Publications

Found 42 results
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Heppner, D. E., Günther, M., Wittlinger, F., Laufer, S. A., and Eck, M. J. (2020) Structural Basis for EGFR Mutant Inhibition by Trisubstituted Imidazole Inhibitors. J Med Chem. 10.1021/acs.jmedchem.0c00200
Heppner, D. E., Wittlinger, F., Beyett, T. S., Shaurova, T., Urul, D. A., Buckley, B., Pham, C. D., Schaeffner, I. K., Yang, B., Ogboo, B. C., May, E. W., Schaefer, E. M., Eck, M. J., Laufer, S. A., and Hershberger, P. A. (2022) Structural Basis for Inhibition of Mutant EGFR with Lazertinib (YH25448). ACS Med Chem Lett. 13, 1856-1863
Lietha, D., Cai, X., Ceccarelli, D. F. J., Li, Y., Schaller, M. D., and Eck, M. J. (2007) Structural basis for the autoinhibition of focal adhesion kinase. Cell. 129, 1177-87
Dempsey, D. R., Viennet, T., Iwase, R., Park, E., Henriquez, S., Chen, Z., Jeliazkov, J. R., Palanski, B. A., Phan, K. L., Coote, P., Gray, J. J., Eck, M. J., Gabelli, S. B., Arthanari, H., and Cole, P. A. (2021) The structural basis of PTEN regulation by multi-site phosphorylation. Nat Struct Mol Biol. 28, 858-868
Yasuda, H., Park, E., Yun, C. -hong, Sng, N. J., Lucena-Araujo, A. R., Yeo, W. - L., Huberman, M. S., Cohen, D. W., Nakayama, S., Ishioka, K., Yamaguchi, N., Hanna, M., Oxnard, G. R., Lathan, C. S., Moran, T., Sequist, L. V., Chaft, J. E., Riely, G. J., Arcila, M. E., Soo, R. A., Meyerson, M., Eck, M. J., Kobayashi, S. S., and Costa, D. B. (2013) Structural, biochemical, and clinical characterization of epidermal growth factor receptor (EGFR) exon 20 insertion mutations in lung cancer. Sci Transl Med. 5, 216ra177
Vizcarra, C. L., Kreutz, B., Rodal, A. A., Toms, A. V., Lu, J., Zheng, W., Quinlan, M. E., and Eck, M. J. (2011) Structure and function of the interacting domains of Spire and Fmn-family formins. Proc Natl Acad Sci U S A. 108, 11884-9
Park, E., Kim, N., Ficarro, S. B., Zhang, Y., Lee, B. Il, Cho, A., Kim, K., Park, A. K. J., Park, W. - Y., Murray, B., Meyerson, M., Beroukhim, R., Marto, J. A., Cho, J., and Eck, M. J. (2015) Structure and mechanism of activity-based inhibition of the EGF receptor by Mig6. Nat Struct Mol Biol. 22, 703-711
Tkacik, E., Li, K., Del Pino, G. Gonzalez-, Ha, B. Hak, Vinals, J., Park, E., Beyett, T. S., and Eck, M. J. (2023) Structure and RAF family kinase isoform selectivity of type II RAF inhibitors tovorafenib and naporafenib. J Biol Chem. 299, 104634
Tu, D., Zhu, Z., Zhou, A. Y., Yun, C. -hong, Lee, K. - E., Toms, A. V., Li, Y., Dunn, G. P., Chan, E., Thai, T., Yang, S., Ficarro, S. B., Marto, J. A., Jeon, H., Hahn, W. C., Barbie, D. A., and Eck, M. J. (2013) Structure and ubiquitination-dependent activation of TANK-binding kinase 1. Cell Rep. 3, 747-58
Park, E., Graziano, B. R., Zheng, W., Garabedian, M., Goode, B. L., and Eck, M. J. (2015) Structure of a Bud6/Actin Complex Reveals a Novel WH2-like Actin Monomer Recruitment Motif. Structure. 23, 1492-1499
Toms, A. V., Deshpande, A., McNally, R., Jeong, Y., Rogers, J. M., Kim, C. Un, Gruner, S. M., Ficarro, S. B., Marto, J. A., Sattler, M., Griffin, J. D., and Eck, M. J. (2013) Structure of a pseudokinase-domain switch that controls oncogenic activation of Jak kinases. Nat Struct Mol Biol. 20, 1221-3
Lu, J., Meng, W., Poy, F., Maiti, S., Goode, B. L., and Eck, M. J. (2007) Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly. J Mol Biol. 369, 1258-69
Tu, D., Graziano, B. R., Park, E., Zheng, W., Li, Y., Goode, B. L., and Eck, M. J. (2012) Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6. Proc Natl Acad Sci U S A. 109, E3424-33
Blair, J. A., Rauh, D., Kung, C., Yun, C. -hong, Fan, Q. - W., Rode, H., Zhang, C., Eck, M. J., Weiss, W. A., and Shokat, K. M. (2007) Structure-guided development of affinity probes for tyrosine kinases using chemical genetics. Nat Chem Biol. 3, 229-38
Yun, C. -hong, Boggon, T. J., Li, Y., Woo, M. S., Greulich, H., Meyerson, M., and Eck, M. J. (2007) Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity. Cancer Cell. 11, 217-27
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Yun, C. -hong, Mengwasser, K. E., Toms, A. V., Woo, M. S., Greulich, H., Wong, K. - K., Meyerson, M., and Eck, M. J. (2008) The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP. Proc Natl Acad Sci U S A. 105, 2070-5
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Li, Z., Lu, W., Beyett, T. S., Ficarro, S. B., Jiang, J., Tse, J., Kim, A. Yong- Ju, Marto, J. A., Che, J., Jänne, P. A., Eck, M. J., Zhang, T., and Gray, N. S. (2024) ZNL0325, a Pyrazolopyrimidine-Based Covalent Probe, Demonstrates an Alternative Binding Mode for Kinases. J Med Chem. 67, 2837-2848

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