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- W2042665557 endingPage "4760" @default.
- W2042665557 startingPage "4739" @default.
- W2042665557 abstract "Protein phosphatases, as the counterpart to protein kinases, are essential for homeostatic balance of cell signaling. Small chemical compounds that modulate the specific activity of phosphatases can be powerful tools to elucidate the biological functions of these enzymes. More importantly, many phosphatases are central players in the development of pathological pathways where inactivation can reverse or delay the onset of human diseases. Therefore, potent inhibitors for such phosphatases can be of great therapeutic benefit. In contrast to the seemingly identical enzymatic mechanism and structural characterization of eukaryotic protein kinases, protein phosphatases evolved from diverse ancestors, resulting in different domain architectures, reaction mechanisms and active site properties. In this review, we discuss for each family of serine/threonine protein phosphatases their involvement in biological processes and corresponding strategies for small chemical intervention. Recent advances in modern drug discovery technologies have markedly facilitated the identification of selective inhibitors for some members of the phosphatase family. Furthermore, the rapid growth in knowledge about structure-activity relationships related to possible new drug targets has aided the discovery of natural product inhibitors for the phosphatase family. This review summarizes the current state of investigation of the small molecules that regulate the function of serine/threonine phosphatases, the challenges presented and also strategies to overcome these obstacles." @default.
- W2042665557 created "2016-06-24" @default.
- W2042665557 creator A5050112368 @default.
- W2042665557 creator A5063087410 @default.
- W2042665557 creator A5077042443 @default.
- W2042665557 creator A5085239188 @default.
- W2042665557 creator A5086664284 @default.
- W2042665557 date "2013-09-05" @default.
- W2042665557 modified "2023-09-27" @default.
- W2042665557 title "Viewing serine/threonine protein phosphatases through the eyes of drug designers" @default.
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