Chemical Approaches for Modulating Lysine Post-Translational Modifications, by George Burslem, PhD, Assistant Professor of Biochemistry and Biophysics, University of Pennsylvania, School of Medicine

George Burslem, PhD, Assistant Professor of Biochemistry and Biophysics, University of Pennsylvania, School of Medicine
George Burslem, PhD, Assistant Professor of Biochemistry and Biophysics, University of Pennsylvania, School of Medicine

 

The Department of Chemistry Presents, via In Person and Online Zoom Presentation:  George Burslem, PhD, Assistant Professor of Biochemistry and Biophysics, University of Pennsylvania, School of Medicine

This is an online and in-person seminar

Post-translational modifications (PTMs) are key modulators of protein function and are crucial for the successful function of a cell. They can act as methods for signal transduction, alter the localization of a protein or signal that a protein is no longer required, as well as many other functions. Research in the Burslem lab employs a highly interdisciplinary approach to develop chemical tools to interrogate and modulate two important classes of post-translational modifications at lysine side chains, namely ubiquitination and acetylation.

This talk will focus on the development of chemical tools to modulate PTMs relevant to disease. The first half of the talk will focus on the use of heterobifunctional compounds to induce specific PTMs, for example ubiquitination for targeted protein degradation. The second half will focus the development of new compound libraries and approaches for the identification of inhibitors of lysine PTM editing enzymes. 

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