ArticleProteins2014
Talin-driven inside-out activation mechanism of platelet αIIbβ3 integrin probed by multimicrosecond, all-atom molecular dynamics simulations.
Article in Proteins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Selective inhibition of platelet inflammatory tether formation via force-modulated vibrational states of integrin αIIbβ3.Journal of molecular modeling · 2026Article
- Temporal phosphoproteomics reveals key regulators of procoagulant COAT platelet generation.Blood vessels, thrombosis & hemostasis · 2026Article
- Elucidating the dynamics of integrin αIIbβ3 from native platelet membranes by cryo-EM with build-and-retrieve method.Blood advances · 2025Article
- Review
- An efficient alpha helix model and simulation framework for stationary electrostatic interaction force estimation.Scientific reports · 2021Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Kindlin Is Mechanosensitive: Force-Induced Conformational Switch Mediates Cross-Talk among Integrins.Biophysical journal · 2019Article
- [The progresses in research and treatment of inherited platelet disorders].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2018Article
- [Special type of Glanzmann's thrombasthenia].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2018Article
- Regulation of inside-out β1-integrin activation by CDCP1.Oncogene · 2018Article
- α-Actinin Induces a Kink in the Transmembrane Domain of βBiophysical journal · 2017Article
- The Integrin Receptor in Biologically Relevant Bilayers: Insights from Molecular Dynamics Simulations.The Journal of membrane biology · 2017Article
- A model for cyclic mechanical reinforcement.Scientific reports · 2016Article
- αIIbβ3: structure and function.Journal of thrombosis and haemostasis : JTH · 2015Review
- The dual structural roles of the membrane distal region of the α-integrin cytoplasmic tail during integrin inside-out activation.Journal of cell science · 2015Article
- αIIbβ3 variants defined by next-generation sequencing: predicting variants likely to cause Glanzmann thrombasthenia.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Platelet aggregation is the consequence of the binding of extracellular bivalent ligands such as fibrinogen and von Willebrand factor to the high affinity, active state of integrin αIIbβ3. This state is achieved through a so-called "inside-out" mechanism characterized by the membrane-assisted formation of a complex between the F2 and F3 subdomains of intracellular protein talin and the integrin β3 tail. Here, we present the results of multi-microsecond, all-atom molecular dynamics simulations carried on the complete transmembrane (TM) and C-terminal (CT) domains of αIIbβ3 integrin in an explicit lipid-water environment, and in the presence or absence of the talin-1 F2 and F3 subdomains. These large-scale simulations provide unprecedented molecular-level insights into the talin-driven inside-out activation of αIIbβ3 integrin. Specifically, they suggest a preferred conformation of the complete αIIbβ3 TM/CT domains in a lipid-water environment, and testable hypotheses of key intermolecular interactions between αIIbβ3 integrin and the F2/F3 domains of talin-1. Notably, not only do these simulations give support to a stable left-handed reverse turn conformation of the αIIb juxtamembrane motif rather than a helical turn, but they raise the question as to whether TM helix separation is required for talin-driven integrin activation.
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Registered trials
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