We aim to uncover the role of several conserved endoplasmic reticulum protein complexes that facilitate biogenesis of different secretory and membrane proteins and maintain protein homeostasis within the endoplasmic reticulum. Main methods that we use are chemical and structural biology, which include single particle Cryo-EM methods and molecular dynamics simulations. This work aims at understanding the function of these membrane protein complexes and to identify new therapeutic strategies to diseases that involve protein misfolding.
We use small molecule chemical probes to specifically perturb and study specific nodes of the endoplasmic reticulum protein homeostasis network. We aim to use these synthetic and natural product small molecules to study specific intermediates in the dynamic process of secretory protein biogenesis and ER protein quality control. Ultimately, these molecules can provide novel starting points for development of new therapeutic small molecules.