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dc.contributor.authorT. Oberg, Christopheren_US
dc.contributor.authorBlanchard, Helenen_US
dc.contributor.authorLeffler, Hakonen_US
dc.contributor.authorJ. Nilsson, Ulfen_US
dc.date.accessioned2017-05-03T14:15:04Z
dc.date.available2017-05-03T14:15:04Z
dc.date.issued2008en_US
dc.date.modified2011-06-09T22:41:13Z
dc.identifier.issn0960894Xen_US
dc.identifier.doi10.1016/j.bmcl.2008.05.066en_AU
dc.identifier.urihttp://hdl.handle.net/10072/21598
dc.description.abstractA series of O2 and O3-derivatized methyl ߭d-talopyranosides were synthesized and evaluated in vitro as inhibitors of the galactose-binding galectin-1, -2, -3, -4 (N- and C-terminal domains), 8 (N-terminal domain), and 9 (N-terminal domain). Galectin-4C and 8N were found to prefer the d-talopyranose configuration to the natural ligand d-galactopyranose configuration. Derivatization at talose O2 and/or O3 provided selective submillimolar inhibitors for these two galectins.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherElsevieren_US
dc.publisher.placeUnited Kingdomen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom3691en_US
dc.relation.ispartofpageto3694en_US
dc.relation.ispartofissue13en_US
dc.relation.ispartofjournalBioorganic and Medicinal Chemistry Lettersen_US
dc.relation.ispartofvolume18en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchcode250302en_US
dc.titleProtein subtype-targeting through ligand epimerization: Talose-selectivity of galectin-4 and galectin-8en_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2008
gro.hasfulltextNo Full Text


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