A5041745808- Peptidase Inhibition and Analysis
- Ubiquitin and proteasome pathways
- Pancreatic and Hepatic Oncology Research
- Esophageal and GI Pathology
- Machine Learning in Healthcare
- Drug-Induced Adverse Reactions
- Clinical Nutrition and Gastroenterology
- Heparin-Induced Thrombocytopenia and Thrombosis
- Dysphagia Assessment and Management
- Gastrointestinal disorders and treatments
- Medical Imaging and Analysis
- Cancer-related gene regulation
- Pancreatitis Pathology and Treatment
- Autophagy in Disease and Therapy
- Cancer Immunotherapy and Biomarkers
Hospital of the University of Pennsylvania
2019-2024
University of Pennsylvania
2022-2023
Ludwig Cancer Research
2014-2015
University of California, San Diego
2015
A variety of cellular pathways are regulated by protein modifications with ubiquitin-family proteins. SUMO, the Small Ubiquitin-like MOdifier, is covalently attached to lysine on target proteins via a cascade reaction catalyzed E1, E2, and E3 enzymes. major barrier understanding diverse regulatory roles SUMO has been lack suitable methods identify sumoylation sites. Here we developed mass-spectrometry (MS) based approach combining chemical enzymatic We applied this method analyze...
Protein sumoylation is a reversible post‐translational modification that regulates nuclear processes including gene transcription, transport and DNA repair. Like ubiquitin, SUMO attached to the lysine side chains of target proteins via cascade E1‐activating, E2‐conjugating, E3‐ligating enzymes, it removed by SUMO‐specific isopeptidases. Hundreds are known be sumoylated in yeast saccharomyces cerevisiae, however, relatively little about precise site(s) most proteins. This due lack suitable...