ArticleThe Journal of physiology2002
Characterization of the cross-bridge force-generating step using inorganic phosphate and BDM in myofibrils from rabbit skeletal muscles.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 111 citations in OpenAlex.
- 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
- The influence of biological sex on the metabolic basis of skeletal muscle fatigue in vivo.The Journal of physiology · 2025Article
- Theoretical treatment of tension transients in muscle following sudden changes in orthophosphate concentration: implications for energy transduction.Journal of muscle research and cell motility · 2025Article
- Skeletal Muscle Fatigue in Rats Is More Consistently Related to Increased Inorganic Phosphate Concentration Than Acidosis.Acta physiologica (Oxford, England) · 2025Article
- Delayed phosphate release can highly improve energy efficiency of muscle contraction.Biophysical journal · 2025Article
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Characterizing the concentration and load dependence of phosphate binding to rabbit fast skeletal actomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A Muscle Physiology-Based Framework for Quantifying Training Load in Resistance Exercises.Sports (Basel, Switzerland) · 2025Article
- A mechanokinetic actomyosin model predicts different orthophosphate sensitivities of force and ATP turnover rate during isometric muscle contraction.Frontiers in physiology · 2025Article
- Cumulative effects of HThe Journal of physiology · 2025Article
- Considering the effect of Pi rebinding on myosin dynamics based on the distinct functions of cardiac and skeletal myosin.Frontiers in physiology · 2025Article
- Phosphate rebinding induces force reversal via slow backward cycling of cross-bridges.Frontiers in physiology · 2024Article
- Creatine Kinase Equilibration and ΔGInternational journal of molecular sciences · 2023Article
- Effects of shortening velocity on the stiffness to force ratio during isometric force redevelopment suggest mechanisms of residual force depression.Scientific reports · 2023Article
- Multistep orthophosphate release tunes actomyosin energy transduction.Nature communications · 2022Article
- Mavacamten has a differential impact on force generation in myofibrils from rabbit psoas and human cardiac muscle.The Journal of general physiology · 2021Article
- Phosphate has dual roles in cross-bridge kinetics in rabbit psoas single myofibrils.The Journal of general physiology · 2021Article
- Sarcomere Length Nonuniformity and Force Regulation in Myofibrils and Sarcomeres.Biophysical journal · 2020Review
- Hypothesis: Single Actomyosin Properties Account for Ensemble Behavior in Active Muscle Shortening and Isometric Contraction.International journal of molecular sciences · 2020Article
- The Location and Rate of the Phosphate Release Step in the Muscle Cross-Bridge Cycle.Biophysical journal · 2020Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The inhibitory effects of inorganic phosphate (P(i)) on isometric force in striated muscle suggest that in the ATPase reaction P(i) release is coupled to force generation. Whether P(i) release and the power stroke are synchronous events or force is generated by an isomerization of the quaternary complex of actomyosin and ATPase products (AM.ADP.P(i)) prior to the following release of P(i) is still controversial. Examination of the dependence of isometric force on [P(i)] in rabbit fast (psoas; 5-15 degrees C) and slow (soleus; 15-20 degrees C) myofibrils was used to test the two-step hypothesis of force generation and P(i) release. Hyperbolic fits of force-[P(i)] relations obtained in fast and slow myofibrils at 15 degrees C produced an apparent asymptote as [P(i)]-->infinity of 0.07 and 0.44 maximal isometric force (i.e. force in the absence of P(i)) in psoas and soleus myofibrils, respectively, with an apparent K(d) of 4.3 mM in both. In each muscle type, the force-[P(i)] relation was independent of temperature. However, 2,3-butanedione 2-monoxime (BDM) decreased the apparent asymptote of force in both muscle types, as expected from its inhibition of the force-generating isomerization. These data lend strong support to models of cross-bridge action in which force is produced by an isomerization of the AM.ADP.P(i) complex immediately preceding the P(i) release step.
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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.