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

Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids

Aminoff, D. (1961) · Biochemical Journal · doi:10.1042/bj0810384 · Cited by 1,898 · see citing works

Application of a Microtechnique to Viral Serological Investigations

Sever, J. L. (1962) · The Journal of Immunology · doi:10.4049/jimmunol.88.3.320 · Cited by 1,615 · see citing works

Isolation of paramyxovirus glycoproteins. Association of both hemagglutinating and neuraminidase activities with the larger SV5 glycoprotein

Scheid, A., Caliguiri, L. A., Compans, R. W., & Choppin, P. W. (1972) · Virology · doi:10.1016/0042-6822(72)90418-7 · Cited by 325 · see citing works

Isolation and Purification of the Envelope Proteins of Newcastle Disease Virus

Scheid, A., & Choppin, P. W. (1973) · Journal of Virology · doi:10.1128/jvi.11.2.263-271.1973 · Cited by 293 · see citing works

Über 2-Desoxy-2.3-dehydro-sialinsäuren, II. Kompetitive Hemmung derVibrio-cholerae-Neuraminidase durch 2-Desoxy-2.3-dehyro-N-acyl-neuraminsäuren

Meindl, P., & Tuppy, H. (1969) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1969.350.2.1088 · Cited by 113 · see citing works

�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 · see citing works

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 · see citing works

Competitive inhibition of Vibrio cholerae neuraminic acids

Meindl, P. (1969) · Medical Entomology and Zoology · Cited by 61 · see citing works

Neuraminidase inhibition and viral chemotherapy

Haskell, T. H., Peterson, F. E., Watson, D., Plessas, N. R., & Culbertson, T. (1970) · Journal of Medicinal Chemistry · doi:10.1021/jm00298a027 · Cited by 51 · see citing works

Undisturbed release of influenza virus in the presence of univalent antineuraminidase antibodies

Becht, H., Hämmerling, U., & ROTT, R. (1971) · Virology · doi:10.1016/0042-6822(71)90035-3 · Cited by 51 · see citing works

Isolation and characterization of influenza virus recombinants with high and low neuraminidase activity

Palese, P., & Schulman, J. L. (1974) · Virology · doi:10.1016/0042-6822(74)90123-8 · Cited by 40 · see citing works

Synthetic inhibitors of Vibrio cholerae neuraminidase and neuraminidases of some influenza virus strains

Khorlin, A. Y., Privalova, I. M., Zakstelskaya, L. Y., & Molibog, E. V. (1970) · FEBS Letters · doi:10.1016/0014-5793(70)80214-9 · Cited by 38 · see citing works

[2-Deoxy-2,3-dehydrosialic acids. II. Competitive inhibition of Vibrio cholerae neuraminidase by 2-deoxy-2,3-dehydro-N-acylneuraminic acids].

Meindl, P., & Tuppy, H. (1969) · PubMed · Cited by 37 · see citing works

Einfluß von 2-Desoxy-2.3-dehydro-N-acetylneuraminsäure auf Myxovirus-Neuraminidasen und die Replikation von Influenza- und Newcastle Disease Virus / Influence of 2-Deoxy-2,3-dehydro-N-acetylneuraminic Acid on Myxovirus-neuraminidases and the Replication of Influenza- and Newcastle Disease Virus

Meindl, P., Bodo, G., Lindner, J., & Palese, P. (1971) · Zeitschrift für Naturforschung B · doi:10.1515/znb-1971-0812 · Cited by 28 · see citing works

The Effect of Azo Dyes on Myxovirus Neuraminidase and on Virus Multiplication

Becht, H., & Drzeniek, R. (1968) · Journal of General Virology · doi:10.1099/0022-1317-2-2-261 · Cited by 23 · see citing works

�ber synthetische Ketoside der N-Acetyl-d-neuramins�ure, 3. Mitt.: Darstellung des Phenyl-?-ketosides der N-Acetyl-d-neuramins�ure und seines ?-Anomeren

Meindl, P., & Tuppy, H. (1967) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/bf00901096 · Cited by 19 · see citing works

Synthese und Eigenschaften von 2-Deoxy-2,3-dehydroneuramins�ure sowie neuer N-Acylderivate

Meindl, P., & Tuppy, H. (1973) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/bf00903104 · Cited by 16 · see citing works

Biological roles of glycans

Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635 · see citing works

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 · see citing works

Influenza Neuraminidase Inhibitors Possessing a Novel Hydrophobic Interaction in the Enzyme Active Site: Design, Synthesis, and Structural Analysis of Carbocyclic Sialic Acid Analogues with Potent Anti-Influenza Activity

Kim, C. U., Lew, W., Williams, M. A., Liu, H., Zhang, L., Swaminathan, S., Bischofberger, N., Chen, M. S., Mendel, D. B., Tai, C. Y., et al. (1997) · Journal of the American Chemical Society · doi:10.1021/ja963036t · Cited by 1,100 · see citing works

Neuraminidase Inhibitors for Influenza

Moscona, A. (2005) · New England Journal of Medicine · doi:10.1056/nejmra050740 · Cited by 1,090 · see citing works

Chemistry, Metabolism, and Biological Functions of Sialic Acids

Schauer, R. (1982) · Advances in carbohydrate chemistry and biochemistry · doi:10.1016/s0065-2318(08)60109-2 · Cited by 1,013 · see citing works

Receptor determinants of human and animal influenza virus isolates: Differences in receptor specificity of the H3 hemagglutinin based on species of origin

Rogers, G. N., & Paulson, J. C. (1983) · Virology · doi:10.1016/0042-6822(83)90150-2 · Cited by 943 · see citing works

The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design

Russell, R. J. M., Haire, L. F., Stevens, D. J., Collins, P. J., Lin, Y. P., Blackburn, G. M., Hay, A. J., Gamblin, S. J., & Skehel, J. J. (2006) · Nature · doi:10.1038/nature05114 · Cited by 822 · see citing works

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 788 · see citing works

Glycosidase inhibitors: update and perspectives on practical use

Asano, N. (2003) · Glycobiology · doi:10.1093/glycob/cwg090 · Cited by 717 · see citing works

Parainfluenza Viruses

Henrickson, K. J. (2003) · Clinical Microbiology Reviews · doi:10.1128/cmr.16.2.242-264.2003 · Cited by 497 · see citing works

Drug resistance in influenza A virus: the epidemiology and management

Hussain, M., Galvin, H. D., Haw, T. Y., Nutsford, A. N., & Husain, M. (2017) · Infection and Drug Resistance · doi:10.2147/idr.s105473 · Cited by 441 · see citing works

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 · see citing works

BCX-1812 (RWJ-270201): Discovery of a Novel, Highly Potent, Orally Active, and Selective Influenza Neuraminidase Inhibitor through Structure-Based Drug Design

Babu, Y. S., Chand, P., Bantia, S., Kotian, P. L., Dehghani, A., El-Kattan, Y. A., Lin, T., Hutchison, T. L., Elliott, A. J., Parker, C. D., et al. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm0002679 · Cited by 385 · see citing works

Adult and embryonic mouse neural cell adhesion molecules have different binding properties

Sadoul, R., Hirn, M. H., Bazin, H., Rougon, G. N., & Goridis, C. (1983) · Nature · doi:10.1038/304347a0 · Cited by 351 · see citing works

Influenza virus neuraminidase: Structure, antibodies, and inhibitors

Colman, P. M. (1994) · Protein Science · doi:10.1002/pro.5560031007 · Cited by 334 · see citing works

Exploration of the Sialic Acid World

Schauer, R., & Kamerling, J. P. (2018) · Advances in carbohydrate chemistry and biochemistry · doi:10.1016/bs.accb.2018.09.001 · Cited by 323 · see citing works

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., Ticehurst, J. R., Tilling, J., & Walcott, S. M. (1993) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.37.7.1473 · Cited by 312 · see citing works

Safety and Efficacy of the Neuraminidase Inhibitor GG167 in Experimental Human Influenza

Hayden, F. G. (1996) · JAMA · doi:10.1001/jama.1996.03530280047035 · Cited by 291 · see citing works

Carbohydrate-based drugs launched during 2000−2021

Cao, X., Du, X., Jiao, H., An, Q., Chen, R., Fang, P., Wang, J., & Yu, B. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.05.020 · Cited by 271 · see citing works

Chemistry, biochemistry and biology of sialic acids

Schauer, R., & Kamerling, J. P. (1997) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60624-9 · Cited by 223 · see citing works

Synthetic Approaches to the Neuraminidase Inhibitors Zanamivir (Relenza) and Oseltamivir Phosphate (Tamiflu) for the Treatment of Influenza

Magano, J. (2009) · Chemical Reviews · doi:10.1021/cr800449m · Cited by 218 · see citing works

Gangliosides

Wiegandt, H. (1985) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60022-8 · Cited by 217 · see citing works

Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase

Varghese, J. N., Smith, P. W., Sollis, S. L., Blick, T., Sahasrabudhe, A., McKimm‐Breschkin, J. L., & Colman, P. M. (1998) · Structure · doi:10.1016/s0969-2126(98)00075-6 · Cited by 201 · see citing works

Molecular forms of N-CAM and its RNA in developing and denervated skeletal muscle.

Covault, J., Merlie, J. P., Goridis, C., & Sanes, J. R. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.102.3.731 · Cited by 189 · see citing works

Systematic Structure-Based Design and Stereoselective Synthesis of Novel Multisubstituted Cyclopentane Derivatives with Potent Antiinfluenza Activity

Chand, P., Kotian, P. L., Dehghani, A., El-Kattan, Y. A., Lin, T., Hutchison, T. L., Babu, Y. S., Bantia, S., Elliott, A. J., & Montgomery, J. A. J. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm010277p · Cited by 175 · see citing works

Antiviral Approaches against Influenza Virus

Kumari, R., Sharma, S. D., Kumar, A., Ende, Z. S., Mishina, M., Wang, Y., Falls, Z., Samudrala, R., Pohl, J., Knight, P. R., et al. (2023) · Clinical Microbiology Reviews · doi:10.1128/cmr.00040-22 · Cited by 172 · see citing works

Enzymatic Two‐Step Synthesis of N‐Acetyl‐neuraminic Acid in the Enzyme Membrane Reactor

Kragl, U., Gygax, D., Ghisalba, O., & Wandrey, C. (1991) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199108271 · Cited by 169 · see citing works

Old tricks, new dogs: organocatalytic dienamine activation of α,β-unsaturated aldehydes

Marcos, V., & Alemán, J. (2016) · Chemical Society Reviews · doi:10.1039/c6cs00438e · Cited by 166 · see citing works

Influenza neuraminidase: A druggable target for natural products

Grienke, U., Schmidtke, M., von Grafenstein, S., Kirchmair, J., Liedl, K. R., & Rollinger, J. M. (2011) · Natural Product Reports · doi:10.1039/c1np00053e · Cited by 158 · see citing works

Lectin receptors as markers for Trypanosoma cruzi. Developmental stages and a study of the interaction of wheat germ agglutinin with sialic acid residues on epimastigote cells.

Pereira, M., Loures, M. A. L., Villalta, F., & Andrade, A. F. (1980) · The Journal of Experimental Medicine · doi:10.1084/jem.152.5.1375 · Cited by 158 · see citing works

An enzymatic assay reveals that proteins destined for the apical or basolateral domains of an epithelial cell line share the same late Golgi compartments.

Fuller, S. D., Bravo, R., & Simons, K. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03629.x · Cited by 157 · see citing works

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 · see citing works

Virulence factors of influenza A viruses: WSN virus neuraminidase required for plaque production in MDBK cells

Schulman, J. L., & Palese, P. (1977) · Journal of Virology · doi:10.1128/jvi.24.1.170-176.1977 · Cited by 140 · see citing works

Gangliosides as influenza virus receptors. Variation of influenza viruses and their recognition of the receptor sialo-sugar chains

Suzuki, Y. (1994) · Progress in Lipid Research · doi:10.1016/0163-7827(94)90026-4 · Cited by 139 · see citing works

Studies on cell adhesion and recognition. I. Extent and specificity of cell adhesion triggered by carbohydrate-reactive proteins (glycosidases and lectins) and by fibronectin.

Rauvala, H., Carter, W. G., & Hakomori, S. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.88.1.127 · Cited by 138 · see citing works

Role of sialic acid-containing molecules in paramyxovirus entry into the host cell: A minireview

Villar, E., & Muñoz‐Barroso, I. (2006) · Glycoconjugate Journal · doi:10.1007/s10719-006-5433-0 · Cited by 129 · see citing works

Existing antivirals are effective against influenza viruses with genes from the 1918 pandemic virus

Tumpey, T. M., García‐Sastre, A., Mikulasova, A., Taubenberger, J. K., Swayne, D. E., Palese, P., & Basler, C. F. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212519699 · Cited by 127 · see citing works

An efficient process for production of n-acetylneuraminic acid using n-acetylneuraminic acid aldolase

Mahmoudian, M., NOBLE, D., Drake, C. S., Middleton, R. F., Montgomery, D. S., Piercey, J. E., Ramlakhan, D., Todd, M., & Dawson, M. J. (1997) · Enzyme and Microbial Technology · doi:10.1016/s0141-0229(96)00180-9 · Cited by 127 · see citing works

Anti-influenza agents from Traditional Chinese Medicine

Hu, G., Wang, Y., Xu, J., Gu, Q., Liu, H.-B., Xiao, P., Zhou, J., Liu, Y., Yang, Z., & Su, H. (2010) · Natural Product Reports · doi:10.1039/c0np00005a · Cited by 123 · see citing works

New Approaches to Influenza Chemotherapy

Calfee, D. P., & Hayden, F. G. (1998) · Drugs · doi:10.2165/00003495-199856040-00003 · Cited by 121 · see citing works

Reconstitution of an endocytic fusion event in a cell-free system

Davey, J. F., Hurtley, S. M., & Warren, G. (1985) · Cell · doi:10.1016/0092-8674(85)90236-3 · Cited by 118 · see citing works

Metabolism of Sialic Acids

Corfield, A. P., & Schauer, R. (1982) · Cell biology monographs · doi:10.1007/978-3-7091-8680-0_9 · Cited by 117 · see citing works

Molecular heterogeneity and structural evolution during cerebellar ontogeny detected by monoclonal antibody of the mouse cell surface antigen BSP-2

Hirn, M. H., Ghandour, M. S., Bazin, H., & Goridis, C. (1983) · Brain Research · doi:10.1016/0006-8993(83)91337-9 · Cited by 115 · see citing works

Inhibition of influenza and parainfluenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA)

Palese, P., Schulman, J. L., Bodo, G., & Meindl, P. (1974) · Virology · doi:10.1016/0042-6822(74)90458-9 · Cited by 113 · see citing works

Ligand recognition by influenza virus. The binding of bivalent sialosides.

Glick, G. D., Toogood, P. L., Wiley, D. C., Skehel, J. J., & Knowles, J. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54335-0 · Cited by 113 · see citing works

Antivirals Targeting Influenza A Virus

Das, K. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300455c · Cited by 112 · see citing works

Multiple oligosaccharide chains in the voltage-sensitive Na channel from Electrophorus electricus: Evidence for α-2,8-linked polysialic acid

James, W. M., & Agnew, W. S. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90949-1 · Cited by 110 · see citing works

Molecular aspects of immunoglobulin A1 degradation by oral streptococci

Reinholdt, J., Tomana, M., Mortensen, S. B., & Kilian, M. (1990) · Infection and Immunity · doi:10.1128/iai.58.5.1186-1194.1990 · Cited by 107 · see citing works

Thyroglobulin interactions with thyroid plasma membranes. the existence of specific receptors and their potential role

Consiglio, E., Salvatore, G., Rall, J. E., & Kohn, L. D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50561-5 · Cited by 98 · see citing works

Peramivir (BCX-1812, RWJ-270201): potential new therapy for influenza

Smee, D. F., & Sidwell, R. W. (2002) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.11.6.859 · Cited by 94 · see citing works

In vivo anti-influenza virus activity of plant flavonoids possessing inhibitory activity for influenza virus sialidase

Nagai, T., Miyaichi, Y., Tomimori, T., Suzuki, Y., & Yamada, H. (1992) · Antiviral Research · doi:10.1016/0166-3542(92)90080-o · Cited by 92 · see citing works

Comparative Binding Energy (COMBINE) Analysis of Influenza Neuraminidase−Inhibitor Complexes

Wang, T., & Wade, R. C. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm001070j · Cited by 90 · see citing works

Synthesis of the potent influenza neuraminidase inhibitor 4-guanidino Neu5Ac2en. X-Ray molecular structure of 5-acetamido-4-amino-2,6-anhydro-3,4,5-trideoxy-D-erythro-L-gluco-nononic acid

Chandler, M., Bamford, M. J., Conroy, R., Lamont, B., Patel, B., Patel, V. K., Steeples, I. P., Storer, R., Weir, N. G., Wright, M., et al. (1995) · Journal of the Chemical Society Perkin Transactions 1 · doi:10.1039/p19950001173 · Cited by 89 · see citing works

The HN glycoprotein of sendai virus: Analysis of site(s) involved in hemagglutinating and neuraminidase activities

Portner, A. (1981) · Virology · doi:10.1016/0042-6822(81)90118-5 · Cited by 87 · see citing works

The hemagglutinating and neuraminidase protein of a paramyxovirus: Interaction with neuraminic acid in affinity chromatography

Scheid, A., & Choppin, P. W. (1974) · Virology · doi:10.1016/0042-6822(74)90308-0 · Cited by 86 · see citing works

Mode of action of the anti-influenza virus activity of plant flavonoid, 5,7,4′-trihydroxy-8-methoxyflavone, from the roots of Scutellaria baicalensis

Nagai, T., Moriguchi, R., Suzuki, Y., Tomimori, T., & Yamada, H. (1995) · Antiviral Research · doi:10.1016/0166-3542(94)00062-d · Cited by 85 · see citing works

The Anti-Influenza Virus Agent 4-GU-DANA (Zanamivir) Inhibits Cell Fusion Mediated by Human Parainfluenza Virus and Influenza Virus HA

Greengard, O., Poltoratskaia, N., Leikina, E., Zimmerberg, J. J., & Moscona, A. (2000) · Journal of Virology · doi:10.1128/jvi.74.23.11108-11114.2000 · Cited by 85 · see citing works

Influenza Virus Resistance to Antiviral Therapy

van der Vries, E., Schutten, M., Fraaij, P. L. A., Boucher, C. A., & Osterhaus, A. D. M. E. (2013) · Advances in pharmacology · doi:10.1016/b978-0-12-405880-4.00006-8 · Cited by 84 · see citing works

Low-density lipoprotein modification occurring in human plasma

Tertov, V. V., Kaplun, V. V., Sobenin, I. A., & Orekhov, A. N. (1998) · Atherosclerosis · doi:10.1016/s0021-9150(98)00023-9 · Cited by 84 · see citing works

Total Synthesis of A-315675: A Potent Inhibitor of Influenza Neuraminidase

Hanessian, S., Bayrakdarian, M., & Luo, X. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0126226 · Cited by 83 · see citing works

Studies on cell adhesion and recognition. II. The kinetics of cell adhesion and cell spreading on surfaces coated with carbohydrate-reactive proteins (glycosidases and lectins) and fibronectin.

Carter, W. G., Rauvala, H., & Hakomori, S. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.88.1.138 · Cited by 82 · see citing works

Progress of small molecular inhibitors in the development of anti-influenza virus agents

Wu, X., Wu, X., Sun, Q., Zhang, C., Yang, S., Li, L., & Jia, Z. (2017) · Theranostics · doi:10.7150/thno.17071 · Cited by 79 · see citing works

The Biological Role of Sialic Acid at the Surface of the Cell

Jeanloz, R. W., & Codington, J. F. (1976) · Springer eBooks · doi:10.1007/978-1-4684-2226-9_7 · Cited by 80 · see citing works

Neuraminidase Inhibitors as Anti-Influenza Virus Agents

Kim, C. U., Chen, X., & Mendel, D. B. (1999) · Antiviral chemistry & chemotherapy · doi:10.1177/095632029901000401 · Cited by 76 · see citing works

Development of gene therapy-based strategies for the treatment of eye diseases

Rakoczy, P. E., Shen, W., Lai, M. C., Rolling, F., & Constable, I. J. (1999) · Drug Development Research · doi:10.1002/(sici)1098-2299(199903/04)46:3/4 · Cited by 11 · see citing works

NMR Spectroscopy of Sialic Acids

Vliegenthart, J. F. G., DORLAND, L., van HALBEEK, H., & Haverkamp, J. (1982) · Cell biology monographs · doi:10.1007/978-3-7091-8680-0_7 · Cited by 74 · see citing works

‘Flu’ and structure-based drug design

Wade, R. C. (1997) · Structure · doi:10.1016/s0969-2126(97)00265-7 · Cited by 72 · see citing works

Impact of neuraminidase inhibitors on influenza A(H1N1)pdm09‐related pneumonia: an individual participant data meta‐analysis

Muthuri, S. G., Venkatesan, S., Myles, P. R., Leonardi‐Bee, J., Lim, W. S., Mamun, A. A., Anovadiya, A., de Araújo, W. N., Azziz‐Baumgartner, E., Báez, C., et al. (2015) · Influenza and Other Respiratory Viruses · doi:10.1111/irv.12363 · Cited by 67 · see citing works

Comparison of the anti-influenza virus activity of cyclopentane derivatives with oseltamivir and zanamivir in vivo

Chand, P., Bantia, S., Kotian, P. L., El-Kattan, Y. A., Lin, T., & Babu, Y. S. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.03.048 · Cited by 66 · see citing works

Sialidase Inhibitors with Different Mechanisms

Keil, J. M., Rafn, G. R., Turan, I. M., Aljohani, M. A., Sahebjam-Atabaki, R., & Sun, X. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01258 · Cited by 64 · see citing works

Sialidase down-regulation reduces non-HDL cholesterol, inhibits leukocyte transmigration, and attenuates atherosclerosis in ApoE knockout mice

White, E. J., Gyulay, G., Lhoták, Š., Szewczyk, M. M., Chong, T. M., Fuller, M. T., Dadoo, O., Fox‐Robichaud, A., Austin, R. C., Trigatti, B. L., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004589 · Cited by 64 · see citing works

Parainfluenza virus type 1 reduces the affinity of agonists for muscarinic receptors in guinea-pig lung and heart

Fryer, A. D., El‐Fakahany, E. E., & Jacoby, D. B. (1990) · European Journal of Pharmacology · doi:10.1016/0014-2999(90)90244-z · Cited by 64 · see citing works

Current and novel antiviral strategies for influenza infection

Yen, H. (2016) · Current Opinion in Virology · doi:10.1016/j.coviro.2016.05.004 · Cited by 63 · see citing works

Sendai virus-erythrocyte membrane interaction: quantitative and kinetic analysis of viral binding, dissociation, and fusion

Hoekstra, D., & Klappe, K. (1986) · Journal of Virology · doi:10.1128/jvi.58.1.87-95.1986 · Cited by 62 · see citing works

MANAGING INFLUENZA: AMANTADINE, RIMANTADINE AND BEYOND

Fleming, D. (2001) · International Journal of Clinical Practice · doi:10.1111/j.1742-1241.2001.tb11012.x · Cited by 60 · see citing works

Sensitivity of molecular docking to induced fit effects in influenza virus neuraminidase

Birch, L. M., Murray, C. W., Hartshorn, M. J., Tickle, I. J., & Verdonk, M. L. (2002) · Journal of Computer-Aided Molecular Design · doi:10.1023/a:1023844626572 · Cited by 60 · see citing works

2,3-dehydro-4-epi-N-acetylneuraminic acid; a neuraminidase inhibitor

Kumar, V., Kessler, J., Scott, M. E., PATWARDHAN, B. H., Tanenbaum, S. W., & Flashner, M. (1981) · Carbohydrate Research · doi:10.1016/s0008-6215(00)80711-9 · Cited by 60 · see citing works

Analogs of zanamivir with modified C4-substituents as the inhibitors against the group-1 neuraminidases of influenza viruses

Wen, W., Wang, S., Tsai, K., Cheng, Y. E., Yang, A., Fang, J., & Wong, C. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.04.010 · Cited by 59 · see citing works

New ganglioside analogs that inhibit influenze virus sialidase

Suzuki, Y., Sato, K., Kiso, M., & Hasegawa, A. (1990) · Glycoconjugate Journal · doi:10.1007/bf01073378 · Cited by 58 · see citing works

Inhibition of Parainfluenza Virus Type 3 and Newcastle Disease Virus Hemagglutinin-Neuraminidase Receptor Binding: Effect of Receptor Avidity and Steric Hindrance at the Inhibitor Binding Sites

Porotto, M., Murrell, M. T., Greengard, O., Lawrence, M. C., McKimm‐Breschkin, J. L., & Moscona, A. (2004) · Journal of Virology · doi:10.1128/jvi.78.24.13911-13919.2004 · Cited by 57 · see citing works

Antivirals against animal viruses

Villa, T. G., Feijoo-Siota, L., Rama, J. L. R., & Ageitos, J. M. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.09.029 · Cited by 54 · see citing works

Anti-Influenza Drugs: The Development of Sialidase Inhibitors

von Itzstein, M., & Thomson, R. J. (2008) · Handbook of experimental pharmacology · doi:10.1007/978-3-540-79086-0_5 · Cited by 53 · see citing works

Synthesis and influenza virus sialidase inhibitory activity of analogues of 4-guanidino-Neu5Ac2en (GG167) with modified 5-substituents

Smith, P., Starkey, I. D., HOWES, P. D., Sollis, S. L., Keeling, S. P., Cherry, P., von Itzstein, M., Wu, W., & Jin, B. (1996) · European Journal of Medicinal Chemistry · doi:10.1016/0223-5234(96)80447-8 · Cited by 50 · see citing works

Oseltamivir-resistant influenza?

Moscona, A. (2004) · The Lancet · doi:10.1016/s0140-6736(04)16947-x · Cited by 50 · see citing works

On the side-chain conformation of N-acetylneuraminic acid and its epimers at C-7, C-8, and C-7,8

Christian, R., Schulz, G., Brandstetter, H. H., & Zbiral, E. (1987) · Carbohydrate Research · doi:10.1016/0008-6215(87)80195-7 · Cited by 49 · see citing works

An efficient method for introducing defined lipids into the plasma membrane of mammalian cells.

Gerrit van, M. E. E. R., & Simons, K. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.5.1365 · Cited by 47 · see citing works

Neuraminidase Inhibitors and their Role in Avian and Pandemic Influenza

Crusat, M., & de Jong, M. D. (2007) · Antiviral Therapy · doi:10.1177/135965350701200s07.1 · Cited by 45 · see citing works

Synthesis of a Phosphonic Acid Analogue of N‐Acetyl‐2,3‐didehydro‐2‐deoxyneuraminic Acid, an Inhibitor of Vibrio cholerae Sialidase

Vasella, A. T., & Wyler, R. (1991) · Helvetica Chimica Acta · doi:10.1002/hlca.19910740223 · Cited by 46 · see citing works

Sialidase and Sialyltransferase Inhibitors: Targeting Pathogenicity and Disease

Bowles, W., & Gloster, T. M. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.705133 · Cited by 45 · see citing works

Recent Advances in Computer-Aided Drug Design as Applied to Anti-Influenza Drug Discovery

Mallipeddi, P. L., Kumar, G., White, S. W., & Webb, T. R. (2014) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026614666140929153812 · Cited by 44 · see citing works

2,3-Didehydro-2-deoxysialic acids structurally varied at C-5 and their behaviour towards the sialidase from Vibrio cholerae

Schreiner, E. P., Zbiral, E., Kleineidam, R. G., & Schauer, R. (1992) · Carbohydrate Research · doi:10.1016/0008-6215(92)84150-q · Cited by 43 · see citing works

Synthesis and inhibitory activity of benzoic acid and pyridine derivatives on influenza neuraminidase

Chand, P., Kotian, P. L., Morris, P. E., Bantia, S., Walsh, D. A., & Babu, Y. S. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.01.042 · Cited by 43 · see citing works

A rapid and sensitive assay for neuraminidase using peanut lectin hemagglutination: Application to Vibrio cholera and Trypanosoma cruzi

Pereira, M. E. A. (1983) · Journal of Immunological Methods · doi:10.1016/0022-1759(83)90206-5 · Cited by 43 · see citing works

Synaptosomal Sialyltransferase Glycosylates Surface Proteins that Are Inaccessible to the Action of Membrane‐Bound Sialidase

Breen, K. C., & Regan, C. M. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb00737.x · Cited by 43 · see citing works

Novel α- and β-Amino Acid Inhibitors of Influenza Virus Neuraminidase

Kati, W. M., Montgomery, D., Maring, C. J., Stoll, V. S., Giranda, V. L., Chen, X., Laver, W. G., Kohlbrenner, W. E., & Norbeck, D. W. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.9.2563-2570.2001 · Cited by 42 · see citing works

Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface

Hu, H., Shioda, T., Moriya, C., Xin, X., Hasan, M. K., Miyake, K., Shimada, T., & Nagai, Y. (1996) · Journal of Virology · doi:10.1128/jvi.70.11.7462-7470.1996 · Cited by 42 · see citing works

Strategies for Antiviral Drug Discovery

Jones, P. (1998) · Antiviral chemistry & chemotherapy · doi:10.1177/095632029800900401 · Cited by 41 · see citing works

Oseltamivir Analogues Bearing N-Substituted Guanidines as Potent Neuraminidase Inhibitors

Mooney, C. A., Johnson, S. A., Hart, P. ‘., van Ufford, L. Q., de Haan, C. A. M., Moret, E. E., & Martin, N. I. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401977j · Cited by 40 · see citing works

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

Waxham, M. N., & S.Wolinsky, J. (1986) · Virology · doi:10.1016/0042-6822(86)90050-4 · Cited by 40 · see citing works

Influenza Viruses: Harnessing the Crucial Role of the M2 Ion-Channel and Neuraminidase toward Inhibitor Design

Mtambo, S. E., Amoako, D. G., Somboro, A. M., Agoni, C., Lawal, M. M., Gumede, N. S., Khan, R. B., & Kumalo, H. M. (2021) · Molecules · doi:10.3390/molecules26040880 · Cited by 38 · see citing works

Einfluß von 2-Desoxy-2.3-dehydro-N-acetylneuraminsäure auf Myxovirus-Neuraminidasen und die Replikation von Influenza- und Newcastle Disease Virus / Influence of 2-Deoxy-2,3-dehydro-N-acetylneuraminic Acid on Myxovirus-neuraminidases and the Replication of Influenza- and Newcastle Disease Virus

Meindl, P., Bodo, G., Lindner, J., & Palese, P. (1971) · Zeitschrift für Naturforschung B · doi:10.1515/znb-1971-0812 · Cited by 28 · see citing works

Acyl Amino Acid Derivatives as Novel Inhibitors of Influenza Neuraminidase

Kondoh, M., Furutani, T., Azuma, M., Ooshima, H., & Kato, J. (1997) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.61.870 · Cited by 13 · see citing works

Inhibition of influenza and parainfluenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA)

Palese, P., Schulman, J. L., Bodo, G., & Meindl, P. (1974) · Virology · doi:10.1016/0042-6822(74)90458-9 · Cited by 113 · see citing works

Inhibition Studies onVibrio choleraeNeuraminidase

Brossmer, R., KEILICH, G., & Ziegler, D. (1977) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1977.358.1.391 · Cited by 17 · see citing works

Inhibition of Influenza Virus Replication by 2-Deoxy-2,3-Dehydro-N-Trifluoroacetylneuraminic Acid (Fana)

Schulman, J. L., & Palese, P. (1976) · Springer eBooks · doi:10.1007/978-1-4684-3129-2_32