Dr. M.P.C. (Monique) Mulder

I am an independent group leader working at the interface between chemistry and cell biology to unravel the dynamic mechanisms of the multifaceted post-translational modification of substrate proteins by ubiquitin and ubiquitin-like proteins.

I completed my PhD in Medicinal Chemistry at Utrecht University in 2012. Following this work, I took advantage of my chemistry background as a postdoctoral researcher at the Netherlands Cancer Institute where I combined my expertise with a wide range of chemical biology techniques to interrogate the complex Ubiquitin Proteasome System .
This work, which continues to actively develop in my group at the LUMC, set the basis for our current studies on E3 ligases and the role of the ubiquitin proteasome system in neurodegeneration.

Besides my research activities I am a board member of the Young Faculty Network (YFN), manager of the Peptide Facility and a teacher for courses in the Biomedical Science Program.

In the Mulder lab, my team and I investigate the fascinating world of protein post-translational modification, with a special focus on ubiquitination. Our mission is to understand how ubiquitin directs the removal of misfolded proteins through the proteasome, a crucial step in maintaining cellular health and preventing the accumulation of harmful protein aggregates implicated in various diseases. Blending chemistry and cell biology, we investigate the enzymatic pathways responsible for tagging misfolded proteins with ubiquitin. By using synthetic tools like ubiquitin-based chemical probes, we can visualize transient ubiquitylation intermediates, which helps us identify potential targets for therapies. Additionally, we develop small molecules and methods to break down specific proteins, tapping into the power of the ubiquitin system to develop innovative treatments for diseases.
Our work is embedded within the LUMC Neuroscience and Academic Pharma themes for innovation.