Explores post-translational modifications and folding processes in the endoplasmic reticulum, using examples like the influenza virus and protein misfolding diseases.
Explores proteolytic cleavage, post-translational modifications, protein folding, chaperones, genetic diseases, glycosylation, and quality control in protein synthesis.
Explores the molecular chaperone action of small heat shock proteins in proteostasis, focusing on their interaction with misfolded proteins and amyloid fibrils.
Explores the design and validation of targeted protein degraders, including PROTACs and molecular glue compounds, emphasizing the importance of proper analyses and validations in TPD research.
Explores molecular glues as new drug modalities, focusing on binding forces, energetics, biomolecular interactions, quantification, drug development, and structural characterization.
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.
