ArticleNature methods2012
Ultrafast force-clamp spectroscopy of single molecules reveals load dependence of myosin working stroke.
Article in Nature methods, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 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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Who cites it
82 citing papers in PubMed, 143 citations in OpenAlex.
- Cross-bridge model for predicting muscle short-range stiffness during movement.PLoS computational biology · 2026Article
- Light-Guided Molecular Patterning for High-Throughput Single-Molecule Mechanical Characterization.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Interaction Between an Individual Cohesin Complex and DNA Revealed by Optical Tweezers and Single-Molecule Microscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- S2Tag, a novel affinity tag for the capture and immobilization of coiled-coil proteins: Application to the study of human β-cardiac myosin.The Journal of biological chemistry · 2025Article
- Ndc80 complex, a conserved coupler for kinetochore-microtubule motility, is a sliding molecular clutch.Science advances · 2025Article
- Delayed phosphate release can highly improve energy efficiency of muscle contraction.Biophysical journal · 2025Article
- FAIR data for optical tweezers experiments.Biophysical journal · 2025Review
- Dual-fiber optical tweezers integrating high-sensitivity structured-light displacement measurement system on fiber end-face.Scientific reports · 2025Article
- High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- High resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory.bioRxiv : the preprint server for biology · 2025Article
- The order of things: phosphate release or the power stroke, which does actomyosin do first?Frontiers in physiology · 2025Review
- Multiple pathways of the actin-myosin cycle in energy transduction and the release of orthophosphate in muscle.Frontiers in physiology · 2025Review
- Considering the effect of Pi rebinding on myosin dynamics based on the distinct functions of cardiac and skeletal myosin.Frontiers in physiology · 2025Article
- Single-Molecule Investigation of Load-Dependent Actomyosin Dissociation Kinetics for Cardiac and Slow Skeletal Myosin.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Modeling thick filament activation suggests a molecular basis for force depression.Biophysical journal · 2024Article
- Phosphate rebinding induces force reversal via slow backward cycling of cross-bridges.Frontiers in physiology · 2024Article
- A mutation in switch I alters the load-dependent kinetics of myosin Va.Nature communications · 2023Article
- Cooperativity of myosin II motors in the non-regulated and regulated thin filaments investigated with high-speed AFM.The Journal of general physiology · 2023Article
- Particle Localization Using Local Gradients and Its Application to Nanometer Stabilization of a Microscope.ACS nano · 2022Article
- α-catenin switches between a slip and an asymmetric catch bond with F-actin to cooperatively regulate cell junction fluidity.Nature communications · 2022Article
22 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We describe a dual-trap force-clamp configuration that applies constant loads between a binding protein and an intermittently interacting biological polymer. The method has a measurement delay of only ∼10 μs, allows detection of interactions as brief as ∼100 μs and probes sub-nanometer conformational changes with a time resolution of tens of microseconds. We tested our method on molecular motors and DNA-binding proteins. We could apply constant loads to a single motor domain of myosin before its working stroke was initiated (0.2-1 ms), thus directly measuring its load dependence. We found that, depending on the applied load, myosin weakly interacted (<1 ms) with actin without production of movement, fully developed its working stroke or prematurely detached (<5 ms), thus reducing the working stroke size with load. Our technique extends single-molecule force-clamp spectroscopy and opens new avenues for investigating the effects of forces on biological processes.
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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.