C. J. Gloeckner

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 uses biophysical methods to show that autophosphorylation inhibits LRRK2 dimerization, suggesting it as a negative regulator with implications for Parkinson's disease.

This study identifies a kinase-dependent negative feedback mechanism regulating LRRK2 Roc G domain activity through autophosphorylation of T1343, affecting GTP hydrolysis kinetics.

This study identifies and characterizes Nanobodies that modulate LRRK2 activity through non-ATP-competitive mechanisms, offering new tools for Parkinson's disease research and therapy.

This study identifies K136 acetylation as a key modifier of TDP-43's RNA binding and phase separation, leading to pathological aggregation, and shows SIRT1's role in deacetylating and reducing this aggregation.

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