Explores protein aggregation in neurodegenerative diseases, emphasizing the need to rethink treatment strategies and understand the role of post-translational modifications.
Explores the conformational and functional flexibility of Hsp70 molecular chaperones, focusing on folding intermediates and the Hsp70 functional cycle.
Explores the evolution and function of protein-repair machineries, emphasizing the role of ATP-fueled unfolding machines in preventing protein aggregation and promoting proper folding.
Explores protein aggregation control through optimal strategies, inhibitors, and spatial regulation using liquid compartments, shedding light on drug interventions and aggregate dynamics.
Explores the molecular chaperone action of small heat shock proteins in proteostasis, focusing on their interaction with misfolded proteins and amyloid fibrils.
Explores proteinopathy mapping, connecting proteotoxicity to intrinsic functions of aggregation-prone proteins, with a focus on alpha-synuclein and Parkinson's Disease.
Delves into protein aggregation mechanisms using C. elegans, covering misfolding, aggregation pathways, kinetics, chaperones, and stochastic nucleation.
