<p>In panel A, hydrogen bond contacts are presented (dotted lines), which are formed between zanamivir and active site residues in the I223R mutant (purple, PDB ID code 4B7N). The insert displays the interactions between the same residues in the I223R mutant ligand-free structure (blue, PDB ID code 4B7M). In panel B, active site residues and hydrogen bonds are displayed, which are formed in the wild type zanamivir structure complex (brown, PDB ID code 4B7Q). The insert displays the I223, S247 and E277 residues in the wild type ligand-free structure.</p
In the context of the recent pandemic threat by the worldwide spread of H5N1 avian influenza, novel ...
textabstractTwo classes of antiviral drugs, neuraminidase inhibitors and adamantanes, are approved f...
The first paper in this series (see previous article) described structure-activity studies of carbox...
<p>In panel A, an overlay of three pandemic neuraminidase structures is presented: I223R mutant liga...
<p>ZMR is shown as ribbon with purple color, and active site residues are colored in brown. Carbon, ...
<p>Salt-bridges and hydrogen bonds are depicted as magenta and orange dashed lines, respectively. Po...
<p>Distribution of the average distance between the atoms O<sub>ε</sub> of E276 and E277 with O<sub>...
Homology modeling and docking methods were used to explore the effects of different mutants on antiv...
<p>(<b>A</b>) Displaying active site of the <i>Pv</i>PM-V Sal-1 (wild type) and its interaction with...
<p>In each panel, zanamivir appears as the same color as the respective NA active site and laninamiv...
<p>(A) Docking conformation of RB19 on WT NA with hydrogen-bonding interactions represented as light...
It is critical to understand the molecular basis of the drug resistance of influenza viruses to effi...
It is critical to understand the molecular basis of the drug resistance of influenza viruses to effi...
<p>Panel A presents the active site of a 2009 pandemic neuraminidase (PDB ID code 4B7M) in an open c...
Left column: visualization of the NS3-4A protease structure and surface of the binding pocket of wi...
In the context of the recent pandemic threat by the worldwide spread of H5N1 avian influenza, novel ...
textabstractTwo classes of antiviral drugs, neuraminidase inhibitors and adamantanes, are approved f...
The first paper in this series (see previous article) described structure-activity studies of carbox...
<p>In panel A, an overlay of three pandemic neuraminidase structures is presented: I223R mutant liga...
<p>ZMR is shown as ribbon with purple color, and active site residues are colored in brown. Carbon, ...
<p>Salt-bridges and hydrogen bonds are depicted as magenta and orange dashed lines, respectively. Po...
<p>Distribution of the average distance between the atoms O<sub>ε</sub> of E276 and E277 with O<sub>...
Homology modeling and docking methods were used to explore the effects of different mutants on antiv...
<p>(<b>A</b>) Displaying active site of the <i>Pv</i>PM-V Sal-1 (wild type) and its interaction with...
<p>In each panel, zanamivir appears as the same color as the respective NA active site and laninamiv...
<p>(A) Docking conformation of RB19 on WT NA with hydrogen-bonding interactions represented as light...
It is critical to understand the molecular basis of the drug resistance of influenza viruses to effi...
It is critical to understand the molecular basis of the drug resistance of influenza viruses to effi...
<p>Panel A presents the active site of a 2009 pandemic neuraminidase (PDB ID code 4B7M) in an open c...
Left column: visualization of the NS3-4A protease structure and surface of the binding pocket of wi...
In the context of the recent pandemic threat by the worldwide spread of H5N1 avian influenza, novel ...
textabstractTwo classes of antiviral drugs, neuraminidase inhibitors and adamantanes, are approved f...
The first paper in this series (see previous article) described structure-activity studies of carbox...