ArticleBiophysical journal2008
Molecular dynamics study of talin-vinculin binding.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 49 citations in OpenAlex.
- A direct computational assessment of vinculin-actin unbinding kinetics reveals catch-bonding behavior.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The unfolded protein response sensor PERK mediates mechanical stress-induced maturation of focal adhesion complexes in glioblastoma cells.FEBS letters · 2024Article
- Molecular dynamics simulations reveal how vinculin refolds partially unfolded talin rod helices to stabilize them against mechanical force.PLoS computational biology · 2024Article
- The actin binding sites of talin have both distinct and complementary roles in cell-ECM adhesion.PLoS genetics · 2024Article
- Advances in modeling cellular mechanical perceptions and responses via the membrane-cytoskeleton-nucleus machinery.Mechanobiology in medicine · 2024Review
- HDAC1/2 control mesothelium/ovarian cancer adhesive interactions impacting on Talin-1-α5β1-integrin-mediated actin cytoskeleton and extracellular matrix protein remodeling.Journal of experimental & clinical cancer research : CR · 2024Article
- Vinculin Y822 is an important determinant of ligand binding.Journal of cell science · 2023Article
- Contribution of mechanical homeostasis to epithelial-mesenchymal transition.Cellular oncology (Dordrecht, Netherlands) · 2022Review
- Cell-extracellular matrix dynamics.Physical biology · 2022Review
- Kindlin Assists Talin to Promote Integrin Activation.Biophysical journal · 2020Article
- When Stiffness Matters: Mechanosensing in Heart Development and Disease.Frontiers in cell and developmental biology · 2020Review
- Kindlin Is Mechanosensitive: Force-Induced Conformational Switch Mediates Cross-Talk among Integrins.Biophysical journal · 2019Article
- Molecular Simulations Suggest a Force-Dependent Mechanism of Vinculin Activation.Biophysical journal · 2017Article
- Mechanosensitive Conformation of Vinculin Regulates Its Binding to MAPK1.Biophysical journal · 2017Article
- Cooperative Vinculin Binding to Talin Mapped by Time-Resolved Super Resolution Microscopy.Nano letters · 2016Article
- Dynamic Regulation of α-Actinin's Calponin Homology Domains on F-Actin.Biophysical journal · 2016Article
- Multiscale mechanobiology: computational models for integrating molecules to multicellular systems.Integrative biology : quantitative biosciences from nano to macro · 2015Review
- The talin dimer structure orientation is mechanically regulated.Biophysical journal · 2014Article
- The interaction of vinculin with actin.PLoS computational biology · 2013Article
- Vinculin activation is necessary for complete talin binding.Biophysical journal · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Cells can sense mechanical force in regulating focal adhesion assembly. One vivid example is the force-induced recruitment of vinculin to reinforce initial contacts between a cell and the extracellular matrix. Crystal structures of the unbound proteins and bound complex between the vinculin head subdomain (Vh1) and the talin vinculin binding site 1 (VBS1) indicate that vinculin undergoes a conformational change upon binding to talin. However, the molecular basis for this event and the precise nature of the binding pathway remain elusive. In this article, molecular dynamics is used to investigate the binding mechanism of Vh1 and VBS1 under minimal constraints to facilitate binding. One simulation demonstrates binding of the two molecules in the complete absence of external force. VBS1 makes early hydrophobic contact with Vh1 by positioning the critical hydrophobic residues (L608, L615, and L622) in the groove formed by helices 1 and 2 of Vh1. The solvent-exposed hydrophobic residues (V619 and L623) then gradually penetrate the hydrophobic core of Vh1, thus further separating helix 1 from helix 2. These critical residues are highly conserved as large hydrophobic side groups in other vinculin binding sites; studies also have demonstrated that these residues are essential in Vh1-VBS1 binding. Similar binding mechanisms are also demonstrated in separate molecular dynamics simulations of Vh1 binding to other vinculin binding sites both in talin and alpha-actinin.
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.