Publications

Found 9 results
Filters: Author is Turk, Benjamin E  [Clear All Filters]
Journal Article
Ha, B. Hak, Davis, M. J., Chen, C., Lou, H. Jane, Gao, J., Zhang, R., Krauthammer, M., Halaban, R., Schlessinger, J., Turk, B. E., and Boggon, T. J. (2012) Type II p21-activated kinases (PAKs) are regulated by an autoinhibitory pseudosubstrate. Proc Natl Acad Sci U S A. 109, 16107-12
Simon, B., Lou, H. Jane, Huet-Calderwood, C., Shi, G., Boggon, T. J., Turk, B. E., and Calderwood, D. A. (2022) Tousled-like kinase 2 targets ASF1 histone chaperones through client mimicry. Nat Commun. 13, 749
Gao, J., Ha, B. Hak, Lou, H. Jane, Morse, E. M., Zhang, R., Calderwood, D. A., Turk, B. E., and Boggon, T. J. (2013) Substrate and inhibitor specificity of the type II p21-activated kinase, PAK6. PLoS One. 8, e77818
Fisher, O. S., Deng, H., Liu, D., Zhang, Y., Wei, R., Deng, Y., Zhang, F., Louvi, A., Turk, B. E., Boggon, T. J., and Su, B. (2015) Structure and vascular function of MEKK3-cerebral cavernous malformations 2 complex. Nat Commun. 6, 7937
Hamill, S., Lou, H. Jane, Turk, B. E., and Boggon, T. J. (2016) Structural Basis for Noncanonical Substrate Recognition of Cofilin/ADF Proteins by LIM Kinases. Mol Cell. 62, 397-408
Chetty, A. K., Sexton, J. A., Ha, B. Hak, Turk, B. E., and Boggon, T. J. (2020) Recognition of physiological phosphorylation sites by p21-activated kinase 4. J Struct Biol. 211, 107553
Chen, C., Ha, B. Hak, Thévenin, A. F., Lou, H. Jane, Zhang, R., Yip, K. Y., Peterson, J. R., Gerstein, M., Kim, P. M., Filippakopoulos, P., Knapp, S., Boggon, T. J., and Turk, B. E. (2014) Identification of a major determinant for serine-threonine kinase phosphoacceptor specificity. Mol Cell. 53, 140-7
Robles, J. Torres, Stiegler, A. L., Boggon, T. J., and Turk, B. E. (2025) Cancer hotspot mutations rewire ERK2 specificity by selective exclusion of docking interactions. J Biol Chem. 10.1016/j.jbc.2025.108348
Casanova-Sepúlveda, G., Sexton, J. A., Turk, B. E., and Boggon, T. J. (2023) Autoregulation of the LIM kinases by their PDZ domain. Nat Commun. 14, 8441