Rational design of potent sialidase-based inhibitors of influenza virus replication
- 1 June 1993
- journal article
- Published by Springer Nature in Nature
- Vol. 363 (6428) , 418-423
- https://doi.org/10.1038/363418a0
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.Keywords
This publication has 39 references indexed in Scilit:
- Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2·2 Å resolutionJournal of Molecular Biology, 1991
- Influenza virus sialidase: effect of calcium on steady-state kinetic parametersBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Emergence and Apparent Transmission of Rimantadine-Resistant Influenza A Virus in FamiliesNew England Journal of Medicine, 1989
- Crystallographic refinement by simulated annealingJournal of Molecular Biology, 1988
- The Thucydides SyndromeNew England Journal of Medicine, 1985
- Complete metal ion requirement of influenza virus N1 neuraminidasesArchiv für die gesamte Virusforschung, 1982
- Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolutionNature, 1981
- Neuraminidase: the specific enzyme of influenza virus and Vibrio choleraeBiochimica et Biophysica Acta, 1957
- MUCINS AND MUCOIDS IN RELATION TO INFLUENZA VIRUS ACTIONImmunology & Cell Biology, 1948
- ADSORPTION OF INFLUENZA HEMAGGLUTININS AND VIRUS BY RED BLOOD CELLSThe Journal of Experimental Medicine, 1942