Our overall research interests continue to center on the structure, function and regulation of two physiologically important classes of hepatic hemoproteins: Cytochromes P450 (P450s, CYPs) and tryptophan 2,3 dioxygenase (TDO).

Our specific goals are to:

(I) explore and mechanistically characterize the endoplasmic reticulum-associated degradation (ERAD) of proteins by exploiting P450s as cellular models; (II) explore the role of proteasomal processing of P450s in drug-induced immunotoxicity; (III) elucidate the role of heme, if any, on the regulation of P450 synthesis; and (IV) to examine the structure-function relationships and heme-mediated regulation of hepatic hemoprotein tryptophan 2,3 dioxygenase (TDO).

A combination of approaches (enzymological, chemical, structural, cell biological, and molecular biological) are being employed in pursuit of these questions.