ArticleThe Journal of cell biology1984
ATP-dependent movement of myosin in vitro: characterization of a quantitative assay.
Article in The Journal of cell biology, 1984. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 121 citations in OpenAlex.
- Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90.Nature communications · 2024Article
- The emergence and transient behaviour of collective motion in active filament systems.Nature communications · 2017Article
- Beam finite-element model of a molecular motor for the simulation of active fibre networks.Proceedings. Mathematical, physical, and engineering sciences · 2016Article
- Diffusion of GPI-anchored proteins is influenced by the activity of dynamic cortical actin.Molecular biology of the cell · 2015Article
- Polar Pattern Formation in Driven Filament Systems Require Non-Binary Particle Collisions.Nature physics · 2015Article
- Random bursts determine dynamics of active filaments.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Allosteric effects of cardiac troponin TNT1 mutations on actomyosin binding: a novel pathogenic mechanism for hypertrophic cardiomyopathy.Archives of biochemistry and biophysics · 2014Article
- Global fit analysis of myosin-5b motility reveals thermodynamics of Mg2+-sensitive acto-myosin-ADP states.PloS one · 2013Article
- A promising new wavelength region for three-photon fluorescence microscopy of live cells.Journal of microscopy · 2012Article
- Transiently crosslinked F-actin bundles.European biophysics journal : EBJ · 2011Article
- Polar patterns of driven filaments.Nature · 2010Article
- Article
- Molecular motor-induced instabilities and cross linkers determine biopolymer organization.Biophysical journal · 2007Article
- Link between the enzymatic kinetics and mechanical behavior in an actomyosin motor.Biophysical journal · 2001Article
- Flexibility of myosin attachment to surfaces influences F-actin motion.Biophysical journal · 1995Article
- Evidence for myosin motors on organelles in squid axoplasm.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Depressed sliding velocity of isolated cardiac myosin from cardiomyopathic hamsters: evidence for an alteration in mechanical interaction of actomyosin.Molecular and cellular biochemistry · 1993Article
- The evolutionary relationship of avian and mammalian myosin heavy-chain genes.Journal of molecular evolution · 1993Article
- Active movement of cardiac myosin on Characeae actin cables.Pflugers Archiv : European journal of physiology · 1992Article
- Assembly of avian skeletal muscle myosins: evidence that homodimers of the heavy chain subunit are the thermodynamically stable form.The Journal of cell biology · 1991Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Sheetz and Spudich (1983, Nature (Lond.), 303:31-35) showed that ATP-dependent movement of myosin along actin filaments can be measured in vitro using myosin-coated beads and oriented actin cables from Nitella. To establish this in vitro movement as a quantitative assay and to understand better the basis for the movement, we have defined the factors that affect the myosin-bead velocity. Beads coated with skeletal muscle myosin move at a rate of 2-6 micron/s, depending on the myosin preparation. This velocity is independent of myosin concentration on the bead surface for concentrations above a critical value (approximately 20 micrograms myosin/2.5 X 10(9) beads of 1 micron in diameter). Movement is optimal between pH 6.8 and 7.5, at KCl concentrations less than 70 mM, at ATP concentrations greater than 0.1 mM, and at Mg2+ concentrations between 2 and 6 mM. From the temperature dependence of bead velocity, we calculate activation energies of 90 kJ/mol below 22 degrees C and 40 kJ/mol above 22 degrees C. Different myosin species move at their own characteristic velocities, and these velocities are proportional to their actin-activated ATPase activities. Further, the velocities of beads coated with smooth or skeletal muscle myosin correlate well with the known in vivo rates of myosin movement along actin filaments in these muscles. This in vitro assay, therefore, provides a rapid, reproducible method for quantitating the ATP-dependent movement of myosin molecules on actin.
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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.