Influenza virus neuraminidase: Structure, antibodies, and inhibitors

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,085

A computational procedure for determining energetically favorable binding sites on biologically important macromolecules

Goodford, P. J. (1985) · Journal of Medicinal Chemistry · doi:10.1021/jm00145a002 · Cited by 2,634

Rational design of potent sialidase-based inhibitors of influenza virus replication

von Itzstein, M., Wu, W.-Y., Kok, G. B., Pegg, M. S., Dyason, J. C., Jin, B., Van Phan, T., Smythe, M. L., White, H. F., Oliver, S. W., et al. (1993) · Nature · doi:10.1038/363418a0 · Cited by 1,862

Shape Complementarity at Protein/Protein Interfaces

Lawrence, M. C., & Colman, P. M. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1648 · Cited by 1,215

Influenza virus M2 protein has ion channel activity

Pinto, L. H., Holsinger, L. J., & Lamb, R. A. (1992) · Cell · doi:10.1016/0092-8674(92)90452-i · Cited by 1,213

Shape complementarity at protein–protein interfaces

Norel, R., Lin, S. L., Wolfson, H. J., & Nussinov, R. (1994) · Biopolymers · doi:10.1002/bip.360340711 · Cited by 1,208

Principles and practice of infectious disease

Cann, K. J. (1990) · Journal of Hospital Infection · doi:10.1016/0195-6701(90)90013-e · Cited by 1,199

Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid

Weis, W., Brown, J. H., Cusack, S., Paulson, J. C., Skehel, J. J., & Wiley, D. C. (1988) · Nature · doi:10.1038/333426a0 · Cited by 1,158

Man-made antibodies

Winter, G., & Milstein, C. (1991) · Nature · doi:10.1038/349293a0 · Cited by 945

Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution

Varghese, J. N., Laver, W. G., & Colman, P. M. (1983) · Nature · doi:10.1038/303035a0 · Cited by 891

Glycoproteins: Their composition, structure and function

Gottschalk, A. (1972) · Medical Entomology and Zoology · Cited by 862

The molecular basis of the specific anti-influenza action of amantadine.

Hay, A. J., Wolstenholme, A. J., Skehel, J. J., & Smith, M. H. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb04038.x · Cited by 847

Structure of the catalytic and antigenic sites in influenza virus neuraminidase

Colman, P. M., Varghese, J. N., & Laver, W. G. (1983) · Nature · doi:10.1038/303041a0 · Cited by 798

Characterization of temperature sensitive influenza virus mutants defective in neuraminidase

Palese, P., Tobita, K., Ueda, M., & Compans, R. W. (1974) · Virology · doi:10.1016/0042-6822(74)90276-1 · Cited by 789

Membrane fusion proteins of enveloped animal viruses

White, J., Kielian, M., & Helenius, A. (1983) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005072 · Cited by 668

Three-dimensional structure of a complex of antibody with influenza virus neuraminidase

Colman, P. M., Laver, W. G., Varghese, J. N., Baker, A. T., Tulloch, P. A., Air, G. M., & Webster, R. G. (1987) · Nature · doi:10.1038/326358a0 · Cited by 553

The Influenza Viruses and Influenza

Tyrrell, D. A. J. (1976) · BMJ · doi:10.1136/bmj.1.6007.465-c · Cited by 537

The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor

Varghese, J. N., McKimm‐Breschkin, J. L., Caldwell, J. B., Kortt, A. A., & Colman, P. M. (1992) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340140302 · Cited by 402

Domain association in immunoglobulin molecules

Chothia, C., Novotný, J., Bruccoleri, R., & Karplus, M. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90137-8 · Cited by 395

Fusion mutants of the influenza virus hemagglutinin glycoprotein

Daniels, R. (1985) · Cell · doi:10.1016/0092-8674(85)90157-6 · Cited by 394

ADSORPTION OF INFLUENZA HEMAGGLUTININS AND VIRUS BY RED BLOOD CELLS

Hirst, G. K. (1942) · Journal of Experimental Medicine · doi:10.1084/jem.76.2.195 · Cited by 315

The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid.

Burmeister, W. P., Ruigrok, R. W., & Cusack, S. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05026.x · Cited by 314

4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid is a highly effective inhibitor both of the sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitro

Woods, J. M., Bethell, R. C., Coates, J. A., Healy, N., Hiscox, S. A., Pearson, B. A., Ryan, D. M., Ticehurst, J., Tilling, J., & Walcott, S. M. (1993) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.37.7.1473 · Cited by 312

Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid

Meindl, P., Bodo, G., Palese, P., Schulman, J., & Tuppy, H. (1974) · Virology · doi:10.1016/0042-6822(74)90080-4 · Cited by 287

Antiviral Activity of Antiserum Specific for an Influenza Virus Neuraminidase

Kilbourne, E. D., Laver, W. G., Schulman, J. L., & Webster, R. G. (1968) · Journal of Virology · doi:10.1128/jvi.2.4.281-288.1968 · Cited by 273

An autoantibody to single‐stranded DNA: Comparison of the three‐dimensional structures of the unliganded fab and a deoxynucleotide–fab complex

Herron, J. N., He, X. M., Ballard, D. W., Blier, P. R., Pace, P. E., Bothwell, A. L. M., Voss, E. W., & Edmundson, A. B. (1991) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340110302 · Cited by 255

Sequence and structure alignment of paramyxovirus hemagglutinin-neuraminidase with influenza virus neuraminidase

Colman, P. M., Hoyne, P. A., & Lawrence, M. C. (1993) · Journal of Virology · doi:10.1128/jvi.67.6.2972-2980.1993 · Cited by 255

Small rearrangements in structures of Fv and Fab fragments of antibody D 1.3 on antigen binding

Bhat, T. N., Bentley, G. A., Fischmann, T. O., Boulot, G., & Poljak, R. J. (1990) · Nature · doi:10.1038/347483a0 · Cited by 250

THE RECEPTOR‐DESTROYING ENZYME OF V. CHOLERAE

Burnet, F., & Stone, J. D. (1947) · Australian Journal of Experimental Biology and Medical Science · doi:10.1038/icb.1947.33 · Cited by 231

Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2·2 Å resolution

Varghese, J. N., & Colman, P. M. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)80068-6 · Cited by 230

Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase.

Crennell, S. J., Garman, E. F., Laver, W. G., Vimr, E. R., & Taylor, G. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.21.9852 · Cited by 228

Major antigen-induced domain rearrangements in an antibody

Stanfield, R. L., Takimoto-Kamimura, M., Rini, J. M., Profy, A. T., & Wilson, I. A. (1993) · Structure · doi:10.1016/0969-2126(93)90024-b · Cited by 209

Structure of Antibody-Antigen Complexes: Implications for Immune Recognition

Colman, P. M. (1988) · Advances in Immunology · doi:10.1016/s0065-2776(08)60364-8 · Cited by 208

Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain

Crennell, S., Garman, E., Laver, G., Vimr, E., & Taylor, G. (1994) · Structure · doi:10.1016/s0969-2126(00)00053-8 · Cited by 205

Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex

Tulip, W. R., Varghese, J. N., Laver, W. G., Webster, R. G., & Colman, P. M. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90687-f · Cited by 201

Evidence for a sialosyl cation transition‐state complex in the reaction of sialidase from influenza virus

CHONG, A. K. J., PEGG, M. S., TAYLOR, N. R., & von ITZSTEIN, M. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17055.x · Cited by 178

Newcastle disease virus contains a linkage-specific glycoprotein sialidase. Application to the localization of sialic acid residues in N-linked oligosaccharides of alpha 1-acid glycoprotein.

Paulson, J. C., Weinstein, J., Dorland, L., van Halbeek, H., & Vliegenthart, J. F. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33573-7 · Cited by 160

Inhibition of sialidases from viral, bacterial and mammalian sources by analogues of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid modified at the C-4 position

Holzer, C. T., von Itzstein, M., Jin, B., Pegg, M. S., Stewart, W. P., & Wu, W.-Y. (1993) · Glycoconjugate Journal · doi:10.1007/bf00731185 · Cited by 155

Influenza B virus neuraminidase can synthesize its own inhibitor

Burmeister, W. P., Henrissat, B., Bosso, C., Cusack, S., & Ruigrok, R. W. H. (1993) · Structure · doi:10.1016/0969-2126(93)90005-2 · Cited by 152

Mucus — a protective secretion of complexity

Allen, A. (1983) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(83)90166-4 · Cited by 148

Recovery of drug-resistant influenza A virus during therapeutic use of rimantadine

Hayden, F. G., Sperber, S. J., Belshe, R. B., Clover, R. D., Hay, A. J., & Pyke, S. D. M. (1991) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.35.9.1741 · Cited by 148

The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody

Malby, R. L., Tulip, W. R., Harley, V. R., McKimm‐Breschkin, J. L., Laver, W. G., Webster, R. G., & Colman, P. M. (1994) · Structure · doi:10.1016/s0969-2126(00)00074-5 · Cited by 140

Recombinant anti‐sialidase single‐chain variable fragment antibody: Characterization, formation of dimer and higher‐molecular‐mass multimers and the solution of the crystal structure of the single‐chain variable fragment/sialidase complex

KORTT, A. A., MALBY, R. L., CALDWELL, J. B., GRUEN, L. C., IVANCIC, N., LAWRENCE, M. C., HOWLETT, G. J., WEBSTER, R. G., HUDSON, P. J., & COLMAN, P. M. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18724.x · Cited by 128

Three-dimensional structure of an antigenic mutant of the influenza virus haemagglutinin

Knossow, M., Daniels, R. S., Douglas, A. R., et al. (1984) · Nature · doi:10.1038/311678a0 · Cited by 124

The specificity of viral and bacterial sialidases for α(2–3)- and α(2–6)-linked sialic acids in glycoproteins

Corfield, A. P., Higa, H. H., Paulson, J. C., & Schauer, R. (1983) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(83)90080-8 · Cited by 121

Selection and analysis of antigenic variants of the neuraminidase of N2 influenza viruses with monoclonal antibodies

Webster, R. G., Hinshaw, V. S., & Laver, W. G. (1982) · Virology · doi:10.1016/0042-6822(82)90510-4 · Cited by 115

Antibody structure

Davies, D. R., & Chacko, S. (1993) · Accounts of Chemical Research · doi:10.1021/ar00032a005 · Cited by 108

Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants

Tulip, W. R., Varghese, J. N., Baker, A. T., van Donkelaar, A., Laver, W. G., Webster, R. G., & Colman, P. M. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)80069-7 · Cited by 103

�ber 2-Deoxy-2,3-dehydro-sialins�uren, 1. Mitt.: Synthese und Eigenschaften von 2-Deoxy-2,3-dehydro-N-acylneuramins�uren und deren Methylestern

Meindl, P., & Tuppy, H. (1969) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/bf00903465 · Cited by 98

Crystallization and peptide maps of neuraminidase “heads” from H2N2 and H3N2 influenza virus strains

Laver, W. G. (1978) · Virology · doi:10.1016/0042-6822(78)90009-0 · Cited by 94

Sugar Residues on Protein

Wagh, P. V., Bahl, O. P., & Elbein, A. D. (1981) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238109113602 · Cited by 90

Crystal structures of two mutant neuraminidase-antibody complexes with amino acid substitutions in the interface

Tulip, W. R., Varghese, J. N., Webster, R. G., Laver, W. G., & Colman, P. M. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90688-g · Cited by 75

MUCINS AND MUCOIDS IN RELATION TO INFLUENZA VIRUS ACTION

Burnet, F. M. (1948) · Immunology and Cell Biology · doi:10.1038/icb.1948.39 · Cited by 63

THE INHIBITION OF NEURAMINIDASE AND ANTIVIRAL ACTION

EDMOND, J. D., JOHNSTON, R. G., Kidd, D. A. A., Rylance, H. J., & Sommerville, R. G. (1966) · British Journal of Pharmacology and Chemotherapy · doi:10.1111/j.1476-5381.1966.tb01673.x · Cited by 62

Recombinant antineuraminidase single chain antibody: Expression, characterization, and crystallization in complex with antigen

Malby, R. L., Caldwell, J. B., GRUEN, L. C., et al. (1993) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340160107 · Cited by 60

Neuraminidase

Colman, P. M. (1989) · Springer eBooks · doi:10.1007/978-1-4613-0811-9_4 · Cited by 48

Structure, Function, and Antigenicity of the Hemagglutinin of Influenza Virus

Wharton, S. A., Weis, W. I., Skehel, J. J., & Wiley, D. C. (1989) · Springer eBooks · doi:10.1007/978-1-4613-0811-9_3 · Cited by 42

Structure of an escape mutant of glycoprotein N2 neuraminidase of influenza virus A/Tokyo/3/67 at 3 Å

Varghese, J. N., Webster, R. G., Laver, W. G., & Colman, P. M. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90344-0 · Cited by 36

Chemical and antigenic characterization of the carbohydrate side chains of an Asian (N2) influenza virus neuraminidases

Ward, C. W., Murray, J. M., Roxburgh, C. M., & Jackson, D. C. (1983) · Virology · doi:10.1016/0042-6822(83)90486-5 · Cited by 29

Variation in Influenza Virus Genes

Smith, F. I., & Palese, P. (1989) · Springer eBooks · doi:10.1007/978-1-4613-0811-9_7 · Cited by 27

Use of the Oral Neuraminidase Inhibitor Oseltamivir in Experimental Human Influenza: Randomized Controlled Trials for Prevention and Treatment

Hayden, F. G., Treanor, J. J., Fritz, R. S., Lobo, M., Betts, R. F., Miller, M., Kinnersley, N., Mills, R. G., Ward, P., & Straus, S. E. (1999) · JAMA · doi:10.1001/jama.282.13.1240 · Cited by 550

The structural biology of type I viral membrane fusion

Colman, P. M., & Lawrence, M. C. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1076 · Cited by 454

Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis.

Bonten, E., van der Spoel, A., Fornerod, M., Grosveld, G., & d'Azzo, A. (1996) · Genes & Development · doi:10.1101/gad.10.24.3156 · Cited by 313

Structure−Activity Relationship Studies of Novel Carbocyclic Influenza Neuraminidase Inhibitors

Kim, C. U., Lew, W., Williams, M. A., Wu, H., Zhang, L., Chen, X., Escarpe, P. A., Mendel, D. B., Laver, W. G., & Stevens, R. C. (1998) · Journal of Medicinal Chemistry · doi:10.1021/jm980162u · Cited by 291

Bitter-sweet symphony: glycan–lectin interactions in virus biology

Van Breedam, W., Pöhlmann, S., Favoreel, H. W., de Groot, R. J., & Nauwynck, H. J. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12052 · Cited by 141