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
Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insights from NMR mapping studies and site-directed mutagenesis.
Authors: Authors: Shekhtman A, Ghose R, Wang D, Cole PA, Cowburn D.
J Mol Biol
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Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling.
Authors: Authors: Lu W, Gong D, Bar-Sagi D, Cole PA.
Mol Cell
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Protein tyrosine kinase Csk-catalyzed phosphorylation of Src containing unnatural tyrosine analogues.
Authors: Authors: Wang D, Cole PA.
J Am Chem Soc
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Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity.
Authors: Authors: Thompson PR, Kurooka H, Nakatani Y, Cole PA.
J Biol Chem
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Bisubstrate ketone analogues as serotonin N-acetyltransferase inhibitors.
Authors: Authors: Kim CM, Cole PA.
J Med Chem
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Probing the mechanism of enzymatic phosphoryl transfer with a chemical trick.
Authors: Authors: Thompson PR, Cole PA.
Proc Natl Acad Sci U S A
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Kinase chips hit the proteomics era.
Authors: Authors: Williams DM, Cole PA.
Trends Biochem Sci
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Mechanistic studies on the alkyltransferase activity of serotonin N-acetyltransferase.
Authors: Authors: Zheng W, Scheibner KA, Ho AK, Cole PA.
Chem Biol
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Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail.
Authors: Authors: Wang D, Huang XY, Cole PA.
Biochemistry
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Mechanism-based design of a protein kinase inhibitor.
Authors: Authors: Parang K, Till JH, Ablooglu AJ, Kohanski RA, Hubbard SR, Cole PA.
Nat Struct Biol
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