Proteins build the molecular workforce of our cells. Aberrations in the proteome, the entire set of proteins, as well as cellular signaling pathways are hallmarks of many diseases and a potential key to personalized therapies. Our research focuses on the development of new technologies to identify and quantify proteins and their post-translational modifications in cells, biofluids and tissues from clinical samples. In particular, we investigate the application of ion mobility mass spectrometry to increase the throughput, sensitivity and coverage of proteome analyses.

• µPhos: a scalable and sensitive platform for functional phosphoproteomics. Oliinyk D, Will A, Schneidmadel FR, Humphrey SJ, Meier F. bioRxiv (2023) https://doi.org/10.1101/2023.04.04.535617

Full list of publications (Google Scholar, ORCID)

• The social and structural architecture of the yeast protein interactome. Michaelis AC, Brunner A, Zwiebel M, Meier F, Strauss MT, Bludau I & Mann M. Nature (2023) https://doi.org/10.1038/s41586-023-06739-5
• Peptide collision cross sections of 22 post-translational modifications. Will A, Oliinyk D, Bleiholder C, Meier F. Anal. Bioanal. Chem. (2023) https://doi.org/10.1007/s00216-023-04957-4
• Ion mobility-resolved phosphoproteomics with dia-PASEF and short gradients. Oliinyk D & Meier F. Proteomics (2022) https://doi.org/10.1002/pmic.202200032
• Trapped Ion Mobility Spectrometry (TIMS) and Parallel Accumulation - Serial Fragmentation (PASEF) in Proteomics. Meier F, Park MA, Mann M. Molecular & Cellular Proteomics (2021) https://doi.org/10.1016/j.mcpro.2021.100138
• Deep learning the collisional cross sections of the peptide universe from a million experimental values. Meier F et al. Nature Communications (2021) https://doi.org/10.1038/s41467-021-21352-8
• diaPASEF: parallel accumulation–serial fragmentation combined with data-independent acquisition. Meier F et al. Nature Methods (2020) https://doi.org/10.1038/s41592-020-00998-0