ArticleProteins2010
The catch bond mechanism between von Willebrand factor and platelet surface receptors investigated by molecular dynamics simulations.
Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- De novo DNA-based catch bonds.Nature chemistry · 2024Article
- Article
- Rate limiting step of the allosteric activation of the bacterial adhesin FimH investigated by molecular dynamics simulations.Proteins · 2024Article
- Development of the Integrated Computer Simulation Model of the Intracellular, Transmembrane, and Extracellular Domain of Platelet Integrin αTH open : companion journal to thrombosis and haemostasis · 2024Article
- Molecular mechanisms of catch bonds and their implications for platelet hemostasis.Biophysical reviews · 2023Review
- Strain stiffening of Ndc80 complexes attached to microtubule plus ends.Biophysical journal · 2022Article
- Physical Characteristics of von Willebrand Factor Binding with Platelet Glycoprotein Ibɑ Mutants at Residue 233 Causing Various Biological Functions.TH open : companion journal to thrombosis and haemostasis · 2022Article
- The Power of Touch: Type 4 Pili, the von Willebrand A Domain, and Surface Sensing by Pseudomonas aeruginosa.Journal of bacteriology · 2022Review
- Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Platelet-type von Willebrand disease: Local disorder of the platelet GPIbα β-switch drives high-affinity binding to von Willebrand factor.Journal of thrombosis and haemostasis : JTH · 2019Article
- Structure of von Willebrand factor A1 on polystyrene determined from experimental and calculated sum frequency generation spectra.Biointerphases · 2018Article
- Amyloid-Like β-Aggregates as Force-Sensitive Switches in Fungal Biofilms and Infections.Microbiology and molecular biology reviews : MMBR · 2018Review
- Specific electrostatic interactions between charged amino acid residues regulate binding of von Willebrand factor to blood platelets.The Journal of biological chemistry · 2017Article
- Mechanism of allosteric propagation across a β-sheet structure investigated by molecular dynamics simulations.Proteins · 2016Article
- Differential surface activation of the A1 domain of von Willebrand factor.Biointerphases · 2016Article
- Force is a signal that cells cannot ignore.Molecular biology of the cell · 2014Review
- Misfolding of vWF to pathologically disordered conformations impacts the severity of von Willebrand disease.Biophysical journal · 2014Article
- Mechanochemitry: a molecular biomechanics view of mechanosensing.Annals of biomedical engineering · 2014Review
- Between Amyloids and Aggregation Lies a Connection with Strength and Adhesion.New journal of science · 2014Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The multi-domain protein von Willebrand factor is crucial in the blood coagulation process at high shear. The A1 domain binds to the platelet surface receptor glycoprotein Ibalpha (GpIb alpha) and this interaction is known to be strengthened by tensile force. The molecular mechanism behind this observation was investigated here by molecular dynamics simulations. The results suggest that the proteins unbind through two distinct pathways depending whether a high-tensile force is applied or whether unbinding happens through thermal fluctuations. In the high-force unbinding pathway the A1 domain was observed to rotate away from the C-terminus of GpIb alpha. In contrast, during thermal unbinding the A1 domain rotated in the opposite direction as in the high-force pathway and the distance between the terminii of A1 and the GpIb alpha C-terminus shortened. This shortening was reduced and the lifetime of the bond extended if a moderate tensile force was applied across the complex. This suggests that the thermal unbinding pathway is inhibited by a moderate tensile force which is in agreement with the catch bond property shown previously in single molecule experiments. A designed mutant of GpIb alpha is suggested here in order to test in vitro the thermal unbinding pathway observed in silico.
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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.