Proceedings of the National Academy of Sciences of the United States of America

About the PNAS Member Editor
Name Schulman, Brenda A.
Location Max Planck Institute of Biochemistry
Primary Field Biochemistry
 Election Citation
Schulman discovered key components and critical features of structural mechanisms of ubiquitin-like (UBL) conjugation, including activation by E1 enzymes, ligation of NEDD8, and mechanisms that activate RING E3 ligase activity of the largest family of ubiquitin ligases. She also demonstrated how N-terminal acetylation of proteins can mediate protein interactions.
 Research Interests
Brenda Schulman's lab studies how proteins and lipids are regulated by becoming covalently linked to the small protein ubiquitin or to structurally related ubiquitin-like proteins (UBLs). This is a widespread mechanism controlling timing, subcellular location, assembly, conformation, and activity of thousands of different human proteins and macromolecules. Defects in ubiquitin and UBL pathways have been associated with numerous diseases, including cancers, neurodegenerative disorders, and viral infections. Thus, understanding mechanisms underlying regulation by ubiquitin and UBLs is of broad importance for understanding signaling pathways and targeting them in diseases. The Schulman lab attacks this problem by integrating top-down and bottom-up mechanistic approaches incorporating cell biology, genetics, biochemistry, chemistry, and structural biology. Schulman is recognized for illuminating the mechanisms of ubiquitin and UBL ligation, and for distinctive biochemical approaches to identify novel in vivo regulatory pathways.

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