The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Rational design of potent sialidase-based inhibitors of influenza virus replication
Abstract
Two potent inhibitors based on the crystal structure of influenza virus sialidase have been designed. These compounds are effective inhibitors not only of the enzyme, but also of the virus in cell culture and in animal models. The results provide an example of the power of rational, computer-assisted drug design, as well as indicating significant progress in the development of a new therapeutic or prophylactic treatment for influenza infection.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Citations
Cites
Goodford, P. J. (1985) · Journal of Medicinal Chemistry · doi:10.1021/jm00145a002 · Cited by 2,642
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
Wilson, I. A., Skehel, J. J., & Wiley, D. C. (1981) · Nature · doi:10.1038/289366a0 · Cited by 2,537
Wiley, D. C., Wilson, I. A., & Skehel, J. J. (1981) · Nature · doi:10.1038/289373a0 · Cited by 1,623
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 1,230
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
Self-citationThe 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 855
Potier, M., Mameli, L., Bélisle, M., Dallaire, L., & Melançon, S. B. (1979) · Analytical Biochemistry · doi:10.1016/0003-2697(79)90362-2 · Cited by 816
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 806
Self-citationCharacterization 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
Henderson, P. J. F. (1972) · Biochemical Journal · doi:10.1042/bj1270321 · Cited by 524
Sialic acids and their role as biological masks
Schauer, R. (1985) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(85)90112-4 · Cited by 522
Emergence and Apparent Transmission of Rimantadine-Resistant Influenza A Virus in Families
Hayden, F. G., Belshe, R. B., Clover, R. D., Hay, A. J., Oakes, M. G., & Soo, W. (1989) · New England Journal of Medicine · doi:10.1056/nejm198912213212502 · Cited by 407
Crystallographic refinement by simulated annealing
Brünger, A. T. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90211-2 · Cited by 405
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
Self-citationNeuraminidase: the specific enzyme of influenza virus and Vibrio cholerae
Gottschalk, A. (1957) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(57)90389-x · Cited by 360
Burmeister, W. P., Ruigrok, R. W. H., & Cusack, S. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05026.x · Cited by 316
ADSORPTION OF INFLUENZA HEMAGGLUTININS AND VIRUS BY RED BLOOD CELLS
Hirst, G. K. (1942) · The Journal of Experimental Medicine · doi:10.1084/jem.76.2.195 · Cited by 316
The Molecular Biology of Influenza Virus Pathogenicity
Klenk, H. D., & ROTT, R. (1988) · Advances in virus research · doi:10.1016/s0065-3527(08)60520-5 · Cited by 315
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
Plaque inhibition assay for drug susceptibility testing of influenza viruses
Hayden, F. G., Cote, K. M., & Douglas, R. G. (1980) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.17.5.865 · Cited by 279
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 231
Self-citationUsing linear and non-linear regression to fit biochemical data
Leatherbarrow, R. J. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90295-m · Cited by 204
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
Self-citation[Enzymatic effect of the influenza virus].
KLENK, E., Faillard, H., & Lempfrid, H. (1955) · PubMed · Cited by 157
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
Self-citationÜber die enzymatische Wirkung von Influenzavirus
Klenk, E., Faillard, H., & Lempfrid, H. (1955) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1955.301.1-2.235 · Cited by 146
Structural carbohydrates in the liver
McIntyre, N. R. (1984) · Gut · doi:10.1136/gut.25.10.1126-a · Cited by 140
Viral and Bacterial Neuraminidases
Drzeniek, R. (1972) · Modern aspects of electrochemistry · doi:10.1007/978-3-642-65444-2_2 · Cited by 134
Langmuir, A. D., Worthen, T. D., Solomon, J., Ray, C. G., & Petersen, E. (1985) · New England Journal of Medicine · doi:10.1056/nejm198510173131618 · Cited by 102
Stoof, J. C., Booij, J., Drukarch, B., & Wolters, E. C. (1992) · European Journal of Pharmacology · doi:10.1016/0014-2999(92)90634-g · Cited by 95
NÖHLE, U., Beau, J., & Schauer, R. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06815.x · Cited by 68
Influenza virus sialidase: effect of calcium on steady-state kinetic parameters
Chong, A. K. J., Pegg, M. S., & von Itzstein, M. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)90526-6 · Cited by 64
Self-citationMUCINS 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
Structure of the lysosomal neuraminidase–β-galactosidase–carboxypeptidase multienzymic complex
Potier, M., Michaud, L., Tranchemontagne, J., & Thauvette, L. (1990) · Biochemical Journal · doi:10.1042/bj2670197 · Cited by 55
Colman, P. M. (1989) · Springer eBooks · doi:10.1007/978-1-4613-0811-9_4 · Cited by 47
Self-citationTintelnot, M., & Andrews, P. R. (1989) · Journal of Computer-Aided Molecular Design · doi:10.1007/bf01590996 · Cited by 45
Dependence of the Activity of an Influenza Virus Neuraminidase Upon Ca2+
Dimmock, N. J. (1971) · Journal of General Virology · doi:10.1099/0022-1317-13-3-481 · Cited by 28
Complete metal ion requirement of influenza virus N1 neuraminidases
Carroll, S. M., & Paulson, J. C. (1982) · Archives of Virology · doi:10.1007/bf01314879 · Cited by 16
Flagged first, then by citations
Research works printed but not linked: 6
- Chong, A. K. J., Pegg, M. S. & von Itzstein, M. Biochem. Int. 24, 165–171 (1991).
- Gottschalk, A. Biochim. biophys. Acta 23, 645–646 (1957). · DOI
- Colman, P. M. & Ward, C. W. Curr. Top. microbiol. Immun. 114, 117–255 (1985).
- Palese, P. & Schulman, J. L. in Chemoprophylaxis and Virus Infections of the Upper Respiratory Tract Vol. 1 (ed. Oxford, J. S.) 189–205 (CRC, Cleveland, 1977).
- von Itzstein, M., Jin, B., Wu, W.-Y. & Chandler, M. Carbohydr. Res. (in the press).
- von Itzstein, M., Wu, W.-Y., Phan, T. V., Danylec, B. & Jin, B. Chem. Abs. 117, 49151y (1991).
Cited by
Sorted by citations
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
“The elegant structure-based design of a modified version of the previously known sialidase inhibitor Neu5Ac2en (791) gave rise to the potent and specific inhibitor zanamivir (Relenza) (792, 793), and later to the structurally related agent oseltamivir (Tamiflu) (794, 795).”
BackgroundBertozzi, C. R., & Kiessling, A. L. L. (2001) · Science · doi:10.1126/science.1059820 · Cited by 1,942
Chen, L., Willis, S. N., Wei, A., Smith, B. J., Fletcher, J. I., Hinds, M. G., Colman, P. M., Day, C. L., Adams, J. M., & Huang, D. C. S. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.030 · Cited by 1,816
Self-citationHow were new medicines discovered?
Swinney, D. C., & Anthony, J. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3480 · Cited by 1,812
Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
Jones, G., Willett, P., & Glen, R. C. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(95)80037-9 · Cited by 1,548
Metadata
- Authors
- 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., Colman, P. M., Varghese, J. N., Ryan, D. M., Woods, J. M., Bethell, R. C., Hotham, V. J., Cameron, J. M., & Penn, C. R.
- Affiliations
- Monash University (AU)
- Commonwealth Scientific and Industrial Research Organisation (AU)
- Venue
- Nature
- Published
- 1993-06
- Volume
- 363
- Issue
- 6428
- Pages
- 418-423
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2086358466
- Cited by
- 1,862
- References
- 38
- Citations by year
- 2026: 27 · 2025: 25 · 2024: 34 · 2023: 30 · 2022: 46 · 2021: 50 · 2020: 60 · 2019: 50 · 2018: 58 · 2017: 45 · 2016: 68 · 2015: 48 · 2014: 71 · 2013: 83 · 2012: 84
- FWCI
- 58.57
- Type
- journal article
- Language
- en
- Update notices
- correction (1993-10-28)
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Griffith Research Online (submittedVersion)
- Topics
- Health Sciences › Medicine › Epidemiology › Influenza Virus Research Studies
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
- Keywords
- influenza virus, sialidase inhibitors, neuraminidase, rational drug design, computer-aided drug design, antiviral agents, influenza treatment, prophylaxis, enzyme inhibition
- MeSH terms
- Animals, Antiviral Agents, Cell Line, Disease Models, Animal, Female, Ferrets, Guanidines, Humans, Influenza, Human, Models, Molecular, Neuraminidase, Influenza A virus, Viral Plaque Assay, Pyrans, Sheep, Sialic Acids, Virus Replication, Drug Design, Computer-Aided Design, Mice, Zanamivir
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review