Publications
Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8. Cell. 157, 1671-84
(2014) Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes. Structure. 21, 42-53
(2013) A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nat Struct Mol Biol. 18, 947-9
(2011) Principles of paralog-specific targeted protein degradation engaging the C-degron E3 KLHDC2. Nat Commun. 15, 8829
(2024) Piperidinyl Ureas Chemically Control Defective in Cullin Neddylation 1 (DCN1)-Mediated Cullin Neddylation. J Med Chem. 61, 2680-2693
(2018) N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex. Science. 334, 674-8
(2011) E3 ligase autoinhibition by C-degron mimicry maintains C-degron substrate fidelity. Mol Cell. 83, 770-786.e9
(2023) E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification. Mol Cell. 33, 483-95
(2009) (2010)