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Thrombin inhibitors block the serine protease that converts fibrinogen into fibrin at the end of coagulation. Thrombin also activates platelets and other cells through protease-activated receptors (PARs). The receptor cloned in 1991 showed that thrombin cleaves the receptor N-terminus and unmasks a tethered ligand. Direct inhibitors bind the active site and are used in coagulation, platelet and vascular research. Dabigatran came from a structure-based design program reported in 2002, and dabigatran etexilate is its orally available prodrug. Argatroban, bivalirudin, inogatran and ximelagatran are further direct thrombin inhibitors. Atopaxar hydrobromide acts on the receptor side as a PAR-1 antagonist, whereas RWJ-445167 inhibits both thrombin and factor Xa.
Thrombin receptor peptide ligand is a selective antagonist of the thrombin receptor, inhibiting its activation and downstream signaling. This compound exhibits antithrombotic properties, making it suitable for research focused on thrombotic disorders and cardiovascular diseases. Its ability to modulate thrombin activity positions it as a valuable tool for studying platelet aggregation and related pathways.
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