Explores protein aggregation control through optimal strategies, inhibitors, and spatial regulation using liquid compartments, shedding light on drug interventions and aggregate dynamics.
Delves into protein aggregation mechanisms using C. elegans, covering misfolding, aggregation pathways, kinetics, chaperones, and stochastic nucleation.
Explores proteostasis regulation through chaperone interactions and post-translational modifications, revealing insights into protein quality control mechanisms.
Explores beta-hairpins in polyglutamine protein aggregation, focusing on Huntington's disease and the molecular mechanisms behind toxic fibril formation.
Explores protein aggregation in neurodegenerative diseases, emphasizing the need to rethink treatment strategies and understand the role of post-translational modifications.
Explores the molecular chaperone action of small heat shock proteins in proteostasis, focusing on their interaction with misfolded proteins and amyloid fibrils.
Explores the mechanisms of ALS, focusing on SOD1 pathology, including toxic gain of function, protein misfolding, ER stress, and mitochondrial dysfunction.
Explores proteinopathy mapping, connecting proteotoxicity to intrinsic functions of aggregation-prone proteins, with a focus on alpha-synuclein and Parkinson's Disease.
