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- W2980245376 abstract "Significance Myosin-binding protein C (MyBP-C) is a critical component of the skeletal muscle sarcomere, muscle’s smallest contractile unit. MyBP-C’s importance is evident by genetic mutations leading to human myopathies, such as distal arthrogryposis (i.e., club foot). However, the molecular basis of MyBP-C’s functional impact on skeletal muscle contractility is far from certain. Complicating matters further is the expression of fast- and slow-type MyBP-C isoforms that depend on whether the muscle is fast- or slow-twitch. Using multiscale proteomic, biophysical, and mathematical modeling approaches, we defined the expression, localization, and modulatory capacities of these distinct skeletal MyBP-C isoforms in rat skeletal muscles. Each MyBP-C isoform modulates muscle contractility differentially, providing the capacity to fine-tune a muscle’s mechanical performance as physiological demands arise." @default.
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- W2980245376 date "2019-10-07" @default.
- W2980245376 modified "2023-10-16" @default.
- W2980245376 title "Skeletal MyBP-C isoforms tune the molecular contractility of divergent skeletal muscle systems" @default.
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- W2980245376 doi "https://doi.org/10.1073/pnas.1910549116" @default.
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