoretical binding constant, Ki, calculations for neuraminidase aromatic inhibitors designed on the basis of the active site structure of influenza virus neuraminidase.
A benzoic acid inhibitor induces a novel conformational change in the active site of Influenza B virus neuraminidase.
Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site.
Site-directed mutation of the active site of influenza neuraminidase and implications for the catalytic mechanism.
STRUCTURE OF ANTIGENIC SITES ON INFLUENZA VIRUS PROTEINS