ArticleScience advances2021
Crystal structure of ADAMTS13 CUB domains reveals their role in global latency.
Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The trial behind it
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Who cites it
24 citing papers in PubMed, 49 citations in OpenAlex.
- 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
- Novel cryptic ADAMTS13 epitopes uncover a distinct open ADAMTS13 conformation in immune-mediated TTP.Haematologica · 2026Article
- The ADAMTS family: from extracellular matrix proteases to orchestrators of fibrosis.Cell communication and signaling : CCS · 2026Review
- The landscape of ADAMTS13-related tests in thrombotic thrombocytopenic purpura: a review.Frontiers in medicine · 2026Review
- Determining ADAMTS13 Conformation for the Diagnosis of Immune Thrombotic Thrombocytopenic Purpura and Prediction of Relapse.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Molecular Dynamics Simulations with NAMD and Trajectory Analysis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Trp1250, Lys1252, and Arg1367 of ADAMTS13 comprise a hot spot for anti-CUB domain antibodies in patients with iTTP.Blood advances · 2025Article
- Stealth hemostatic anchors with vWF-driven navigation and plasmin-triggered tranexamic release for hematoma containment in cerebral hemorrhage.Asian journal of pharmaceutical sciences · 2025Article
- Ovochymase 2 is a key regulatory factor modulating proteolytic pathways and sperm maturation in the mammalian epididymis†.Biology of reproduction · 2025Article
- Open or closed? Understanding the molecular mechanisms and clinical implications of ADAMTS13's conformation.HemaSphere · 2025Review
- 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
- Unraveling antibody-induced structural dynamics in the ADAMTS13 CUB1-2 domains via HDX-MS.Blood advances · 2025Article
- N-glycan shielded CUB domains of ADAMTS13 prevent binding of C-terminal antibodies in patients with immune-mediated TTP.Blood advances · 2025Article
- Mechanistic insight into multiple antibody binding to ADAMTS13 in immune thrombotic thrombocytopenic purpura.Research and practice in thrombosis and haemostasis · 2024Article
- Two-way Dispatched function in Sonic hedgehog shedding and transfer to high-density lipoproteins.eLife · 2024Article
- CUB domains are not required for OVCH2 function in sperm maturation in the mouse epididymis.Andrology · 2024Article
- Management and follow-up of pregnancy-onset thrombotic thrombocytopenic purpura: the French experience.Blood advances · 2024Article
- Hemophagocytic lymphohistiocytosis is associated with deficiency and closed conformation of ADAMTS-13.Research and practice in thrombosis and haemostasis · 2024Article
- A novel mechanism underlying allosteric regulation of ADAMTS-13 revealed by hydrogen-deuterium exchange plus mass spectrometry.Research and practice in thrombosis and haemostasis · 2023Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
ADAMTS13 is a plasma metalloprotease that is essential for the regulation of von Willebrand factor (VWF) function, mediator of platelet recruitment to sites of blood vessel damage. ADAMTS13 function is dynamically regulated by structural changes induced by VWF binding that convert it from a latent to active conformation. ADAMTS13 global latency is manifest by the interaction of its C-terminal CUB1-2 domains with its central Spacer domain. We resolved the crystal structure of the ADAMTS13 CUB1-2 domains revealing a previously unreported configuration for the tandem CUB domains. Docking simulations between the CUB1-2 domains with the Spacer domain in combination with enzyme kinetic functional characterization of ADAMTS13 CUB domain mutants enabled the mapping of the CUB1-2 domain site that binds the Spacer domain. Together, these data reveal the molecular basis of the ADAMTS13 Spacer-CUB interaction and the control of ADAMTS13 global latency.
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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.