Explores proteolytic cleavage, post-translational modifications, protein folding, chaperones, genetic diseases, glycosylation, and quality control in protein synthesis.
Explores proteostasis regulation through chaperone interactions and post-translational modifications, revealing insights into protein quality control mechanisms.
Explores translation, mutations, ribosome function, protein folding, and degradation processes, emphasizing the genetic code's role in protein synthesis.
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 protein folding, amino acids, RNA translation, and attractive forces, emphasizing the importance of native state conformation and compact structures.
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 the molecular chaperone action of small heat shock proteins in proteostasis, focusing on their interaction with misfolded proteins and amyloid fibrils.
