ArticleProtein science : a publication of the Protein Society2023
Structural hierarchy of mechanical extensibility in human von Willebrand factor multimers.
Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Arterial human blood flow can be stopped by cables of VWF and platelets without coagulation.Blood advances · 2025Article
- Natural variants of von Willebrand factor R1205 causing von Willebrand disease with accelerated von Willebrand factor clearance: In silico docking models and energetics of the interaction with both LRP1 and GpIb A1 domain.PLoS computational biology · 2025Article
- Cryptic Extensibility in von Willebrand Factor Revealed by Molecular Nanodissection.International journal of molecular sciences · 2024Article
- Structural hierarchy of mechanical extensibility in human von Willebrand factor multimers.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The von Willebrand factor (VWF) is a multimeric glycoprotein composed of 80- to 120-nm-long protomeric units and plays a fundamental role in mediating platelet function at high shear. The exact nature of the shear-induced structural transitions have remained elusive; uncovering them requires the high-resolution quantitative analysis of gradually extended VWF. Here, we stretched human blood-plasma-derived VWF with molecular combing and analyzed the axial structure of the elongated multimers with atomic force microscopy. Protomers extended through structural intermediates that could be grouped into seven distinct topographical classes. Protomer extension thus progresses through the uncoiling of the C
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