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dc.contributor.authorvonItzstein, M
dc.contributor.authorDyason, JC
dc.contributor.authorOliver, SW
dc.contributor.authorWhite, HF
dc.contributor.authorWu, WY
dc.contributor.authorKok, GB
dc.contributor.authorPegg, MS
dc.date.accessioned2019-01-30T12:31:14Z
dc.date.available2019-01-30T12:31:14Z
dc.date.issued1996
dc.date.modified2009-04-17T05:30:50Z
dc.identifier.issn0022-2623
dc.identifier.doi10.1021/jm950294c
dc.identifier.urihttp://hdl.handle.net/10072/22239
dc.description.abstractThe development of sialidase inhibitor-based potential anti-influenza drugs using rational drug design techniques has been of recent interest. The present study details an investigation of the active site of influenza virus sialidase by using the program GRID in an attempt to design more potent inhibitors in the hope they will eventually lead to anti-influenza drugs. A number of different probes (amino, carboxy, hydroxy, methyl, etc.) have been used in an effort to determine the functional groups most likely to improve the binding of the starting template 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en). The data have correctly predicted the binding regions for the carboxylate, acetamido (NH and methyl), and glycerol (OH) groups of N-acetylneuraminic acid. Moreover, the data suggest that the addition of certain functionalities (amino group) at the C-4 position should enhance the overall binding.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherAmerican Chemical Society
dc.publisher.placeUnited States
dc.relation.ispartofpagefrom391
dc.relation.ispartofpageto399
dc.relation.ispartofissue2
dc.relation.ispartofjournalJournal of Medicinal Chemistry
dc.relation.ispartofvolume39
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchOrganic chemistry
dc.subject.fieldofresearchPharmacology and pharmaceutical sciences
dc.subject.fieldofresearchPharmacology and pharmaceutical sciences not elsewhere classified
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode3405
dc.subject.fieldofresearchcode3214
dc.subject.fieldofresearchcode321499
dc.titleA Study of the Active Site of Influenza Virus Sialidase: An Approach to the Rational Design of Novel Anti-influenza Drugs
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued1996
gro.hasfulltextNo Full Text
gro.griffith.authorvon Itzstein, Mark


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