ArticleBiophysical journal2002
Mammalian cardiac muscle thick filaments: their periodicity and interactions with actin.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- A FRET assay to monitor different structural states of human β-cardiac myosin including the interacting-heads motif.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A FRET assay to quantitate levels of the human β-cardiac myosin interacting heads motif based on its near-atomic resolution structure.bioRxiv : the preprint server for biology · 2024Article
- Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filaments.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Through Thick and Thin--Interfilament Communication in Muscle.Biophysical journal · 2015Article
- Zebrafish cardiac muscle thick filaments: isolation technique and three-dimensional structure.Biophysical journal · 2014Article
- Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.Journal of structural biology · 2011Article
- Cardiac myosin binding protein-C is essential for thick-filament stability and flexural rigidity.Biophysical journal · 2009Article
- Blebbistatin stabilizes the helical order of myosin filaments by promoting the switch 2 closed state.Biophysical journal · 2008Article
- Myosin filament 3D structure in mammalian cardiac muscle.Journal of structural biology · 2008Article
- The structure of isolated cardiac Myosin thick filaments from cardiac Myosin binding protein-C knockout mice.Biophysical journal · 2008Article
- Three-dimensional structure of vertebrate cardiac muscle myosin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- X-ray diffraction studies of the thick filament in permeabilized myocardium from rabbit.Biophysical journal · 2006Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Cardiac muscle has been extensively studied, but little information is available on the detailed macromolecular structure of its thick filament. To elucidate the structure of these filaments I have developed a procedure to isolate the cardiac thick filaments for study by electron microscopy and computer image analysis. This procedure uses chemical skinning with Triton X-100 to avoid contraction of the muscle that occurs using the procedures previously developed for isolation of skeletal muscle thick filaments. The negatively stained isolated filaments appear highly periodic, with a helical repeat every third cross-bridge level (43 nm). Computed Fourier transforms of the filaments show a strong set of layer lines corresponding to a 43-nm near-helical repeat out to the 6th layer line. Additional meridional reflections extend to at least the 12th layer line in averaged transforms of the filaments. The highly periodic structure of the filaments clearly suggests that the weakness of the layer lines in x-ray diffraction patterns of heart muscle is not due to an inherently more disordered cross-bridge arrangement. In addition, the isolated thick filaments are unusual in their strong tendency to remain bound to actin by anti-rigor oriented cross-bridges (state II or state III cross-bridges) under relaxing conditions.
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