BBS Faculty Member - Philip Cole

Philip Cole

Deparment of Medicine, BWH
Department of Biological Chemistry and Molecular Pharmacology, HMS

Harvard Medical School
New Research Building, Room 168C
77 Avenue Louis Pasteur
Boston, MA 02115
Tel: 617-525-5208
Email: pacole@bwh.harvard.edu



Our research involves the chemical biology of protein post-translational modifcations (PTMs) in the context of signaling, epigenetics, and cancer. We develop and apply chemical approaches including protein semisynthesis and small molecule probes to the study of protein phosphorylation, acetylation, ubiquitination, and other PTMs in enzymes and cellular networks. We are currently investigating the functions, regulation, and mechanisms of PTEN lipid phosphatase, Akt protein kinase, NEDD4 ubiquitin ligases, LSD1 histone demethylase, HDAC1 deacetylase, the CoREST complex, and p300/CBP acetyltransferase. We strive to translate our findings in signaling and epigenetics to identify novel therapeutic opportunities for the treatment of cancer and other diseases.



Last Update: 10/5/2017



Publications

Henager, S., Chu, N., Chen, Z., Bolduc, D. M., Dempsey, D. R., Hwang, Y., Wells, J., Cole, P.A. (2016) Enzyme-Catalyzed Expressed Protein Ligation Nature Methods 13, 925-927.

Chen, Z., Jiang, H., Xu, W., Li, X., Dempsey, D. R., Zhang, X., Devreotes, P., Wolberger, C., Amzel, M., Gabelli, S., and Cole, P.A. (2017) A Tunable Brake for HECT Ubiquitin Ligases
Molecular Cell 66, 345-357.

Lasko, L.M., Jakob, C.G., Edalji, R.P., Qiu, W., Montgomery, D., Digiammarino, E., Hansen, T.M., Risl, R., Frey, R., Manaves, V., Shaw, B., Algire, M., Hessler, P., Lam, L., Uziel, T., Faivre, E., Ferguson, D., Buchanan, F., Martin, R.L., Torrent, M., Chiang, G. G., Karukurichi, K., Langston, J. W., de Vries, P., Van Drie, J.H., McElligott, D., Kesicki, E., Marmorstein, R., Sun, C., Cole, P.A., Rosenberg, S.H., Michaelides, M.R., Lai, A., Bromberg, K.D. (2017) Discovery of a Potent Catalytic p300/CBP Inhibitor that Targets Lineage-Specific Tumors
Nature, in press.



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