Woo
Christina Woo
Assistant Professor of Chemistry and Chemical Biology

Department of Chemistry and Chemical Biology
Mallinckrodt 314
12 Oxford Street
Cambridge, MA 02138
Tel: 617-496-9921
Email: cwoo@chemistry.harvard.edu

Website:
www.woolab.org
Lab Size: Between 5-10

Summary

Many biological processes are governed by chemical signals relayed through protein networks. These small molecule signals can inhibit, enhance, or impart new functions to proteins through direct associations to regulatory hotspots on a protein that drive alteration of the broader proteomic network.  Despite the biological and medicinal significance of these hotspots, it is not yet possible to systematically discover, understand, and control their regulatory outcomes.  My research program aims to innovate large-scale approaches to illuminate and exploit chemical regulation of proteins.  We operate at the forefront of chemical glycobiology, to illuminate nature’s use of regulatory hotspots in sugar-based signaling pathways, and chemical proteomics, to reveal tractable hotspot mimics in cells and new mechanisms for therapeutic intervention.  Achievement of these goals will quantitatively change our understanding of and provide new concepts for unraveling how small molecules alter protein interaction networks, and thereby open new frontiers in the control of living systems and strategies for the design of new therapeutic modalities to treat human disease..

Publications

  1. Joiner, C. M.; Levine, Z.; Aongangkhen, C.; Woo, C. M.; Walker, S. “Aspartate residues within TPR lumen drive O-GlcNAc transferase substrate selection.” J Am Chem Soc 2019, in press.
  2. Flaxman, H. A.; Chang, C. F.; Wu, H. Y.; Woo, C. M. “A binding site hotspot map of the FKBP–rapamycin–FRB ternary complex by photo-affinity labeling and mass spectrometry.” J Am Chem Soc 2019, in press.
  3. Darabedian, N.; Gao, J.; Chuh, K.N.; Woo, C. M.; Pratt, M. R. “The metabolic chemical reporter 6-azido-6-deoxy-glucose reveals an unexpected substrate promiscuity of O-GlcNAc transferase and the potential for protein modification by O-glucose.” J Am Chem Soc 2018, 140, 7092.
  4. Gao, J.; Mfuh, A.; Amako, Y.; Woo, C. M. “Small molecule interactome mapping by photo-affinity labeling reveals binding site hotspots for the NSAIDs.” J Am Chem Soc 2018, 140, 4259.
  5. Chang, C.F.; Mfuh, A.; Gao, J.; Wu, H.Y.; Woo, C. M. “Synthesis of an electronically-tuned minimally interfering alkynyl photo-affinity label to measure small molecule–protein interactions.” Tetrahedron, 2018, 74, 3273.
  6. Woo, C. M.; Lund, P. J.; Huang, A. C.; Davis, M. M.; Bertozzi, C. R.; Pitteri, S. J. “Mapping and quantification of over 2,000 O-linked glycopeptides in activated human T cells with isotope-targeted glycoproteomics (IsoTaG).” Mol Cell Proteomics 2018, 17, 764.

Flaxman, H. A.; Woo, C. M. “Mapping the small molecule interactome by mass spectrometry.” Biochemistry 2018, 57, 186