The Microcystins and Nodularins: Cyclic Polypeptide Inhibitors of PP1 and PP2A

Authors: Gulledge B.M.; Aggen J.B.; Huang H..B.; Nairn A.C.; Chamberlin A.R.

Source: Current Medicinal Chemistry, Volume 9, Number 22, November 2002 , pp. 1991-2003(13)

Publisher: Bentham Science Publishers

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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

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929867023368845

Publication date: 2002-11-01

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Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.