Our research interests span the gap between biology and chemistry. We are intrigued by the roles of protein posttranslational modifications in the complexity of epigenetic regulation. The research program integrates multidisciplinary approaches to elucidate how specific modifications occur and the molecular mechanisms through which these modifications regulate gene transcription in physiological and pathological processes. Our research focuses on two of these dynamic modifications: O-GlcNAcylation and methylation.
- Lazarus MB*, Jiang J*, Kapuria V, Bhuiyan T, Janetzko J, Zandberg WF, Vocadlo DJ, Herr W, Walker S. HCF-1 is cleaved in the active site of O-GlcNAc transferase. (*equal contribution) Science (2013), 342, 1235-9.
- Lazarus, MB*; Jiang, J*; Gloster, TM; Zandberg, WF; Whitworth, GE; Vocadlo, DJ; Walker, S. Structural snapshots of the reaction coordinate for O-GlcNAc transferase. (*equal contribution) Nature Chemical Biology (2012), 8, 966-8.
- Jiang, J*; Lazarus, MB*; Pasquina, L; Sliz, P; Walker, S. A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase. (*equal contribution) Nature Chemical Biology (2012), 8, 72-7.