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• W2529451330 endingPage "a026484" @default.
• W2529451330 startingPage "a026484" @default.
• W2529451330 abstract "The dynamic regulation of covalent modifications to histones is essential for maintaining genomic integrity and cell identity and is often compromised in cancer. Aberrant expression of histone lysine demethylases has been documented in many types of blood and solid tumors, and thus demethylases represent promising therapeutic targets. Recent advances in high-throughput chemical screening, structure-based drug design, and structure-activity relationship studies have improved both the specificity and the in vivo efficacy of demethylase inhibitors. This review will briefly outline the connection between demethylases and cancer and will provide a comprehensive overview of the structure, specificity, and utility of currently available demethylase inhibitors. To date, a select group of demethylase inhibitors is being evaluated in clinical trials, and additional compounds may soon follow from the bench to the bedside." @default.
• W2529451330 created "2016-10-14" @default.
• W2529451330 creator A5051695126 @default.
• W2529451330 creator A5067072554 @default.
• W2529451330 creator A5079320246 @default.
• W2529451330 date "2016-10-06" @default.
• W2529451330 modified "2023-10-16" @default.
• W2529451330 title "Histone Lysine Demethylase Inhibitors" @default.
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