Chapter title |
Identification and characterization of small-molecule inhibitors of lysine acetyltransferases.
|
---|---|
Chapter number | 28 |
Book title |
Cancer Epigenetics
|
Published in |
Methods in molecular biology, November 2014
|
DOI | 10.1007/978-1-4939-1804-1_28 |
Pubmed ID | |
Book ISBNs |
978-1-4939-1803-4, 978-1-4939-1804-1
|
Authors |
Liao D, Daiqing Liao, Liao, Daiqing |
Abstract |
Lysine acetyltransferases (KATs) acetylate various proteins including histones, transcription factors, metabolic enzymes, and other cellular substrates. Protein acetylation significantly impacts protein stability and function. Certain KATs such as p300 (KAT3B) are overexpressed in cancer cells and are linked to tumor progression and drug resistance. Thus, pharmacologic inhibition of KATs represents a new strategy for cancer therapy. Quantitative biochemical assays of KAT enzymatic activity have been developed and adapted for high-throughput screens of small-molecule compounds to discover specific KAT inhibitors. Such compounds are useful probes for understanding the cellular functions of these critical enzymes and importantly, they may be further developed as anticancer therapeutics. Here we describe a fluorescence-based KAT activity assay and cell-based validation of KAT inhibition by small-molecule compounds. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Unknown | 4 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 1 | 25% |
Professor > Associate Professor | 1 | 25% |
Student > Bachelor | 1 | 25% |
Researcher | 1 | 25% |
Readers by discipline | Count | As % |
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Biochemistry, Genetics and Molecular Biology | 2 | 50% |
Agricultural and Biological Sciences | 2 | 50% |