Shourya S. Roy Burman

Dana-Farber Cancer Institute and Harvard Medical School

Shourya S. Roy Burman is a research fellow at Dana-Farber Cancer Institute and Harvard Medical School. As a member of Dr. Eric Fischer’s group, he designs new systems for targeted protein degradation using computational modeling and design, biophysical and biochemical techniques, and flow cytometry. He is the recipient of the Cancer Research Institute Irvington Postdoctoral Fellowship for his research on the use of compound-mediated protein degradation in cell therapies. Dr. Roy Burman obtained his PhD in Chemical and Biomolecular Engineering from Jeffrey Gray’s group at the Johns Hopkins University, where he developed algorithms for protein modeling as a part of the Rosetta Macromolecular Modeling Suite. Prior to that, he received his bachelor’s degree in Bioengineering from the Indian Institute of Technology Kanpur. Dr. Roy Burman’s research identified that the position of ubiquitinatable lysines on a target protein in a ternary complex with the E3 ubiquitin ligase is the single most important intrinsic feature that determines its tractability to targeted degradation approaches. His protein docking algorithms have been widely used to model degrader-induced complexes and guide the design of new molecules.

Mikołaj Słabicki

Broad Institute and Dana-Farber Cancer Institute

Mikołaj Słabicki is a Group Leader in the Program at the Broad Institute, a member of Dr. Benamin Ebert’s Laboratory, and a Senior Staff Scientist at the Dana-Farber Cancer Institute. Dr. Słabicki employs functional genomics, high-throughput screening, chemical biology, cell biology, and biochemical techniques to identify and characterize new molecular glue degraders and novel mechanisms of targeted protein degradation. Dr. Słabicki is a founding co-organizer of the Dana-Farber Targeted Protein Degradation Webinar series that features biweekly talks from experts in the field. Dr. Słabicki’s research expanded the repertoire of molecular glue degraders and showed that the CDK inhibitor, CR8, induced degradation of cyclin K without a canonical substrate receptor. His research also identified an alternative mechanism of targeted protein degradation, in which a small molecule, BI-3802, induces the highly specific, reversible polymerization and subsequent degradation of the transcription repressor BCL6. Dr. Słabicki graduated with an M.S. in Biotechnology from the Technical University of Łódź, in Poland and completed his PhD under the guidance of Dr. Frank Buchholz at the Max Planck Institute of Molecular Cell Biology and Genetics in Dresden, Germany. Dr. Słabicki completed his post-doctoral research as a Marie Skłodowska Curie Scholar in Dr. Benjamin Ebert’s laboratory at the Dana-Farber Institute in Boston, United States, and in Stefan Fröhling’s laboratory at the German Research Center in Heidelberg, Germany.

Luke Simpson

The University of Dundee

Luke Simpson is a Cell Biology Scientist in the Centre for Targeted Protein Degradation (CeTPD) at the University of Dundee, UK, as part of the PROTAC Drug Discovery collaboration between Professor Alessio Ciulli and Boehringer Ingelheim (AC-BI). Luke’s work involves the development, optimisation, and implementation of cell-based assays to robustly profile and characterise novel protein degraders. To investigate each stage of the degradation cascade and aid in rational degrader design, Luke and his team employ various cell-based technologies to analyse PROTAC target engagement, ternary complex formation, ubiquitylation, degradation kinetics, and mechanism of action. Previously, Luke completed his MSc in Biomedical Science at the University of Aberdeen, UK, and his PhD in the Medical Research Council Protein Phosphorylation & Ubiquitylation (MRC PPU) Unit at the University of Dundee under the supervision of Professor Gopal Sapkota and Dr. Ian Ganley. Here, Luke’s doctoral research centred around exploring technologies for targeted protein modification and involved combining nanobody- and PROTAC-based technologies for targeted protein degradation.