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
Chemical approaches to the study of protein tyrosine kinases and their implications for mechanism and inhibitor design.
Authors: Authors: Cole PA, Sondhi D, Kim K.
Pharmacol Ther
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Indoleamine analogs as probes of the substrate selectivity and catalytic mechanism of serotonin N-acetyltransferase.
Authors: Authors: Khalil EM, De Angelis J, Cole PA.
J Biol Chem
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Expressed protein ligation: a general method for protein engineering.
Authors: Authors: Muir TW, Sondhi D, Cole PA.
Proc Natl Acad Sci U S A
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Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (EC 2.3.1.87).
Authors: Authors: De Angelis J, Gastel J, Klein DC, Cole PA.
J Biol Chem
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Peptide and protein phosphorylation by protein tyrosine kinase Csk: insights into specificity and mechanism.
Authors: Authors: Sondhi D, Xu W, Songyang Z, Eck MJ, Cole PA.
Biochemistry
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Divalent ion effects and insights into the catalytic mechanism of protein tyrosine kinase Csk.
Authors: Authors: Grace MR, Walsh CT, Cole PA.
Biochemistry
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Chaperone-assisted protein expression.
Authors: Authors: Cole PA.
Structure
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The role of the catalytic base in the protein tyrosine kinase Csk.
Authors: Authors: Cole PA, Grace MR, Phillips RS, Burn P, Walsh CT.
J Biol Chem
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Evaluation of the catalytic mechanism of recombinant human Csk (C-terminal Src kinase) using nucleotide analogs and viscosity effects.
Authors: Authors: Cole PA, Burn P, Takacs B, Walsh CT.
J Biol Chem
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Mechanism and inhibition of cytochrome P-450 aromatase.
Authors: Authors: Cole PA, Robinson CH.
J Med Chem
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