ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2004
Adenosine diphosphate and strain sensitivity in myosin motors.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 127 papers.
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Who cites it
127 citing papers in PubMed, 187 citations in OpenAlex.
- Isometric slow- and fast-contracting skeletal muscle fibres have more similar cellular and molecular properties at 37°C than at 25°C in older adults.The Journal of physiology · 2026Article
- Phosphate and acidosis cause fibre type-specific changes to cellular and molecular contractile mechanics at 37°C in skeletal muscle from older adults.Experimental physiology · 2026Article
- Load-Dependent Effects of Sodium Glucose Co-Transporter Inhibitors on Work in Human Hypertrophic Cardiomyopathy Living Myocardial Slices.bioRxiv : the preprint server for biology · 2026Article
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Functional control of myosin motors in the cardiac cycle.Nature reviews. Cardiology · 2025Review
- Multiple pathways of the actin-myosin cycle in energy transduction and the release of orthophosphate in muscle.Frontiers in physiology · 2025Review
- A mechanokinetic actomyosin model predicts different orthophosphate sensitivities of force and ATP turnover rate during isometric muscle contraction.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
- Dual effect of N-terminal deletion of cardiac myosin essential light chain in mitigating cardiomyopathy.iScience · 2024Article
- Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024Review
- Communication between DNA and nucleotide binding sites facilitates stepping by the RecBCD helicase.Nucleic acids research · 2024Article
- Excitable dynamics driven by mechanical feedback in biological tissues.Communications physics · 2024Article
- Double-headed binding of myosin II to F-actin shows the effect of strain on head structure.Journal of structural biology · 2023Article
- Matching Mechanics and Energetics of Muscle Contraction Suggests Unconventional Chemomechanical Coupling during the Actin-Myosin Interaction.International journal of molecular sciences · 2023Article
- Single-molecule mechanics and kinetics of cardiac myosin interacting with regulated thin filaments.Biophysical journal · 2023Article
- Conformational changes linked to ADP release from human cardiac myosin bound to actin-tropomyosin.The Journal of general physiology · 2023Article
- MgADP Promotes Myosin Head Movement toward Actin at Low [CaInternational journal of molecular sciences · 2022Article
- Multistep orthophosphate release tunes actomyosin energy transduction.Nature communications · 2022Article
- Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia.Science advances · 2022Article
- Inorganic phosphate accelerates cardiac myofilament relaxation in response to lengthening.Frontiers in physiology · 2022Article
67 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
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The release of adenosine diphosphate (ADP) from the actomyosin cross-bridge plays an important role in the adenosine-triphosphate-driven cross-bridge cycle. In fast contracting muscle fibres, the rate at which ADP is released from the cross-bridge correlates with the maximum shortening velocity of the muscle fibre, and in some models the rate of ADP release defines the maximum shortening velocity. In addition, it has long been thought that the rate of ADP release could be sensitive to the load on the cross-bridge and thereby provide a molecular explanation of the Fenn effect. However, direct evidence of a strain-sensitive ADP-release mechanism has been hard to come by for fast muscle myosins. The recently published evidence for a strain-sensing mechanism involving ADP release for slower muscle myosins, and in particular non-muscle myosins, is more compelling and can provide the mechanism of processivity for motors such as myosin V. It is therefore timely to examine the evidence for this strain-sensing mechanism. The evidence presented here will argue that a strain-sensitive mechanism of ADP release is universal for all myosins but the basic mechanism has evolved in different ways for different types of myosin. Furthermore, this strain-sensing mechanism provides a way of coordinating the action of multiple myosin motor domains in a single myosin molecule, or in complex assemblies of myosins over long distances without invoking a classic direct allosteric or cooperative communication between motors.
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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.