The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Focal adhesions: Structure and dynamics
Abstract
Interactions of cells with the extracellular matrix are essential for the control of tissue remodelling, cell migration, and embryogenesis. At the cell—extracellular matrix contact points, specialized structures are formed and termed focal adhesions, where transmembrane adhesion receptors provide a structural link between the actin cytoskeleton and the extracellular matrix components. Numerous structural and regulatory proteins assemble at the cytoplasmic face of focal adhesions in a Rho‐dependent fashion.
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Citations
Cites
Cell Migration: A Physically Integrated Molecular Process
Lauffenburger, D. A., & Horwitz, A. F. (1996) · Cell · doi:10.1016/s0092-8674(00)81280-5 · Cited by 3,915
Protein modules and signalling networks
Pawson, T. (1995) · Nature · doi:10.1038/373573a0 · Cited by 2,420
Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
Schlaepfer, D. D., Hanks, S. K., Hunter, T., & Geer, P. V. D. (1994) · Nature · doi:10.1038/372786a0 · Cited by 1,595
Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
Amano, M., Chihara, K., Kimura, K., Fukata, Y., Nakamura, N., Matsuura, Y., & Kaibuchi, K. (1997) · Science · doi:10.1126/science.275.5304.1308 · Cited by 1,077
Regulation of Cell Migration by the Calcium-dependent Protease Calpain
Huttenlocher, A., Palecek, S. P., Lu, Q., Zhang, W., Mellgren, R. L., Lauffenburger, D. A., Ginsberg, M. H., & Horwitz, A. F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.32719 · Cited by 390 · cited 1×
“However, a previous study suggested that calpain was rather implicated in the disassembly of focal adhesions during cell migration (Huttenlocher et al., 1997).”
BackgroundA truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation
Ito, A., Kataoka, T. R., Watanabe, M., Nishiyama, K., Mazaki, Y., Sabe, H., Kitamura, Y., & Nojima, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.4.562 · Cited by 159 · cited 2×
“, 1999), and the serine/threonine phosphatase PP2A (Ito et al., 2000).”
Background
Cited by
Biocompatible polymer materials: Role of protein–surface interactions
Chen, H., Yuan, L., Song, W., Wu, Z., & Li, D. (2008) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2008.07.006 · Cited by 706
Cheng, C. Y., & Mruk, D. D. (2002) · Physiological Reviews · doi:10.1152/physrev.00009.2002 · Cited by 567
Wang, Y., Lu, Y., Zhang, Y., Ning, Z., Li, Y., Zhao, Q., Lu, H., Huang, R., Xia, X., Feng, Q., et al. (2015) · Nature Genetics · doi:10.1038/ng.3280 · Cited by 434
Mechanically induced osteogenic differentiation – the role of RhoA, ROCKII and cytoskeletal dynamics
Arnsdorf, E. J., Tummala, P., Kwon, R. Y., & Jacobs, C. R. (2009) · Journal of Cell Science · doi:10.1242/jcs.036293 · Cited by 396
Vimentin as an Integral Regulator of Cell Adhesion and Endothelial Sprouting
Dave, J. M., & Bayless, K. J. (2014) · Microcirculation · doi:10.1111/micc.12111 · Cited by 179
Metadata
- Authors
- Petit, V., & Thiery, J.
- Venue
- Biology of the Cell
- Publisher
- Wiley
- Published
- 2000-10
- Volume
- 92
- Issue
- 7
- Pages
- 477-494
- ISSN
- 0248-4900 (ISSN-L)
- 1768-322X
- OpenAlex
- W1996016298
- Cited by
- 392
- References
- 6
- FWCI
- 6.90
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
