ArticleBlood2009
A novel binding site for ADAMTS13 constitutively exposed on the surface of globular VWF.
Article in Blood, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
56 citing papers in PubMed, 115 citations in OpenAlex.
- Trial
- Residues Arg568 and Phe592 contribute to an antigenic surface for anti-ADAMTS13 antibodies in the spacer domain.Haematologica · 2011Trial
- 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
- Trp1250, Lys1252, and Arg1367 of ADAMTS13 comprise a hot spot for anti-CUB domain antibodies in patients with iTTP.Blood advances · 2025Article
- Nanosilicates promote angiogenesis through activation of ROS-mediated WNT/β-catenin pathway.Science advances · 2025Article
- Development of a protease-resistant ADAMTS13 to improve stability against proteolytic degradation.Blood advances · 2025Article
- Probing rare von Willebrand disease-causing mutations in the D4 and C-domains of von Willebrand factor.Research and practice in thrombosis and haemostasis · 2025Article
- Arginine Methylation by PRMT1 Affects ADAMTS13 Secretion and Enzymatic Activity.Arteriosclerosis, thrombosis, and vascular biology · 2025Article
- Unfolded von Willebrand factor binds protein S and reduces anticoagulant activity.Blood vessels, thrombosis & hemostasis · 2025Article
- Mechanisms of ADAMTS13 regulation.Journal of thrombosis and haemostasis : JTH · 2022Review
- Identification of von Willebrand factor D4 domain mutations in patients of Afro-Caribbean descent: In vitro characterization.Research and practice in thrombosis and haemostasis · 2022Article
- A human monoclonal antibody against the distal carboxyl terminus of ADAMTS-13 modulates its susceptibility to an inhibitor in thrombotic thrombocytopenic purpura.Journal of thrombosis and haemostasis : JTH · 2021Article
- Predicting pathological von Willebrand factor unraveling in elongational flow.Biophysical journal · 2021Article
- Thrombotic Thrombocytopenic Purpura: Pathophysiology, Diagnosis, and Management.Journal of clinical medicine · 2021Review
- Antibodies that conformationally activate ADAMTS13 allosterically enhance metalloprotease domain function.Blood advances · 2020Article
- Insights Into Immunothrombosis: The Interplay Among Neutrophil Extracellular Trap, von Willebrand Factor, and ADAMTS13.Frontiers in immunology · 2020Review
- Domain-specific mechanical modulation of VWF-ADAMTS13 interaction.Molecular biology of the cell · 2019Article
- Exploring the "minimal" structure of a functional ADAMTS13 by mutagenesis and small-angle X-ray scattering.Blood · 2019Article
- Hairpin and allosteric regulation in ADAMTS13.Blood · 2019Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
ADAMTS13 metalloprotease regulates the multimeric size of von Willebrand factor (VWF) by cleaving the Tyr1605-Met1606 bond in the VWF A2 domain. The mechanisms of VWF recognition by ADAMTS13 have yet to be fully resolved. Most studies have focused on the role of exosites within the VWF A2 domain, involved in interaction with the ADAMTS13 spacer domain. In the present study, we expressed different C-terminal domain VWF fragments and evaluated their binding to ADAMTS13 and its truncated mutants, MDTCS and del(TSP5-CUB). Using plate binding assay and surface plasmon resonance, we identified a novel ADAMTS13 binding site (K(D) approximately 86 nM) in the region of VWF spanning residues 1874 to 2813, which includes the VWF D4 domain and that interacts with the C-terminal domains of ADAMTS13. We show that the interaction occurs even when VWF is in static conditions, assumed to be globular and where the VWF A2 domain is hidden. We demonstrate that C-terminal VWF fragments, as well as an antibody specifically directed toward the VWF D4 domain, inhibit VWF proteolysis by ADAMTS13 under shear conditions. We propose that this novel VWF C-terminal binding site may participate as the initial step of a multistep interaction ultimately leading to proteolysis of VWF by ADAMTS13.
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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.