ArticleNature communications2014
Theory of rapid force spectroscopy.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed.
- Single-Molecule Force Spectroscopy: Experiments, Analysis, and Simulations.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Assessment of the Adhesion to Decellularized Cardiac Patches of Stem Cells Through Single-Cell Force Spectroscopy (SCFS).Biomimetics (Basel, Switzerland) · 2026Article
- On the distance to the transition state of protein folding in optical tweezers experiments.Biophysical reviews · 2025Review
- Long-term memory induced correction to Arrhenius law.Nature communications · 2024Article
- Single-molecule magnetic tweezers to probe the equilibrium dynamics of individual proteins at physiologically relevant forces and timescales.Nature protocols · 2024Review
- Polymer time crystal: Mechanical activation of reversible bonds by low-amplitude high frequency excitations.Science advances · 2024Article
- Ebola Virus Glycoprotein Strongly Binds to Membranes in the Absence of Receptor Engagement.ACS infectious diseases · 2024Article
- Physicochemical Nature of SARS-CoV-2 Spike Protein Binding to Human Vimentin.ACS applied materials & interfaces · 2023Article
- Anisotropic Friction in a Ligand-Protein Complex.Nano letters · 2023Article
- Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level.Nature communications · 2022Article
- Force transduction creates long-ranged coupling in ribosomes stalled by arrest peptides.Biophysical journal · 2021Article
- Biological physics by high-speed atomic force microscopy.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2020Review
- Heterogeneous and rate-dependent streptavidin-biotin unbinding revealed by high-speed force spectroscopy and atomistic simulations.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Optimization of Protein-Protein Interaction Measurements for Drug Discovery Using AFM Force Spectroscopy.IEEE transactions on nanotechnology · 2019Article
- Calcium increases titin N2A binding to F-actin and regulated thin filaments.Scientific reports · 2018Article
- Article
- Improving estimation of kinetic parameters in dynamic force spectroscopy using cluster analysis.The Journal of chemical physics · 2018Article
- Developing a molecular picture of soil organic matter-mineral interactions by quantifying organo-mineral binding.Nature communications · 2017Article
- Proteins Breaking Bad: A Free Energy Perspective.The journal of physical chemistry letters · 2017Article
- Single molecule force spectroscopy data and BD- and MD simulations on the blood protein von Willebrand factor.Data in brief · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In dynamic force spectroscopy, single (bio-)molecular bonds are actively broken to assess their range and strength. At low loading rates, the experimentally measured statistical distributions of rupture forces can be analysed using Kramers' theory of spontaneous unbinding. The essentially deterministic unbinding events induced by the extreme forces employed to speed up full-scale molecular simulations have been interpreted in mechanical terms, instead. Here we start from a rigorous probabilistic model of bond dynamics to develop a unified systematic theory that provides exact closed-form expressions for the rupture force distributions and mean unbinding forces, for slow and fast loading protocols. Comparing them with Brownian dynamics simulations, we find them to work well also at intermediate pulling forces. This renders them an ideal companion to Bayesian methods of data analysis, yielding an accurate tool for analysing and comparing force spectroscopy data from a wide range of experiments and simulations.
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.