Mechanism-based Inactivation of Prostatic Acid Phosphatase
Authors
Affiliations
Protein phosphatases play important roles in the regulation of cell growth and metabolism, yet little is known about their enzymatic mechanism. By extrapolation from data on inhibitors of other types of hydrolases, an inhibitor of prostatic acid phosphatase was designed that is likely to function as a mechanism-based phosphotyrosine phosphatase inactivator. This molecule, 4-(fluoromethyl)phenyl phosphate, represents a useful paradigm for the design of potent and specific phosphatase inhibitors.
Proximitomics by Reactive Species.
Zhang S, Tang Q, Zhang X, Chen X ACS Cent Sci. 2024; 10(6):1135-1147.
PMID: 38947200 PMC: 11212136. DOI: 10.1021/acscentsci.4c00373.
Noninvasive NIR Imaging of Senescence Labeling.
Liu J, Ma X, Cui C, Chen Z, Wang Y, Deenik P J Med Chem. 2021; 64(24):17969-17978.
PMID: 34752102 PMC: 10880455. DOI: 10.1021/acs.jmedchem.1c01313.
Li Y, Song H, Xue C, Fang Z, Xiong L, Xie H Chem Sci. 2020; 11(23):5889-5894.
PMID: 32874510 PMC: 7449546. DOI: 10.1039/d0sc01273d.
Long Wavelength TCF-Based Fluorescent Probe for the Detection of Alkaline Phosphatase in Live Cells.
Gwynne L, Sedgwick A, Gardiner J, Williams G, Kim G, Lowe J Front Chem. 2019; 7:255.
PMID: 31119120 PMC: 6508040. DOI: 10.3389/fchem.2019.00255.
Covalent inhibition of protein tyrosine phosphatases.
Ruddraraju K, Zhang Z Mol Biosyst. 2017; 13(7):1257-1279.
PMID: 28534914 PMC: 5663200. DOI: 10.1039/c7mb00151g.