Andrés E. Leschziner

This study identifies 'unlatching' as a common mechanism for Parkinson's disease-associated LRRK2 variants, showing increased membrane localization and decreased S935 phosphorylation.

This paper elucidates the structural mechanisms by which LRRK2 is activated and autoinhibited, showing how mutations affect these processes and suggesting therapeutic strategies.

This study identifies glucose 6-phosphate (G6P) as a second trigger for Glk1p polymerization and shows that ADP causes filament disassembly, linking metabolic state to enzyme polymerization.

This study uses in-cell cryo-electron tomography to compare how type I and type II kinase inhibitors affect LRRK2-I2020T filament formation and microtubule association in cells.

The paper uses cryo-EM to identify an early intermediate state in dynein activation by LIS1, termed Pre-Chi, and shows its functional importance through mutational analysis.

This study determines the structure of the Dsup and HMGN nucleosome-binding motif using cryo-EM, revealing their binding to the nucleosome acidic patch.

Hybrid type-II inhibitors RN277 and RN341 target inactive LRRK2 with far fewer kinase off-targets than Rebastinib, preserve S935 phosphorylation, and rescue kinesin motility in vitro.

The paper uses cryo-EM to visualize intermediate states of dynein activation pathway by analyzing structures of dynein and dynein-Lis1 bound to ATP.

The paper tests Oskar variants in vivo to assess their role in germ plasm assembly, finding that the LOTUS domain is critical for mRNA recruitment despite the current model attributing this function to the OSK domain.

This study uses cryo-ET to show that LRRK2 can form microtubule-bound filaments in its autoinhibited state, with structural differences compared to active-LRRK2 filaments.

This study develops a high-affinity DARPin that binds to LRRK2's WD40 domain, improving structural analysis and revealing its role in disrupting LRRK2 filaments and Rab8A phosphorylation.

This study reveals structural insights into the RSC chromatin remodeling complex by showing how ARP binding induces conformational changes and enhances nucleosome remodeling.

The paper solves a high-resolution structure of a stalled RNA polymerase II elongation complex using streptavidin affinity grids to overcome air-water interface interactions.