ArticleJournal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology2011
Variation in the determinants of power of chemically skinned type I rat soleus muscle fibres.
Article in Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 13 citations in OpenAlex.
- A Comparison of the Force-Velocity Relationship of Bonobo and Human Muscle Fibers.Journal of experimental zoology. Part A, Ecological and integrative physiology · 2025Article
- Calcium-dependent titin-thin filament interactions in muscle: observations and theory.Journal of muscle research and cell motility · 2020Review
- The load dependence of muscle's force-velocity curve is modulated by alternative myosin converter domains.American journal of physiology. Cell physiology · 2019Article
- Hill's equation of muscle performance and its hidden insight on molecular mechanisms.The Journal of general physiology · 2013Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We explored to which extent maximal velocity of shortening (Vmax), force per cross-sectional area (specific tension, Po) and curvature of the force-velocity relationship (a/Po in the Hill equation) contribute to differences in peak power of single, chemically skinned rat type I fibres. Force-velocity relationships were determined from isotonic contractions of 94 maximally activated fibres. Peak power (±SD) was 3.50±1.64 WL(-1). There was a tenfold range of peak power and five-, six- and fourfold ranges for Po, Vmax and a/Po, respectively. None of the differences between fibres was explicable by differences in myosin heavy or light chain composition. The inverse relationship between a/Po and Vmax suggests a similar underlying cause. Fitting the data to the Huxley (Progr Biophys Biophys Chem 7:255-318, 1957) cross-bridge model showed that the rate constant g (2) and the sum of the rate constants (f+g(1)) co-varied, both being low in the slowest fibres. Approximately 16% of the variation in Po could be explained by variation in the proportion of attached cycling cross-bridges (f/(f+g(1))), but the origin of most of the variance in Po remains unknown.
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Registered trials
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