ArticleBiophysical journal2005
Dynamic force spectroscopy of glycoprotein Ib-IX and von Willebrand factor.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- Molecular Force Sensors for Biological Application.International journal of molecular sciences · 2024Review
- Probing Ligand-Receptor Interaction in Living Cells Using Force Measurements With Optical Tweezers.Frontiers in bioengineering and biotechnology · 2020Article
- Probing force in living cells with optical tweezers: from single-molecule mechanics to cell mechanotransduction.Biophysical reviews · 2019Review
- Shear-Induced Extensional Response Behaviors of Tethered von Willebrand Factor.Biophysical journal · 2019Article
- Internal Tensile Force and A2 Domain Unfolding of von Willebrand Factor Multimers in Shear Flow.Biophysical journal · 2018Article
- Intermolecular interactions between glycomodules of plant cell wall arabinogalactan-proteins and extensins.Cell surface (Amsterdam, Netherlands) · 2018Article
- Modelling of platelet-fibrin clot formation in flow with a DPD-PDE method.Journal of mathematical biology · 2016Article
- Exploiting the kinetic interplay between GPIbα-VWF binding interfaces to regulate hemostasis and thrombosis.Blood · 2014Article
- Interrogating biology with force: single molecule high-resolution measurements with optical tweezers.Biophysical journal · 2013Review
- The linker between the D3 and A1 domains of vWF suppresses A1-GPIbα catch bonds by site-specific binding to the A1 domain.Protein science : a publication of the Protein Society · 2013Article
- Multiscale model of platelet translocation and collision.Journal of computational physics · 2013Article
- Exploring the energy profile of human IgG/rat anti-human IgG interactions by dynamic force spectroscopy.The protein journal · 2012Article
- The catch bond mechanism between von Willebrand factor and platelet surface receptors investigated by molecular dynamics simulations.Proteins · 2010Article
- The mechanism of VWF-mediated platelet GPIbalpha binding.Biophysical journal · 2010Article
- Methods and estimations of uncertainties in single-molecule dynamic force spectroscopy.European biophysics journal : EBJ · 2009Article
- Platelet adhesive dynamics. Part II: high shear-induced transient aggregation via GPIbalpha-vWF-GPIbalpha bridging.Biophysical journal · 2008Article
- FimH forms catch bonds that are enhanced by mechanical force due to allosteric regulation.The Journal of biological chemistry · 2008Article
- Influence of Brownian motion on blood platelet flow behavior and adhesive dynamics near a planar wall.Langmuir : the ACS journal of surfaces and colloids · 2007Article
- Mechanics of cellular adhesion to artificial artery templates.Biophysical journal · 2006Article
- Dynamic force spectroscopy of E. coli P pili.Biophysical journal · 2006Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The first stage in hemostasis is the binding of the platelet membrane receptor glycoprotein (GP) Ib-IX complex to the A1 domain of von Willebrand factor in the subendothelium. A bleeding disorder associated with this interaction is platelet-type von Willebrand disease, which results from gain-of-function (GOF) mutations in amino acid residues 233 or 239 of the GP Ibalpha subunit of GP Ib-IX. Using optical tweezers and a quadrant photodetector, we investigated the binding of A1 to GOF and loss-of-function mutants of GP Ibalpha with mutations in the region containing the two known naturally occurring mutations. By dynamically measuring unbinding force profiles at loading rates ranging from 200-20,000 pN/s, we found that the bond strengths between A1 and GP Ibalpha GOF mutants (233, 235, 237, and 239) were significantly greater than the A1/wild-type GP Ib-IX bond at all loading rates examined (p < 0.05). In addition, mutants 231 and 232 exhibited significantly lower bond strengths with A1 than the wild-type receptors (p < 0.05). We computed unloaded dissociation rate constant (k(off)(0)) values for interactions involving mutant and wild-type GP Ib-IX receptors with A1 and found the A1/wild-type GP Ib-IX k(off)(0) value of 5.47 +/- 0.25 s(-1) to be significantly greater than the GOF k(off)(0) values and significantly less than the loss-of-function k(off)(0) values. Our data illustrate the importance of the bond kinetics associated with the VWF/GP Ib-IX interaction in hemostasis and also demonstrate the drastic changes in binding that can occur when only a single amino acid of GP Ibalpha is altered.
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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.