The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
[18] Purification of muscle actin
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Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Cited by
Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
Eden, S., Rohatgi, R., Podtelejnikov, A. V., Mann, M., & Kirschner, M. W. (2002) · Nature · doi:10.1038/nature00859 · Cited by 835
Self- and actin-templated assembly of Mammalian septins
Kinoshita, M., Field, C. M., Coughlin, M. L., Straight, A. F., & Mitchison, T. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00366-0 · Cited by 526
Autophagy Impairment in Muscle Induces Neuromuscular Junction Degeneration and Precocious Aging
Carnio, S., LoVerso, F., Baraibar, M. A., Longa, E., Khan, M. M., Maffei, M., Reischl, M., Canepari, M., Loefler, S., Kern, H., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.061 · Cited by 423
Anillin binds nonmuscle myosin II and regulates the contractile ring
Straight, A. F., Field, C. M., & Mitchison, T. J. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0758 · Cited by 283
Functional diversity among a family of human skeletal muscle myosin motors
Resnicow, D. I., Deacon, J. C., Warrick, H. M., Spudich, J. A., & Leinwand, L. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913527107 · Cited by 116
Targeting the sarcomere to correct muscle function
Hwang, P. M., & Sykes, B. D. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4554 · Cited by 114
Oliveira, S. M., Zhang, Y.-H., Solis, R. S., Isackson, H., Bellahcene, M., Yavari, A., Pinter, K., Davies, J. K., Ge, Y., Ashrafian, H., et al. (2012) · Circulation Research · doi:10.1161/circresaha.111.259952 · Cited by 86
Direct Regulation of Striated Muscle Myosins by Nitric Oxide and Endogenous Nitrosothiols
Evangelista, A. M., Rao, V. S., Filo, A. R., Marozkina, N. V., Doctor, A., Jones, D. R., Gaston, B., & Guilford, W. H. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011209 · Cited by 69
Macromolecular crowding: effects on actin polymerisation
Lindner, R. A., & Ralston, G. B. (1997) · Biophysical Chemistry · doi:10.1016/s0301-4622(97)00011-2 · Cited by 68
Myosin is reversibly inhibited by S-nitrosylation
Nogueira, L., Figueiredo-Freitas, C., Casimiro-Lopes, G., Magdesian, M. H., Assreuy, J., & Sorenson, M. M. (2009) · Biochemical Journal · doi:10.1042/bj20091144 · Cited by 67
Effective Top-Down LC/MS+ Method for Assessing Actin Isoforms as a Potential Cardiac Disease Marker
Chen, Y.-C., Ayaz-Guner, S., Peng, Y., Lane, N. M., Locher, M. R., Kohmoto, T., Larsson, L., Moss, R. L., & Ge, Y. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b01745 · Cited by 31
Trimethylamine N-oxide suppresses the activity of the actomyosin motor
Kumemoto, R., Yusa, K., Shibayama, T., & Hatori, K. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.06.006 · Cited by 31
ATP turnover by individual myosin molecules hints at two conformers of the myosin active site
Amrute-Nayak, M., Lambeck, K.-A., Radocaj, A., Huhnt, H. E., Scholz, T., Hahn, N., Tsiavaliaris, G., Walter, W. J., & Brenner, B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1316390111 · Cited by 21
Zeng, W. W., Komaniecki, G., Liu, J., Lin, H., & Mao, Y. (2026) · eLife · doi:10.7554/elife.106975 · Cited by 1
Pires, I., Hung, Y.-F., Bergmann, U., Molloy, J. E., & Kursula, I. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102634 · Cited by 1
Metadata
- Authors
- Pardee, J. D., & Aspudich, J.
- Venue
- Methods in Enzymology
- Publisher
- Elsevier
- Published
- 1982
- Volume
- 85 Pt B
- Pages
- 164-181
- ISSN
- 0076-6879 (ISSN-L)
- OpenAlex
- W2058497997
- Cited by
- 1,186
- References
- 1
- FWCI
- 11.39
- Type
- book chapter
- 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.
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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.
