Department of Molecular Sociology (MS)
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Protein complexes are a fundamental organisational unit of the proteome. They are functionally fine-tuned towards context-specific needs, i.e. with respect to cell types or across individuals. We are interested in how protein complexes are assembled and how variations in their stoichiometry alter their function. We use methods such as cross-linking mass spectrometry, thermal protein profiling, quantitative proteomics and data mining to study the dynamics of protein complex architecture.
Disentangling Genetic and Environmental Effects on the Proteotypes of Individuals.
Cell. 2019 May 16;177(5):1308-1318.e10. doi: 10.1016/j.cell.2019.03.015.
Pervasive Protein Thermal Stability Variation during the Cell Cycle.
Cell. 2018 May 31;173(6):1495-1507.e18. doi: 10.1016/j.cell.2018.03.053.
Landscape of nuclear transport receptor cargo specificity.
Mol Syst Biol. 2017 Dec 18;13(12):962. doi: 10.15252/msb.20177608.
Spatiotemporal variation of mammalian protein complex stoichiometries.
Genome Biol. 2016 Mar 14;17:47. doi: 10.1186/s13059-016-0912-5.
Integrated Transcriptome and Proteome Analyses Reveal Organ-Specific Proteome Deterioration in Old Rats.
Cell Syst. 2015 Sep 23;1(3):224-37. doi: 10.1016/j.cels.2015.08.012.
Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines.
Mol Syst Biol. 2013;9:648. doi: 10.1038/msb.2013.4.