Full text
PDF


Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bagni M. A., Cecchi G., Colomo F., Poggesi C. Tension and stiffness of frog muscle fibres at full filament overlap. J Muscle Res Cell Motil. 1990 Oct;11(5):371–377. doi: 10.1007/BF01739758. [DOI] [PubMed] [Google Scholar]
- Bagni M. A., Cecchi G., Schoenberg M. A model of force production that explains the lag between crossbridge attachment and force after electrical stimulation of striated muscle fibers. Biophys J. 1988 Dec;54(6):1105–1114. doi: 10.1016/S0006-3495(88)83046-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cecchi G., Griffiths P. J., Taylor S. Muscular contraction: kinetics of crossbridge attachment studied by high-frequency stiffness measurements. Science. 1982 Jul 2;217(4554):70–72. doi: 10.1126/science.6979780. [DOI] [PubMed] [Google Scholar]
- Cooke R., White H., Pate E. A model of the release of myosin heads from actin in rapidly contracting muscle fibers. Biophys J. 1994 Mar;66(3 Pt 1):778–788. doi: 10.1016/s0006-3495(94)80854-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Finer J. T., Simmons R. M., Spudich J. A. Single myosin molecule mechanics: piconewton forces and nanometre steps. Nature. 1994 Mar 10;368(6467):113–119. doi: 10.1038/368113a0. [DOI] [PubMed] [Google Scholar]
- Ford L. E., Huxley A. F., Simmons R. M. Tension responses to sudden length change in stimulated frog muscle fibres near slack length. J Physiol. 1977 Jul;269(2):441–515. doi: 10.1113/jphysiol.1977.sp011911. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ford L. E., Huxley A. F., Simmons R. M. Tension transients during the rise of tetanic tension in frog muscle fibres. J Physiol. 1986 Mar;372:595–609. doi: 10.1113/jphysiol.1986.sp016027. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ford L. E., Huxley A. F., Simmons R. M. The relation between stiffness and filament overlap in stimulated frog muscle fibres. J Physiol. 1981 Feb;311:219–249. doi: 10.1113/jphysiol.1981.sp013582. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Harada Y., Sakurada K., Aoki T., Thomas D. D., Yanagida T. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J Mol Biol. 1990 Nov 5;216(1):49–68. doi: 10.1016/S0022-2836(05)80060-9. [DOI] [PubMed] [Google Scholar]
- Higuchi H., Goldman Y. E. Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibres. Nature. 1991 Jul 25;352(6333):352–354. doi: 10.1038/352352a0. [DOI] [PubMed] [Google Scholar]
- Huxley A. F. A note suggesting that the cross-bridge attachment during muscle contraction may take place in two stages. Proc R Soc Lond B Biol Sci. 1973 Feb 27;183(1070):83–86. doi: 10.1098/rspb.1973.0006. [DOI] [PubMed] [Google Scholar]
- Huxley A. F. Muscular contraction. J Physiol. 1974 Nov;243(1):1–43. [PMC free article] [PubMed] [Google Scholar]
- Huxley A. F., Simmons R. M. Proposed mechanism of force generation in striated muscle. Nature. 1971 Oct 22;233(5321):533–538. doi: 10.1038/233533a0. [DOI] [PubMed] [Google Scholar]
- Huxley H. E., Stewart A., Sosa H., Irving T. X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle. Biophys J. 1994 Dec;67(6):2411–2421. doi: 10.1016/S0006-3495(94)80728-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ishijima A., Harada Y., Kojima H., Funatsu T., Higuchi H., Yanagida T. Single-molecule analysis of the actomyosin motor using nano-manipulation. Biochem Biophys Res Commun. 1994 Mar 15;199(2):1057–1063. doi: 10.1006/bbrc.1994.1336. [DOI] [PubMed] [Google Scholar]
- Julian F. J., Morgan D. L. Tension, stiffness, unloaded shortening speed and potentiation of frog muscle fibres at sarcomere lengths below optimum. J Physiol. 1981;319:205–217. doi: 10.1113/jphysiol.1981.sp013902. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lombardi V., Piazzesi G., Linari M. Rapid regeneration of the actin-myosin power stroke in contracting muscle. Nature. 1992 Feb 13;355(6361):638–641. doi: 10.1038/355638a0. [DOI] [PubMed] [Google Scholar]
- Lombardi V., Piazzesi G. The contractile response during steady lengthening of stimulated frog muscle fibres. J Physiol. 1990 Dec;431:141–171. doi: 10.1113/jphysiol.1990.sp018324. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Naber N., Lorenz M., Cooke R. The orientation of spin-probes attached to Cys374 on actin in oriented gels. J Mol Biol. 1994 Feb 25;236(3):703–709. doi: 10.1006/jmbi.1994.1183. [DOI] [PubMed] [Google Scholar]
- Naber N., Ostap E. M., Thomas D. D., Cooke R. Orientation and rotational dynamics of spin-labeled phalloidin bound to actin in muscle fibers. Proteins. 1993 Dec;17(4):347–354. doi: 10.1002/prot.340170403. [DOI] [PubMed] [Google Scholar]
- Nishizaka T., Yagi T., Tanaka Y., Ishiwata S. Right-handed rotation of an actin filament in an in vitro motile system. Nature. 1993 Jan 21;361(6409):269–271. doi: 10.1038/361269a0. [DOI] [PubMed] [Google Scholar]
- Oosawa F. Actin-actin bond strength and the conformational change of F-actin. Biorheology. 1977;14(1):11–19. doi: 10.3233/bir-1977-14102. [DOI] [PubMed] [Google Scholar]
- Ostap E. M., Yanagida T., Thomas D. D. Orientational distribution of spin-labeled actin oriented by flow. Biophys J. 1992 Oct;63(4):966–975. doi: 10.1016/S0006-3495(92)81684-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wakabayashi K., Sugimoto Y., Tanaka H., Ueno Y., Takezawa Y., Amemiya Y. X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction. Biophys J. 1994 Dec;67(6):2422–2435. doi: 10.1016/S0006-3495(94)80729-5. [DOI] [PMC free article] [PubMed] [Google Scholar]