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pubmed-article:9873734pubmed:abstractTextThis paper describes the discovery of glycosyl acceptor analogs as potent and selective inhibitors of alpha-1,3- and beta-1,4-galactosyltransferases. Incorporation of an appropriate aromatic group to the aglycon position of the enzyme's acceptors results in a strong inhibition, representing the first and most potent small uncharged molecules as selective inhibitors of these two enzymes and thus providing a new strategy for the development of selective glycosyltransferase inhibitors.lld:pubmed
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pubmed-article:9873734pubmed:authorpubmed-author:TakayamaSSlld:pubmed
pubmed-article:9873734pubmed:authorpubmed-author:WongC HCHlld:pubmed
pubmed-article:9873734pubmed:authorpubmed-author:ChungS JSJlld:pubmed
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pubmed-article:9873734pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:9873734pubmed:year1998lld:pubmed
pubmed-article:9873734pubmed:articleTitleAcceptor substrate-based selective inhibition of galactosyltransferases.lld:pubmed
pubmed-article:9873734pubmed:affiliationDepartment of Chemistry, Scripps Research Institute, La Jolla, CA 92037, USA.lld:pubmed
pubmed-article:9873734pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9873734pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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