ArticleNano letters2016
Titin-Based Nanoparticle Tension Sensors Map High-Magnitude Integrin Forces within Focal Adhesions.
Article in Nano letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
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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
55 citing papers in PubMed, 94 citations in OpenAlex.
- Measuring cellular force using DNA-based tension probes: from ensemble to single-molecule studies.Nature protocols · 2026Review
- Focal adhesion in the tumour metastasis: from molecular mechanisms to therapeutic targets.Biomarker research · 2025Review
- Digital and Tunable Genetically Encoded Tension Sensors Based on Engineered Coiled-Coils.Angewandte Chemie (International ed. in English) · 2025Article
- Analytical methods in studying cell force sensing: principles, current technologies and perspectives.Regenerative biomaterials · 2025Review
- Measuring Integrin Force Loading Rates Using a Two-Step DNA Tension Sensor.Journal of the American Chemical Society · 2024Article
- Article
- Molecular Force Sensors for Biological Application.International journal of molecular sciences · 2024Review
- A portable electrochemical DNA sensor for sensitive and tunable detection of piconewton-scale cellular forces.bioRxiv : the preprint server for biology · 2024Article
- Measuring integrin force loading rates using a two-step DNA tension sensor.bioRxiv : the preprint server for biology · 2024Article
- Molecular Compressive Force Sensor for Mapping Forces at the Cell-Substrate Interface.Journal of the American Chemical Society · 2024Article
- Detection of cellular traction forces via the force-triggered Cas12a-mediated catalytic cleavage of a fluorogenic reporter strand.Nature biomedical engineering · 2023Article
- Article
- DNA Nanotechnology for Investigating Mechanical Signaling in the Immune System.Angewandte Chemie (International ed. in English) · 2023Review
- All-Covalent Nuclease-Resistant and Hydrogel-Tethered DNA Hairpin Probes Map pN Cell Traction Forces.ACS applied materials & interfaces · 2023Article
- A multi-scale clutch model for adhesion complex mechanics.PLoS computational biology · 2023Article
- Filopodial adhesive force in discrete nodes revealed by integrin molecular tension imaging.Current biology : CB · 2022Article
- The magnitude of LFA-1/ICAM-1 forces fine-tune TCR-triggered T cell activation.Science advances · 2022Article
- Biophysical Approaches for Applying and Measuring Biological Forces.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
- Molecular Tension Probes to Quantify Cell-Generated Mechanical Forces.Molecules and cells · 2022Review
- The biophysics of cancer: emerging insights from micro- and nanoscale tools.Advanced nanobiomed research · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Mechanical forces transmitted through integrin transmembrane receptors play important roles in a variety of cellular processes ranging from cell development to tumorigenesis. Despite the importance of mechanics in integrin function, the magnitude of integrin forces within adhesions remains unclear. Literature suggests a range from 1 to 50 pN, but the upper limit of integrin forces remains unknown. Herein we challenge integrins with the most mechanically stable molecular tension probe, which is comprised of the immunoglobulin 27th (I27) domain of cardiac titin flanked with a fluorophore and gold nanoparticle. Cell experiments show that integrin forces unfold the I27 domain, suggesting that integrin forces exceed ∼30-40 pN. The addition of a disulfide bridge within I27 "clamps" the probe and resists mechanical unfolding. Importantly, incubation with a reducing agent initiates SH exchange, thus unclamping I27 at a rate that is dependent on the applied force. By recording the rate of S-S reduction in clamped I27, we infer that integrins apply 110 ± 9 pN within focal adhesions of rat embryonic fibroblasts. The rates of S-S exchange are heterogeneous and integrin subtype-dependent. Nanoparticle titin tension sensors along with kinetic analysis of unfolding demonstrate that a subset of integrins apply tension many fold greater than previously reported.
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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.