Dr. Udeshi completed her PhD from the University of Virginia and completed her post-doctoral work at the Broad Institute where she has a strong focus in area of protein ubiquitination.

Protein ubiquitylation is a post-translational protein modification involved in a plethora of cellular processes, whereby ubiquitin moieties are transferred by ubiquitin ligases to distinct protein substrates. Defects in the ubiquitin system are at the root of many acquired and hereditary diseases. Because of the complex biology and transient nature of ubiquitin modifications, the field has lacked comprehensive and unbiased approaches to detect ubiquitin changes in disease-relevant settings and therapeutic approaches at the interface of ubiquitin ligases and their substrates. Antibodies directed at ubiquitin remnants (K-?-GG) have significantly improved the ability to monitor ubiquitylation in cell culture models using mass spectrometry. Using state-of-the art proteomic-based techniques, we are now able to measure >10,000 ubiquitylation sites from cell line and tissue samples. Using these techniques we have profiled drugs that potential target E3 ubiquitin ligase to elucidate their mechanism of action and identify important targets in cancer biology.