ArticleJournal of muscle research and cell motility1993
Distribution of connectin (titin), nebulin and alpha-actinin at myotendinous junctions of chicken pectoralis muscles: an immunofluorescence and immunoelectron microscopic study.
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 3 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
3 citing papers in PubMed, 11 citations in OpenAlex.
- Proteomic analysis of laser capture microscopy purified myotendinous junction regions from muscle sections.Proteome science · 2014Article
- Isoforms of alpha-actinin from cardiac, smooth, and skeletal muscle form polar arrays of actin filaments.The Journal of cell biology · 2000Article
- The muscle Z band: lessons in stress management.Journal of muscle research and cell motility · 1994Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The distribution of connectin (titin), nebulin and alpha-actinin in the areas of myotendinous junctions of chicken pectoralis muscles was examined by immunocytochemical methods. Staining with antibodies against connectin (4C9, SM1 and P1200) and nebulin formed 'doublets' flanking nonterminal Z-bands; near the end of muscle fibres 'singlets' were seen within the terminal sarcomere on the side adjacent to the terminal Z-bands. The apical regions of muscle processes, where no myosin filaments are present although actin filaments exist, were reactive with anti-nebulin but not with anti-connectin. Antibodies against pectoralis (skeletal muscle type) alpha-actinin stained non terminal Z-bands and that against gizzard (smooth muscle type) the sarcolemma. Terminal Z-bands were unreactive with both of these antibodies. These findings indicate that, although terminal and nonterminal Z-bands differ in their molecular composition, connectin and nebulin filaments appear to link myosin and actin filaments, respectively, to both Z-band types.
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