A fusing mumps virus variant selected from a nonfusing parent with the neuraminidase inhibitor 2-deoxy-2,3-dehydro-N-acetylneuraminic acid.

[1]  G. Air,et al.  Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase. , 1985, Virology.

[2]  M. Waxham,et al.  Purification and amino-terminal protein sequence analysis of the mumps virus fusion protein. , 1985, Virology.

[3]  M. Waxham,et al.  Detailed immunologic analysis of the structural polypeptides of rubella virus using monoclonal antibodies. , 1985, Virology.

[4]  M. Waxham,et al.  Protective effects of glycoprotein-specific monoclonal antibodies on the course of experimental mumps virus meningoencephalitis , 1985, Journal of virology.

[5]  P. Rollin,et al.  Rabies virulence: effect on pathogenicity and sequence characterization of rabies virus mutations affecting antigenic site III of the glycoprotein , 1985, Journal of virology.

[6]  C. Orvell.  The reactions of monoclonal antibodies with structural proteins of mumps virus. , 1984, Journal of immunology.

[7]  J. Wolinsky,et al.  Conversion of nonfusing mumps virus infections to fusing infections by selective proteolysis of the HN glycoprotein. , 1983, Virology.

[8]  T. Kanda,et al.  Neuraminidase activity and syncytial formation in variants of parainfluenza 3 virus , 1983, Infection and immunity.

[9]  M. Waxham,et al.  Biosynthesis of mumps virus F glycoprotein: non-fusing strains efficiently cleave the F glycoprotein precursor. , 1983, The Journal of general virology.

[10]  I. Wilson,et al.  Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity , 1983, Nature.

[11]  D. Spriggs,et al.  Attenuated reovirus type 3 strains generated by selection of haemagglutinin antigenic variants , 1982, Nature.

[12]  M. Waxham,et al.  Differentiation of mumps virus strains with monoclonal antibody to the HN glycoprotein , 1982, Infection and immunity.

[13]  J. Wolinsky,et al.  Biochemical features of mumps virus neuraminidases and their relationship with pathogenicity. , 1981, Virology.

[14]  I. Wilson,et al.  Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution , 1981, Nature.

[15]  S. Schlesinger,et al.  A role for oligosaccharides in glycoprotein biosynthesis , 1980 .

[16]  W. J. Bean,et al.  Similar frequencies of antigenic variants in Sendai, vesicular stomatitis, and influenza A viruses. , 1980, Virology.

[17]  B. Jubelt,et al.  Comparative studies of five strains of mumps virus in vitro and in neonatal hamsters: evaluation of growth, cytopathogenicity, and neurovirulence , 1980, Journal of medical virology.

[18]  G. Thomas,et al.  The synthesis of 4-methylumbelliferyl alpha-ketoside of N-acetylneuraminic acid and its use in a fluorometric assay for neuraminidase. , 1980, Analytical biochemistry.

[19]  G. Air,et al.  Antigenic drift in type A influenza virus: sequence differences in the hemagglutinin of Hong Kong (H3N2) variants selected with monoclonal hybridoma antibodies. , 1979, Virology.

[20]  A. Scheid,et al.  Protease activation mutants of sendai virus. Activation of biological properties by specific proteases. , 1976, Virology.

[21]  P. Palese,et al.  Inhibition of influenza and parainfluenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA). , 1974, Virology.

[22]  P. Palese,et al.  Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid. , 1974, Virology.

[23]  L. Weiss.  STUDIES ON CELL DEFORMABILITY : I. Effect of Surface Charge. , 1965 .