A Targeted Library of Small-Molecule, Tyrosine, and Dual-Specificity Phosphatase Inhibitors Derived from a Rational Core Design and Random Side Chain Variation†

Biochemistry ◽  
1997 ◽  
Vol 36 (50) ◽  
pp. 15965-15974 ◽  
Author(s):  
Robert L. Rice ◽  
James M. Rusnak ◽  
Fumiaki Yokokawa ◽  
Shiho Yokokawa ◽  
Donald J. Messner ◽  
...  
Keyword(s):  
Small Molecule ◽  
Side Chain ◽  
Phosphatase Inhibitors ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity ◽  
Targeted Library

Identification of new Cdc25 dual specificity phosphatase inhibitors in a targeted small molecule array

2000 ◽  
Vol 8 (6) ◽  
pp. 1451-1466 ◽  
Author(s):  
Alexander P Ducruet ◽  
Robert L Rice ◽  
Kenji Tamura ◽  
Fumiaki Yokokawa ◽  
Shiho Yokokawa ◽  
...  
Keyword(s):  
Small Molecule ◽  
Phosphatase Inhibitors ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity

scholarly journals Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate

2015 ◽  
Vol 71 (2) ◽  
pp. 199-205 ◽  
Author(s):  
George T. Lountos ◽  
Scott Cherry ◽  
Joseph E. Tropea ◽  
David S. Waugh
Keyword(s):  
Crystal Structure ◽  
Structural Analysis ◽  
Phosphatase Activity ◽  
Small Molecule ◽  
Molecular Basis ◽  
Protein Tyrosine Phosphatases ◽  
Simple Method ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity ◽  
Nitrophenyl Phosphate

4-Nitrophenyl phosphate (p-nitrophenyl phosphate, pNPP) is widely used as a small molecule phosphotyrosine-like substrate in activity assays for protein tyrosine phosphatases. It is a colorless substrate that upon hydrolysis is converted to a yellow 4-nitrophenolate ion that can be monitored by absorbance at 405 nm. Therefore, the pNPP assay has been widely adopted as a quick and simple method to assess phosphatase activity and is also commonly used in assays to screen for inhibitors. Here, the first crystal structure is presented of a dual-specificity phosphatase, human dual-specificity phosphatase 22 (DUSP22), in complex with pNPP. The structure illuminates the molecular basis for substrate binding and may also facilitate the structure-assisted development of DUSP22 inhibitors.

scholarly journals Cdc25B Dual-Specificity Phosphatase Inhibitors Identified in a High-Throughput Screen of the NIH Compound Library

2009 ◽  
Vol 7 (3) ◽  
pp. 250-265 ◽  
Author(s):  
Paul A. Johnston ◽  
Caleb A. Foster ◽  
Marni Brisson Tierno ◽  
Tong Ying Shun ◽  
Sunita N. Shinde ◽  
...  
Keyword(s):  
High Throughput ◽  
High Throughput Screen ◽  
Compound Library ◽  
Phosphatase Inhibitors ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity

Cell-Active Dual Specificity Phosphatase Inhibitors Identified by High-Content Screening

2003 ◽  
Vol 10 (8) ◽  
pp. 733-742 ◽  
Author(s):  
Andreas Vogt ◽  
Kathleen A Cooley ◽  
Marni Brisson ◽  
Michael G Tarpley ◽  
Peter Wipf ◽  
...  
Keyword(s):  
High Content Screening ◽  
Phosphatase Inhibitors ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity

Identification of a Potent and Selective Pharmacophore for Cdc25 Dual Specificity Phosphatase Inhibitors.

2002 ◽  
Vol 61 (4) ◽  
pp. 720-728 ◽  
Author(s):  
John S. Lazo ◽  
Kaoru Nemoto ◽  
Katharine E. Pestell ◽  
Kathleen Cooley ◽  
Eileen C. Southwick ◽  
...  
Keyword(s):  
Phosphatase Inhibitors ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity

CDC25A and B Dual-Specificity Phosphatase Inhibitors: Potential Agents for Cancer Therapy

2009 ◽  
Vol 16 (15) ◽  
pp. 1831-1849 ◽  
Author(s):  
Antonio Lavecchia ◽  
Carmen Di Giovanni ◽  
Ettore Novellino
Keyword(s):  
Cancer Therapy ◽  
Phosphatase Inhibitors ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity

Discovery and Characterization of Novel Small Molecule Inhibitors of Human Cdc25B Dual Specificity Phosphatase

2004 ◽  
Vol 66 (4) ◽  
pp. 824-833 ◽  
Author(s):  
Marni Brisson ◽  
Theresa Nguyen ◽  
Andreas Vogt ◽  
Jack Yalowich ◽  
Angela Giorgianni ◽  
...  
Keyword(s):  
Small Molecule ◽  
Small Molecule Inhibitors ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity
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