The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Rho GTPases in cancer cell biology
Open accessAbstract
Rho GTPases contribute to multiple cellular processes that could affect cancer progression, including cytoskeletal dynamics, cell cycle progression, transcriptional regulation, cell survival and vesicle trafficking. In vitro several Rho GTPases have oncogenic activity and/or can promote cancer cell invasion, and this correlates with increased expression and activity in a variety of cancers. Conversely, other family members appear to act as tumour suppressors and are deleted, mutated or downregulated in some cancers. Genetic models are starting to provide new information on how Rho GTPases affect cancer development and progression. Here, we discuss how Rho GTPases could contribute to different steps of cancer progression, including proliferation, survival, invasion and metastasis.
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Citations
Cites
RHO GTPASES: Biochemistry and Biology
Jaffe, A. B., & Hall, A. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.020604.150721 · Cited by 3,009
Tumour invasion and metastasis initiated by microRNA-10b in breast cancer
Ma, L., Teruya-Feldstein, J., & Weinberg, R. A. (2007) · Nature · doi:10.1038/nature06174 · Cited by 2,605
Gaggioli, C., Hooper, S., Hidalgo-Carcedo, C., Grosse, R., Marshall, J. F., Harrington, K., & Sahai, E. (2007) · Nature Cell Biology · doi:10.1038/ncb1658 · Cited by 1,589
PDK1 Regulates Cancer Cell Motility by Antagonising Inhibition of ROCK1 by RhoE
Pinner, S., & Sahai, E. (2008) · Nature Cell Biology · doi:10.1038/ncb1675 · Cited by 267
Li, X., Bu, X., Lu, B., Avraham, H., Flavell, R. A., & Lim, B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1158-1171.2002 · Cited by 153
Gu, Y., Chae, H.-D., Siefring, J. E., Jasti, A. C., Hildeman, D. A., & Williams, D. A. (2006) · Nature Immunology · doi:10.1038/ni1396 · Cited by 110
Chae, H.-D., Lee, K. E., Williams, D. A., & Gu, Y. (2008) · Blood · doi:10.1182/blood-2007-06-093237 · Cited by 81
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Regulating Rho GTPases and their regulators
Hodge, R. G., & Ridley, A. J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.67 · Cited by 872
Self-citationTargeting Mitochondrial Glutaminase Activity Inhibits Oncogenic Transformation
Wang, J.-B., Erickson, J. W., Fuji, R., Ramachandran, S., Gao, P., Dinavahi, R., Wilson, K. F., Ambrosio, A. L. B., Dias, S. M. G., Dang, C. V., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.08.009 · Cited by 821
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Montalvo-Ortiz, B. L., Castillo-Pichardo, L., Hernández, E., Humphries-Bickley, T., De La Mota-Peynado, A., Cubano, L. A., Vlaar, C. P., & Dharmawardhane, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.334524 · Cited by 213
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Davis, M. J., Ha, B. H., Holman, E. C., Halaban, R., Schlessinger, J., & Boggon, T. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220895110 · Cited by 180
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Krishnan, K., Steptoe, A. L., Martin, H. C., Pattabiraman, D. R., Nones, K., Waddell, N., Mariasegaram, M., Simpson, P. T., Lakhani, S. R., Vlassov, A., et al. (2013) · RNA · doi:10.1261/rna.042143.113 · Cited by 134
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Zhang, H.-D., Jiang, L.-H., Sun, D.-W., Li, J., & Tang, J.-H. (2015) · Tumor Biology · doi:10.1007/s13277-015-3199-3 · Cited by 69
Seo, Y., Kim, J., Park, S. J., Park, J. J., Cheon, J. H., Kim, W. H., & Kim, T. I. (2020) · Cancers · doi:10.3390/cancers12092554 · Cited by 64
Phosphorylation and Activation of RhoA by ERK in Response to Epidermal Growth Factor Stimulation
Tong, J., Li, L., Ballermann, B., & Wang, Z. (2016) · PLOS ONE · doi:10.1371/journal.pone.0147103 · Cited by 63
Rho A and Rac1: Antagonists moving forward
Salloum, G., Jaafar, L., & El-Sibai, M. (2020) · Tissue and Cell · doi:10.1016/j.tice.2020.101364 · Cited by 36
Xu, X., Omelchenko, T., & Hall, A. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-77 · Cited by 33
“Members of the Rho GTPase family are important regulators of the actin cytoskeleton and of cell polarity and dysregulated Rho pathways have been linked to the process of tumor progression [12].”
BackgroundRajendran, B. K., & Deng, C.-X. (2017) · Oncotarget · doi:10.18632/oncotarget.20404 · Cited by 32
Nomikou, E., Livitsanou, M., Stournaras, C., & Kardassis, D. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2787-y · Cited by 28
Tomino, T., Tajiri, H., Tatsuguchi, T., Shirai, T., Oisaki, K., Matsunaga, S., Sanematsu, F., Sakata, D., Yoshizumi, T., Maehara, Y., et al. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.02.073 · Cited by 24
Zhang, Y., Larraufie, M.-H., Musavi, L., Akkiraju, H., Brown, L. M., & Stockwell, B. R. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b01113 · Cited by 16
Interplay of PKA and Rac: Fine-tuning of Rac localization and signaling
Bachmann, V. A., Bister, K., & Stefan, E. (2013) · Small GTPases · doi:10.4161/sgtp.27281 · Cited by 14
YIN, C.-P., GUAN, S.-H., ZHANG, B., WANG, X.-X., & YUE, S.-W. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.4267 · Cited by 9
Metadata
- Authors
- Vega, F. M., & Ridley, A. J.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2008-05-05
- Volume
- 582
- Issue
- 14
- Pages
- 2093-2101
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2060630299
- Cited by
- 779
- References
- 7
- FWCI
- 17.12
- Type
- journal article
- Language
- en
- Open access
- bronze
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