The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The Mechanism of Muscle Contractio
Abstract
Knowledge of the mechanism of contraction has been obtained from studies of the interaction of actin and myosin in solution, from an elucidation of the structure of muscle fibers, and from measurements of the mechanics and energetics of fiber contraction. Many of the states and the transition rates between them have been established for the hydrolysis of ATP by actin and myosin subfragments in solution. A major goal is to now understand how the kinetics of this interaction are altered when it occurs in the organized array of the myofibril. Early work on the structure of muscle suggested that changes in the orientation of myosin cross-bridges were responsible for the generation of force. More recently, fluorescent and paramagnetic probes attached to the cross-bridges have suggested that at least some domains of the cross-bridges do not change orientation during force generation. A number of properties of active cross-bridges have been defined by measurements of steady state contractions of fibers and by the transients which follow step changes in fiber length or tension. Taken together these studies have provided firm evidence that force is generated by a cyclic interaction in which a myosin cross-bridge attaches to actin, exerts force through a "powerstroke" of 12 nm, and is then released by the binding of ATP. The mechanism of this interaction at the molecular level remains unknown.
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Citations
Cites
The variation in isometric tension with sarcomere length in vertebrate muscle fibres
Gordon, A. M., Huxley, A. F., & Julian, F. J. (1966) · The Journal of Physiology · doi:10.1113/jphysiol.1966.sp007909 · Cited by 3,152
Structural Changes in Muscle During Contraction: Interference Microscopy of Living Muscle Fibres
HUXLEY, A. F., & NIEDERGERKE, R. (1954) · Nature · doi:10.1038/173971a0 · Cited by 1,608
Dissociation of the actin.subfragment 1 complex by adenyl-5'-yl imidodiphosphate, ADP, and PPi.
Greene, L. E., & Eisenberg, E. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86209-9 · Cited by 151
Cited by
Single myosin molecule mechanics: piconewton forces and nanometre steps
Finer, J. T., Simmons, R. M., & Spudich, J. A. (1994) · Nature · doi:10.1038/368113a0 · Cited by 1,915
Direct observation of kinesin stepping by optical trapping interferometry
Svoboda, K., Schmidt, C. F., Schnapp, B. J., & Block, S. M. (1993) · Nature · doi:10.1038/365721a0 · Cited by 1,910
Bead movement by single kinesin molecules studied with optical tweezers
Block, S. M., Goldstein, L. S. B., & Schnapp, B. J. (1990) · Nature · doi:10.1038/348348a0 · Cited by 1,038
Movement of microtubules by single kinesin molecules
Howard, J., Hudspeth, A. J., & Vale, R. D. (1989) · Nature · doi:10.1038/342154a0 · Cited by 885
Fisher, A. J., Smith, C. A., Thoden, J., Smith, R., Sutoh, K., Holden, H. M., & Rayment, I. (1995) · Biochemistry · doi:10.1021/bi00028a004 · Cited by 600
Metadata
- Authors
- Cooke, R., & Holmes, K. C.
- Venue
- Critical Reviews in Biochemistry
- Publisher
- Informa UK Limited
- Published
- 1986-01
- Volume
- 21
- Issue
- 1
- Pages
- 53-118
- ISSN
- 0045-6411 (ISSN-L)
- 1040-8355
- OpenAlex
- W2218720641
- Cited by
- 427
- References
- 3
- FWCI
- 5.75
- Type
- journal article
- Language
- en
- Open access
- closed
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