The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
Direct Redox Regulation of F-Actin Assembly and Disassembly by Mical
Open accessAbstract
A protein involved in redox signaling disassembles actin filaments and alters their reassembly.
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Citations
Cites
Lee, T., & Luo, L. (1999) · Neuron · doi:10.1016/s0896-6273(00)80701-1 · Cited by 2,571
Actin, a Central Player in Cell Shape and Movement
Pollard, T. D., & Cooper, J. A. (2009) · Science · doi:10.1126/science.1175862 · Cited by 2,088
Stamler (2001) · doi:10.1016/s0092-8674(01)00495-0 · Cited by 1,261
Dominguez, R., & Holmes, K. C. (2011) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-042910-155359 · Cited by 1,211
A Dynamic Pathway for Calcium-Independent Activation of CaMKII by Methionine Oxidation
Erickson, J. R., Joiner, M.-L. A., Guan, X., Kutschke, W., Yang, J., Oddis, C. V., Bartlett, R. K., Lowe, J. S., O'Donnell, S. E., Aykin-Burns, N., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.048 · Cited by 1,122
The many faces of actin: matching assembly factors with cellular structures
Chhabra, E. S., & Higgs, H. N. (2007) · Nature Cell Biology · doi:10.1038/ncb1007-1110 · Cited by 744
The nature of the globular- to fibrous-actin transition
Oda, T., Iwasa, M., Aihara, T., Maéda, Y., & Narita, A. (2009) · Nature · doi:10.1038/nature07685 · Cited by 644
Spector, I., Shochet, N. R., Blasberger, D., & Kashman, Y. (1989) · Cell Motility · doi:10.1002/cm.970130302 · Cited by 580
The Crystal Structure of Uncomplexed Actin in the ADP State
Otterbein, L. R., Graceffa, P., & Dominguez, R. (2001) · Science · doi:10.1126/science.1059700 · Cited by 526
Effects of cytochalasin D and latrunculin B on mechanical properties of cells
Wakatsuki, T., Schwab, B., Thompson, N. C., & Elson, E. L. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.1025 · Cited by 471
Cited by
Redox-based reagents for chemoselective methionine bioconjugation
Lin, S., Yang, X., Jia, S., Weeks, A. M., Hornsby, M., Lee, P. S., Nichiporuk, R. V., Iavarone, A. T., Wells, J. A., Toste, F. D., et al. (2017) · Science · doi:10.1126/science.aal3316 · Cited by 513
Semaphorins and their Signaling Mechanisms
Alto, L. T., & Terman, J. R. (2017) · Methods in Molecular Biology · doi:10.1007/978-1-4939-6448-2_1 · Cited by 429
Self-citationRedox Signaling by Reactive Electrophiles and Oxidants
Parvez, S., Long, M. J. C., Poganik, J. R., & Aye, Y. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00698 · Cited by 359
Methionine oxidation and reduction in proteins
Kim, G., Weiss, S. J., & Levine, R. L. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.038 · Cited by 311
Wilson, C., & González-Billault, C. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00381 · Cited by 238
Metadata
- Authors
- Hung, R.-J., Pak, C. W., & Terman, J. R.
- Venue
- Science
- Published
- 2011-12-23
- Volume
- 334
- Issue
- 6063
- Pages
- 1710-1713
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2007898976
- Cited by
- 317
- References
- 55
- FWCI
- 6.79
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Direct Redox Regulation of F-Actin Assembly and Disassembly by Mical. https://app.cochat.ai/papers/10.1126/science.1211956
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- Hung, R.-J., Pak, C. W., & Terman, J. R. (2011). Direct Redox Regulation of F-Actin Assembly and Disassembly by Mical. Science. https://doi.org/10.1126/science.1211956
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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.
