Explores proteostasis regulation through chaperone interactions and post-translational modifications, revealing insights into protein quality control mechanisms.
Explores the mechanisms of ALS, focusing on SOD1 pathology, including toxic gain of function, protein misfolding, ER stress, and mitochondrial dysfunction.
Explores protein aggregation control through optimal strategies, inhibitors, and spatial regulation using liquid compartments, shedding light on drug interventions and aggregate dynamics.
Explores the selective promiscuity in binding of the E. coli Hsp70 chaperone to unfolded or misfolded protein substrates, examining its implications in protein folding mechanisms.
Delves into protein aggregation mechanisms using C. elegans, covering misfolding, aggregation pathways, kinetics, chaperones, and stochastic nucleation.
