My research focuses on understanding how proteins are regulated through post-translational modifications (PTMs), such as SUMOylation. These modifications act like molecular switches, shaping key cellular processes by changing protein function, interactions, and stability.

In recent work, I helped develop a new search strategy in MaxQuant to better identify large, complex protein-based modifiers: what we call Sequence-Based Modifiers (SBMs). By accounting for their unique fragmentation patterns, our method significantly improves the detection of SUMO-modified peptides across different cell types and species.

This approach not only increases the accuracy of mass spectrometry data analysis, but also opens the door to deeper insights into how PTMs regulate cellular biology. Ultimately, my work aims to expand the toolkit for studying protein modifications and to uncover new layers of protein regulation in health and disease.

Publications

  • Lennartsson C, Kyriakidou P, Nielsen ML, Olsen JV, Cox J, Hendriks IA. (2025).
    Improved peptide search for identification of SUMO and sequence-based modifications, in MaxSBM.
    Published in bioRxiv, p. 2025.08.27.672604. Link to article

  • Lennartsson C, Hendriks IA. (2025).
    Native and endogenous SUMO site identification using mass spectrometry (NESSI-MS).
    In Methods in Molecular Biology. New York, NY: Springer US; p. 31–56. (Methods in molecular biology (Clifton, N.J.)). Link to article

  • Saar, Daniel, et al. (2024).
    The myotubularin related proteins and the untapped interaction potential of their disordered C-terminal regions.
    Published in Proteins, Wiley. Link to article

  • Rebak, Alexandra S., et al. (2024).
    A Quantitative and Site-Specific Atlas of the Citrullinome Reveals Widespread Existence of Citrullination and Insights into PADI4 Substrates.
    Published in Nature Structural & Molecular Biology, 31(6), 977–995. Link to article