Selective inhibition of glycosyltransferases by bivalent imidazolium salts

…, JZ Vlahakis, WA Szarek, I Brockhausen

文献索引：Gao, Yin; Vlahakis, Jason Z.; Szarek, Walter A.; Brockhausen, Inka Bioorganic and Medicinal Chemistry, 2013 , vol. 21, # 5 p. 1305 - 1311

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被引用次数: 16

摘要

Galactosyltransferases (GalTs) extend the glycan chains of mammalian glycoproteins by adding Gal to terminal GlcNAc residues, and thus build the scaffolds for biologically important glycan structures. We have shown that positively charged bivalent imidazolium salts in which the two imidazolium groups are linked by an aliphatic chain of 20 or 22 carbons form potent inhibitors of purified human β3-GalT5, using GlcNAcβ-benzyl as ...