The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle
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Citations
Cites
Proposed Mechanism of Force Generation in Striated Muscle
HUXLEY, A. F., & SIMMONS, R. M. (1971) · Nature · doi:10.1038/233533a0 · Cited by 2,272
Huxley, H. E. (1969) · Science · doi:10.1126/science.164.3886.1356 · Cited by 1,959
Fluorescent phallotoxin, a tool for the visualization of cellular actin.
Wulf, E., Deboben, A., Bautz, F. A., Faulstich, H., & Wieland, T. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4498 · Cited by 786
Titin: major myofibrillar components of striated muscle.
Wang, K., McClure, J., & Tu, A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.8.3698 · Cited by 546
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
Direct observation of motion of single F-actin filaments in the presence of myosin
Yanagida, T., Nakase, M., Nishiyama, K., & Oosawa, F. (1984) · Nature · doi:10.1038/307058a0 · Cited by 478
Self-citationCross-bridge model of muscle contraction. Quantitative analysis
Eisenberg, E., Hill, T. L., & Chen, Y. (1980) · Biophysical Journal · doi:10.1016/s0006-3495(80)85126-5 · Cited by 378
Ca2+-SPECIFIC REMOVAL OF Z LINES FROM RABBIT SKELETAL MUSCLE
Busch, W. A., Stromer, M. H., Goll, D. E., & Suzuki, A. (1972) · The Journal of Cell Biology · doi:10.1083/jcb.52.2.367 · Cited by 376
Interaction of actin with phalloidin:
Dancker, P., Löw, I., Hasselbach, W., & Wieland, T. (1975) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(75)90196-8 · Cited by 273
The Correlation of Reaction Kinetics and Substrate Binding with the Mechanism of Pyruvate Kinase
Reynard, A. M., Hass, L. F., Jacobsen, D. D., & Boyer, P. D. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64071-2 · Cited by 255
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
Funatsu, T., Harada, Y., Tokunaga, M., Saito, K., & Yanagida, T. (1995) · Nature · doi:10.1038/374555a0 · Cited by 1,047
Self-citationForce and velocity measured for single kinesin molecules
Svoboda, K., & Block, S. M. (1994) · Cell · doi:10.1016/0092-8674(94)90060-4 · Cited by 909
A single myosin head moves along an actin filament with regular steps of 5.3 nanometres
Kitamura, K., Tokunaga, M., Iwane, A. H., & Yanagida, T. (1999) · Nature · doi:10.1038/16403 · Cited by 530
Self-citation
Metadata
- Authors
- Yanagida, T., Arata, T., & Oosawa, F.
- Venue
- Nature
- Published
- 1985-07
- Volume
- 316
- Issue
- 6026
- Pages
- 366-369
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2002527385
- Cited by
- 260
- References
- 20
- FWCI
- 8.19
- Type
- journal article
- Language
- en
- Open access
- closed
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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- CoChat. (2026). Citation check: Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle. https://app.cochat.ai/papers/10.1038/316366a0
- The paper
- Yanagida, T., Arata, T., & Oosawa, F. (1985). Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle. Nature. https://doi.org/10.1038/316366a0
Data sources
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.
