Publications

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Wing, R. A., Bailey, S., and Steitz, T. A. (2008) Insights into the replisome from the structure of a ternary complex of the DNA polymerase III alpha-subunit. J Mol Biol. 382, 859-69
Winter, J. M., Cascio, D., Dietrich, D., Sato, M., Watanabe, K., Sawaya, M. R., Vederas, J. C., and Tang, Y. (2015) Biochemical and Structural Basis for Controlling Chemical Modularity in Fungal Polyketide Biosynthesis. J Am Chem Soc. 137, 9885-93
Winter, G. E., Buckley, D. L., Paulk, J., Roberts, J. M., Souza, A., Dhe-Paganon, S., and Bradner, J. E. (2015) DRUG DEVELOPMENT. Phthalimide conjugation as a strategy for in vivo target protein degradation. Science. 348, 1376-81
R Wiseman, L., Zhang, Y., Lee, K. P. K., Harding, H. P., Haynes, C. M., Price, J., Sicheri, F., and Ron, D. (2010) Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. Mol Cell. 38, 291-304
Witkowski, W. A., and Hardy, J. A. (2011) A designed redox-controlled caspase. Protein Sci. 20, 1421-31
Wittenborn, E. C. (2017) Structural Enzymology of Bacterial Carbon Fixation and Storage. Ph.D. thesis, Massachusetts Institute of Technology, Cambridge, Massachusetts
Wittenborn, E. C., Merrouch, M., Ueda, C., Fradale, L., Léger, C., Fourmond, V., Pandelia, M. - E., Dementin, S., and Drennan, C. L. (2018) Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase. Elife. 10.7554/eLife.39451
Wittenborn, E. C., Guendon, C., Merrouch, M., Benvenuti, M., Fourmond, V., Léger, C., Drennan, C. L., and Dementin, S. (2020) The Solvent-Exposed Fe-S D-Cluster Contributes to Oxygen-Resistance in Ni-Fe Carbon Monoxide Dehydrogenase. ACS Catal. 10, 7328-7335
Wittenborn, E. C., Cohen, S. E., Merrouch, M., Léger, C., Fourmond, V., Dementin, S., and Drennan, C. L. (2019) Structural insight into metallocofactor maturation in carbon monoxide dehydrogenase. J Biol Chem. 294, 13017-13026
Wittenborn, E. C., Jost, M., Wei, Y., Stubbe, J. A., and Drennan, C. L. (2016) Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator. J Biol Chem. 291, 25264-25277
Wittlinger, F., Ogboo, B. C., Shevchenko, E., Damghani, T., Pham, C. D., Schaeffner, I. K., Oligny, B. T., Chitnis, S. P., Beyett, T. S., Rasch, A., Buckley, B., Urul, D. A., Shaurova, T., May, E. W., Schaefer, E. M., Eck, M. J., Hershberger, P. A., Poso, A., Laufer, S. A., and Heppner, D. E. (2024) Linking ATP and allosteric sites to achieve superadditive binding with bivalent EGFR kinase inhibitors. Commun Chem. 7, 38
Wittlinger, F., Heppner, D. E., To, C., Günther, M., Shin, B. Hee, Rana, J. K., Schmoker, A. M., Beyett, T. S., Berger, L. M., Berger, B. - T., Bauer, N., Vasta, J. D., Corona, C. R., Robers, M. B., Knapp, S., Jänne, P. A., Eck, M. J., and Laufer, S. A. (2021) Design of a "Two-in-One" Mutant-Selective Epidermal Growth Factor Receptor Inhibitor That Spans the Orthosteric and Allosteric Sites. J Med Chem. 10.1021/acs.jmedchem.1c00848
Wohlever, M. L., Mateja, A., McGilvray, P. T., Day, K. J., and Keenan, R. J. (2017) Msp1 Is a Membrane Protein Dislocase for Tail-Anchored Proteins. Mol Cell. 67, 194-202.e6
Wojcik, J., Lamontanara, A. Joaquim, Grabe, G., Koide, A., Akin, L., Gerig, B., Hantschel, O., and Koide, S. (2016) Allosteric Inhibition of Bcr-Abl Kinase by High Affinity Monobody Inhibitors Directed to the Src Homology 2 (SH2)-Kinase Interface. J Biol Chem. 291, 8836-47
Wolfe, L. S., Calabrese, M. F., Nath, A., Blaho, D. V., Miranker, A. D., and Xiong, Y. (2010) Protein-induced photophysical changes to the amyloid indicator dye thioflavin T. Proc Natl Acad Sci U S A. 107, 16863-8
Wong, S. J., Gearhart, M. D., Taylor, A. B., Nanyes, D. R., Ha, D. J., Robinson, A. K., Artigas, J. A., Lee, O. J., Demeler, B., P Hart, J., Bardwell, V. J., and Kim, C. A. (2016) KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires Cooperation between PCGF1 and BCORL1. Structure. 24, 1795-1801
Wong, E. V., Cao, W., Vörös, J., Merchant, M., Modis, Y., Hackney, D. D., Montpetit, B., and De La Cruz, E. M. (2016) P(I) Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5). J Mol Biol. 428, 492-508
Wong, C., Fujimori, D. Galonić, Walsh, C. T., and Drennan, C. L. (2009) Structural analysis of an open active site conformation of nonheme iron halogenase CytC3. J Am Chem Soc. 131, 4872-9
Wong, Y. Liang, Anzola, J. V., Davis, R. L., Yoon, M., Motamedi, A., Kroll, A., Seo, C. P., Hsia, J. E., Kim, S. K., Mitchell, J. W., Mitchell, B. J., Desai, A., Gahman, T. C., Shiau, A. K., and Oegema, K. (2015) Cell biology. Reversible centriole depletion with an inhibitor of Polo-like kinase 4. Science. 348, 1155-60
Wright, N. J., and Lee, S. - Y. (2019) Structures of human ENT1 in complex with adenosine reuptake inhibitors. Nat Struct Mol Biol. 26, 599-606
Wu, X., Chi, R. J., Baskin, J. M., Lucast, L., Burd, C. G., De Camilli, P., and Reinisch, K. M. (2014) Structural insights into assembly and regulation of the plasma membrane phosphatidylinositol 4-kinase complex. Dev Cell. 28, 19-29
Wu, K., Peng, G., Wilken, M., Geraghty, R. J., and Li, F. (2012) Mechanisms of host receptor adaptation by severe acute respiratory syndrome coronavirus. J Biol Chem. 287, 8904-11
Wu, H., Hu, C., Wang, A., Weisberg, E. L., Chen, Y., Yun, C. - H., Wang, W., Liu, Y., Liu, X., Tian, B., Wang, J., Zhao, Z., Liang, Y., Li, B., Wang, L., Wang, B., Chen, C., Buhrlage, S. J., Qi, Z., Zou, F., Nonami, A., Li, Y., Fernandes, S. M., Adamia, S., Stone, R. M., Galinsky, I. A., Wang, X., Yang, G., Griffin, J. D., Brown, J. R., Eck, M. J., Liu, J., Gray, N. S., and Liu, Q. (2016) Discovery of a BTK/MNK dual inhibitor for lymphoma and leukemia. Leukemia. 30, 173-81
Wu, X., and Rapoport, T. A. (2021) Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (Legobodies). Proc Natl Acad Sci U S A. 10.1073/pnas.2115001118
Wu, A., Salom, D., Hong, J. D., Tworak, A., Watanabe, K., Pardon, E., Steyaert, J., Kandori, H., Katayama, K., Kiser, P. D., and Palczewski, K. (2023) Structural basis for the allosteric modulation of rhodopsin by nanobody binding to its extracellular domain. Nat Commun. 14, 5209

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