Quercetin -3-rutinoside Inhibits Protein
Disulfide Isomerase by Binding to its b ′ x domain.
The disulfide isomerase ERp57 is required for fibrin deposition in vivo.
Protein
disulfide isomerase inhibitors constitute a new class of antithrombotic agents.
A critical role for extracellular protein
disulfide isomerase during thrombus formation in mice.
Limiting role of protein
disulfide isomerase in the expression of collagen - tailed acetylcholinesterase forms in muscle.
Protein
disulfide isomerase capture during thrombus formation in vivo depends on the presence of β3 integrins.
Endothelium - derived but not platelet - derived protein
disulfide isomerase is required for thrombus formation in vivo.
Extracellular protein
disulfide isomerase regulates ligand - binding activity of αMβ2 integrin and neutrophil recruitment during vascular inflammation.