ArticleActa neuropathologica1993
Size and localization of dystrophin molecule: immunoelectron microscopic and freeze etching studies of muscle plasma membranes of murine skeletal myofibers.
Article in Acta neuropathologica, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 18 citations in OpenAlex.
- Costameres, dense plaques and podosomes: the cell matrix adhesions in cardiovascular mechanosensing.Journal of muscle research and cell motility · 2019Review
- Absence of Dystrophin Disrupts Skeletal Muscle Signaling: Roles of Ca2+, Reactive Oxygen Species, and Nitric Oxide in the Development of Muscular Dystrophy.Physiological reviews · 2016Review
- In situ molecular association of dystrophin with actin revealed by sensitized emission immuno-resonance energy transfer.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Visualization of the subsarcolemmal cytoskeleton network of mouse skeletal muscle cells by en face views and application to immunoelectron localization of dystrophin.Journal of muscle research and cell motility · 1995Article
- Ultrastructural localization of the C-terminus of the 43-kd dystrophin-associated glycoprotein and its relation to dystrophin in normal murine skeletal myofiber.The American journal of pathology · 1995Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ultrastructure and mode of existence of the dystrophin molecule and its relations to actin filaments were examined in murine skeletal myofibers. Electron microscopy of freeze-etched replicas of gold-labelled dystrophin molecules in quick-freeze, deep-etch, rotary-shadow preparations revealed rod-like structures 108.2 +/- 16.3 nm long and 3.1 +/- 1.5 nm thick. Some dystrophin molecules appeared to link their ends to form anastomosing networks; others were separate from each other. The dystrophin molecules were parallel or nearly parallel to the inner surface of the muscle plasma membrane. Double immuno-labelling transmission electron microscopy using N- and C-terminal dystrophin antibodies showed that the group mean distances of the N- and C-terminal signals from the muscle plasma membrane were 52.7 +/- 8.1 nm and 45.9 +/- 11.3 nm, respectively, which were not significantly different. Histograms of the distribution of the N- and C-terminal distances from the muscle plasma membrane had similar patterns with peaks 10-20 nm from the membrane. This was consistent with the findings of the mode of existence of dystrophin molecules seen in freeze-etched replicas. Finally, the dystrophin molecules were linked with the most peripheral sarcoplasmic actin like filaments, end to side as well as end to end.
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