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Journal of Molecular Biology|May 20, 1991
Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolutionM A Saper, P J Bjorkman, D C WileyVirology|February 1, 1986
Studies of influenza haemagglutinin-mediated membrane fusionS A Wharton, J J Skehel, D C WileyThe Journal of General Virology|March 1, 1985
Amino acid sequences of haemagglutinins of influenza viruses of the H3 subtype isolated from horsesR S Daniels, J J Skehel, D C WileyEuropean Journal of Immunology|September 29, 2000
A disulfide-linked natural killer cell receptor dimer has higher affinity for HLA-C than wild-type monomerQ R Fan, E O Long, D C WileyThe Journal of Biological Chemistry|May 19, 2000
Cobalt-mediated dimerization of the human natural killer cell inhibitory receptorQ R Fan, E O Long, D C WileyVirology|May 18, 2000
Temperature dependence of fusion by sendai virusS A Wharton, J J Skehel, D C WileyCell|November 19, 1993
The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2D R Madden, D N Garboczi, D C WileyNature|January 29, 1981
Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variationD C Wiley, I A Wilson, J J SkehelJournal of Virology|January 1, 1986
Comparative analyses of the specificities of anti-influenza hemagglutinin antibodies in human seraM L Wang, J J Skehel, D C WileyThe Journal of Biological Chemistry|August 29, 1997
Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA. Influence of electrostatic interactions on stability and redox propertiesA Jacobi, M Huber-Wunderlich, J Hennecke, et al.Pageof 18