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Nature|November 26, 1992
Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middleH C Guo, T S Jardetzky, T P Garrett, et al.The EMBO Journal|January 16, 1995
Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformationS A Wharton, L J Calder, R W Ruigrok, et al.Virology|December 1, 1986
Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomesR W Ruigrok, S R Martin, S A Wharton, et al.Journal of Molecular Biology|March 4, 1994
Crystals of a fragment of influenza haemagglutinin in the low pH induced conformationP A Bullough, F M Hughson, A C Treharne, et al.Nature|July 7, 1983
Single amino acid substitutions in influenza haemagglutinin change receptor binding specificityG N Rogers, J C Paulson, R S Daniels, et al.Acta Crystallographica. Section D, Biological Crystallography|November 1, 1995
Human class II MHC molecule HLA-DR1: X-ray structure determined from three crystal formsJ H Brown, T S Jardetzky, L J Stern, et al.The EMBO Journal|January 1, 1990
The structure of a membrane fusion mutant of the influenza virus haemagglutininW I Weis, S C Cusack, J H Brown, et al.Proceedings of the National Academy of Sciences of the United States of America|December 19, 1995
A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformationJ Chen, S A Wharton, W Weissenhorn, et al.Molecular Cell|August 21, 2001
Herpes simplex virus glycoprotein D bound to the human receptor HveAA Carfí, S H Willis, J C Whitbeck, et al.Acta Crystallographica. Section D, Biological Crystallography|September 1, 1996
Crystallization and preliminary X-ray diffraction studies of the influenza C virus glycoproteinP B Rosenthal, F Formanowski, A C Treharne, et al.Pageof 18