ArticleBiophysical journal2021
Intradimer forces and their implication for conformations of von Willebrand factor multimers.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- von Willebrand Factor fibers formed at pathological high shear provide a scaffold for α-synuclein binding and aggregation.Scientific reports · 2026Article
- The interplay between adsorption and aggregation of von Willebrand factor chains in shear flows.Biophysical journal · 2023Article
- Biomechanical activation of blood platelets via adhesion to von Willebrand factor studied with mesoscopic simulations.Biomechanics and modeling in mechanobiology · 2023Article
- Distribution and history of extensional stresses on vWF surrogate molecules in turbulent flow.Scientific reports · 2022Article
- Article
- Exposure of Von Willebrand Factor Cleavage Site in A1A2A3-Fragment under Extreme Hydrodynamic Shear.Polymers · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The largest blood glycoprotein von Willebrand factor (VWF) responds to hydrodynamic stresses in the bloodstream with abrupt conformation changes, thus increasing its adhesivity to platelets and collagen. Arterial and microvascular hemostasis relies on mechanical and physicochemical properties of this macromolecule. Recently, it was discovered that the mechanical properties of VWF are controlled by multiple pH-dependent interactions with opposite trends within dimeric subunits. In this work, computer simulations reveal the effect of these intradimer forces on the conformation of VWF multimers in various hydrodynamic conditions. A coarse-grained computer model of VWF has been proposed and parameterized to give a good agreement with experimental data. The simulations suggest that strong attraction between VWF D4 domains increases the resistance to elongation under shear stress, whereas even intermediate attraction between VWF C domains contributes to VWF compaction in nonsheared fluid. It is hypothesized that the detailed subdimer dynamics of VWF concatamers may be one of the biophysical regulators of initial hemostasis and arterial thrombosis.
Indexed as
Identifiers
What OpenQuestion holds
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.