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References from A Potent Anti-influenza Compound Blocks Fusion through Stabilization of the Prefusion Conformation of the Hemagglutinin Protein. Local targets link to admitted publications; unresolved targets remain external evidence.
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External reference
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Structural characterization of an early fusion intermediate of influenza virus hemagglutinin
10.1128/jvi.02430-10 · 2011 · External reference
Specific single or double proline substitutions in the “spring-loaded” coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity
10.1083/jcb.141.6.1335 · 1998 · External reference
Biosensor-based small molecule fragment screening with biolayer interferometry
10.1007/s10822-011-9439-8 · 2011 · External reference
Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein
10.1128/jvi.02238-08 · 2009 · External reference
Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity
10.1016/0092-8674(92)90140-8 · 1992 · External reference
Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin
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A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains
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A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins
10.1126/science.1205669 · 2011 · External reference
Structural and genetic basis for development of broadly neutralizing influenza antibodies
10.1038/nature11371 · 2012 · External reference
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Antibody recognition of a highly conserved influenza virus epitope
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Universal influenza virus vaccines: need for clinical trials
10.1038/ni.2761 · 2014 · External reference
Influenza virus hemagglutinin stalk-based antibodies and vaccines
10.1016/j.coviro.2013.07.007 · 2013 · External reference
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2013 · External reference
Antiviral treatment of hepatitis C
10.1136/bmj.g3308 · 2014 · External reference
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Characterization of ligand binding by saturation transfer difference NMR spectroscopy
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Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
10.1021/ja0100120 · 2001 · External reference
