M.S. Biology, Georgia State University, Atlanta, GA 2013
B.S. Biology, Georgia State University, Atlanta, GA 2011
Histone acetyltransferases (HATs) mediate the transfer of an acetyl group from the cofactor, acetyl-CoA, to the ε- amino group of specific lysines in diverse protein substrates, most notably nuclear histones. HATs are classified into several main families which include GCN5/PCAF, MYST, and CBP/p300 . The deregulation of HATs is connected to a number of disease states [2, 3]. Reliable and rapid biochemical assays for HATs are critical for understanding biological functions of protein acetylation, as well as for screening small-molecule inhibitors of HAT enzymes. I am interested in designing novel chemical biology tools and methods to detect HAT enzymatic activity.
Marmorstein, R., Structure and function of histone acetyltransferases. Cell Mol Life Sci, 2001. 58(5-6): p. 693-703.
Gusterson, R.J., et al., The Transcriptional Co-activators CREB-binding Protein (CBP) and p300 Play a Critical Role in Cardiac Hypertrophy That Is Dependent on Their Histone Acetyltransferase Activity. Journal of Biological Chemistry, 2003. 278(9): p. 6838-6847.
Isharwal, S., et al., p300 (histone acetyltransferase) biomarker predicts prostate cancer biochemical recurrence and correlates with changes in epithelia nuclear size and shape. The Prostate, 2008. 68(10): p. 1097-1104.
- Pharmaceutical and Biomedical Science outstanding Junior Graduate Student of the Year, 2015
- National Science Foundation Graduate Research Fellowship Program, 2015 – present
- Biotech scholars, 2011
- Molecular Basis of Disease Program, 2011
- Louis Stokes Alliances for Minority Participation (LSAMP), 2010