ArticleJournal of muscle research and cell motility2005
Can the passive elasticity of muscle be explained directly from the mechanics of individual titin molecules?
Article in Journal of muscle research and cell motility, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed, 9 citations in OpenAlex.
- Superhelical architecture of the myosin filament-linking protein myomesin with unusual elastic properties.PLoS biology · 2012Article
- Pulling single molecules of titin by AFM--recent advances and physiological implications.Pflugers Archiv : European journal of physiology · 2008Review
- Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin.The EMBO journal · 2008Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent progress in understanding the role of titin/connectin in muscle elasticity has been heavily based on results from single molecule mechanical experiments. The shape of force-extension curves from such data is similar to curves from muscle fibres and it has been tempting to assume that muscle elasticity can be extrapolated directly from the single molecule data. In this paper we discuss some of the factors that act on titin in the sarcomere that are likely to preclude such a direct extrapolation.
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