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• W2156804885 abstract "The development of anticancer therapeutics that target Cdc25 phosphatases is now an active area of research. A complete understanding of the Cdc25 catalytic mechanism would certainly allow a more rational inhibitor design. However, the identity of the catalytic acid used by Cdc25 has been debated and not established unambiguously. Results of molecular dynamics simulations with a calibrated hybrid potential for the first reaction step catalyzed by Cdc25B in complex with its natural substrate, the Cdk2-pTpY/CycA protein complex, are presented here. The calculated reaction free-energy profiles are in very good agreement with experimental measurements and are used to discern between different proposals for the general acid. In addition, the simulations give useful insight on interactions that can be explored for the design of inhibitors specific to Cdc25." @default.
• W2156804885 created "2016-06-24" @default.
• W2156804885 creator A5002609699 @default.
• W2156804885 date "2008-11-04" @default.
• W2156804885 modified "2023-09-25" @default.
• W2156804885 title "The Catalytic Acid in the Dephosphorylation of the Cdk2-pTpY/CycA Protein Complex by Cdc25B Phosphatase" @default.
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• W2156804885 doi "https://doi.org/10.1021/jp8070019" @default.
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