P03437Uniprot
Fold
Class
Family
Origin
Species
Available structures
Related proteins
> 50% identity
> 50% identity
PubMed
C. Barbey-Martin, B. Gigant, T. Bizebard, L. J. Calder, S. A. Wharto, J. J. Skehel, M. Knossow
An antibody that prevents the hemagglutinin low pH fusogenic transition. Virology 2002
An antibody that prevents the hemagglutinin low pH fusogenic transition. Virology 2002
PubMed
Fleury D, Daniels R, Skehel J, Knossow M, Bizebard T.
Structural evidence for recognition of a single epitope by two distinct antibodies. Proteins 2000
Structural evidence for recognition of a single epitope by two distinct antibodies. Proteins 2000
PubMed
Fleury, D., Barrere, B., Bizebard, T., Daniels, R.S., Skehel, J.J., Knossow, M.
A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the receptor binding site Nat. Struct. Biol. 1999
A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the receptor binding site Nat. Struct. Biol. 1999
PubMed
Chen J, Lee KH, Steinhauer DA, Stevens DJ, Skehel JJ, Wiley DC
Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation Cell. 1998
Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation Cell. 1998
PubMed
Fleury D, Wharton S, Skehel J, Knossow M, Bizebard T.
Antigen distortion allows influenza virus to escape neutralization. Nature structural biology 1998
Antigen distortion allows influenza virus to escape neutralization. Nature structural biology 1998
PubMed
Bullough, P.A., Hughson, F.M., Skehel, J.J., Wiley, D.C.
Structure of influenza haemagglutinin at the pH of membrane fusion Nature 1994
Structure of influenza haemagglutinin at the pH of membrane fusion Nature 1994
PubMed
Sauter, N.K., Hanson, J.E., Glick, G.D., Brown, J.H., Crowther, R.L., Park, S.J., Skehel, J.J., Wiley, D.C.
Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography Biochemistry 1992
Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography Biochemistry 1992
PubMed
Weis, W.I., Brunger, A.T., Skehel, J.J., Wiley, D.C.
Refinement of the influenza virus hemagglutinin by simulated annealing J. Mol. Biol. 1990
Refinement of the influenza virus hemagglutinin by simulated annealing J. Mol. Biol. 1990
PubMed
Weis, W.I., Brunger, A.T., Skehel, J.J., Wiley, D.C.
Refinement of the influenza virus hemagglutinin by simulated annealing J. Mol. Biol. 1990
Refinement of the influenza virus hemagglutinin by simulated annealing J. Mol. Biol. 1990
PubMed
Weis, W.I., Brunger, A.T., Skehel, J.J., Wiley, D.C.
Refinement of the influenza virus hemagglutinin by simulated annealing J. Mol. Biol. 1990
Refinement of the influenza virus hemagglutinin by simulated annealing J. Mol. Biol. 1990
PubMed
Weis, W.I., Brunger, A.T., Skehel, J.J., Wiley, D.C.
Refinement of the influenza virus hemagglutinin by simulated annealing J. Mol. Biol. 1990
Refinement of the influenza virus hemagglutinin by simulated annealing J. Mol. Biol. 1990
PubMed
Yasutake, Y., Suzuki, T., Kawaguchi, A., Nobusawa, E.
Crystal structure of a influenza A virus (A/Aichi/2/1968 H3N2) hemagglutinin in C2 space group 0
Crystal structure of a influenza A virus (A/Aichi/2/1968 H3N2) hemagglutinin in C2 space group 0
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