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Most of the 25,000 genes identified in the human genome are alternatively spliced, and their protein products are often modified post-translationally to offer functional diversities to living cells. These processes include ubiquitination, phosphorylation, methylation, acetylation and many others.
On the other hand, aberrant cell signaling events caused by dysregulated protein modifications often lead to altered protein homeostasis and cellular functions, facilitating the development of cancer and other human disorders. These modifications and their functional interaction play a key role in governing tumorigenesis. Inhibitors that target these key cell fate enzymatic regulators — including kinases, E3 ligases, methyltransferases and acetyltransferases — have attracted extensive attention as biomarkers and anti-cancer drug targets.
The major focus of the Cancer Research Institute's Biochemistry Program is to understand how aberrant cell signaling pathways affect cell cycle regulation, and how they lead to genomic instability and subsequent tumorigenesis. Ultimately, we hope that a deeper mechanistic understanding of these critical cell fate regulators will guide the development of novel therapeutic approaches to combating cancer and other human disorders.