ArticleNature communications2019
Crystal structure and substrate-induced activation of ADAMTS13.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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Who cites it
50 citing papers in PubMed, 82 citations in OpenAlex.
- Genomic and Structural Analysis of Gamete Recognition Proteins in a Broadcast Spawning Echinoderm Mesocentrotus franciscanus.Journal of molecular evolution · 2026Article
- Human monoclonal and polyclonal anti-ADAMTS13 antibodies in immune thrombotic thrombocytopenic purpura: variable mechanisms of inhibition.Journal of thrombosis and haemostasis : JTH · 2026Article
- Pathological Allostery in ADAMTS13: Autoantibody-Induced Modulation and Its Role in Immune Thrombotic Thrombocytopenic Purpura (iTTP).Pharmaceuticals (Basel, Switzerland) · 2026Review
- Functional Characterization of the VWF p.Cys2163Tyr Variant Reveals Impaired Secretion and Intracellular Processing.Biomolecules · 2026Article
- Von Willebrand disease: A century of progress.Research and practice in thrombosis and haemostasis · 2026Review
- Novel cryptic ADAMTS13 epitopes uncover a distinct open ADAMTS13 conformation in immune-mediated TTP.Haematologica · 2026Article
- Landscape and Spectrum of VWF Variants in Type 2 Von Willebrand Disease: Insights from a German Patient Cohort.Thrombosis and haemostasis · 2026Article
- Determining ADAMTS13 Conformation for the Diagnosis of Immune Thrombotic Thrombocytopenic Purpura and Prediction of Relapse.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The landscape of ADAMTS13-related tests in thrombotic thrombocytopenic purpura: a review.Frontiers in medicine · 2026Review
- ADAMTS13 as a thromboinflammatory brake at the vascular-immune interface: from viral immunothrombosis to the tumor microenvironment.Frontiers in immunology · 2026Review
- Molecular Dynamics Simulations with NAMD and Trajectory Analysis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Thrombotic thrombocytopaenic purpura.European heart journal. Case reports · 2025Article
- Open or closed? Understanding the molecular mechanisms and clinical implications of ADAMTS13's conformation.HemaSphere · 2025Review
- Development of a protease-resistant ADAMTS13 to improve stability against proteolytic degradation.Blood advances · 2025Article
- A Disintegrin and Metalloprotease with Thrombospondin Motif, Member 13, and Von Willebrand Factor in Relation to the Duality of Preeclampsia and HIV Infection.International journal of molecular sciences · 2025Review
- Carbamylation is Instrumental in End-Stage Kidney Disease Coagulopathies: The Impact on von Willebrand Factor and Platelet Functionality.Thrombosis and haemostasis · 2025Article
- Role of von Willebrand factor (VWF), platelets, and aberrant flow in the initiation of venous thrombosis.Science advances · 2025Article
- Cleavage of Cartilage Oligomeric Matrix Protein (COMP) by ADAMTS4 generates a neoepitope associated with osteoarthritis and other forms of degenerative joint disease.Matrix biology : journal of the International Society for Matrix Biology · 2025Article
- ADAMTS13 Improves Hepatic Platelet Accumulation in Pyrrolizidine Alkaloids-induced Liver Injury.Journal of clinical and translational hepatology · 2025Article
- The Highs and Lows of ADAMTS13 Activity.Journal of clinical medicine · 2024Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Platelet recruitment to sites of blood vessel damage is highly dependent upon von Willebrand factor (VWF). VWF platelet-tethering function is proteolytically regulated by the metalloprotease ADAMTS13. Proteolysis depends upon shear-induced conformational changes in VWF that reveal the A2 domain cleavage site. Multiple ADAMTS13 exosite interactions are involved in recognition of the unfolded A2 domain. Here we report through kinetic analyses that, in binding VWF, the ADAMTS13 cysteine-rich and spacer domain exosites bring enzyme and substrate into proximity. Thereafter, binding of the ADAMTS13 disintegrin-like domain exosite to VWF allosterically activates the adjacent metalloprotease domain to facilitate proteolysis. The crystal structure of the ADAMTS13 metalloprotease to spacer domains reveals that the metalloprotease domain exhibits a latent conformation in which the active-site cleft is occluded supporting the requirement for an allosteric change to enable accommodation of the substrate. Our data demonstrate that VWF functions as both the activating cofactor and substrate for ADAMTS13.
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Registered trials
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