The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The Regulation of Rabbit Skeletal Muscle Contraction
Open accessAbstract
Actin purified by a new, simple, and rapid purification procedure activated the ATPase activity of both heavy meromyosin and Subfragment 1 of heavy meromyosin, and this activation was not inhibited by the removal of Ca2+. Preparations of tropomyosin-troponin inhibited (by 85%) both the acto-heavy meromyosin and acto-Subfragment 1 ATPases in the absence of, but not in the presence of, Ca2+. This inhibition was shown to result from binding of the tropomyosin-troponin complex solely to actin and in a ratio of about 1 mole of tropomyosin-troponin to 7 moles of actin.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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
Bubb, M. R., Senderowicz, A. M., Sausville, E. A., Duncan, K. L., & Korn, E. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36545-6 · Cited by 811
Blanchoin, L., Amann, K. J., Higgs, H. N., Marchand, J.-B., Kaiser, D. A., & Pollard, T. D. (2000) · Nature · doi:10.1038/35010008 · Cited by 586
Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
Harada, Y., Sakurada, K., Aoki, T., Thomas, D. D., & Yanagida, T. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80060-9 · Cited by 522
Microscopic analysis of polymerization dynamics with individual actin filaments
Fujiwara, I., Takahashi, S., Tadakuma, H., Funatsu, T., & Ishiwata, S. (2002) · Nature Cell Biology · doi:10.1038/ncb841 · Cited by 420
Phosphorylation of microtubule-associated proteins regulates their interaction with actin filaments.
Selden, S. C., & Pollard, T. D. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32333-0 · Cited by 314
Structure of Arp2/3 Complex in Its Activated State and in Actin Filament Branch Junctions
Volkmann, N., Amann, K. J., Stoilova-McPhie, S., Egile, C., Winter, D. C., Hazelwood, L., Heuser, J. E., Li, R., Pollard, T. D., & Hanein, D. (2001) · Science · doi:10.1126/science.1063025 · Cited by 258
The interaction of actin filaments with microtubules and microtubule-associated proteins.
Griffith, L. M., & Pollard, T. D. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34254-6 · Cited by 252
p140Sra-1 (specifically Rac1-associated protein) is a novel specific target for Rac1 small GTPase
Kobayashi, K., Kuroda, S., Fukata, M., Nakamura, T., Nagase, T., Nomura, N., Matsuura, Y., Yoshida-Kubomura, N., Iwamatsu, A., & Kaibuchi, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.291 · Cited by 244
Oxidation of F-actin controls the terminal steps of cytokinesis
Frémont, S., Hammich, H., Bai, J., Wioland, H., Klinkert, K., Rocancourt, M., Kikuti, C., Stroebel, D., Romet-Lemonne, G., Pylypenko, O., et al. (2017) · Nature Communications · doi:10.1038/ncomms14528 · Cited by 181
Dissociation of the actin.subfragment 1 complex by adenyl-5'-yl imidodiphosphate, ADP, and PPi.
Greene, L. E., & Eisenberg, E. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86209-9 · Cited by 151
The proline-rich domain of tau plays a role in interactions with actin
He, H. J., Wang, X. S., Pan, R., Wang, D. L., Liu, M. N., & He, R. Q. (2009) · BMC Cell Biology · doi:10.1186/1471-2121-10-81 · Cited by 142
Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range
Thomas, D. D., Seidel, J. C., & Gergely, J. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90259-6 · Cited by 137
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
Myosin Va bound to phagosomes binds to F-actin and delays microtubule-dependent motility
Al-Haddad, A., Shonn, M. A., Redlich, B., Blocker, A., Burkhardt, J. K., Yu, H., Hammer, J. A., Weiss, D. G., Steffen, W., Griffiths, G., et al. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.9.2742 · Cited by 102
Berg, P. A., Sayers, T., Wiedmann, K. H., Klöppel, G., & Lindner, H. (1980) · The Lancet · doi:10.1016/s0140-6736(80)92397-1 · Cited by 93
Structural Effects of Cofilin on Longitudinal Contacts in F-actin
Bobkov, A. A., Muhlrad, A., Kokabi, K., Vorobiev, S., Almo, S. C., & Reisler, E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01008-2 · Cited by 70
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
DOC-2/DAB2 Is the Binding Partner of Myosin VI
Inoue, A., Sato, O., Homma, K., & Ikebe, M. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6636 · Cited by 65
Modulation of formin processivity by profilin and mechanical tension
Cao, L., Kerleau, M., Suzuki, E. L., Wioland, H., Jouet, S., Guichard, B., Lenz, M., Romet-Lemonne, G., & Jegou, A. (2018) · eLife · doi:10.7554/elife.34176 · Cited by 61
Structure-based Analysis of High Pressure Adaptation of α-Actin
Morita, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302328200 · Cited by 58
A τ Fragment Containing a Repetitive Sequence Induces Bundling of Actin Filaments
Moraga, D. M., Nuñez, P., Garrido, J., & Maccioni, R. B. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03611.x · Cited by 56
Effect of temperature on the mechanism of actin polymerization
Zimmerle, C. T., & Frieden, C. (1986) · Biochemistry · doi:10.1021/bi00369a014 · Cited by 45
Oliveira, C. A., Kashman, Y., & Mantovani, B. (1996) · Chemico-Biological Interactions · doi:10.1016/0009-2797(96)03695-2 · Cited by 43
Changes in actin synthesis and alpha-actin-mRNA content in rat muscle during immobilization
Watson, P. A., Stein, J. P., & Booth, F. W. (1984) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1984.247.1.c39 · Cited by 40
Nakamura, T. Y., Yamamoto, I., Nishitani, H., Matozaki, T., Suzuki, T., Wakabayashi, S., Shigekawa, M., & Goshima, K. (1995) · The Journal of cell biology · doi:10.1083/jcb.131.2.509 · Cited by 39
Myosin-V makes two brownian 90° rotations per 36-nm step
Komori, Y., Iwane, A. H., & Yanagida, T. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1298 · Cited by 31
The Uncoupling of the Effects of Formins on the Local and Global Dynamics of Actin Filaments
Kupi, T., Gróf, P., Nyitrai, M., & Belágyi, J. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.11.058 · Cited by 19
mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells
Hatano, T., Lim, T. C., Billault-Chaumartin, I., Dhar, A., Gu, Y., Massam-Wu, T., Scott, W., Adishesha, S., Chapa-y-Lazo, B., Springall, L., et al. (2022) · Journal of Cell Science · doi:10.1242/jcs.260288 · Cited by 19
TLNRD1 is a CCM complex component and regulates endothelial barrier integrity
Ball, N. J., Ghimire, S., Follain, G., Pajari, A. O., Wurzinger, D., Vaitkevičiūtė, M., Cowell, A. R., Berki, B., Ivaska, J., Paatero, I., et al. (2024) · Journal of Cell Biology · doi:10.1083/jcb.202310030 · Cited by 11
Kramer, D. A., Narvaez-Ortiz, H. Y., Patel, U., Shi, R., Shen, K., Nolen, B. J., Roche, J., & Chen, B. (2023) · eLife · doi:10.7554/elife.88492 · Cited by 7
Dimerization of GAS2 mediates crosslinking of microtubules and F-actin
An, J., Imasaki, T., Narita, A., Niwa, S., Sasaki, R., Makino, T., Nitta, R., & Kikkawa, M. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00415-2 · Cited by 5
Functional comparison of full‐length palladin to isolated actin binding domain
Albraiki, S., Ajiboye, O., Sargent, R., & Beck, M. R. (2023) · Protein Science · doi:10.1002/pro.4638 · Cited by 4
Integrated structural model of the palladin–actin complex using XL ‐ MS , docking, NMR , and SAXS
Sargent, R., Liu, D. H., Yadav, R., Glennenmeier, D., Bradford, C., Urbina, N., & Beck, M. R. (2025) · Protein Science · doi:10.1002/pro.70122 · Cited by 3
Metadata
- Authors
- Spudich, J. A., & Watt, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1971-08
- Volume
- 246
- Issue
- 15
- Pages
- 4866-4871
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1538692246
- Cited by
- 4,493
- References
- 1
- FWCI
- 33.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
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.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
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.
