Vascular　thiol　isomerases　(VTIs)　encompass　proteins　such　as　protein　disulfide　isomerase　(PDI),　endoplasmic　reticulum　protein　5　(ERp5),　ERp46,　ERp57,　ERp72,　thioredoxin-related　transmembrane　protein　1　(TMX1),　and　TMX4,　and　play　pivotal　functions　in　platelet　aggregation　and　formation　of　thrombosis.　Investigating　vascular　thiol　isomerases,　their　substrates　implicated　in　thrombosis,　the　underlying　regulatory　mechanisms,　and　the　development　of　inhibitors　targeting　these　enzymes　represents　a　rapidly　advancing　frontier　within　vascular　biology.　In　this　review,　we　summarize　the　structural　characteristics　and　functional　attributes　of　VTIs,　describe　the　associations　between　these　enzymes　and　thrombosis,　and　outline　the　progress　in　developing　inhibitors　of　VTIs　for　potential　antithrombotic　therapeutic　applications.