ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2018
Structure before function: myosin binding protein-C slow is a structural protein with regulatory properties.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- From bedside to bench: A multimodal approach uncovering the molecular basis of theProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Sex-dependent and muscle-specific progression of the MYBPC1 E248K Myotrem myopathy in response to aging.JCI insight · 2025Article
- Pulsatile Myofilament Activity in Myotrem Myopathy Associated with Myogenic Tremor.International journal of molecular sciences · 2025Article
- Functional role of myosin-binding protein H in thick filaments of developing vertebrate fast-twitch skeletal muscle.The Journal of general physiology · 2024Article
- Compound heterozygous variants in MYBPC1 lead to severe distal arthrogryposis type-1 manifestations.Gene · 2024Article
- Functional role of myosin-binding protein H in thick filaments of developing vertebrate fast-twitch skeletal muscle.bioRxiv : the preprint server for biology · 2024Article
- Myosin-binding protein C regulates the sarcomere lattice and stabilizes the OFF states of myosin heads.Nature communications · 2024Article
- Unlocking the Role of sMyBP-C: A Key Player in Skeletal Muscle Development and Growth.bioRxiv : the preprint server for biology · 2023Article
- Myosin-binding protein C forms C-links and stabilizes OFF states of myosin.bioRxiv : the preprint server for biology · 2023Article
- Cryo-electron tomography of intact cardiac muscle reveals myosin binding protein-C linking myosin and actin filaments.Journal of muscle research and cell motility · 2023Article
- Etiology of genetic muscle disorders induced by mutations in fast and slow skeletal MyBP-C paralogs.Experimental & molecular medicine · 2023Review
- Skeletal myopathy in a rat model of postmenopausal heart failure with preserved ejection fraction.Journal of applied physiology (Bethesda, Md. : 1985) · 2022Article
- Article
- Fast skeletal myosin-binding protein-C regulates fast skeletal muscle contraction.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Skeletal MyBP-C isoforms tune the molecular contractility of divergent skeletal muscle systems.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Heterozygous variants in MYBPC1 are associated with an expanded neuromuscular phenotype beyond arthrogryposis.Human mutation · 2019Article
- Skeletal myosin binding protein-C: An increasingly important regulator of striated muscle physiology.Archives of biochemistry and biophysics · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Myosin binding protein-C slow (sMyBP-C) comprises a family of accessory proteins in skeletal muscles that bind both myosin and actin filaments. Herein, we examined the role of sMyBP-C in adult skeletal muscles using in vivo gene transfer and clustered regularly interspaced short palindromic repeats technology to knock down all known sMyBP-C variants. Our findings, confirmed in two different skeletal muscles, demonstrated efficient knockdown (KD) of sMyBP-C (>70%) resulting in notably decreased levels of thick, but not thin, filament proteins ranging from ∼50% for slow and fast myosin to ∼20% for myomesin. Consistent with this, A bands were selectively distorted, and sarcomere length was significantly reduced. Contrary to earlier in vitro studies showing that addition of recombinant sMyBP-C slows down the formation of actomyosin crossbridges, our work demonstrates that KD of sMyBP-C in intact myofibers results in decreased contraction and relaxation kinetics under no-load conditions. Similarly, KD muscles develop markedly reduced twitch and tetanic force and contraction velocity. Taken together, our results show that sMyBP-C is essential for the regular organization and maintenance of myosin filaments into A bands and that its structural role precedes its ability to regulate actomyosin crossbridges.-Geist, J., Ward, C. W., Kontrogianni-Konstantopoulos, A. Structure before function: myosin binding protein-C slow is a structural protein with regulatory properties.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.