Molecular events regulating O-GlcNAcylation during heart injury• Optimized techniques for the quantitative assessment of intracellular glycosylation in murine hearts by both immunobloting and galactosyltransferase labeling/click chemistry. • Investigated signaling pathways that regulate intracellular glycosylation in male and female murine hearts in response to injury by biochemical approaches.• Performed radiolabelled and fluorescence-based assays detecting enzymatic activity of intracellular glycosyltransferases and hexosaminidases.• Extracted and quantitatively assessed the levels of nucleotide sugars in murine hearts using high-performance anion exchange chromatography (HPAEC) techniques.• Performed perfusions on murine hearts ex-vivo using the Langendorff apparatus to collect hearts exposed to ischemia and ischemia/reperfusion injury.• These findings led to two first-author publications - Analytical Biochemistry and Journal of Biological Chemistry and a second-author publication - Current Protocols. • Authored a book chapter in Encyclopedia of Cell Biology on the regulation of cell physiology by O-GlcNAc and published a review as a second-author in Comprehensive Glycoscience. • Mentored and trained two graduate students and a post-doctoral fellow on several biochemical & molecular biology techniques.Validation of potential positive regulators of the CARD11 dependent NF-kB activation pathway•Used CRISPR/Cas9 system to knockout potential positive regulators of the NF-kB pathway and measured the activation of NF-kB using fluorescence-activated cell sorting (FACS).Validation of potential substrates of UBE3A, an E3 ubiquitin ligase, to better understand Angelman syndrome.• Compared protein expression by western blot to identify potential substrates of UBE3A in mouse models to identify novel mechanisms by which defects in UBE3A lead to Angelman syndrome.

Structure-Activity relationship of Efavirenz mediated activation of the Pregnane X Receptor• Cloned and purified the human Pregnane X Receptor ligand-binding domain tethered to a co-activator, SRC1 peptide (PXR-lbd-SRC1), through a pentapeptide linker.• Performed isothermal titration calorimetry to determine the thermodynamic parameters of Pregnane X Receptor interaction with different efavirenz analogs in solution.• Used Time-Resolved FRET analysis to determine the differences in binding affinity of efavirenz and its analogues to PXR. • Performed molecular docking simulations of efavirenz and its various analogues on PXR-lbd-SRC1, which identified the underlying cause of divergence in activation of PXR by efavirenz and its primary metabolite, 8-OH efavirenz.• Grew crystals of protein-drug complexes using vapor diffusion crystallization techniques.• Mounted crystals to an X-ray generator and collected X-ray diffraction data sets.• Translated X-ray diffraction data into 3-D models to determine structural determinants of binding and transcriptional activation of PXR by different efavirenz analogs.• These findings contributed to my Master's thesis project and led to a first-author publication in ChemMedChem.