Reactivity of Cdc25 phosphatase at low pH and with thiophosphorylated protein substrate
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Drug Discovery,Molecular Biology,Biochemistry
Reference37 articles.
1. Transfer of the PO32- group, comprehensive biological catalysis: A mechanistic reference,1998
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1. Mechanism of Cdc25B Phosphatase with the Small Molecule Substrate p-Nitrophenyl Phosphate from QM/MM-MFEP Calculations;The Journal of Physical Chemistry B;2009-03-20
2. Cdc25 Phosphatases: Structure, Specificity, and Mechanism;Biochemistry;2007-03-01
3. Temperature dependence of binding and catalysis for the Cdc25B phosphatase;Biophysical Chemistry;2007-02
4. Experimental Validation of the Docking Orientation of Cdc25 with Its Cdk2−CycA Protein Substrate;Biochemistry;2005-11-24
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