The DOI matches its Crossref record; 219 of the 219 references it cites were found in a registry or an index.
Tropomyosin-Based Regulation of the Actin Cytoskeleton in Time and Space
Abstract
Tropomyosins are rodlike coiled coil dimers that form continuous polymers along the major groove of most actin filaments. In striated muscle, tropomyosin regulates the actin-myosin interaction and, hence, contraction of muscle. Tropomyosin also contributes to most, if not all, functions of the actin cytoskeleton, and its role is essential for the viability of a wide range of organisms. The ability of tropomyosin to contribute to the many functions of the actin cytoskeleton is related to the temporal and spatial regulation of expression of tropomyosin isoforms. Qualitative and quantitative changes in tropomyosin isoform expression accompany morphogenesis in a range of cell types. The isoforms are segregated to different intracellular pools of actin filaments and confer different properties to these filaments. Mutations in tropomyosins are directly involved in cardiac and skeletal muscle diseases. Alterations in tropomyosin expression directly contribute to the growth and spread of cancer. The functional specificity of tropomyosins is related to the collaborative interactions of the isoforms with different actin binding proteins such as cofilin, gelsolin, Arp 2/3, myosin, caldesmon, and tropomodulin. It is proposed that local changes in signaling activity may be sufficient to drive the assembly of isoform-specific complexes at different intracellular sites.
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Cites
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Cited by
Fiber Types in Mammalian Skeletal Muscles
Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022
Single-cell mRNA quantification and differential analysis with Census
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A systematic nomenclature for mammalian tropomyosin isoforms
Geeves, M. A., Hitchcock-DeGregori, S. E., & Gunning, P. W. (2015) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-014-9389-6 · Cited by 183
Self-citationDatta, A., Deng, S., Gopal, V., Yap, K. C.-H., Halim, C. E., Lye, M. L., Ong, M. S., Tan, T. Z., Sethi, G., Hooi, S. C., et al. (2021) · Cancers · doi:10.3390/cancers13081882 · Cited by 184
In-depth proteomic analysis of human tropomyosin by top-down mass spectrometry
Peng, Y., Yu, D., Gregorich, Z., Chen, X., Beyer, A. M., Gutterman, D. D., & Ge, Y. (2013) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-013-9352-y · Cited by 42
Metadata
- Authors
- Gunning, P., O’neill, G., & Hardeman, E.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2008-01
- Volume
- 88
- Issue
- 1
- Pages
- 1-35
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2162225623
- Cited by
- 478
- References
- 219
- FWCI
- 2.04
- Type
- journal article
- Language
- en
- Open access
- closed
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