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dc.contributor.authorMohan, Sankar
dc.contributor.authorPinto, B Mario
dc.date.accessioned2020-06-17T22:26:06Z
dc.date.available2020-06-17T22:26:06Z
dc.date.issued2018
dc.identifier.issn0008-4042
dc.identifier.doi10.1139/cjc-2017-0343
dc.identifier.urihttp://hdl.handle.net/10072/394692
dc.description.abstractInfluenza pandemics are an ongoing threat for the human population, as the avian influenza viruses H5N1 and H7N9 continue to circulate in the bird population and the chance of avian to human transmission increases. Neuraminidase, a glycoprotein located on the surface of the influenza virus, plays a crucial role in the viral replication process and, hence, has proven to be a useful target enzyme for the treatment of influenza infections. The discovery that certain subtypes of influenza neuraminidase have an additional cavity, the 150 cavity, near the substrate binding site has triggered considerable interest in the design of influenza inhibitors that exploit this feature. Currently available antiviral drugs, neuraminidase inhibitors oseltamivir and zanamivir, were designed using crystal structures predating this discovery by some years. This mini review is aimed at summarizing our group’s efforts, together with related work from other groups, on neuraminidase inhibitors that are designed to exploit both the catalytic site and the 150 cavity. The design of a parent scaffold that yields a potent inhibitor that is active in cell culture assays and retains activity against several neuraminidases from mutant strains is also described. Finally, the role of serendipity in the discovery of a new class of potent neuraminidase inhibitors with a novel spirolactam scaffold is also highlighted.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherCanadian Science Publishing
dc.relation.ispartofpagefrom91
dc.relation.ispartofpageto101
dc.relation.ispartofissue2
dc.relation.ispartofjournalCanadian Journal of Chemistry
dc.relation.ispartofvolume96
dc.subject.fieldofresearchChemical Sciences
dc.subject.fieldofresearchcode03
dc.titleExploration of the 150 cavity and the role of serendipity in the discovery of inhibitors of influenza virus A neuraminidase
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationMohan, S; Pinto, BM, Exploration of the 150 cavity and the role of serendipity in the discovery of inhibitors of influenza virus A neuraminidase, Canadian Journal of Chemistry, 2018, 96 (2), pp. 91-101
dc.date.updated2020-06-16T23:38:11Z
dc.description.versionAccepted Manuscript (AM)
gro.rights.copyright© The Author(s) 2018. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
gro.hasfulltextFull Text
gro.griffith.authorPinto, Mario M.


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