R. Fernandez-Busnadiego

This study identifies Ldo16/45 as proteins forming a tether-complex with Vac8 to create vCLIP contact sites between lipid droplets and vacuoles, linking LD biogenesis and breakdown.

This study shows that the AAA+ chaperone VCP disaggregates Tau fibrils and generates seeding-active Tau as a byproduct, suggesting a role in aggregate removal and spreading in tauopathies.

This study uses cryo-ET to show that neuronal alpha-Synuclein inclusions contain fibrils intermixed with cellular membranes and are nucleated by oligomers.

This study demonstrates that plunge freezing can vitrify large biological specimens like mouse cardiomyocytes and Drosophila tissues, enabling efficient cryo-FIB/ET analysis of their molecular architecture.

This study shows that polyQ expansion in HTT does not change the structure of the HTT-HAP40 complex, as revealed by biophysical and cryo-EM analyses.

This study shows that amyloid-like aggregates impair lysosomal function in neurons by sequestering AP-31, leading to neurotoxicity.

The paper identifies Tcb proteins as mediators of ER curvature at ER-PM contact sites, facilitating lipid transport to maintain plasma membrane integrity under stress.