The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Focal adhesion kinase: the first ten years
Open accessAbstract
The protein tyrosine kinase focal adhesion kinase (FAK) plays a prominent role in integrin signaling. FAK activation, demonstrated by an increase in phosphorylation of Tyr397 as well as other sites in the protein, is best understood in the context of the engagement of integrins at the cell surface. Activation of FAK results in recruitment of a number of SH2-domain- and SH3-domain-containing proteins, which mediate signaling to several downstream pathways. FAK-dependent activation of these pathways has been implicated in a diverse array of cellular processes, including cell migration, growth factor signaling, cell cycle progression and cell survival.
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Cites
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
Unconventional Rac-GEF activity is mediated through the Dock180–ELMO complex
Brugnera, E., Haney, L., Grimsley, C., Lu, M., Walk, S. F., Tosello-Trampont, A.-C., Macara, I. G., Madhani, H., Fink, G. R., & Ravichandran, K. S. (2002) · Nature Cell Biology · doi:10.1038/ncb824 · Cited by 576
The Arf GTPase-activating protein ASAP1 regulates the actin cytoskeleton
Randazzo, P. A., Andrade, J., Miura, K., Brown, M. T., Long, Y.-Q., Stauffer, S., Roller, P., & Cooper, J. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.070552297 · Cited by 210
Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins
Meller, N., Irani-Tehrani, M., Kiosses, W. B., Del Pozo, M. A., & Schwartz, M. A. (2002) · Nature Cell Biology · doi:10.1038/ncb835 · Cited by 171
Cited by
Focal adhesion kinase: in command and control of cell motility.
Mitra, S. K., Hanson, D. A., & Schlaepfer, D. D. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1549 · Cited by 2,335
Physiology of cell volume regulation in vertebrates
Hoffmann, E. K., Lambert, I. H., & Pedersen, S. F. (2009) · Physiological Reviews · doi:10.1152/physrev.00037.2007 · Cited by 1,441
FAK in cancer: mechanistic findings and clinical applications
Sulzmaier, F. J., Jean, C., & Schlaepfer, D. D. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3792 · Cited by 1,381
RAS Interaction with PI3K: More Than Just Another Effector Pathway
Castellano, E., & Downward, J. (2011) · Genes & Cancer · doi:10.1177/1947601911408079 · Cited by 762
Keselowsky, B. G., Collard, D. M., & Garcı́a, A. J. (2004) · Biomaterials · doi:10.1016/j.biomaterials.2004.01.062 · Cited by 627
Metadata
- Authors
- Parsons, J. T.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2003-04-15
- Volume
- 116
- Issue
- 8
- Pages
- 1409-1416
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2171179595
- Cited by
- 1,373
- References
- 4
- FWCI
- 39.68
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
