Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle-Reference-Cited by-同舟云学术

Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle

Published:1995-06 Issue:6533 Volume:375 Page:688-691
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Irving Malcolm,St Claire Alien Taylor,Sabido-David Cibele,Craik James S.,Brandmeier Birgit,Kendrick-Jones John,Corrie John E. T.,Trentham David R.,Goldman Yale E.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/375688a0.pdf

Reference35 articles.

1. Huxley, H. E. Science 164, 1356–1366 (1969).

2. Lymn, R. W. & Taylor, E. W. Biochemistry 10, 4617–4624 (1971).

3. Huxley, A. F. J. Physiol., Lond. 243, 1–43 (1974).

4. Reedy, M. K., Holmes, K. C. & Tregear, R. T. Nature 207, 1276–1280 (1965).

5. Cooke, R. CRC Crit. Rev. Biochem. 21, 53–118 (1986).

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