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E. B. Fauman, J. P. Cogswell, B. Lovejoy, W. J. Rocque, W. Holmes, V. G. Montana, H. Piwnica-Worms, M. J. Rink and M. A. Saper, “Crystal Structure of the Catalytic Domain of the Human Cell Cycle Control Phosphatase, Cdc25A,” Cell, Vol. 93, No. 4, 1998, pp. 617-625. doi:10.1016/S0092-8674(00)81190-3

has been cited by the following article:

• TITLE: The Complementarity Effect for Cdc25 Phosphatase Inhibitors

  AUTHORS: Wassila Soufi, Meriem Merad, Faïza Boukli, Saïd Ghalem

  KEYWORDS: Cancer, Cdc25 Phosphatase, Molecular Modeling (MM, DM, and Docking), Naphtoquinone

  JOURNAL NAME: Advances in Molecular Imaging, Vol.1 No.2, August 5, 2011

  ABSTRACT: Cdc25 phosphatase have been regarded as attractive drug targets for anticancer therapies due to the correlation of their over expression with a wide variety of cancers. They are key regulators of cell cycle progression and play a central role in the checkpoint response to DNA damage. The role of Cdc25 s in cancer has become increasingly evident in recent years. More than 20 studies of patient samples are from diverse cancers show significant overexpression of Cdc25 with frequent correlation to clinical outcome. Recent screening and design efforts have yielded novel classes of inhibitors that show specificity for the Cdc25 s over other phosphatases and cause cell cycle arrest in vivo. Until now, quinone derivatives are among the most efficient inhibitors of Cdc25 phosphatase activity. Our research objective is to study the inhibition of the phosphathase Cdc25 through the molecular modeling methods.