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Recent development in the design of sialyltransferase inhibitors
Author(s) -
Wang Xiaofang,
Zhang LiHe,
Ye XinShan
Publication year - 2003
Publication title -
medicinal research reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.868
H-Index - 130
eISSN - 1098-1128
pISSN - 0198-6325
DOI - 10.1002/med.10030
Subject(s) - sialyltransferase , glycoconjugate , biochemistry , substrate specificity , enzyme , computational biology , immune system , biology , chemistry , immunology
Sialylation at the non‐reducing end of glycoconjugates is an important biological process in cellular recognitions, tumor metastases, and immune responses, which are mediated by a family of enzymes known as sialyltransferases. Inhibition of sialyltransferases may prove useful in elucidating the biological functions of sialylation and may have therapeutic applications. This review summarizes the recent development in this field with particular focus on the strategies used for the design of carbohydrate mimetics and the structure‐activity relationships of substrate‐based sialyltransferase inhibitors. © 2002 Wiley Periodicals, Inc. Med Res Rev, 23, No. 1, 32–47, 2003; Published online in Wiley InterScience ( www.interscience.wiley.com ). DOI 10.1002/med.10030