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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.
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.
Cell|February 1, 1985
Fusion mutants of the influenza virus hemagglutinin glycoproteinR S Daniels, J C Downie, A J Hay, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 1, 1984
A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibodyJ J Skehel, D J Stevens, R S Daniels, et al.
The Journal of Biological Chemistry|March 25, 1988
Conformational aspects of the acid-induced fusion mechanism of influenza virus hemagglutinin. Circular dichroism and fluorescence studiesS A Wharton, R W Ruigrok, S R Martin, et al.
Virology|February 28, 1998
Studies of the binding properties of influenza hemagglutinin receptor-site mutantsJ Martín, S A Wharton, Y P Lin, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 12, 1996
Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activityD A Steinhauer, J Martín, Y P Lin, et al.
Acta Crystallographica. Section D, Biological Crystallography|April 27, 1999
X-ray crystallographic determination of the structure of the influenza C virus haemagglutinin-esterase-fusion glycoproteinX Zhang, P B Rosenthal, F Formanowski, et al.
Virology|May 18, 2000
Electron microscopy of the human respiratory syncytial virus fusion protein and complexes that it forms with monoclonal antibodiesL J Calder, L González-Reyes, B García-Barreno, et al.
The EMBO Journal|April 1, 1996
The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptideW Weissenhorn, S A Wharton, L J Calder, et al.
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