The Cravatt Lab
Protein and Ligand Discovery on a Global Scale
Genomics has revolutionized our understanding of the genetic basis of human physiology and disease. Nonetheless, many disease-relevant genes code for proteins that remain poorly characterized and therapeutically unactionable due, in large part, to a dearth of selective chemical tools. Our research aims to address this challenge by developing and applying innovative chemical proteomic platforms, such as activity-based protein profiling, to enrich our understanding of disease-relevant proteins and to accelerate the discovery of chemical probes for these proteins.
Recent Publications
Ogasawara, D., Konrad, D. B., Tan, Z. Y., Carey, K. L., Luo, J., Won, S. J., Li, H., Carter, T. R., DeMeester, K. E., Njomen, E., Schreiber, S. L., Xavier, R. J., Melillo, B., & Cravatt, B. F. (2024). Chemical tools to expand the ligandable proteome: Diversity-oriented synthesis-based photoreactive stereoprobes. Cell Chem Biol. https://doi.org/10.1016/j.chembiol.2024.10.005
Won, S. J., Zhang, Y., Reinhardt, C. J., Hargis, L. M., MacRae, N. S., DeMeester, K. E., Njomen, E., Remsberg, J. R., Melillo, B., Cravatt, B. F., & Erb, M. A. (2024). Redirecting the pioneering function of FOXA1 with covalent small molecules. Mol Cell. https://doi.org/10.1016/j.molcel.2024.09.024
Njomen, E., Hayward, R. E., DeMeester, K. E., Ogasawara, D., Dix, M. M., Nguyen, T., Ashby, P., Simon, G. M., Schreiber, S. L., Melillo, B., & Cravatt, B. F. (2024). Multi-tiered chemical proteomic maps of tryptoline acrylamide–protein interactions in cancer cells. Nature Chemistry. https://doi.org/10.1038/s41557-024-01601-1
Cover Illustration by David S. Goodsell, RCSB Protein Data Bank. doi: 10.2210/rcsb_pdb/goodsell-gallery-041