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.
Explores proteinopathy mapping, connecting proteotoxicity to intrinsic functions of aggregation-prone proteins, with a focus on alpha-synuclein and Parkinson's Disease.
Explores translation, mutations, ribosome function, protein folding, and degradation processes, emphasizing the genetic code's role in protein synthesis.
Examines how a receptor regulates proteostasis in C. elegans, emphasizing the importance of maintaining cellular function and preventing protein misfolding diseases.
Explores the molecular chaperone action of small heat shock proteins in proteostasis, focusing on their interaction with misfolded proteins and amyloid fibrils.
Explores the application of control theory to manage protein aggregation processes, focusing on amyloid fibers and their implications in various diseases.
