ArticleProceedings of the National Academy of Sciences of the United States of America2001
Mapping the actin filament with myosin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 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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Who cites it
80 citing papers in PubMed, 139 citations in OpenAlex.
- Single-Molecule Investigation of Load-Dependent Actomyosin Dissociation Kinetics for Cardiac and Slow Skeletal Myosin.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Membrane-bound myosin IC drives the chiral rotation of the gliding actin filament around its longitudinal axis.Scientific reports · 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
- Myosin essential light chain 1sa decelerates actin and thin filament gliding on β-myosin molecules.The Journal of general physiology · 2022Article
- Cardiac ventricular myosin and slow skeletal myosin exhibit dissimilar chemomechanical properties despite bearing the same myosin heavy chain isoform.The Journal of biological chemistry · 2022Article
- α-catenin switches between a slip and an asymmetric catch bond with F-actin to cooperatively regulate cell junction fluidity.Nature communications · 2022Article
- The Synergic Role of Actomyosin Architecture and Biased Detachment in Muscle Energetics: Insights in Cross Bridge Mechanism Beyond the Lever-Arm Swing.International journal of molecular sciences · 2021Article
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- The Transient Mechanics of Muscle Require Only a Single Force-Producing Cross-Bridge State and a 100 Å Working Stroke.Biology · 2020Article
- Hypothesis: Single Actomyosin Properties Account for Ensemble Behavior in Active Muscle Shortening and Isometric Contraction.International journal of molecular sciences · 2020Article
- Single-molecule analysis reveals that regulatory light chains fine-tune skeletal myosin II function.The Journal of biological chemistry · 2020Article
- MyBP-C: one protein to govern them all.Journal of muscle research and cell motility · 2020Review
- Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview.International journal of molecular sciences · 2019Review
- Spreading of perturbations in myosin group kinetics along actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The load dependence of muscle's force-velocity curve is modulated by alternative myosin converter domains.American journal of physiology. Cell physiology · 2019Article
- Comparing models with one versus multiple myosin-binding sites per actin target zone: The power of simplicity.The Journal of general physiology · 2019Article
- Nonlinear Actomyosin Elasticity in Muscle?Biophysical journal · 2019Article
- Linear Chains of HER2 Receptors Found in the Plasma Membrane Using Liquid-Phase Electron Microscopy.Biophysical journal · 2018Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
20 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
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural studies have shown that the heads of the myosin motor molecule bind preferentially to "target zones" of favorably oriented sites on the helices of the actin filament. We present direct evidence for target zones from the interactions of a single myosin head with an actin filament held between two optically trapped beads. With compliant traps, thermal motions of the filament allow the fixed myosin-S1 to interact with at least two zones, observed as a bi-modal distribution of filament displacements due to myosin binding, whose spacing is near the 36-nm helix repeat distance. The number of binding events and the "apparent working stroke" (mean displacement with myosin bound), vary periodically as the filament is moved past the fixed myosin by displacing the traps; observed periods are close to 36 nm and the apparent stroke varies from 0-10 nm. We also observe a strong modulation at the 5.5-nm actin monomer repeat confirming that myosin interacts with a single strand and that the actin is not free to rotate. Each interaction can be assigned to an actin monomer and each active zone on the helix is made up of three actin monomers.
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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.