Publications
Structures of N-terminally processed KRAS provide insight into the role of N-acetylation. Sci Rep. 9, 10512
(2019) Structure of the SHOC2-MRAS-PP1C complex provides insights into RAF activation and Noonan syndrome. Nat Struct Mol Biol. 29, 966-977
(2022) Structural Insights into the SPRED1-Neurofibromin-KRAS Complex and Disruption of SPRED1-Neurofibromin Interaction by Oncogenic EGFR. Cell Rep. 32, 107909
(2020) Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ.. Proc Natl Acad Sci U S A. 113, E6766-E6775
(2016) Reduced dynamic complexity allows structure elucidation of an excited state of KRAS. Commun Biol. 6, 594
(2023) KRAS interaction with RAF1 RAS-binding domain and cysteine-rich domain provides insights into RAS-mediated RAF activation. Nat Commun. 12, 1176
(2021) internal tandem duplication disrupts GTPase-activating protein (GAP) binding to activate oncogenic signaling. J Biol Chem. 10.1074/jbc.RA119.011080
(2020) (2024)