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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 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.
