ArticleProceedings of the National Academy of Sciences of the United States of America1999
Two heads of myosin are better than one for generating force and motion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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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
81 citing papers in PubMed, 201 citations in OpenAlex.
- The structure of the native cardiac crossbridge in the rigor state.Science advances · 2026Article
- Reconstitution of actomyosin networks in cell-sized liposomes dissects distinct mechanisms of membrane blebbing and symmetry breaking.Science advances · 2026Article
- Cellular elasticity drives mechano-adaptation against fluid shear stress.Journal of cell science · 2025Article
- Engineering filamentous myosins for optical control of contractility.bioRxiv : the preprint server for biology · 2025Article
- Article
- Delayed phosphate release can highly improve energy efficiency of muscle contraction.Biophysical journal · 2025Article
- Deciphering Mechanochemical Influences of Emergent Actomyosin Crosstalk Using QCM-D.Cellular and molecular bioengineering · 2025Article
- Measuring emergent mechanical changes in cytoskeletal ensemblesFrontiers in cell and developmental biology · 2025Article
- Deciphering Mechanochemical Influences of Emergent Actomyosin Crosstalk using QCM-D.bioRxiv : the preprint server for biology · 2024Article
- Philament: A filament tracking program to quickly and accurately analyze in vitro motility assays.Biophysical reports · 2024Article
- Optical Tweezers Apparatus Based on a Cost-Effective IR Laser-Hardware and Software Description.Sensors (Basel, Switzerland) · 2024Article
- Double-headed binding of myosin II to F-actin shows the effect of strain on head structure.Journal of structural biology · 2023Article
- Optimal cell traction forces in a generalized motor-clutch model.Biophysical journal · 2023Article
- Single-molecule mechanics and kinetics of cardiac myosin interacting with regulated thin filaments.Biophysical journal · 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
- The membrane-actin linker ezrin acts as a sliding anchor.Science advances · 2022Article
- Rapid assembly of a polar network architecture drives efficient actomyosin contractility.Cell reports · 2022Article
- Muscle active force-length curve explained by an electrophysical model of interfilament spacing.Biophysical journal · 2022Article
- Anisotropic Elasticity of the Myosin Motor in Muscle.International journal of molecular sciences · 2022Article
- A reverse stroke characterizes the force generation of cardiac myofilaments, leading to an understanding of heart function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
21 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 2 institutions in 1 country.
Funding
Abstract
Several classes of the myosin superfamily are distinguished by their "double-headed" structure, where each head is a molecular motor capable of hydrolyzing ATP and interacting with actin to generate force and motion. The functional significance of this dimeric structure, however, has eluded investigators since its discovery in the late 1960s. Using an optical-trap transducer, we have measured the unitary displacement and force produced by double-headed and single-headed smooth- and skeletal-muscle myosins. Single-headed myosin produces approximately half the displacement and force (approximately 6 nm; 0.7 pN) of double-headed myosin (approximately 10 nm; 1.4 pN) during a unitary interaction with actin. These data suggest that muscle myosins require both heads to generate maximal force and motion.
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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.