ArticleBiophysical journal2003
Forced detachment of the CD2-CD58 complex.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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.
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Who cites it
19 citing papers in PubMed, 66 citations in OpenAlex.
- Binding of Soluble Ligands to Membrane Receptors: A Molecular Dynamics Simulation Study.The journal of physical chemistry. B · 2025Article
- Shock-Induced Damage Mechanism of Perineuronal Nets.Biomolecules · 2021Article
- Structure-based identification of inhibitors disrupting the CD2-CD58 interactions.Journal of computer-aided molecular design · 2021Article
- Steered molecular dynamic simulations of conformational lock of Cu, Zn-superoxide dismutase.Scientific reports · 2019Article
- Investigating cyclic peptides inhibiting CD2-CD58 interactions through molecular dynamics and molecular docking methods.Journal of computer-aided molecular design · 2018Article
- Simulation of Reversible Protein-Protein Binding and Calculation of Binding Free Energies Using Perturbed Distance Restraints.Journal of chemical theory and computation · 2017Article
- Theoretical study of enzymatically catalyzed tautomerization of carbon acids in aqueous solution: quantum calculations and steered molecular dynamics simulations.Journal of molecular modeling · 2016Article
- Exploring peptide/MHC detachment processes using hierarchical natural move Monte Carlo.Bioinformatics (Oxford, England) · 2016Article
- A computational model of the glycine tautomerization reaction in aqueous solution.Journal of molecular modeling · 2014Article
- Insights into Ligand-Protein Binding from Local Mechanical Response.Journal of chemical theory and computation · 2011Article
- Elasticity and rupture of a multi-domain neural cell adhesion molecule complex.Biophysical journal · 2009Article
- Protein-protein interaction investigated by steered molecular dynamics: the TCR-pMHC complex.Biophysical journal · 2008Article
- A structure-based sliding-rebinding mechanism for catch bonds.Biophysical journal · 2007Article
- Sequential unfolding of individual helices of bacterioopsin observed in molecular dynamics simulations of extraction from the purple membrane.Biophysical journal · 2006Article
- Partitioning of anesthetics into a lipid bilayer and their interaction with membrane-bound peptide bundles.Biophysical journal · 2006Article
- Molecular simulation of the binding of nerve growth factor peptide mimics to the receptor tyrosine kinase A.Biophysical journal · 2006Article
- Scalable molecular dynamics with NAMD.Journal of computational chemistry · 2005Article
- Change of the unbinding mechanism upon a mutation: a molecular dynamics study of an antibody-hapten complex.Protein science : a publication of the Protein Society · 2005Article
- Pulling-speed-dependent force-extension profiles for semiflexible chains.Biophysical journal · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The force-induced detachment of the adhesion protein complex CD2-CD58 was studied by steered molecular dynamics simulations. The forced detachment of CD2 and CD58 shows that the system can respond to an external force by two mechanisms, which depend on the loading rate. At the rapid loading rates of 70 and 35 pN/ps (pulling speeds of 1 and 0.5 A/ps) the two proteins unfold before they separate, whereas at slower loading rates of 7 and 3.5 pN/ps (pulling speeds of 0.1 and 0.05 A/ps), the proteins separate before the domains can unfold. When subjected to a constant force of 400 pN, the two proteins separated without significant structural distortion. These findings suggest that protein unfolding is not coupled to the adhesive function of CD2 and CD58. The simulations further confirm that salt bridges primarily determine the tensile strength of the protein-to-protein bond, and that the order of salt bridge rupture depends mainly on the position of the bond, relative to the line of action of the applied force. Salt bridges close to this line break first. The importance of each of the salt bridges for adhesion, determined from the simulations, correlates closely with their role in cell-to-cell adhesion and equilibrium binding determined by site-directed mutagenesis experiments.
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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.