Explores proteinopathy mapping, connecting proteotoxicity to intrinsic functions of aggregation-prone proteins, with a focus on alpha-synuclein and Parkinson's Disease.
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.
Explores the molecular chaperone action of small heat shock proteins in proteostasis, focusing on their interaction with misfolded proteins and amyloid fibrils.
