Picture of Phil Cole

Philip A. Cole, M.D., Ph.D.

Professor of Medicine and Biological Chemistry and Molecular Pharmacology

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. 

Phil Cole graduated from Yale University with a B.S. in Chemistry in 1984 and then spent a year as a Churchill Scholar at the University of Cambridge.  Cole went on to obtain M.D. and Ph.D. degrees from Johns Hopkins where he pursued research in bioorganic chemistry in 1991.  Cole then entered clinical and post-doctoral training at Brigham and Women's Hospital and Harvard Medical School prior to joining Rockefeller University in 1996 as a junior lab head.  In 1999, Cole returned to Johns Hopkins as professor and director of pharmacology where he served until 2017, when he moved to Harvard Medical School and Brigham and Women's Hospital as professor of medicine and biological chemistry and molecular pharmacology.  His research interests are in the area of chemical biology, protein post-translational modifications, cell signaling, and epigenetics.

Research:

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.

Address: 

New Research Building

77 Avenue Louis Pasteur

Room 168C

Boston, MA 02115

Publications View
Inhibition of Epstein-Barr virus-induced growth proliferation by a nuclear antigen EBNA2-TAT peptide.
Authors: Authors: Farrell CJ, Lee JM, Shin EC, Cebrat M, Cole PA, Hayward SD.
Proc Natl Acad Sci U S A
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Inhibition of Epstein-Barr virus-induced growth proliferation by a nuclear antigen EBNA2-TAT peptide.
Authors: Authors: Farrell CJ, Lee JM, Shin EC, Cebrat M, Cole PA, Hayward SD.
Proc Natl Acad Sci U S A
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Selective HAT inhibitors as mechanistic tools for protein acetylation.
Authors: Authors: Zheng Y, Thompson PR, Cebrat M, Wang L, Devlin MK, Alani RM, Cole PA.
Methods Enzymol
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Selective HAT inhibitors as mechanistic tools for protein acetylation.
Authors: Authors: Zheng Y, Thompson PR, Cebrat M, Wang L, Devlin MK, Alani RM, Cole PA.
Methods Enzymol
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Conversion of a tyrosine kinase protein substrate to a high affinity ligand by ATP linkage.
Authors: Authors: Shen K, Cole PA.
J Am Chem Soc
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Conversion of a tyrosine kinase protein substrate to a high affinity ligand by ATP linkage.
Authors: Authors: Shen K, Cole PA.
J Am Chem Soc
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Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation.
Authors: Authors: Zheng W, Zhang Z, Ganguly S, Weller JL, Klein DC, Cole PA.
Nat Struct Biol
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Protein tyrosine kinases Src and Csk: a tail's tale.
Authors: Authors: Cole PA, Shen K, Qiao Y, Wang D.
Curr Opin Chem Biol
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Novel bisubstrate analog inhibitors of serotonin N-acetyltransferase: the importance of being neutral.
Authors: Authors: Zheng W, Cole PA.
Bioorg Chem
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Synthesis and analysis of potential prodrugs of coenzyme A analogues for the inhibition of the histone acetyltransferase p300.
Authors: Authors: Cebrat M, Kim CM, Thompson PR, Daugherty M, Cole PA.
Bioorg Med Chem
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