The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Actin polymerization. The mechanism of action of cytochalasin D.
Open accessAbstract
Fluorescence changes using actin covalently labeled with N-(1-pyrenyl)iodoacetamide have been used to determine the effect of cytochalasin D on actin polymerization. A mechanism for the effect of cytochalasin D on actin polymerization is presented, which explains the experimental observation of a cytochalasin D-induced increase in the initial rate of polymerization and a decrease in the final extent of the reaction. Central to this mechanism is the Mg2+-dependent formation of cytochalasin D-induced dimers. The dimers serve as nuclei to enhance the polymerization rate. Binding of Mg2+ to a low affinity site on the dimer induces a conformational change which can be observed as a rapid fluorescence increase. A subsequent time-dependent fluorescence decrease observed prior to polymerization appears to represent ATP hydrolysis resulting in dissociation of the dimer and release of actin monomers containing ADP. We postulate that a slow rate of exchange of ATP for bound ADP relative to hydrolysis results in the accumulation of monomers containing ADP. As these monomers have a high critical concentration, the final extent of polymerization is reduced dramatically. The Mg2+ dependence of the final extent of polymerization in the presence of cytochalasin D is also explained in the context of this mechanism.
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Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
The Regulation of Rabbit Skeletal Muscle Contraction
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Mechanism of action of cytochalasin B on actin
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Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization
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Cytochalasin inhibits the rate of elongation of actin filament fragments
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Cooper, J. A. (1987) · The Journal of cell biology · doi:10.1083/jcb.105.4.1473 · Cited by 2,009
Forscher, P., & Smith, S. J. (1988) · The Journal of cell biology · doi:10.1083/jcb.107.4.1505 · Cited by 854
Spector, I., Shochet, N. R., Blasberger, D., & Kashman, Y. (1989) · Cell Motility · doi:10.1002/cm.970130302 · Cited by 580
Tumour-associated mutant p53 drives the Warburg effect
Zhang, C., Liu, J., Liang, Y., Wu, R., Zhao, Y., Hong, X., Lin, M., Yu, H., Liu, L., Levine, A. J., et al. (2013) · Nature Communications · doi:10.1038/ncomms3935 · Cited by 434
Cytoskeletal prestress regulates nuclear shape and stiffness in cardiac myocytes
Lee, H., Adams, W. J., Alford, P. W., McCain, M. L., Feinberg, A. W., Sheehy, S. P., Goss, J. A., & Parker, K. K. (2015) · Experimental Biology and Medicine · doi:10.1177/1535370215583799 · Cited by 45
Metadata
- Authors
- Goddette, D. W., & Frieden, C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1986-12
- Volume
- 261
- Issue
- 34
- Pages
- 15974-15980
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1549239847
- Cited by
- 273
- References
- 27
- FWCI
- 3.19
- Type
- journal article
- Language
- en
- Open access
- hybrid
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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.