Research in the Shinde Laboratory focuses on understanding the structure, folding, and evolution of proteins, and in particular, how the interactions and dynamics of proteases can regulate their biological functions. The laboratory has recently focused such efforts on a small but vital family of proteases coined proprotein convertases,which are responsible for the proteolytic maturation of pro-protein substrates along the secretory pathway. Proprotein convertases constitute a family of serine endoproteases that activate other proteins ranging from growth factors and receptors to extracellular matrix proteins and even other protease systems that control disease. We are still a long way from having a comprehensive understanding of the mechanisms organelle specific protease activation in cells, the many roles of convertases inside of cells,and the relation between human single nucleotide polymorphisms (SNPs) and specific disease phenotypes. The laboratory studies these proteases by combining biochemical, biophysical, and computational approaches. In addition the lab is developing approaches to create selective, high affinity inhibitors that can discern individual proprotein convertases family members. Given their vital roles, proprotein convertases are now considered to be attractive targets for the development of powerful novel therapeutics.

The Shinde Laboratory also collaborates extensively with researchers on various aspects of structure, function, dynamics, and modeling of transporter function in parasites, copper transporting ATPases in mammals, and protein modification in the tumor progression. These projects help to better understand the mechanisms of complex biological systems in the spirit of mutually beneficial scientific collaboration, while exposing students and researchers to techniques and questions that span the biomedical spectrum.