[HTML][HTML] Quercetin-3-rutinoside inhibits protein disulfide isomerase by binding to its b′ x domain
L Lin, S Gopal, A Sharda, F Passam, SR Bowley… - Journal of Biological …, 2015 - ASBMB
Quercetin-3-rutinoside inhibits thrombus formation in a mouse model by inhibiting
extracellular protein disulfide isomerase (PDI), an enzyme required for platelet thrombus
formation and fibrin generation. Prior studies have identified PDI as a potential target for
novel antithrombotic agents. Using a fluorescence enhancement-based assay and
isothermal calorimetry, we show that quercetin-3-rutinoside directly binds to the b′ domain
of PDI with a 1: 1 stoichiometry. The binding of quercetin-3-rutinoside to PDI induces a more …
extracellular protein disulfide isomerase (PDI), an enzyme required for platelet thrombus
formation and fibrin generation. Prior studies have identified PDI as a potential target for
novel antithrombotic agents. Using a fluorescence enhancement-based assay and
isothermal calorimetry, we show that quercetin-3-rutinoside directly binds to the b′ domain
of PDI with a 1: 1 stoichiometry. The binding of quercetin-3-rutinoside to PDI induces a more …