Florian Stengel

This study identifies VDAC2 as a regulator of BAX activation by stabilizing a primed, membrane-inserted intermediate in the BAX activation pathway.

This study identifies Rlig1 as a regulator of ribosome function and translation under oxidative stress by showing its interaction with ribosomal proteins and its role in maintaining translational activity.

This study investigates how the p97/VCP mutation D395G increases redox sensitivity, leading to oxidative inactivation and contributing to neurodegeneration.

This study introduces ketolysine (KeK), a non-hydrolyzable acetyllysine analog, which remains stable in cells and affects p53-mediated transcription, unlike acetyllysine (AcK) which is deacetylated.

This study uses proximity labeling and phosphoproteomics to analyze LRRK1 and LRRK2 interactomes and phosphorylation sites, identifying novel substrates and the impact of inhibitors.

The paper identifies novel kinase:Rab pairs and characterizes substrate recognition determinants for Rab phosphorylation by kinases like LRRK2.

The paper identifies lipoamide as a small molecule that dissolves stress granules and improves outcomes in ALS models by modulating redox-sensitive proteins.

This study develops a kinetic model to describe cross-link formation in protein-protein interactions and identifies optimal cross-linker concentrations for maximizing cross-link yield.

This study identifies Sbh1/Sec61β as a specific signal peptide receptor that recognizes and guides substrates into the Sec61 channel through its cytosolic IDR and conserved regions.

This study identifies a bias in proteome-wide crosslinking towards high-abundant proteins and shows how optimizing kinetic parameters can enhance detection of lower-abundant proteins.