ArticleBiophysical journal2006
Effects of the number of actin-bound S1 and axial force on X-ray patterns of intact skeletal muscle.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- The distinctive mechanical and structural signatures of residual force enhancement in myofibers.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Myosin-binding protein C regulates the sarcomere lattice and stabilizes the OFF states of myosin heads.Nature communications · 2024Article
- Myosin-binding protein C forms C-links and stabilizes OFF states of myosin.bioRxiv : the preprint server for biology · 2023Article
- Non-cross Bridge Viscoelastic Elements Contribute to Muscle Force and Work During Stretch-Shortening Cycles: Evidence From Whole Muscles and Permeabilized Fibers.Frontiers in physiology · 2021Article
- Monitoring the myosin crossbridge cycle in contracting muscle: steps towards 'Muscle-the Movie'.Journal of muscle research and cell motility · 2019Review
- Effects of myosin inhibitors on the X-ray diffraction patterns of relaxed and calcium-activated rabbit skeletal muscle fibers.Biophysics and physicobiology · 2018Article
- A cross-bridge cycle with two tension-generating steps simulates skeletal muscle mechanics.Biophysical journal · 2013Article
- Crossbridge and filament compliance in muscle: implications for tension generation and lever arm swing.Journal of muscle research and cell motility · 2010Review
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8 authors.
Funding
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Abstract
Effects of the number of actin-bound S1 and of axial tension on x-ray patterns from tetanized, intact skeletal muscle fibers were investigated. The muscle relaxant, BDM, reduced tetanic M3 meridional x-ray reflection intensity (I(M3)), M3 spacing (d(M3)), and the equatorial I(11)/I(10) ratio in a manner consistent with a reduction in the fraction of S1 bound to actin rather than by generation of low-force S1-actin isomers. At complete force suppression, I(M3) was 78% of its relaxed value. BDM distorted dynamic I(M3) responses to sinusoidal length oscillations in a manner consistent with an increased cross-bridge contribution to total sarcomere compliance, rather than a changed S1 lever orientation in BDM. When the number of actin-bound S1 was varied by altering myofilament overlap, tetanic I(M3) at low overlap was similar to that in high [BDM] (79% of relaxed I(M3)). Tetanic d(M3) dependence on active tension in overlap experiments differed from that observed with BDM. At high BDM, tetanic d(M3) approached its relaxed value (14.34 nm), whereas tetanic d(M3) at low overlap was 14.50 nm, close to its value at full overlap (14.56 nm). This difference in tetanic d(M3) behavior was explicable by a nonlinear thick filament compliance which is extended by both active and passive tension.
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