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• W2058659664 abstract "The p53 protein, a guardian of the genome, is inactivated by mutations or deletions in approximately half of human tumors. While in the rest of human tumors, p53 is expressed in wild-type form, yet it is inhibited by over-expression of its cellular regulators MDM2 and MDMX proteins. Although the p53-binding sites within the MDMX and MDM2 proteins are closely related, known MDM2 small-molecule inhibitors have been shown experimentally not to bind to its homolog, MDMX. As a result, the activity of these inhibitors including Nutlin3 is compromised in tumor cells over-expressing MDMX, preventing these compounds from fully activating the p53 protein. Here, we applied the relaxed complex scheme (RCS) to allow for the full receptor flexibility in screening for dual-inhibitors that can mutually antagonize the two p53-regulator proteins. First, we filtered the NCI diversity set, DrugBank compounds and a derivative library for MDM2-inhibitors against 28 dominant MDM2-conformations. Then, we screened the MDM2 top hits against the binding site of p53 within the MDMX target. Results described herein identify a set of compounds that have been computationally predicted to ultimately activate the p53 pathway in tumor cells retaining the wild-type protein." @default.
• W2058659664 created "2016-06-24" @default.
• W2058659664 creator A5026525918 @default.
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• W2058659664 date "2010-02-01" @default.
• W2058659664 modified "2023-09-27" @default.
• W2058659664 title "Ensemble-based virtual screening reveals dual-inhibitors for the p53–MDM2/MDMX interactions" @default.
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• W2058659664 doi "https://doi.org/10.1016/j.jmgm.2009.12.003" @default.
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• W2058659664 hasPublicationYear "2010" @default.
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