The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Fluorescent actin filaments move on myosin fixed to a glass surface.
Open accessAbstract
Single actin filaments stabilized with fluorescent phalloidin exhibit ATP-dependent movement on myosin filaments fixed to a surface. At pH 7.4 and 24 degrees C, the rates of movement average 3-4 micron/s with skeletal muscle myosin and 1-2 micron/s with Dictyostelium myosin. These rates are very similar to those measured in our previous myosin movement assays. The rates of movement are relatively independent of the type of actin used. The filament velocity shows a broad pH optimum between 7.0 and 9.0, and the concentration of ATP required for half-maximal velocity is 50 microM. Evidence was obtained to suggest that movement of actin over myosin requires at most the number of heads in a single thick filament. This system provides a practical, quantitative myosin-movement assay with purified proteins.
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Citations
Cites
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Self-citation[18] Purification of muscle actin
Pardee, J. D., & Aspudich, J. (1982) · Methods in Enzymology · doi:10.1016/0076-6879(82)85020-9 · Cited by 1,186
Movement of myosin-coated fluorescent beads on actin cables in vitro
Sheetz, M. P., & Spudich, J. A. (1983) · Nature · doi:10.1038/303031a0 · Cited by 511
Self-citationA model for the myosin molecule
Wayne Kielley, W., & Harrington, W. F. (1960) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(60)90037-8 · Cited by 502
Direct observation of motion of single F-actin filaments in the presence of myosin
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Chapter 18 Purification of Muscle Actin
Pardee, J. D., & Spudich, J. A. (1982) · Methods in Cell Biology · doi:10.1016/s0091-679x(08)60661-5 · Cited by 402
Self-citationVale, R. D., Schnapp, B. J., Reese, T. S., & Sheetz, M. P. (1985) · Cell · doi:10.1016/0092-8674(85)90204-1 · Cited by 348
A Miniature Flow Cell Designed for Rapid Exchange of Media Under High-power Microscope Objectives
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Light chain phosphorylation regulates the movement of smooth muscle myosin on actin filaments.
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Self-citationBiochemical and structural characterization of actin from Dictyostelium discoideum.
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Cited by
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
Sarcopenia: Aging-Related Loss of Muscle Mass and Function
Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797
Movement of microtubules by single kinesin molecules
Howard, J., Hudspeth, A. J., & Vale, R. D. (1989) · Nature · doi:10.1038/342154a0 · Cited by 885
Synthetische molekulare Motoren und mechanische Maschinen
Kay, E. R., Leigh, D. A., & Zerbetto, F. (2007) · Angewandte Chemie · doi:10.1002/ange.200504313 · Cited by 624
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Self-citation
Metadata
- Authors
- Kron, S. J., & Spudich, J. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1986-09
- Volume
- 83
- Issue
- 17
- Pages
- 6272-6276
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2026836008
- Cited by
- 853
- References
- 14
- FWCI
- 7.88
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Kron, S. J., & Spudich, J. A. (1986). Fluorescent actin filaments move on myosin fixed to a glass surface. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.83.17.6272
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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.
