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dc.contributor.authorJohnson, LL
dc.contributor.authorHouston, TA
dc.date.accessioned2017-05-03T13:55:45Z
dc.date.available2017-05-03T13:55:45Z
dc.date.issued2002
dc.identifier.issn0040-4039
dc.identifier.doi10.1016/S0040-4039(02)02196-2
dc.identifier.urihttp://hdl.handle.net/10072/7014
dc.description.abstractBoronic acids were tethered to iminosugars in compounds such as 8 and 13 in order to increase their affinity for cell surfaces where glycoprotein processing enzymes are operative. Surprisingly, this modification diminished a-mannosidase inhibition while increasing ߭galactosidase inhibitory activity (8: Ki=2.0ױ0-4 M versus E. coli ߭galactosidase). The presence of a boronate in 8 and 13 has a profound impact on the specificity of this inhibition.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherPergamon
dc.publisher.placeUK
dc.relation.ispartofpagefrom8905
dc.relation.ispartofpageto8908
dc.relation.ispartofedition2002
dc.relation.ispartofjournalTetrahedron Letters
dc.relation.ispartofvolume43
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchOrganic chemistry
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode3405
dc.titleA drug targeting motif for glycosidase inhibitors: an iminosugar-boronate shows unexpectedly selective b-galactosidase inhibition
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2015-05-11T00:49:04Z
gro.hasfulltextNo Full Text
gro.griffith.authorHouston, Todd A.


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