ReviewJournal of thrombosis and haemostasis : JTH2022
ADAMTS13 conformations and mechanism of inhibition in immune thrombotic thrombocytopenic purpura.
Review in Journal of thrombosis and haemostasis : JTH, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- High Anti-ADAMTS13 IgG Levels after Plasma Exchange Predict Delayed ADAMTS13 Normalization in Immune-Mediated Thrombotic Thrombocytopenic Purpura.Thrombosis and haemostasis · 2026Article
- The landscape of ADAMTS13-related tests in thrombotic thrombocytopenic purpura: a review.Frontiers in medicine · 2026Review
- Assays for Plasma ADAMTS13 Activity and Inhibitors Using Recombinant FRETS-VWF73 Peptide.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Current standards and novel concepts in thrombotic thrombocytopenic purpura.Frontiers in medicine · 2026Review
- Open or closed? Understanding the molecular mechanisms and clinical implications of ADAMTS13's conformation.HemaSphere · 2025Review
- Anti-ADAMTS13 Autoantibodies in Immune-Mediated Thrombotic Thrombocytopenic Purpura.Antibodies (Basel, Switzerland) · 2025Review
- The Phenomenon of Thrombotic Microangiopathy in Cancer Patients.International journal of molecular sciences · 2024Review
- ADAMTS13 in the New Era of TTP.International journal of molecular sciences · 2024Review
- Hemophagocytic lymphohistiocytosis is associated with deficiency and closed conformation of ADAMTS-13.Research and practice in thrombosis and haemostasis · 2024Article
- Immune thrombotic thrombocytopenic purpura: pathogenesis and novel therapies: a narrative review.Annals of blood · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
ADAMTS13, a plasma metalloprotease that cleaves von Willebrand factor, is crucial for normal hemostasis. Acquired autoantibody-mediated deficiency of plasma ADAMTS13 results in a potentially fatal blood disorder, immune thrombotic thrombocytopenic purpura (iTTP). Plasma ADAMTS13 protease appears to exist in multiple conformations. Under physiological conditions, plasma ADAMTS13 exists predominantly in its "closed" conformation (or latent form), which may be activated by lowering pH, ligand binding, and binding of an antibody against the distal domains of ADAMTS13. In patients with iTTP, polyclonal antibodies target at various domains of ADAMTS13. However, nearly all inhibitory antibodies bind the spacer domain, whereas antibodies that bind the distal C-terminal domains may activate ADAMTS13 through removing its allosteric inhibition. Additionally, the anti-C-terminal antibodies may alter the potency of inhibitory antibodies towards ADAMTS13 activity. This review summarizes some of the most recent knowledge about the ADAMTS13 conformation and its mechanism of inhibition by its autoantibodies.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.