ArticleBiophysical journal1995
Flexibility of myosin attachment to surfaces influences F-actin motion.
Article in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 55 citations in OpenAlex.
- Mavacamten inhibits myosin activity by stabilizing the myosin interacting-heads motif and stalling motor force generation.Science advances · 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
- IsJournal of developmental biology · 2025Review
- Dynamic clamping induces rotation-to-beating transition of pinned filaments in gliding assays.Journal of the Royal Society, Interface · 2025Article
- Myosin II Filament Dynamics in Actin Networks Revealed with Interferometric Scattering Microscopy.Biophysical journal · 2020Article
- Comparative analysis of widely used methods to remove nonfunctional myosin heads for the in vitro motility assay.Journal of muscle research and cell motility · 2018Article
- Distinct sites in tropomyosin specify shared and isoform-specific regulation of myosins II and V.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Structural basis for drug-induced allosteric changes to human β-cardiac myosin motor activity.Nature communications · 2015Article
- Regulation of nonmuscle myosin II by tropomyosin.Biochemistry · 2014Article
- A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin.The Journal of biological chemistry · 2013Article
- Human Tonic and Phasic Smooth Muscle Myosin Isoforms Are Unresponsive to the Loop 1 Insert.ISRN structural biology · 2013Article
- Regulation of actin-myosin interaction by conserved periodic sites of tropomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Alternative S2 hinge regions of the myosin rod affect myofibrillar structure and myosin kinetics.Biophysical journal · 2009Article
- Bidirectional cooperative motion of molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Models of motor-assisted transport of intracellular particles.Biophysical journal · 2001Article
- Temperature change does not affect force between single actin filaments and HMM from rabbit muscles.Biophysical journal · 2000Article
- Imaging of thermal activation of actomyosin motors.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Glycine 699 is pivotal for the motor activity of skeletal muscle myosin.The Journal of cell biology · 1996Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
We have analyzed the dependence of actin filament sliding movement on the mode of myosin attachment to surfaces. Monoclonal antibodies (mAbs) that bind to three distinct sites were used to tether myosin to nitrocellulose-coated glass. One antibody reacts with an epitope on the regulatory light chain (LC2) located at the head-rod junction. The other two react with sites in the rod domain, one in the S2 region near the S2-LMM hinge, and the other at the C terminus of the myosin rod. This method of attachment provides a means of controlling the flexibility and density of myosin on the surface. Fast skeletal muscle myosin monomers were bound to the surfaces through the specific interaction with these mAbs, and the sliding movement of fluorescently labeled actin filaments was analyzed by video microscopy. Each of these antibodies produced stable myosin-coated surfaces that supported uniform motion of actin over the course of several hours. Attachment of myosin through the anti-S2 and anti-LMM mAbs yielded significantly higher velocities (10 microns/s at 30 degrees C) than attachment through anti-LC2 (4-5 microns/s at 30 degrees C). For each antibody, we observed a characteristic value of the myosin density for the onset of F-actin motion and a second critical density for velocity saturation. The specific mode of attachment influences the velocity of actin filaments and the characteristic surface density needed to support movement.
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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.