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.
Keywords: Microcystins, PP1, PP2A, threonine phosphatases
Current Medicinal Chemistry
Title: The Microcystins and Nodularins: Cyclic Polypeptide Inhibitors of PP1 and PP2A
Volume: 9 Issue: 22
Author(s): B. M. Gulledge, J. B. Aggen, H.- B. Huang, A. C. Nairn and A. R. Chamberlin
Affiliation:
Keywords: Microcystins, PP1, PP2A, threonine phosphatases
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.
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Cite this article as:
Gulledge M. B., Aggen B. J., Huang B. H.-, Nairn C. A. and Chamberlin R. A., The Microcystins and Nodularins: Cyclic Polypeptide Inhibitors of PP1 and PP2A, Current Medicinal Chemistry 2002; 9 (22) . https://dx.doi.org/10.2174/0929867023368845
DOI https://dx.doi.org/10.2174/0929867023368845 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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