Dual-Specificity Phosphatase CDC25A/B Inhibitor Identified from a Focused Library with Nonelectrophilic Core Structure | Zendy

Ayako Tsuchiya | Zendy; Go Hirai | Zendy; Yusuke Koyama | Zendy; Kana Oonuma | Zendy; Yuko Otani | Zendy; Hiroyuki Osada | Zendy; Mikiko Sodeoka | Zendy

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Dual-Specificity Phosphatase CDC25A/B Inhibitor Identified from a Focused Library with Nonelectrophilic Core Structure

Author(s) -

Ayako Tsuchiya,

Go Hirai,

Yusuke Koyama,

Kana Oonuma,

Yuko Otani,

Hiroyuki Osada,

Mikiko Sodeoka

Publication year - 2012

Publication title -

acs medicinal chemistry letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.065

H-Index - 66

ISSN - 1948-5875

DOI - 10.1021/ml2002778

Subject(s) - cdc25a , dephosphorylation , phosphatase , chemistry , cyclin dependent kinase 1 , derivative (finance) , biochemistry , enzyme , cell cycle , cell , cell cycle checkpoint , financial economics , economics

Focused libraries of enamine derivatives with a nonacidic, nonelectrophilic core structure were screened for inhibitors of dual-specificity protein phosphatases, and an o-hydroxybenzyl derivative RE44 (10d) was identified as a selective inhibitor of CDC25A/B. This inhibitor induced cell-cycle arrest of tsFT210 cells at the G2/M phase and inhibited dephosphorylation of the CDC25B substrate CDK1. Unlike most quinone-based inhibitors, 10d does not generate reactive oxygen species.

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