ArticleJournal of muscle research and cell motility2013
Myofilament lattice structure in presence of a skeletal myopathy-related tropomyosin mutation.
Article in Journal of muscle research and cell motility, 2013. 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, 6 citations in OpenAlex.
- Mandibular muscle troponin of the Florida carpenter ant Camponotus floridanus: extending our insights into invertebrate CaJournal of muscle research and cell motility · 2021Article
- X-ray diffraction from flight muscle with a headless myosin mutation: implications for interpreting reflection patterns.Frontiers in physiology · 2014Article
- Introducing a special edition of the Journal of Muscle Research and Cell Motility on tropomyosin: form and function.Journal of muscle research and cell motility · 2013Article
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Authors and funding
2 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human tropomyosin mutations deregulate skeletal muscle contraction at the cellular level. One key feature is the slowing of the kinetics of force development. The aim of the present study was to characterize the potential underlying molecular mechanisms by recording and analyzing the X-ray diffraction patterns of human membrane-permeabilized muscle cells expressing a particular β-tropomyosin mutation (E41K). During resting conditions, the d1,0 lattice spacing, Δ1,0 and I1,1 to I1,0 ratio were not different from control values. These results suggest that, in presence of the E41K β-tropomyosin mutation, the myofilament lattice geometry is well maintained and therefore may not have any detrimental influence on the contraction mechanisms and thus, on the rate of force generation.
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