ArticleBlood2022
Structures of VWF tubules before and after concatemerization reveal a mechanism of disulfide bond exchange.
Article in Blood, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- Cryogenic electron microscopy and coagulation factors.Current opinion in hematology · 2026Review
- Molecular mechanism of cleavage at R271 during prothrombin activation revealed by cryo-EM.Blood · 2026Article
- Flow molecular dynamics simulations reveal mechano-presentation of von Willebrand factor through glycan-modulated autoinhibitory modules.APL bioengineering · 2026Article
- Article
- FRET Visualization of High Mechanosensation of von Willebrand Factor to Hydrodynamic Force.Biosensors · 2025Article
- MUC5AC filaments illuminate the structural diversification of respiratory and intestinal mucins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Weibel-Palade bodies - secretory organelles at the interface of inflammation and hemostasis.Frontiers in cell and developmental biology · 2025Review
- Article
- O-glycan determinants regulate VWF trafficking to Weibel-Palade bodies.Blood advances · 2024Article
- Conformational activation and inhibition of von Willebrand factor by targeting its autoinhibitory module.Blood · 2024Article
- VWD domain stabilization by autocatalytic Asp-Pro cleavage.Protein science : a publication of the Protein Society · 2024Article
- The Prothrombin-Prothrombinase Interaction.Sub-cellular biochemistry · 2024Review
- The interplay between adsorption and aggregation of von Willebrand factor chains in shear flows.Biophysical journal · 2023Article
- The effects of free Cys residues on the structure, activity, and tetrameric stability of mammalian uricase.Applied microbiology and biotechnology · 2023Article
- Cryo-EM structure of coagulation factor V short.Blood · 2023Article
- Altered Storage and Function of von Willebrand Factor in Human Cardiac Microvascular Endothelial Cells Isolated from Recipient Transplant Hearts.International journal of molecular sciences · 2023Article
- Assembly of von Willebrand factor tubules with in vivo helical parameters requires A1 domain insertion.Blood · 2022Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
von Willebrand factor (VWF) is an adhesive glycoprotein that circulates in the blood as disulfide-linked concatemers and functions in primary hemostasis. The loss of long VWF concatemers is associated with the excessive bleeding of type 2A von Willebrand disease (VWD). Formation of the disulfide bonds that concatemerize VWF requires VWF to self-associate into helical tubules, yet how the helical tubules template intermolecular disulfide bonds is not known. Here, we report electron cryomicroscopy (cryo-EM) structures of VWF tubules before and after intermolecular disulfide bond formation. The structures provide evidence that VWF tubulates through a charge-neutralization mechanism and that the A1 domain enhances tubule length by crosslinking successive helical turns. In addition, the structures reveal disulfide states before and after disulfide bond-mediated concatemerization. The structures and proposed assembly mechanism provide a foundation to rationalize VWD-causing mutations.
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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.