Abstract
Our group has investigated in-depth the highly conserved interaction between the redox chaperone Protein Disulfide Isomerase A1 (PDIA1) and the glycolytic enzyme alpha-enolase (ENO1). ENO1 also acts as a non-canonical plaminogen receptor and mediates its conversion to plasmin, a serinoprotease relevant to cell remodeling. Our hypothesis is that PDIA1 modulates plasmin activation via thiol…