| Literature DB >> 12369867 |
B M Gulledgea1, J B Aggena, H-B Huangb, A C Nairnc, A R Chamberlin.
Abstract
The serine/threonine phosphatases are inhibited by a variety of natural toxins, including the microcystins and nodularins. Progress in understanding the details of the biosynthetic origin and the binding of these compounds is discussed, as is the progress made in synthesizing the members of these families. Additionally, the work by several groups to either synthesize simplified analogues that are still potent, or introduce selectivity for PP1 over PP2A are discussed. Finally, the properties of a series of five new truncated analogues are examined.Entities:
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Year: 2002 PMID： 12369867 DOI： 10.2174/0929867023368845
Source DB: PubMed Journal: Curr Med Chem ISSN： 0929-8673 Impact factor: 4.530