Faculty Summaries
James S. Duncan, PhD
James S. Duncan, PhD
Assistant Professor
Office Phone: 215-728-2565
Lab Phone: 215-728-2565
Office: P3039


  • Cooper, M.J., Cox, N.J., Zimmerman, E.I,. Dewar, B.J., Duncan, J.S., Whittle, M.C., Nguyen, T.A., Jones, L.S., Ghose Roy, S., Smalley, D.M., Kuan, P.F., Richards, K.L., Christopherson, R.I., Jin, J., Frye, S.V, Johnson, G.L., Baldwin, A.S., Graves, L.M. Application of multiplexed kinase inhibitor beads to study kinome adaptations in drug-resistant leukemia. PLoS One 8:e66755, 2013. 
  • Graves, L.M., Duncan, J.S., Whittle, M.C., Johnson, G.L.  The dynamic nature of the kinome.  Biochem. J. 450:1-8, 2013.  (Review)
  • Duncan, J.S., Whittle, M.C., Nakamura, K., Abell, A.N., Midland, A.A., Zawistowski, J.S., Johnson, N.L., Granger, D.A., Vincent, N.J., Darr, D.B., Usary, J., Kuan, P.F., Smalley, D.M., Major, B., He, X., Hoadley, K., Zhou, B., Sharpless, N.E., Perou, C.M., Kim, W.Y., Gomez, S.M., Chen, X., Jin, J., Frye, S.V., Earp, H.S., Graves, L.M., Johnson, G.L.  Dynamic reprogramming of the kinome in response to targeted MEK inhibition in triple negative breast cancer.  Cell 149:307-321, 2012.
  • Roberts, P.J., Usary, J., Darr, D., Dillon, P.M., Pfefferle, A.D., Whittle, M.C., Duncan, J.S., Johnson, S.M., Combest, A., Jin, J., Zamboni, W.C., Johnson, G.L., Perou, C.M., Sharpless, N.E.  Combined PI3K/mTOR and MEK inhibition provides broad antitumor activity in faithful murine cancer models.   Clin. Cancer Res. 18:5290-5303, 2012. 
  • Midland, A.A., Whittle, M.C., Duncan, J.S., Abell, A.N., Nakamura, K., Zawistowski, J.S., Carey, L.A., Earp, H.S., Graves, L.M., Gomez, S.M., Johnson, G.L.  Defining the expressed breast cancer kinome.  Cell Res. 22:620-623, 2012. 
  • Duncan, J.S., Haystead, T.A., Litchfield, D.W. Chemoproteomic characterization of protein kinase inhibitors using immobilized ATP.  Kinase Inhibitors: Methods and Protocols, Methods Mol. Biol.  795:119-134, 2012. 
  • Gyenis, L., Duncan, J.S., Turowec, J.P., Bretner, M., Litchfield, D.W. Unbiased functional proteomics strategy for protein kinase inhibitor validation and identification of bona fide protein kinase substrates: Application to identification of EEF1FD as a substrate for CK2. J. Proteome Res. 10:4887-4901, 2011.  
  • Turowec, J.P., Duncan, J.S., Gloor, G.B., Litchfield, D.W.  Regulation of caspase pathways by protein kinase CK2: identification of proteins with overlapping CK2 and caspase consensus motifs.  Mol. Cell Biochem. 356:159-167, 2011. 
  • Duncan, J.S., Turowec, J.P., Wu, C., Duncan, K.E., Vilk, G., Wu, C. Luscher, B., Li, S.C., Gloor, G.B. Litchfield, D.W.  A peptide-based target screen implicates the protein kinase CK2 in the global regulation of caspase signaling.  Sci. Signal. 4:ra30. 2011.   
  • Turowec, J.P., Duncan, J.S., French, A.C., Gyenis, L., St. Denis, N.A., Vilk, G., Litchfield, D.W.  Protein kinase CK2 is a constitutively active enzyme that promotes cell survival: strategies to identify CK2 substrates and manipulate its activity in mammalian cells. Methods Enzymol. 484:471-493, 2010. 
  • Duncan, J.S., Turowec, J.P., Vilk, G., Li, S.S., Gloor, G.B., Litchfield, D.W. Regulation of cell proliferation and survival: convergence of protein kinases and caspases. Biochim. Biophys. Acta 1804:505-510, 2010. 
  • Kerman, K., Song, H., Duncan, J.S., Litchfield, D.W., Kraatz, H-B.  Peptide biosensors for the electrochemical measurement of protein kinase activity.  Anal. Chem, 80:9395-9401, 2008. 
  • Duncan, J.S., Gyenis, L., Lenehan, J., Bretner, M., Graves, LM., Haystead, TA., Litchfield, DW. An unbiased evaluation of CK2 inhibitors by chemo-proteomics: characterization of inhibitor effects on CK2 and identification of novel inhibitor targets. Mol. Cell Proteomics 7:1077-1088, 2008. 
  • Duncan, J.S., Litchfield, D.W. Too much of a good thing: the role of protein kinase CK2 in tumorigenesis and prospects for therapeutic inhibition of CK2.  Biochim. Biophys. Acta. 1784:33-47, 2008.
  • Zien, P., Duncan, J.S., Skierski, J., Bretner, M., Litchfield, D.W., Shugar, D. Tetrabromobenzotriazole (TBBt) and tetrabromobenzimidazole (TBBz) as selective inhibitors of protein kinase CK2:  Evaluation of their effects on cells and different molecular forms of human CK2.  Biochim. Biophys. Acta 1754:271-280, 2005.