Influenza haemagglutinin: illuminating fusion
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference24 articles.
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2. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid;Weiss;Nature,1988
3. The structure of the influenza haemagglutinin at the pH of membrane fusion;Bullough;Nature,1994
4. Monoclonal antibodies localize events in the folding, assembly, and intracellular transport of the influenza virus hemagglutinin glycoprotein;Yewdell;Cell,1988
5. Folding, trimerization and transport are sequential events in the biogenesis of influenza virus hemagglutinin;Copeland;Cell,1988
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1. The Tailless Icosahedral Membrane Virus PRD1 Localizes the Proteins Involved in Genome Packaging and Injection at a Unique Vertex;Journal of Virology;2003-07-15
2. Formation and Characterization of the Trimeric Form of the Fusion Protein of Semliki Forest Virus;Journal of Virology;2000-09
3. Cryo-Electron Microscopy Reveals the Functional Organization of an Enveloped Virus, Semliki Forest Virus;Molecular Cell;2000-02
4. The first step: activation of the semliki forest virus spike protein precursor causes a localized conformational change in the trimeric spike;Journal of Molecular Biology;1998-10
5. Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy.;The EMBO Journal;1995-11
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