Aging and major diseases such as cancer and neurodegeneration are intimately linked to genomic instability and epigenomic dysregulation, with post-translational modifications of histones and their regulatory enzymes playing a pivotal role. Histones, integral components of chromosomes, regulate DNA folding structure and gene transcription through the formation of nucleosomes. These histones undergo a variety of post-translational modifications, such as lysine acylation, methylation, ubiquitination, and serine phosphorylation. The complexity of their combinatorial patterns and the extensive enzymatic control over these processes have not been fully understood to this day.
 
Our research group employs methods from synthetic chemistry, chemical biology, biochemistry, structural biology, and cell biology to delve into the molecular mechanisms of diseases from the perspective of molecular structure and function. This aids in the development of novel small molecule inhibitors or agonists as potential strategies for treating related diseases. Concurrently, we are dedicated to advancing innovative protein chemistry techniques to address some of the challenging questions in the field of life sciences.