Home
About
Overview
Sharing Data
ORCID
Help
History (1)
Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site.
See All Pages
Find People
Find Everything
Login
to edit your profile (add a photo, awards, links to other websites, etc.)
Edit My Profile
My Person List (
0
)
Return to Top
Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site.
Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site. J Mol Biol. 1999 Nov 12; 293(5):1107-19.
View in:
PubMed
subject areas
Benzoic Acid
Benzoic Acid
Binding Sites
Binding Sites
Conserved Sequence
Conserved Sequence
Crystallization
Crystallization
Crystallography, X-Ray
Crystallography, X-Ray
Drug Design
Drug Design
Electrons
Electrons
Enzyme Inhibitors
Enzyme Inhibitors
Hydrogen Bonding
Hydrogen Bonding
Influenza A virus
Influenza A virus
Influenza B virus
Influenza B virus
Inhibitory Concentration 50
Inhibitory Concentration 50
Models, Molecular
Models, Molecular
Molecular Conformation
Molecular Conformation
Molecular Sequence Data
Molecular Sequence Data
N-Acetylneuraminic Acid
N-Acetylneuraminic Acid
Neuraminidase
Neuraminidase
Structure-Activity Relationship
Structure-Activity Relationship
Water
Water