ArticleJournal of muscle research and cell motility1998
Assembly of force-expressed troponin-I isoforms in myofibrils of cultured cardiac and fast skeletal muscle cells as studied by epitope tagging.
Article in Journal of muscle research and cell motility, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed, 5 citations in OpenAlex.
- Thin-filament-binding domains of cardiac and fast skeletal muscle troponin I isoforms as studied by epitope tagging.Journal of muscle research and cell motility · 1999Article
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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
The isoform-specific assembly of cardiac and skeletal muscle troponin-I (CTnI and FTnI, respectively) on to myofibrils (MFs) was investigated. Epitope tagging was used to monitor the intracellular localization of exogenously introduced constructs to myofibrillar structures in cultured chicken cardiac and fast skeletal (breast) muscle cells. Exogenous CTnI and FTnI were incorporated into endogenous MFs of cardiac and breast muscle cells with high affinity, respectively. In the case of CTnI and FTnI with breast and cardiac muscle cells respectively, CTnI was not incorporated into breast MFs but FTnI was assembled on to cardiac MFs. To determine which portion of TnI is responsible for incorporation into these MFs, we constructed chimeric TnIs with the head and tail of CTnI replaced by those of FTnI. The behaviour of these chimeras depends on the tail of TnIs. These results suggest that the tail regions of TnIs bind to cardiac and breast MFs, and that this affinity of TnI tails is responsible for the assembly of FTnI on to cardiac MFs.
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