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• W8436765 abstract "Affinity alkylating derivatives of naturally occurring molecules were originally developed to target and probe the substrate/ligand-binding sites of enzymes and receptors. These reagents, by virtue of their ability to covalently attach to the substrate/ligand-binding pockets of target enzymes/receptors, provide valuable structural information of the host and the guest, focusing on the dynamic interaction between the two. Our laboratory developed affinity and photoaffinity labeling derivatives of 1,25-dihydroxyvitamin D3 [1,25(OH)2D] to probe the ligand-binding domain of nuclear vitamin D receptor (VDR). With these studies we obtained crucial information about the ligand contact points and three-dimensional geometry of the ligand-binding domain of VDR, in relation to the biological properties of 1,25(OH)2D. 1,25(OH)2D is an anticancer agent, albeit with severe toxicity at pharmacological doses. We observed that an affinity alkylating derivative of 1,25(OH)2D strongly inhibits the growth of various cancer cells and causes these cells to undergo apoptosis, demonstrating strong potential of this affinity analog of 1,25(OH)2D as an anticancer agent. This article summarizes the results of various studies involving affinity alkylating derivatives of vitamin D metabolites to investigate structural–functional aspects of VDR, as well as development of these reagents as potential therapeutic agents in cancer." @default.
• W8436765 created "2016-06-24" @default.
• W8436765 creator A5083027908 @default.
• W8436765 date "2010-01-01" @default.
• W8436765 modified "2023-09-23" @default.
• W8436765 title "Affinity Alkylating Vitamin D Analogs as Molecular Probes and Therapeutic Agents" @default.
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• W8436765 doi "https://doi.org/10.1007/978-1-60327-303-9_58" @default.
• W8436765 hasPublicationYear "2010" @default.
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