Daiqing Liao, Ph.D.
Office: BSB B1-014
Phone: (352) 273-8188
Education and Training
Ph.D. – University of British Columbia, Canada (1993)
M.S. – Peking University, China (1986)
B.S. – Hunan University, China (1983)
Yale University School of Medicine (1994-1997)
Protein lysine acetyltransferases (KATs) catalyze the acetyl attachment to lysine side chains of protein substrates that include histones and many other cellular proteins. Deacetylases (HDACs) catalyze the reverse reaction to remove the attached acetyl group. Acetylation of protein substrates impacts their stability and functions in a variety of cellular pathways such as gene transcription, intracellular trafficking and metabolisms. Both KATs and HDACs are implicated in human diseases and represent rational therapeutic targets. The research in the Liao laboratory focuses on understanding cell-biological functions of these enzymes in virology, epigenetics and cancer biology, as well as on discovery, characterization, and optimization of novel small-molecule inhibitors of these enzymes for cancer therapy. In collaboration with the high-throughput screen facilities at Scripps Florida at Jupiter and the Sanford Burnham Medical Research Institute at Lake Nona, we aim at identifying novel lead KAT and HDAC inhibitors. We use in vitro biochemical as well as cell-based assays to validate their activities. We also collaborate with medicinal chemists to optimize the lead compounds to improve the target potency and specificity as well as drug-like properties of the lead compounds. We use mouse tumor models to determine in vivo anticancer efficacy of the small-molecule inhibitors. Ultimately, our optimized KAT and HDAC inhibitors may lead to novel therapy for treating cancer patients and other human diseases.
Wang, Y, Stowe, RL, Pinello, CE, Tian, G, Madoux, F, Li, D., Zhao, LY, Li, JL, Wang, Y, Wang, YR, Ma, H, Hodder, P, Roush, WR, and Liao, D (2015). Identification of HDAC Inhibitors with Benzoylhydrazide scaffold that Selectively Inhibit Class I HDACs. Chem Biol, 22(2):273-84. | PubMed
Yang, H, Salz, TH, Zajac-Kaye, M, Liao, D, Huang, S, and Qiu, Y (2014). The overexpression of histone deacetylases in cancer cells is controlled by interplay of transcription factors and epigenetic modulators. FASEB J, 28(10):4265-79. | PubMed
Santiago, A, Li, D, Zhao, LY, Godsey, AC, Liao D (2013). p53 SUMOylation promotes its nuclear export by facilitating its release from the nuclear export receptor CRM1. Mol. Biol. Cell, 24(17): 2739-2752. | PubMed
Yang H, Pinello CE, Luo J, Li D, Wang Y, Zhao LY, Jahn, SC, Saldanha, SA, Planck, J, Geary, KR, Ma, H, Law BK, Roush, WR, Hodder, P, Liao, D. Small-molecule inhibitors of acetyltransferase p300 identified by high-throughput screening are potent anticancer agents. Molecular Cancer Therapeutics. 2013; 12(5):610-20. (This article is the editors pick of the May 2013 issue of Molecular Cancer Therapeutics that has been determined a “must read” by the journal editors.) | Pubmed
Li Q, Zhao LY, Zheng Z, Yang H, Santiago A, Liao D. Inhibition of p53 by adenovirus type 12 E1B-55K deregulates cell cycle control and sensitizes tumor cells to genotoxic agents. J Virol. 2011; 85:7976-88. | Pubmed
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