ArticleBiophysical journal2005
Multi-step fibrinogen binding to the integrin (alpha)IIb(beta)3 detected using force spectroscopy.
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 49 papers.
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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.
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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.
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Who cites it
49 citing papers in PubMed.
- Selective inhibition of platelet inflammatory tether formation via force-modulated vibrational states of integrin αIIbβ3.Journal of molecular modeling · 2026Article
- Sono-Mechanogenetics: Linking Ultrasound Physics With Cellular Mechanobiology.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Biomechanical anticoagulation by spherical platelets in extracorporeal systems.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- All-atom simulations reveal distinct pathways for αCellular and molecular life sciences : CMLS · 2026Article
- Characterization of the interaction between the Sec61 translocon complex and ppαF using optical tweezers.Protein science : a publication of the Protein Society · 2024Article
- Article
- Activated αeLife · 2020Article
- Fibrinogen binding is affected by amino acid substitutions in C-terminal repeat region of fibronectin binding protein A.Scientific reports · 2019Article
- Drug-induced activation of integrin alpha IIb beta 3 leads to minor localized structural changes.PloS one · 2019Article
- Regulatory element in fibrin triggers tension-activated transition from catch to slip bonds.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Single-molecule measurements of the effect of force on Thy-1/αvβ3-integrin interaction using nonpurified proteins.Molecular biology of the cell · 2018Article
- Effect of pH and ionic strength on the binding strength of anti-PF4/polyanion antibodies.European biophysics journal : EBJ · 2017Article
- Strong Binding of Platelet Integrin αIIbβ3 to Fibrin Clots: Potential Target to Destabilize Thrombi.Scientific reports · 2017Article
- βBiophysical journal · 2017Article
- Engineered isopeptide bond stabilized fibrin inspired nanoscale peptide based sealants for efficient blood clotting.Scientific reports · 2017Article
- Anti-platelet factor 4/polyanion antibodies mediate a new mechanism of autoimmunity.Nature communications · 2017Article
- Mechanistic Basis for the Binding of RGD- and AGDV-Peptides to the Platelet Integrin αIIbβ3.Biochemistry · 2017Article
- Single-Molecule Interactions of a Monoclonal Anti-DNA Antibody with DNA.BioNanoScience · 2017Article
- αIIbβ3 binding to a fibrinogen fragment lacking the γ-chain dodecapeptide is activation dependent and EDTA inducible.Blood advances · 2017Article
- Laminin-111-derived peptide conjugated fibrin hydrogel restores salivary gland function.PloS one · 2017Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The regulated ability of integrin alphaIIbbeta3 to bind fibrinogen plays a crucial role in platelet aggregation and hemostasis. We have developed a model system based on laser tweezers, enabling us to measure specific rupture forces needed to separate single receptor-ligand complexes. First of all, we performed a thorough and statistically representative analysis of nonspecific protein-protein binding versus specific alphaIIbbeta3-fibrinogen interactions in combination with experimental evidence for single-molecule measurements. The rupture force distribution of purified alphaIIbbeta3 and fibrinogen, covalently attached to underlying surfaces, ranged from approximately 20 to 150 pN. This distribution could be fit with a sum of an exponential curve for weak to moderate (20-60 pN) forces, and a Gaussian curve for strong (>60 pN) rupture forces that peaked at 80-90 pN. The interactions corresponding to these rupture force regimes differed in their susceptibility to alphaIIbbeta3 antagonists or Mn2+, an alphaIIbbeta3 activator. Varying the surface density of fibrinogen changed the total binding probability linearly >3.5-fold but did not affect the shape of the rupture force distribution, indicating that the measurements represent single-molecule binding. The yield strength of alphaIIbbeta3-fibrinogen interactions was independent of the loading rate (160-16,000 pN/s), whereas their binding probability markedly correlated with the duration of contact. The aggregate of data provides evidence for complex multi-step binding/unbinding pathways of alphaIIbbeta3 and fibrinogen revealed at the single-molecule level.
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