ArticleThe EMBO journal1991
A nucleation--elongation mechanism for the self-assembly of side polar sheets of smooth muscle myosin.
Article in The EMBO journal, 1991. 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, 33 citations in OpenAlex.
- Evaluation of fendiline treatment in VP40 system with nucleation-elongation process: a computational model of Ebola virus matrix protein assembly.Microbiology spectrum · 2024Article
- Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021Review
- Evidence for S2 flexibility by direct visualization of quantum dot-labeled myosin heads and rods within smooth muscle myosin filaments moving on actin in vitro.The Journal of general physiology · 2021Article
- The kinetics underlying the velocity of smooth muscle myosin filament sliding on actin filaments in vitro.The Journal of biological chemistry · 2014Article
- Myosin filaments in smooth muscle cells do not have a constant length.The Journal of physiology · 2013Article
- Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- The carboxyl-terminal isoforms of smooth muscle myosin heavy chain determine thick filament assembly properties.The Journal of cell biology · 2002Article
- Myorod, a thick filament protein in molluscan smooth muscles: isolation, polymerization and interaction with myosin.Journal of muscle research and cell motility · 2001Article
- Myosin filament structure in vertebrate smooth muscle.The Journal of cell biology · 1996Article
- Core binding factor beta-smooth muscle myosin heavy chain chimeric protein involved in acute myeloid leukemia forms unusual nuclear rod-like structures in transformed NIH 3T3 cells.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Role of the COOH-terminal nonhelical tailpiece in the assembly of a vertebrate nonmuscle myosin rod.The Journal of cell biology · 1992Article
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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
Self-assembled filaments of smooth muscle myosin were observed by low dose electron microscopy to be flat side-polar sheets, in which the component molecules appeared straight and close-packed. Fraying experiments released small oligomers, in which molecules were staggered in parallel by about +/- 14 nm relative to two immediate neighbours, and were bound also to an antiparallel partner via a approximately 14 nm overlap at the very tip of the tail. We suggest a filament model which preserves these packing relationships. Adding stoichiometric amounts of MgATP to the filaments caused them to disassemble completely by progressive loss of material from their ends, at a limiting rate equivalent to about 2 monomers per second per end in physiological saline. The rate of the competing association reaction varied linearly with the monomer concentration, as determined in pressure-jump experiments. This suggests that myosin monomers, rather than dimers or higher oligomers, are the building blocks of these filaments. Shearing and annealing of assembled filaments appeared negligible on a time scale of a few hours. In consequence, filament number and filament length were dependent on the rate at which monomers were supplied to the assembly reaction, and on the number of filaments already present at the start of the assembly reaction.
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