Christian Johannes Gloeckner

This study identifies sephin1's mechanism of action in proteostasis disruption by showing it binds G-actin, causes cytoskeleton misfolding, and modulates autophagy through mTORC1-TFEB and GCN2-eIF2-CHOP pathways.

This study identifies a LRRK2-regulatory network through proximity proteomics and structural analysis, showing its link to centrosomes and how its conformation and activity state influence interactions.

This study identifies a regulatory feedback loop between LRRK2 and PP2A phosphatases in Parkinson's disease, showing that LRRK2 phosphorylates PP2A to disrupt its function and contribute to neuronal death.

This study identifies differentially expressed micro-RNAs in LRRK2 G2019S mutation carriers using induced pluripotent stem cell-derived neurons, showing no linear correlation with LRRK2 activity.

This study develops a method to predict protein-protein direct interactions and stable complexes using co-expression and co-evolution data, achieving high AUROC scores and better performance than existing tools.

The paper characterizes the proteomic changes in dopaminergic neurons with the LRRK2 G2019S mutation and identifies potential biomarkers for Parkinson's disease.

This paper solves the structure of a bacterial Roco protein in its GTP-bound state using cryo-EM and nanobodies, revealing conformational changes and allosteric activation mechanisms.

This study reevaluates the autoinhibition mechanism of Rabex5 by analyzing structural changes and nucleotide exchange activity, revealing new regulatory roles for Ubiquitin binding domains.