Publications, 2005-2009
N. Yokoyama, I. Ischenko, M.J. Hayman, and W.T. Miller (2005). The C-terminus of the RON tyrosine kinase plays an autoinhibitory role. J. Biol. Chem 280, 8893-8900.
H. Qiu, F. Zappaosta, W. Su, R.S. Annan, and W.T. Miller (2005). Interaction between Brk kinase and insulin receptor substrate-4. Oncogene 24, 5656-5664.
N. Yokoyama, C.D. deBakker, F. Zappacosta, M.J. Huddleston, R.S. Annan, K.S. Ravichandran, and W.T. Miller (2005). Identification of tyrosine residues on ELMO1 that are phosphorylated by the Src-family kinase Hck. Biochemistry 44, 8841-8849.
L. Carlisle-Moore, C.R. Gordon, C.A. Machutta, W.T. Miller, and P.J. Tonge (2005). Substrate recognition by the human fatty acid synthase. J. Biol. Chem 280, 42612-42618.
N. Yokoyama, J. Lougheed, and W.T. Miller (2005). Phosphorylation of WASP by the Cdc42-associated kinase ACK1: Dual hydroxyamino acid specificity in a tyrosine kinase. J. Biol. Chem 280, 42219-42226.
J. DaSilva, H.-J. Kim, L.Z. Xu, W.T. Miller, and D. Bar-Sagi (2006). Regulation of Sprouty stability by MNK1-dependent phosphorylation. Mol. Cell. Biol. 26, 1898-1907.
N. Yokoyama and W.T. Miller (2006). Purification and enzyme activity of ACK1. Methods Enz. 406, 250-260..
L. Liu, Y. Gao, W.T. Miller, V. Poli, and N.C. Reich (2006). Identification of STAT3 as a specific substrate of the breast tumor kinase (Brk). Oncogene 25, 4904-4912.
P. Patwardhan, Y. Shen, G. Goldberg, and W.T. Miller (2006). Individual Cas phosphorylation sites are dispensable for processive phosphorylation by Src and anchorage-independent cell growth . J. Biol. Chem 281, 20689-20697.
W. Li and W.T. Miller (2006). Role of the activation loop tyrosines in regulation of the insulin-like growth factor I receptor tyrosine kinase. J. Biol. Chem 281, 23785-23791.
S.R. Hubbard and W.T. Miller (2007). Receptor tyrosine kinases: mechanisms of activation and signaling. Curr. Opin. Cell Biol. 19, 117-123.
B.P. Craddock, C. Cotter, and W.T. Miller (2007). Autoinhibition of the insulin-like growth factor I receptor by the juxtamembrane region. FEBS Lett. 581, 3235-3240.
S.S. Yadav and W.T. Miller (2007). Cooperative activation of Src-family kinases by SH3 and SH2 ligands. Cancer Lett 257, 116-123.
P. Patwardhan and W.T. Miller (2007). Processive phosphorylation: mechanism and biological importance. Cell Signal. 19, 2218-2226.
H. Chen, J. Ma, W. Li, A.V. Eliseenkova, C. Xu, T.A. Neubert, W.T. Miller, and M. Mohammadi (2007). A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases. Molecular Cell. 27, 717-730.
N. King, M.J. Westbrook, S.L. Young, A. Kuo, M. Abedin, J. Chapman, S. Fairclough, U. Hellsten, Y. Isogai, I. Letunic, M. Marr, D. Pincus, N. Putnam, A. Rokas, K.J. Wright, R. Zuzow, W. Dirks, M. Good, D. Goodstein, D. Lemons, W. Li, J. Lyons, A. Morris, S. Nichols, D.J. Richter, A. Salamov, JGI Sequencing, P. Bork, W.A. Lim, G. Manning, W.T. Miller, W. McGinnis, H. Shapiro, R. Tjian, I.V. Grigoriev, and D. Rohhsar (2008). The genome of the choanoflagellate Monosiga brevicollis and the origins of metazoans. Nature 451, 783-788.
W. Li, S.L. Young, N. King, and W.T. Miller (2008). Signaling properties of a non-metazoan Src kinase and the evolutionary history of Src negative regulation. J. Biol. Chem. 283, 15491-15501.
G. Manning, S.L. Young, W.T. Miller, and Y. Zhai (2008). The protist, Monosiga brevicollis, has a tyrosine kinase signaling network more elaborate and diverse than found in any metazoan. Proc. Natl. Acad. Sci. USA. 105, 9674-9679.
J. Wu, W. Li, B.P. Craddock, K.W. Foreman, M.J. Mulvihill, Q.Ji, W.T. Miller, and S.R. Hubbard (2008). Small-molecule inhibition and activation loop trans-autophosphorylation of the IGF1 receptor. EMBO Journal. 27, 1985-1994.
B. Xiang, K. Chatti, H. Qiu, B. Lakshmi, A. Krasnitz, J. Hicks, W.T. Miller, and S.K. Muthuswamy (2008). Brk is coamplified with ErbB2 to promote proliferation in breast cancer. Proc. Natl. Acad. Sci. USA. 105, 12463-12468.
S.S. Yadav and W.T. Miller (2008). The evolutionarily conserved arrangement of domains in Src family kinases is important for substrate recognition. Biochemistry 47, 10871-10880.
E. Ozkirimli, S.S. Yadav, W.T. Miller, and C.B. Post (2008). An electrostatic network and long-range regulation of Src kinases. Protein Science 17, 1871-1880.
H. Chen, C. Xu, J. Ma, A.V. Eliseenkova, W. Li, P.M. Pollock, N. Pitteloud, W.T. Miller, T.A. Neubert, and M. Mohammadi (2008). A crystallographic snapshot of tyrosine trans-autophosphorylation in action. Proc. Natl. Acad. Sci. USA 105, 19660-19665.
W. Li, S. Scarlata, and W.T. Miller (2009). Evidence for convergent evolution in the signaling properties of a choanoflagellate tyrosine kinase. Biochemistry 48, 5180-5186.
P. Patwardhan, K. Shiba, C. Gordon, B.P. Craddock, M. Tamiko, and W.T. Miller (2009). Synthesis of functional signaling domains by combinatorial polymerization of phosphorylation motifs. ACS Chem. Biol 4, 751-758.
S.S. Yadav, B.J. Yeh, B.P. Craddock, W.A. Lim, and W.T. Miller (2009). Reengineering the signaling properties of a Src family kinase. Biochemistry 48, 10956-10962.