Publications

Found 10 results
Filters: Author is Stiegler, Amy L  [Clear All Filters]
2014
Stiegler, A. L., Zhang, R., Liu, W., and Boggon, T. J. (2014) Structural determinants for binding of sorting nexin 17 (SNX17) to the cytoplasmic adaptor protein Krev interaction trapped 1 (KRIT1). J Biol Chem. 289, 25362-73
2015
Fisher, O. S., Liu, W., Zhang, R., Stiegler, A. L., Ghedia, S., Weber, J. L., and Boggon, T. J. (2015) Structural basis for the disruption of the cerebral cavernous malformations 2 (CCM2) interaction with Krev interaction trapped 1 (KRIT1) by disease-associated mutations. J Biol Chem. 290, 2842-53
2017
Stiegler, A. L., and Boggon, T. J. (2017) p190RhoGAP proteins contain pseudoGTPase domains. Nat Commun. 8, 506
2018
Stiegler, A. L., and Boggon, T. J. (2018) The N-Terminal GTPase Domain of p190RhoGAP Proteins Is a PseudoGTPase. Structure. 10.1016/j.str.2018.07.015
2019
Chehayeb, R. Jaber, Stiegler, A. L., and Boggon, T. J. (2019) Crystal structures of p120RasGAP N-terminal SH2 domain in its apo form and in complex with a p190RhoGAP phosphotyrosine peptide. PLoS One. 14, e0226113
2020
Chehayeb, R. Jaber, Wang, J., Stiegler, A. L., and Boggon, T. J. (2020) The GTPase-activating protein p120RasGAP has an evolutionarily conserved "FLVR-unique" SH2 domain. J Biol Chem. 295, 10511-10521
2022
Chau, J. E., Vish, K. J., Boggon, T. J., and Stiegler, A. L. (2022) SH3 domain regulation of RhoGAP activity: Crosstalk between p120RasGAP and DLC1 RhoGAP. Nat Commun. 13, 4788
Stiegler, A. L., Vish, K. J., and Boggon, T. J. (2022) Tandem engagement of phosphotyrosines by the dual SH2 domains of p120RasGAP. Structure. 30, 1603-1614.e5
2025
Paul, M. E., Chen, D., Vish, K. J., Lartey, N. L., Hughes, E., Freeman, Z. T., Saunders, T. L., Stiegler, A. L., King, P. D., and Boggon, T. J. (2025) The C2 domain augments Ras GTPase-activating protein catalytic activity. Proc Natl Acad Sci U S A. 122, e2418433122
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