The DOI matches its Crossref record; 108 of the 108 references it cites were found in a registry or an index.
Mechanism of Actomyosin Atpase and the Problem of Muscle Contractio
Abstract
Publisher Summary This chapter discusses the mechanism of actomyosin ATPase and the problem of muscle contraction. Actomyosin, like any other enzyme, brings about the hydrolysis of its substrate by a series of intermediate steps. The purpose of kinetic studies is to determine the sequence of intermediate steps in the mechanism and to measure the respective rate constants. The well known sliding filament model of Hanson and Huxley attributes the shortening of a sarcomere to the relative motion of the thin filaments with respect to the thick filaments. Experiments have failed to detect any change in thick and thin filament lengths with sarcomere length. The force that produces sliding or the development of tension at fixed length must be attributed either to the direct action, and consequently the movement of the cross bridges, or to electrostatic and van der Waals forces possibly mediated by the cross bridge projections but not requiring to and fro movements of the bridges
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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
Muscle Structure and Theories of Contraction
Huxley, A. F. (1957) · Progress in Biophysics and Biophysical Chemistry · doi:10.1016/s0096-4174(18)30128-8 · Cited by 2,318
Proposed Mechanism of Force Generation in Striated Muscle
HUXLEY, A. F., & SIMMONS, R. M. (1971) · Nature · doi:10.1038/233533a0 · Cited by 2,272
ATPase Activity of Myosin Correlated with Speed of Muscle Shortening
Bárány, M. (1967) · The Journal of General Physiology · doi:10.1085/jgp.50.6.197 · Cited by 1,968
Huxley, H. E. (1969) · Science · doi:10.1126/science.164.3886.1356 · Cited by 1,959
HUXLEY, H., & HANSON, J. (1954) · Nature · doi:10.1038/173973a0 · Cited by 1,751
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
Huxley, H. E. (1963) · Journal of Molecular Biology · doi:10.1016/s0022-2836(63)80008-x · Cited by 1,466
Mechanism of adenosine triphosphate hydrolysis by actomyosin
Lymn, R. W., & Taylor, E. W. (1971) · Biochemistry · doi:10.1021/bi00801a004 · Cited by 1,321
Self-citationHuxley, H. E., & Brown, W. (1967) · Journal of Molecular Biology · doi:10.1016/s0022-2836(67)80046-9 · Cited by 1,097
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
On the attribution and additivity of binding energies
Jencks, W. P. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.7.4046 · Cited by 912
Spudich, J. A. (1994) · Nature · doi:10.1038/372515a0 · Cited by 438
Thin Filament Proteins and Thin Filament-Linked Regulation of Vertebrate Muscle Contractio
Leavis, P. C., Gergely, J., & Szent-Gyorgyi, A. G. (1984) · Critical Reviews in Biochemistry · doi:10.3109/10409238409108717 · Cited by 406
Kinesin ATPase: rate-limiting ADP release
Hackney, D. D. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.17.6314 · Cited by 239
Metadata
- Authors
- Taylor, E. W., & Trenlham, D. R.
- Venue
- CRC Critical Reviews in Biochemistry
- Publisher
- Informa UK Limited
- Published
- 1979-01
- Volume
- 6
- Issue
- 2
- Pages
- 103-164
- ISSN
- 0045-6411 (ISSN-L)
- OpenAlex
- W2171718050
- Cited by
- 406
- References
- 108
- FWCI
- 2.82
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
