Luke McAlary

This study maps the mutational landscape of SOD1 by analyzing monomer folding and dimerization, identifying protein destabilization as a key driver of ALS and uncovering potential therapeutic targets.

This paper shows that HspB1 and HspB5 differentially regulate TDP-43LCD condensation and aggregation, with HspB1 increasing dynamic exchange and HspB5 delaying pathological transition.

This paper introduces a passivation-free platform using lipid-coated water-in-oil droplets for fluorescence spectroscopy, enabling accurate measurements of molecular dynamics in nanolitre volumes.

This paper introduces a subcellular mass spectrometry imaging technique that enhances lipid and nucleotide detection using transmission geometry ambient laser desorption and plasma ionisation.

The paper identifies amyloidogenic regions in beta-strands II and III of SOD1 that modulate aggregation and toxicity in ALS mutants, showing that proline mutations reduce these effects.

The paper designs and tests SOD1 mutants using computational methods, showing that a destabilizing mutant causes ALS-like phenotypes while a stabilizing mutant rescues them in zebrafish.

This study shows that SOD1A4V aggregation disrupts ubiquitin homeostasis in an ALS cell model, leading to UPS dysfunction and altered mitochondrial function.