Monomeric inhibitors of influenza neuraminidase enhance the hemagglutination inhibition activities of polyacrylamides presenting multiple C-sialoside groups.

[1]  G. Whitesides,et al.  Polyacrylamides Bearing Pendant α-Sialoside Groups Strongly Inhibit Agglutination of Erythrocytes by Influenza Virus: The Strong Inhibition Reflects Enhanced Binding through Cooperative Polyvalent Interactions , 1996 .

[2]  G M Whitesides,et al.  Effective inhibitors of hemagglutination by influenza virus synthesized from polymers having active ester groups. Insight into mechanism of inhibition. , 1995, Journal of medicinal chemistry.

[3]  Pascal Rigolet,et al.  Structure of influenza virus haemagglutinin complexed with a neutralizing antibody , 1995, Nature.

[4]  P. Colman,et al.  Three‐dimensional structure of the complex of 4‐guanidino‐Neu5Ac2en and influenza virus neuraminidase , 1995, Protein science : a publication of the Protein Society.

[5]  P. Colman Influenza virus neuraminidase: Structure, antibodies, and inhibitors , 1994, Protein science : a publication of the Protein Society.

[6]  M G Rossmann,et al.  Viral cell recognition and entry. , 1994, Protein science : a publication of the Protein Society.

[7]  G M Whitesides,et al.  Polyacrylamides bearing pendant alpha-sialoside groups strongly inhibit agglutination of erythrocytes by influenza A virus: multivalency and steric stabilization of particulate biological systems. , 1994, Journal of medicinal chemistry.

[8]  B. Barrère,et al.  Synthesis of transition-state analogues as potential inhibitors of sialidase from Influenza virus. , 1994, Carbohydrate research.

[9]  B. Jin,et al.  The synthesis of 2,3-didehydro-2,4-dideoxy-4-guanidinyl-N-acetylneuraminic acid: a potent influenza virus sialidase inhibitor. , 1994, Carbohydrate research.

[10]  D. M. Ryan,et al.  Rational design of potent sialidase-based inhibitors of influenza virus replication , 1993, Nature.

[11]  G. Whitesides,et al.  Neuraminidase-resistant hemagglutination inhibitors: acrylamide copolymers containing a C-glycoside of N-acetylneuraminic acid. , 1993, Journal of medicinal chemistry.

[12]  R. Roy,et al.  Solid-phase synthesis of dendritic sialoside inhibitors of influenza A virus haemagglutinin , 1993 .

[13]  J. Skehel,et al.  Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography. , 1994, Biochemistry.

[14]  T. G. Hill,et al.  Carbohydrate materials bearing neuraminidase-resistant C-glycosides of sialic acid strongly inhibit the in vitro infectivity of influenza virus. , 1992, Journal of medicinal chemistry.

[15]  G. Whitesides,et al.  The agglutination of erythrocytes by influenza virus is strongly inhibited by liposomes incorporating an analog of sialyl gangliosides , 1992 .

[16]  Lawrence H. Pinto,et al.  Influenza virus M2 protein has ion channel activity , 1992, Cell.

[17]  S Cusack,et al.  The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. , 1992, The EMBO journal.

[18]  J. Knowles,et al.  Molecular recognition of bivalent sialosides by influenza virus , 1991 .

[19]  W. Filipowicz,et al.  Alteration of the RNA polymerase specificity of U3 snRNA genes during evolution and in vitro , 1991, Cell.

[20]  E. Schreiner,et al.  Structural Variations on N‐acetylneuraminic acid, 20. Synthesis of some 2,3‐didehydro‐2‐deoxysialic Acids structurally varied at C‐4 and their behavior towards Sialidase from Vibrio cholerae , 1991 .

[21]  G. Whitesides,et al.  Polyacrylamides bearing pendant .alpha.-sialoside groups strongly inhibit agglutination of erythrocytes by influenza virus , 1991 .

[22]  N. Bovin,et al.  Synthetic polymeric sialoside inhibitors of influenza virus receptor‐binding activity , 1990, FEBS letters.

[23]  B. Eaton,et al.  The site of bluetongue virus attachment to glycophorins from a number of animal erythrocytes. , 1989, The Journal of general virology.

[24]  G M Whitesides,et al.  Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance study. , 1989, Biochemistry.

[25]  J. Paulson,et al.  Basis for the potent inhibition of influenza virus infection by equine and guinea pig alpha 2-macroglobulin. , 1989, The Journal of biological chemistry.

[26]  G. Air,et al.  The neuraminidase of influenza virus , 1989, Proteins.

[27]  P. C. Lee,et al.  Glycophorin is the reovirus receptor on human erythrocytes. , 1987, Virology.

[28]  N. Dimmock Multiple mechanisms of neutralization of animal viruses , 1987 .

[29]  J. Skehel,et al.  The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. , 1987, Annual review of biochemistry.

[30]  J. E. Mellema,et al.  Structure and composition of influenza virus. A small-angle neutron scattering study. , 1985, Journal of molecular biology.

[31]  J. Paulson Interactions of Animal Viruses with Cell Surface Receptors , 1985 .

[32]  J. Paulson,et al.  Differential sensitivity of human, avian, and equine influenza A viruses to a glycoprotein inhibitor of infection: selection of receptor specific variants. , 1983, Virology.

[33]  N. Cox,et al.  Antigenic drift in influenza virus H3 hemagglutinin from 1968 to 1980: multiple evolutionary pathways and sequential amino acid changes at key antigenic sites , 1983, Journal of virology.

[34]  J. Paulson,et al.  Polyoma virus recognizes specific sialyligosaccharide receptors on host cells. , 1981, Virology.

[35]  M. Potier,et al.  Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-D-N-acetylneuraminate) substrate. , 1979, Analytical biochemistry.

[36]  R. Webster,et al.  The epidemiology of influenza. , 1977, Scientific American.

[37]  E. D. Kilbourne Future influenza vaccines and the use of genetic recombinants. , 1969, Bulletin of the World Health Organization.