Author name: Richard Scheltema

Decoding functional surfaceome protein-protein interactions using light-induced cross-linking sites and HyPhoX Sebastian N. Steiner1,2 , Clinton Yu3 , André Zwicky4 , Alexander Leitner5 , Jeffrey W. Bode4 , Lan Huang3, Bernd Wollscheid1,2 1 Institute of Translational Medicine (ITM), Department of Health Sciences and Technology (D-HEST), ETHZürich, Zürich, Switzerland2 Swiss Institute of Bioinformatics (SIB), Lausanne, Switzerland3

Combining XL-MS and LiP-MS to gain detailed molecular understanding about protein structural rearrangements upon perturbations Cathy Marulli1, Alexander Leitner1, Paola Picotti1 1 Department of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zurich, Switzerland Introduction: Cells quickly adapt to changing environments by modulating protein structure resulting in altered activity or function. Protein structure is regulated

A new tool to map the conformational proteome in cells to reveal the structural plasticity of the glucocorticoid receptor Chloé Van Leene1,2, Annick Verhee1,2, Tijs Merckaert1,2, Sven Eyckerman1,2, Karolien De Bosscher1,2, Kris Gevaert1,2 1 VIB-UGent Center for Medical Biotechnology, Ghent, Belgium2 UGent Department of Biomolecular Medicine, Ghent, Belgium Introduction: The glucocorticoid receptor (GR) is a

Interaction Proteomics – Master and Commander in Biomedical Research Markku Varjosalo1 1. University of Helsininki Proteins are essential macromolecules participating in a wide range of biological processes, including signal transduction, transcription regulation, immune response, and enzymatic catalysis.. Protein-protein interactions (PPIs) are crucial for these activities and over 80% of proteins interact with others to carry