2024
Wang, W., Atherton, P., Kreft, M., Te Molder, L., van der Poel, S., Hoekman, L., . . . Sonnenberg, A. (2024). Caskin2 is a novel talin- and Abi1-binding protein that promotes cell motility.. Journal of cell science, 137(9), jcs262116. doi:10.1242/jcs.262116DOI: 10.1242/jcs.262116
2022
Atherton, P., Konstantinou, R., Neo, S. P., Wang, E., Balloi, E., Ptushkina, M., . . . Ballestrem, C. (2022). Tensin3 interaction with talin drives the formation of fibronectin-associated fibrillar adhesions. JOURNAL OF CELL BIOLOGY, 221(10). doi:10.1083/jcb.202107022DOI: 10.1083/jcb.202107022
Zuidema, A., Atherton, P., Kreft, M., Hoekman, L., Bleijerveld, O. B., Nagaraj, N., . . . Sonnenberg, A. (2022). PEAK1 Y635 phosphorylation regulates cell migration through association with Tensin3 and integrins.. The Journal of cell biology, 221(8), e202108027. doi:10.1083/jcb.202108027DOI: 10.1083/jcb.202108027
2021
Vinculin is required for neuronal mechanosensing but not for axon outgrowth. (Journal article)
Wang, D. -Y., Melero, C., Albaraky, A., Atherton, P., Jansen, K. A., Dimitracopoulos, A., . . . Ballestrem, C. (2021). Vinculin is required for neuronal mechanosensing but not for axon outgrowth.. Experimental cell research, 407(2), 112805. doi:10.1016/j.yexcr.2021.112805DOI: 10.1016/j.yexcr.2021.112805
2020
Atherton, P., Lausecker, F., Carisey, A., Gilmore, A., Critchley, D., Barsukov, I., & Ballestrem, C. (2020). Relief of talin autoinhibition triggers a force-independent association with vinculin. JOURNAL OF CELL BIOLOGY, 219(1). doi:10.1083/jcb.201903134DOI: 10.1083/jcb.201903134
2019
Light-Induced Molecular Adsorption of Proteins Using the PRIMO System for Micro-Patterning to Study Cell Responses to Extracellular Matrix Proteins. (Journal article)
Melero, C., Kolmogorova, A., Atherton, P., Atherton, P., Derby, B., Reid, A., . . . Ballestrem, C. (2019). Light-Induced Molecular Adsorption of Proteins Using the PRIMO System for Micro-Patterning to Study Cell Responses to Extracellular Matrix Proteins.. Journal of visualized experiments : JoVE, (152). doi:10.3791/60092DOI: 10.3791/60092
Nazgiewicz, A., Atherton, P., Atherton, P., & Ballestrem, C. (2019). GAS2-like 1 coordinates cell division through its association with end-binding proteins.. Scientific reports, 9(1), 5805. doi:10.1038/s41598-019-42242-6DOI: 10.1038/s41598-019-42242-6
2017
Mechanotransduction at the cell-matrix interface. (Journal article)
Jansen, K. A., Atherton, P., & Ballestrem, C. (2017). Mechanotransduction at the cell-matrix interface.. Seminars in cell & developmental biology, 71, 75-83. doi:10.1016/j.semcdb.2017.07.027DOI: 10.1016/j.semcdb.2017.07.027
Low-intensity pulsed ultrasound promotes cell motility through vinculin-controlled Rac1 GTPase activity. (Journal article)
Atherton, P., Lausecker, F., Harrison, A., & Ballestrem, C. (2017). Low-intensity pulsed ultrasound promotes cell motility through vinculin-controlled Rac1 GTPase activity.. Journal of cell science, 130(14), 2277-2291. doi:10.1242/jcs.192781DOI: 10.1242/jcs.192781
Distinct focal adhesion protein modules control different aspects of mechanotransduction. (Journal article)
Stutchbury, B., Atherton, P., Tsang, R., Wang, D. -Y., & Ballestrem, C. (2017). Distinct focal adhesion protein modules control different aspects of mechanotransduction.. Journal of cell science, 130(9), 1612-1624. doi:10.1242/jcs.195362DOI: 10.1242/jcs.195362
Talin gets SHANKed in the fight for integrin activation. (Journal article)
Atherton, P., & Ballestrem, C. (2017). Talin gets SHANKed in the fight for integrin activation.. Nature cell biology, 19(4), 265-267. doi:10.1038/ncb3501DOI: 10.1038/ncb3501
2016
Atherton, P., Stutchbury, B., Jethwa, D., & Ballestrem, C. (2016). Mechanosensitive components of integrin adhesions: Role of vinculin.. Experimental cell research, 343(1), 21-27. doi:10.1016/j.yexcr.2015.11.017DOI: 10.1016/j.yexcr.2015.11.017
2015
Atherton, P., Stutchbury, B., Wang, D. -Y., Jethwa, D., Tsang, R., Meiler-Rodriguez, E., . . . Ballestrem, C. (2015). Vinculin controls talin engagement with the actomyosin machinery.. Nature communications, 6. doi:10.1038/ncomms10038DOI: 10.1038/ncomms10038
