Explores the conformational and functional flexibility of Hsp70 molecular chaperones, focusing on folding intermediates and the Hsp70 functional cycle.
Explores the molecular chaperone action of small heat shock proteins in proteostasis, focusing on their interaction with misfolded proteins and amyloid fibrils.
Explores membrane protein quality control mechanisms at the ER, focusing on ERAD recognition, retrotranslocation, ubiquitination, and degradation of misfolded proteins.
Explores proteostasis regulation through chaperone interactions and post-translational modifications, revealing insights into protein quality control mechanisms.