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ADAMTS13 represents a landmark in a journey that began over 80 years ago with a single clinical case. Thrombotic thrombocytopenic purpura exemplifies how von Willebrand factor can be responsible for life-threatening thrombosis. This review summarizes recent progress on ADAMTS13, which prevents this deadly event.Recent advances are summarized in four main areas. First, the core ADAMTS13-binding site is contained in a short sequence in the A2 domain, but other domains affect this interaction. Mutations from thrombotic thrombocytopenic purpura and von Willebrand disease provide clues for the structural prerequisites and regulation of von Willebrand factor cleavage. Second, studies are unraveling the reasons why urea, BaCl2, and low ionic strength are required to cleave von Willebrand factor under static conditions. Third, studies on thrombotic thrombocytopenic purpura and ADAMTS13-knockout mice suggest that ADAMTS13 deficiency alone may not be sufficient to cause thrombotic thrombocytopenic purpura. Finally, ADAMTS13 could be an antithrombotic agent for thrombotic thrombocytopenic purpura and other thrombotic conditions.Study of ADAMTS13 has exploded since this metalloprotease was characterized. This knowledge reveals the nature of ADAMTS13's interaction with von Willebrand factor and the pathogenesis of clinical thrombotic thrombocytopenic purpura, especially in relation to ADAMTS13.