i. Identification of novel MHC-I presented antigens for cancer vaccine development Developed a PROTAC-based screening platform for MHC-I presented antigen discovery Established automated protocols for MHC-I immunoprecipitations in medium-throughput Conducted immunopeptidomics studies to profile MHC-I presented peptides ii. Screening for compounds that upregulate surface MHC-I expression for enhanced immunotherapies Created an ELISA-based assay to assess the levels of surface MHC-I expression Screened compound libraries to discover small molecules that enhance MHC-I antigen presentation Proteotyped cells treated with MHC-I modulators to obtain mechanistic insights

i. Quantification of ubiquitin flux in live cells Developed SILOW Stable Isotopic Labeling with 18O-Water method to quantify flux of ubiquitination sites in yeast and human cells using LC-MS/MS Made first observations of proteome-wide ubiquitination site turnover in cells ii. Steady-state quantification of cellular ubiquitin in each major chemical form i.e. free, thioester - activated, substrate-conjugated Created and optimized protocols to derivitize ubiquitin Standardized fluorescence-based assays to quantify ubiquitin using an engineered binding protein