ArticleJournal of muscle research and cell motility1993
X-ray diffraction study on mammalian visceral smooth muscles in resting and activated states.
Article in Journal of muscle research and cell motility, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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
7 citing papers in PubMed, 33 citations in OpenAlex.
- Myosin assembly of smooth muscle: from ribbons and side polarity to a row polar helical model.Journal of muscle research and cell motility · 2022Article
- Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021Review
- Reply from Chun Y. Seow.The Journal of physiology · 2015Article
- Blebbistatin, a myosin II inhibitor, suppresses Ca(2+)-induced and "sensitized"-contraction of skinned tracheal muscles from guinea pig.Journal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi · 2013Article
- Direct evidence for functional smooth muscle myosin II in the 10S self-inhibited monomeric conformation in airway smooth muscle cells.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Myosin filament structure in vertebrate smooth muscle.The Journal of cell biology · 1996Article
- Plasticity in canine airway smooth muscle.The Journal of general physiology · 1995Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural changes of guinea pig taenia coli and rat anococcygeus muscle during contraction were studied by X-ray diffraction. The diffraction pattern of the taenia coli showed the 14.4-nm myosin reflection, the 5.9-nm actin layer-line and a diffuse equatorial peak at 1/11.4 nm-1. On application of carbachol, the muscle contracted and the intensity of the 14.4-nm reflection showed a concentration-dependent decrease: the maximum decrease was 24% at 2 x 10(-5) M. Such an intensity decrease was not observed in K-contracture (154 mM). The intensity of the 5.9-nm actin layer-line did not change appreciably on activation. The equatorial peak became broader during contraction. The 14.4-nm myosin reflection of the anococcygeus muscle was weak. Its intensity increased by 106% during contraction induced by 2 x 10(-5) M phenylephrine and by 75% during K-contracture. These results suggest that the number of myosin filaments may increase during contraction of rat anococcygeus muscle but not guinea pig taenia coli.
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