D A Steinhauer

Summary

Affiliation: National Institute for Medical Research
Country: UK

Publications

  1. ncbi request reprint Role of hemagglutinin cleavage for the pathogenicity of influenza virus
    D A Steinhauer
    National Institute for Medical Research, The Ridgeway, London, Mill Hill, NW7 1AA, United Kingdom
    Virology 258:1-20. 1999
  2. pmc Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
    S A Wharton
    Division of Virology, MRC National Institute for Medical Research, Mill Hill, London, UK
    EMBO J 14:240-6. 1995
  3. pmc Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics
    K J Cross
    National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
    EMBO J 20:4432-42. 2001
  4. ncbi request reprint The structure and receptor binding properties of the 1918 influenza hemagglutinin
    S J Gamblin
    Medical Research Council MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
    Science 303:1838-42. 2004

Collaborators

Detail Information

Publications4

  1. ncbi request reprint Role of hemagglutinin cleavage for the pathogenicity of influenza virus
    D A Steinhauer
    National Institute for Medical Research, The Ridgeway, London, Mill Hill, NW7 1AA, United Kingdom
    Virology 258:1-20. 1999
    ..Here influenza virus pathogenicity is discussed, with an emphasis on the role of HA0 cleavage as a determining factor...
  2. pmc Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
    S A Wharton
    Division of Virology, MRC National Institute for Medical Research, Mill Hill, London, UK
    EMBO J 14:240-6. 1995
    ....
  3. pmc Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics
    K J Cross
    National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
    EMBO J 20:4432-42. 2001
    ..Viruses were also obtained with serine, leucine or phenylalanine as the N-terminal residue, but these replicated to significantly lower levels than wild-type virus with glycine at this position...
  4. ncbi request reprint The structure and receptor binding properties of the 1918 influenza hemagglutinin
    S J Gamblin
    Medical Research Council MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
    Science 303:1838-42. 2004
    ..They explain how the 1918 HA, while retaining receptor binding site amino acids characteristic of an avian precursor HA, is able to bind human receptors and how, as a consequence, the virus was able to spread in the human population...